ID   Q50214_METMT   PRELIMINARY;   PRT;   163 AA.
AC   Q50214;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   30-MAY-2006, entry version 25.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrI;
OS   Methanococcoides methylutens.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=2226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=96174929; PubMed=8590683;
RA   Springer E., Sachs M.S., Woese C.R., Boone D.R.;
RT   "Partial gene sequences for the A subunit of methyl-coenzyme M
RT   reductase (mcrI) as a phylogenetic tool for Methanosarcinaceae.";
RL   Int. J. Syst. Bacteriol. 45:554-559(1995).
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DR   EMBL; U22235; AAC43410.1; -; Genomic_DNA.
DR   HSSP; P07962; 1E6Y.
DR   SMR; Q50214; 1-163.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     163    163
SQ   SEQUENCE   163 AA;  17548 MW;  9E1945AD201B2C68 CRC64;
     GSYMSGGVGF TQYATAAYTN NILDDNLYYN VDYINDKYDG AANKGTDNKV KATMDVVKDI
     ATESTIYGLE NYEKYPTALE DHFGGSQRAT VLSAAAGSAT ALATGNGNAG LSAWYLSMYL
     HKEAHGRLGF FGFDLQDQCG ATNVFSFQSD EGLPVELRGP NYP
//

ID   Q8NKL4_9EURY   PRELIMINARY;   PRT;   239 AA.
AC   Q8NKL4;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   30-MAY-2006, entry version 13.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogenic archaeon.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=198240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Galand P.E., Saarnio S., Fritze H., Yrjala K.;
RT   "Depth related diversity of methanogen Archaea in Finnish oligotrophic
RT   fen.";
RL   FEMS Microbiol. Ecol. 42:441-449(2002).
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DR   EMBL; AJ489768; CAD33991.2; -; Genomic_DNA.
DR   HSSP; P07962; 1E6Y.
DR   SMR; Q8NKL4; 1-238.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   InterPro; IPR003183; MCR_alpha_N.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
FT   NON_TER       1      1
FT   NON_TER     239    239
SQ   SEQUENCE   239 AA;  25658 MW;  7FC48B771D61AC25 CRC64;
     FIAAYNMCAG EAAVADLAFA AKHASLVEMA NMLPARRARG PNEPGGLSFG FMADMVQTDR
     IYPDDPVRSP LEVVAAGCML YDQIWLGSYM SGGVGFTQYA TAAYTDNILD DYSYYGNDYA
     KKYGANGKAP KTMDVVNDIA TEVTLYGIEQ YEKYPTTLED HFGGSQRATV LAAASGVAAA
     IATGNSNAGL SAWYLSMLLH KDAWGRLGFY GYDLQDQCGS TNVFSVRSDE GSPDELRGA
//

ID   O93734_9EURY   PRELIMINARY;   PRT;   330 AA.
AC   O93734;
DT   01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1999, sequence version 1.
DT   30-MAY-2006, entry version 22.
DE   F420-dependent alcohol dehydrogenase (Fragment).
GN   Name=adf;
OS   Methanoculleus thermophilus.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales;
OC   Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=2200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Berk H., Thauer R.K.;
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   PubMed=15016352; DOI=10.1016/j.str.2004.02.010;
RA   Aufhammer S.W., Warkentin E., Berk H., Shima S., Thauer R.K.,
RA   Ermler U.;
RT   "Coenzyme binding in F420-dependent secondary alcohol dehydrogenase, a
RT   member of the bacterial luciferase family.";
RL   Structure 12:361-370(2004).
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DR   EMBL; Y18729; CAA77275.1; -; Genomic_DNA.
DR   PDB; 1RHC; X-ray; A=1-330.
DR   InterPro; IPR011251; Luciferase_like.
DR   Pfam; PF00296; Bac_luciferase; 1.
FT   NON_TER     330    330
SQ   SEQUENCE   330 AA;  37158 MW;  CD1528E3B0AF11EB CRC64;
     MKTQIGYFAS LEQYRPMDAL EQAIRAEKVG FDSVWVDDHF HPWYHDNAQS AQAWAWMGAA
     LQATKKVFIS TCITCPIMRY NPAIVAQTFA TLRQMYPGRV GVAVGAGEAM NEVPVTGEWP
     SVPVRQDMTV EAVKVMRMLW ESDKPVTFKG DYFTLDKAFL YTKPDDEVPL YFSGMGPKGA
     KLAGMYGDHL MTVAAAPSTL KNVTIPKFEE GAREAGKDPS KMEHAMLIWY SVDPDYDKAV
     EALRFWAGCL VPSMFKYKVY DPKEVQLHAN LVHCDTIKEN YMCATDAEEM IKEIERFKEA
     GINHFCLGNS SPDVNFGIDI FKEVIPAVRD
//

ID   Q50215_9EURY   PRELIMINARY;   PRT;   163 AA.
AC   Q50215;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   30-MAY-2006, entry version 25.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrI;
OS   Methanohalophilus mahii.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=2176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=96174929; PubMed=8590683;
RA   Springer E., Sachs M.S., Woese C.R., Boone D.R.;
RT   "Partial gene sequences for the A subunit of methyl-coenzyme M
RT   reductase (mcrI) as a phylogenetic tool for Methanosarcinaceae.";
RL   Int. J. Syst. Bacteriol. 45:554-559(1995).
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DR   EMBL; U22237; AAC43411.1; -; Genomic_DNA.
DR   HSSP; P07962; 1E6Y.
DR   SMR; Q50215; 1-163.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     163    163
SQ   SEQUENCE   163 AA;  17617 MW;  764122F547B7EDD7 CRC64;
     GSYMSGGVGF TQYSTAAYTN NILDDNLYYD VEYINDKYDG AAEKGIDNKV APSMDVIKDI
     ATESTLYGLE NYEKYPVALE DHFGGSQRAT VLSAAAGSAG SLATGNANAG LSAWYLCMYL
     HKEGHGRLGF FGFDLQDQCG ATNTFSYQSD EGLPHELRGP NYP
//

ID   Q9C4G1_9EURY   PRELIMINARY;   PRT;   157 AA.
AC   Q9C4G1;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   30-MAY-2006, entry version 17.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogen RS-MCR47.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosaetaceae; environmental samples.
OX   NCBI_TaxID=143078;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21217833; PubMed=11321536;
RX   DOI=10.1046/j.1462-2920.2001.00179.x;
RA   Lueders T., Chin K.-J., Conrad R., Friedrich M.;
RT   "Molecular analyses of methyl-coenzyme M reductase alpha-subunit
RT   (mcrA) genes in rice field soil and enrichment cultures reveal the
RT   methanogenic phenotype of a novel archaeal lineage.";
RL   Environ. Microbiol. 3:194-204(2001).
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DR   EMBL; AF313850; AAK16880.1; -; Genomic_DNA.
DR   HSSP; P07962; 1E6Y.
DR   SMR; Q9C4G1; 1-157.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     157    157
SQ   SEQUENCE   157 AA;  16858 MW;  6A87301935FB48DF CRC64;
     GSYMSGGVGF TQYATAAYTN DVLDDFCYYG VDFANDKFGG LAKAPQTLDV AKELGTEVTL
     YGMEQYESFP TLLEDHFGGS QRASVLAAAS GITAAIASGH SQVGLAAWYL SMLLHKEGWG
     RLGFFGYDLQ DQCGPTNVFS YQSDEGNPVE LRGANYP
//

ID   Q59578_METTF   PRELIMINARY;   PRT;   569 AA.
AC   Q59578; O08492; P97184;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   30-MAY-2006, entry version 28.
DE   Tungsten formylmethanofuran dehydrogenase (EC 1.2.99.5).
GN   Name=fwdA;
OS   Methanobacterium thermoformicicum.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=145262;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Marburg/DSM 2133;
RX   MEDLINE=96163477; PubMed=8575452;
RA   Hochheimer A., Schmitz R.A., Thauer R.K., Hedderich R.;
RT   "The tungsten formylmethanofuran dehydrogenase from Methanobacterium
RT   thermoautotrophicum contains sequence motifs characteristic for
RT   enzymes containing molybdopterin dinucleotide.";
RL   Eur. J. Biochem. 234:910-920(1995).
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DR   EMBL; X87970; CAA61213.1; -; Genomic_DNA.
DR   PIR; S63545; S57456.
DR   GO; GO:0018493; F:formylmethanofuran dehydrogenase activity; IEA.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR012027; FwdA.
DR   InterPro; IPR011059; Metal-dep_hydro_comp.
DR   Pfam; PF07969; Amidohydro_3; 1.
DR   PIRSF; PIRSF006453; FwdA; 1.
KW   Oxidoreductase.
SQ   SEQUENCE   569 AA;  62916 MW;  6002F909C6458F99 CRC64;
     MEYIIKNGFV YCPLNNVDGE KMDICLRDGK IVESVSDSAK VIDASGKIVM PGGVDPHSHI
     AGAKVNVGRM YRPEDSRRDA EKFKAGRAGS GFSVPSTFMT GYRYAQMGYT TAMEAAMPPL
     LARHTHEEFH DTPIIDHAAY PLFGNNWFVM EYLKEGDVDA CAAYASWLLK ATKGYTIKIV
     NPAGTEAWGW GGNVHGIHDP APYFDITPAE IIKGLAEVNE KLQLPHSIHL HCNDLGHPGN
     YETTLASFDV PKNIKANPAT GERDTVLYAT HVQFHSYGGT TWRDFVSEAP KIADYVNKND
     HIVIDVGQIT LDETTTMTAD GPMEYDLHSL NGLKWANCDV ELETGSGVVP FIYSARAPVP
     AVQWAIGMEL FLLIDDPAKV CLTTDSPNAG PFTRYPRVIA WLMSNKYRMN LIEGELHKWA
     QRKSTIATVD REYTFSEIAQ ITRSTSAKVL GLSETKGHLG VGADADIAVY NINPETIDPS
     VDYMAIEEGF SRAAYVLKDG EIVVKDGEVV ASPHGRTYWV DTRVDESTYN EVLAKVESKF
     KQYYSVNFAN YPVQDEYLPK SAPVKGVML
//

ID   Q48921_METBU   PRELIMINARY;   PRT;   163 AA.
AC   Q48921;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   30-MAY-2006, entry version 25.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrI;
OS   Methanococcoides burtonii.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=29291;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 6242;
RX   MEDLINE=96174929; PubMed=8590683;
RA   Springer E., Sachs M.S., Woese C.R., Boone D.R.;
RT   "Partial gene sequences for the A subunit of methyl-coenzyme M
RT   reductase (mcrI) as a phylogenetic tool for Methanosarcinaceae.";
RL   Int. J. Syst. Bacteriol. 45:554-559(1995).
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DR   EMBL; U22234; AAC43406.1; -; Genomic_DNA.
DR   HSSP; P07962; 1E6Y.
DR   SMR; Q48921; 1-163.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     163    163
SQ   SEQUENCE   163 AA;  17494 MW;  D1B83159FB0DA521 CRC64;
     GSYMSGGVGF TQYATAAYTN NILDDNLYYN VDYINDKYDG AANKGADNKV KATMDVVKDI
     ATESTIYGIE NYEKYPTALE DHFGGSQRAT VLSAAAGSAT ALATGNGNAG LSGWYLSMYL
     HKEALGRLGF FGFDLQDQCG ATNVFSFQSD EGLPLELRGP NYP
//

ID   Q9C4H3_9EURY   PRELIMINARY;   PRT;   163 AA.
AC   Q9C4H3;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   30-MAY-2006, entry version 16.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogen RS-MCR34.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; environmental samples.
OX   NCBI_TaxID=143058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21217833; PubMed=11321536;
RX   DOI=10.1046/j.1462-2920.2001.00179.x;
RA   Lueders T., Chin K.-J., Conrad R., Friedrich M.;
RT   "Molecular analyses of methyl-coenzyme M reductase alpha-subunit
RT   (mcrA) genes in rice field soil and enrichment cultures reveal the
RT   methanogenic phenotype of a novel archaeal lineage.";
RL   Environ. Microbiol. 3:194-204(2001).
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DR   EMBL; AF313838; AAK16868.1; -; Genomic_DNA.
DR   HSSP; P07962; 1E6Y.
DR   SMR; Q9C4H3; 1-163.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     163    163
SQ   SEQUENCE   163 AA;  17533 MW;  F881F49FA3B2AC71 CRC64;
     GSYMSGGVGF TQYATAAYTD DILDNNVYYD VDYINDKYNG AANVGKDNKV KASLDVVKDI
     ATESTLYGIE TYEKFPTALE DHFGGSQRAT VLAAAAGVAC SLATANANAG LSGWYLSMYL
     HKEAWGRLGF FGYDLQDQCG ATNVLSYQGD EGLPDELRGP NYP
//

ID   Q9C4T7_9ARCH   PRELIMINARY;   PRT;   148 AA.
AC   Q9C4T7;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   30-MAY-2006, entry version 16.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrI;
OS   uncultured archaeon 94D.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=140222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Hougaard E., Westermann P.;
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AF268650; AAK07761.1; -; Genomic_DNA.
DR   HSSP; P07962; 1E6Y.
DR   SMR; Q9C4T7; 1-148.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     148    148
SQ   SEQUENCE   148 AA;  16014 MW;  8FE4799E15A3F012 CRC64;
     TQYATAAYTD DILDNNVYYN VDYINDKYNG AANVGTDNKV KATLDVVKDI ATESTLYGIE
     TYEKFPTALE DHFGGSQRAT VLAAAAGVAT ALATANANAG LSGWYLSMYL HKEAWGRLGF
     FGFDLQDQCG ATNVLSYQGD EGLPDELR
//

ID   Q9C4U9_9ARCH   PRELIMINARY;   PRT;   149 AA.
AC   Q9C4U9;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   30-MAY-2006, entry version 15.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrI;
OS   uncultured archaeon 22C.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=140195;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Hougaard E., Westermann P.;
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AF268623; AAK07749.1; -; Genomic_DNA.
DR   HSSP; P07962; 1E6Y.
DR   SMR; Q9C4U9; 1-149.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     149    149
SQ   SEQUENCE   149 AA;  16054 MW;  96C1717B04EB559E CRC64;
     YMSGGVGFTQ YATAAYTNDV LDDFSYYGVD YANDKFGGFA KAPATIDVAK ELATEVTLYG
     IEQYEAFPTL LEDHFGGSQR AAVLAAASGI TSAIATGHSQ IGLAGWYLSM LLHKEAWGRL
     GFFGYDLQDQ CGPTNVFSYQ SDEGNPLEL
//

ID   Q50386_9EURY   PRELIMINARY;   PRT;   163 AA.
AC   Q50386;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   30-MAY-2006, entry version 25.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrI;
OS   Methanohalophilus.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae.
OX   NCBI_TaxID=2175;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HCM6;
RX   MEDLINE=96174929; PubMed=8590683;
RA   Springer E., Sachs M.S., Woese C.R., Boone D.R.;
RT   "Partial gene sequences for the A subunit of methyl-coenzyme M
RT   reductase (mcrI) as a phylogenetic tool for Methanosarcinaceae.";
RL   Int. J. Syst. Bacteriol. 45:554-559(1995).
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DR   EMBL; U22255; AAC43422.1; -; Genomic_DNA.
DR   HSSP; P07962; 1E6Y.
DR   SMR; Q50386; 1-163.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     163    163
SQ   SEQUENCE   163 AA;  17595 MW;  FD6122A402A2F226 CRC64;
     GSYMSGGVGF TQYSTAAYTN NILDDNLYYD VEYINDKYDG AADKGIDNKV APSMDVIKDI
     ATESTLYGLE NYEKYPVALE DHFGGSQRAT VLSAAAGSAG SLATGNANAG LSAWYLCMYL
     IKEGHGRLGF FGYDLQDQCG ATNTFSYQSD EGLPHELRGP NYP
//

ID   Q977Q9_9CREN   PRELIMINARY;   PRT;   194 AA.
AC   Q977Q9;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   30-MAY-2006, entry version 9.
DE   Uncharacterized protein.
OS   uncultured crenarchaeote 4B7.
OC   Archaea; Crenarchaeota; Thermoprotei; marine archaeal group 1;
OC   environmental samples.
OX   NCBI_TaxID=44557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21633832; PubMed=11772643; DOI=10.1128/AEM.68.1.335-345.2002;
RA   Beja O., Koonin E.V., Aravind L., Taylor L.T., Seitz H., Stein J.L.,
RA   Bensen D.C., Feldman R.A., Swanson R.V., DeLong E.F.;
RT   "Comparative genomic analysis of archaeal genotypic variants in a
RT   single population and in two different oceanic provinces.";
RL   Appl. Environ. Microbiol. 68:335-345(2002).
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DR   EMBL; U40238; AAK66811.1; -; Genomic_DNA.
SQ   SEQUENCE   194 AA;  21665 MW;  0B0E1876DB9B074E CRC64;
     MNYKIPSDAM VGKYTVVADT HFGQIEKSFF VINDFDVVNS VPSSEPSSKV SKIIEKFNRI
     AGNEISITLD EKSTVESTLV PRVIQGSLFT SARGEESSVN LRITTTNGQC IIGPDSNCLV
     TESTRKPGEI YSLVSIDDVN YNIRYSGNDV RLEKFSIVPE DSNSKIVLDT WNVEIIKDDQ
     PSRFYYKVSY VALQ
//

ID   Q9C4G2_9EURY   PRELIMINARY;   PRT;   157 AA.
AC   Q9C4G2;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   30-MAY-2006, entry version 15.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogen RS-MCR46.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=143120;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21217833; PubMed=11321536;
RX   DOI=10.1046/j.1462-2920.2001.00179.x;
RA   Lueders T., Chin K.-J., Conrad R., Friedrich M.;
RT   "Molecular analyses of methyl-coenzyme M reductase alpha-subunit
RT   (mcrA) genes in rice field soil and enrichment cultures reveal the
RT   methanogenic phenotype of a novel archaeal lineage.";
RL   Environ. Microbiol. 3:194-204(2001).
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DR   EMBL; AF313849; AAK16879.1; -; Genomic_DNA.
DR   HSSP; P07962; 1E6Y.
DR   SMR; Q9C4G2; 1-157.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     157    157
SQ   SEQUENCE   157 AA;  16867 MW;  4D6E12DDBA0F8976 CRC64;
     GGYMSGGVGF TMYATPAYTN DILDDYVYWG VDYLANKFGK PGSAKATIET VKDIGTEVTL
     YGIEQYEKYP TTLEDHFGGS QRATVLALAA GTATAMATGH SNAGLSAWYL SMYLHKEAWG
     RLGFYGYDLQ DQCGATNVFS LGSDEGCLGE VRGANYP
//

ID   Q977H6_9EURY   PRELIMINARY;   PRT;   138 AA.
AC   Q977H6;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   30-MAY-2006, entry version 13.
DE   Methyl-coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   uncultured Methanobacterium sp.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanobacterium; environmental samples.
OX   NCBI_TaxID=176306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=22315376; PubMed=12427943;
RA   Luton P.E., Wayne J.M., Sharp R.J., Riley P.W.;
RT   "The mcrA gene as an alternative to 16S rRNA in the phylogenetic
RT   analysis of methanogen populations in landfill.";
RL   Microbiology 148:3521-3530(2002).
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DR   EMBL; AF414031; AAL29280.1; -; Genomic_DNA.
DR   HSSP; P11558; 1HBN.
DR   SMR; Q977H6; 1-138.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     138    138
SQ   SEQUENCE   138 AA;  15223 MW;  602A614E8FA498CF CRC64;
     YTDNILDDFT YFGKEYVEDK YGITEAPNNM DTVLDVASEV TFYALEQFED YPALLETIFG
     GSQRASIVAA AAGCSTAFAT GNAQTGLSGW YLSMYLHKEQ HSRLGFYGYD LQDQCGASNV
     FSIRGDEGLP TELRGANY
//

ID   Q9C4E7_9EURY   PRELIMINARY;   PRT;   239 AA.
AC   Q9C4E7;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   30-MAY-2006, entry version 16.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogen RS-ME29.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; environmental samples.
OX   NCBI_TaxID=143086;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21217833; PubMed=11321536;
RX   DOI=10.1046/j.1462-2920.2001.00179.x;
RA   Lueders T., Chin K.-J., Conrad R., Friedrich M.;
RT   "Molecular analyses of methyl-coenzyme M reductase alpha-subunit
RT   (mcrA) genes in rice field soil and enrichment cultures reveal the
RT   methanogenic phenotype of a novel archaeal lineage.";
RL   Environ. Microbiol. 3:194-204(2001).
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CC   -----------------------------------------------------------------------
DR   EMBL; AF313864; AAK16894.1; -; Genomic_DNA.
DR   HSSP; P11558; 1HBN.
DR   SMR; Q9C4E7; 1-238.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   InterPro; IPR003183; MCR_alpha_N.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
FT   NON_TER       1      1
FT   NON_TER     239    239
SQ   SEQUENCE   239 AA;  25859 MW;  EA6EEA4517DAC8EA CRC64;
     MISAYKQAAG EAATGDFAYA AKHAEVIHMG NALPQRRARG ENEPGGIAFG FLADIVQTGR
     KYPDDPVRQT LDVVAAGAML YDQIWLGSYM SGGVGFTQYA TASYTDNVLD DFTYFGQEYV
     EDKYGMTEAP NNMDTVLDVA SEVNFYALEQ FEEYPALLET IFGGSQRASI VAAAAGCSTA
     FATGNAQTGL SGWYLSMYLH KEQHSRLGFY GYDLQDQCGA SNVFSIRGDE GLPLEARGA
//

ID   Q48922_9EURY   PRELIMINARY;   PRT;   163 AA.
AC   Q48922;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   30-MAY-2006, entry version 25.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrI;
OS   Methanolobus bombayensis.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanolobus.
OX   NCBI_TaxID=38023;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B-1;
RX   MEDLINE=96174929; PubMed=8590683;
RA   Springer E., Sachs M.S., Woese C.R., Boone D.R.;
RT   "Partial gene sequences for the A subunit of methyl-coenzyme M
RT   reductase (mcrI) as a phylogenetic tool for Methanosarcinaceae.";
RL   Int. J. Syst. Bacteriol. 45:554-559(1995).
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DR   EMBL; U22257; AAC43407.1; -; Genomic_DNA.
DR   HSSP; P07962; 1E6Y.
DR   SMR; Q48922; 1-163.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     163    163
SQ   SEQUENCE   163 AA;  17484 MW;  399388A228E6EFD9 CRC64;
     GSYMSGGVGF TQYATAAYCN NILDDNLYYN VDYINDKYDG AANKGTDNKV AANLDVVKDI
     ATESTIYGLE NYEKYPTTLE DHFGGSQRAT SLSAAAGSAV SIATGNGNAG LSGWYLCMYL
     HKEALGRLGF FGYDLQDQCG ATNVLSYQSD EGLALELRGP NYP
//

ID   Q977H5_9EURY   PRELIMINARY;   PRT;   146 AA.
AC   Q977H5;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   30-MAY-2006, entry version 14.
DE   Methyl-coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   uncultured Methanocorpusculum sp.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales;
OC   Methanocorpusculaceae; Methanocorpusculum; environmental samples.
OX   NCBI_TaxID=176309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=22315376; PubMed=12427943;
RA   Luton P.E., Wayne J.M., Sharp R.J., Riley P.W.;
RT   "The mcrA gene as an alternative to 16S rRNA in the phylogenetic
RT   analysis of methanogen populations in landfill.";
RL   Microbiology 148:3521-3530(2002).
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AF414032; AAL29281.1; -; Genomic_DNA.
DR   HSSP; P11558; 1HBN.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     146    146
SQ   SEQUENCE   146 AA;  16360 MW;  7CC6067D71956D53 CRC64;
     YTDNVLDDFT YYGMDYLHDK YKIDWKNPNP KDKVKATQEV VNDIATEVNL YGMEQYEQFP
     TMMEDHFGGS QRAAVLAAAS GITTSIATGN SNAGLNGWYL SMLLHKDGWS RLGFFGYDLQ
     DQCGSANSLS IRPDEGCIGE FRGPNY
//

ID   Q9C4D4_9EURY   PRELIMINARY;   PRT;   239 AA.
AC   Q9C4D4;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   30-MAY-2006, entry version 16.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogen RS-ME44.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; environmental samples.
OX   NCBI_TaxID=143090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21217833; PubMed=11321536;
RX   DOI=10.1046/j.1462-2920.2001.00179.x;
RA   Lueders T., Chin K.-J., Conrad R., Friedrich M.;
RT   "Molecular analyses of methyl-coenzyme M reductase alpha-subunit
RT   (mcrA) genes in rice field soil and enrichment cultures reveal the
RT   methanogenic phenotype of a novel archaeal lineage.";
RL   Environ. Microbiol. 3:194-204(2001).
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CC   -----------------------------------------------------------------------
DR   EMBL; AF313877; AAK16907.1; -; Genomic_DNA.
DR   HSSP; P11558; 1HBN.
DR   SMR; Q9C4D4; 1-238.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   InterPro; IPR003183; MCR_alpha_N.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
FT   NON_TER       1      1
FT   NON_TER     239    239
SQ   SEQUENCE   239 AA;  25806 MW;  3EA01889C8018009 CRC64;
     MISAYKQAAG EAATGDFAYA AKHAEVVHMG SYLPVRRARG ENEPGGIAFG FLADIVQTPR
     AYPDDPVRQT LDAVAAGAML YDQIWLGSYM SGGVGFTQYA TAAYTDNVLD DFTYFGQEYV
     EDKYGMTEAP NNMDTVLDVA SEVNFYALEQ FEDYPALLET IFGGSQRASI VAAAAGCSTA
     FATGNAQTGL SGWYLSMYLH KEQHSRLGFY GYDLQDQCGA SNVFSIRGDE GLPLEARGA
//

ID   Q977I1_9EURY   PRELIMINARY;   PRT;   146 AA.
AC   Q977I1;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   30-MAY-2006, entry version 14.
DE   Methyl-coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   uncultured Methanocorpusculum sp.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales;
OC   Methanocorpusculaceae; Methanocorpusculum; environmental samples.
OX   NCBI_TaxID=176309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=22315376; PubMed=12427943;
RA   Luton P.E., Wayne J.M., Sharp R.J., Riley P.W.;
RT   "The mcrA gene as an alternative to 16S rRNA in the phylogenetic
RT   analysis of methanogen populations in landfill.";
RL   Microbiology 148:3521-3530(2002).
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AF414026; AAL29275.1; -; Genomic_DNA.
DR   HSSP; P11558; 1HBN.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     146    146
SQ   SEQUENCE   146 AA;  16309 MW;  5B6B73519374DB7F CRC64;
     YTDNILDDFT YYGMDYLHDK YKIDTKNPNP NDKVKATQEV VNDIASEVNL YGMEQYEQFP
     TMMEDHFGGS QRAAVLAAAS GITTSIATSN SNAGLNGWYL SMLMHKDGWS RLGFFGYDLQ
     DQCGSANSLS IRPDEGCIGE FRGPNY
//

ID   Q8NKK8_9EURY   PRELIMINARY;   PRT;   239 AA.
AC   Q8NKK8;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   30-MAY-2006, entry version 13.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogenic archaeon.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=198240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Galand P.E., Saarnio S., Fritze H., Yrjala K.;
RT   "Depth related diversity of methanogen Archaea in Finnish oligotrophic
RT   fen.";
RL   FEMS Microbiol. Ecol. 42:441-449(2002).
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CC   -----------------------------------------------------------------------
DR   EMBL; AJ489774; CAD33997.2; -; Genomic_DNA.
DR   HSSP; P07962; 1E6Y.
DR   SMR; Q8NKK8; 1-238.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   InterPro; IPR003183; MCR_alpha_N.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
FT   NON_TER       1      1
FT   NON_TER     239    239
SQ   SEQUENCE   239 AA;  25656 MW;  1A486F1D22686292 CRC64;
     FIAAYNMCAG EAAVADLAFA AKHASLVEMA NMLPARRARG PNEPGGLSFG FMADICQKDR
     IKPDDPVEVS LEVVAAGCML YDQIWLGSYM SGGVGFTQYA TAAYTDNILD DYSYYGNDYA
     KKYGANGKAP KTMDVVNDLA TEVTLYGIEQ YEKYPTTLED HFGGSQRATV LAAASGVTAA
     IATGNSNAGL SAWYQSMLLH KDAWGRLGFY GYDLQDQCGS TNVFSVRSDE GSPDELRGA
//

ID   Q977G2_9EURY   PRELIMINARY;   PRT;   139 AA.
AC   Q977G2;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   30-MAY-2006, entry version 13.
DE   Methyl-coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   Methanobrevibacter ruminantium.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=83816;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 1093;
RX   MEDLINE=22315376; PubMed=12427943;
RA   Luton P.E., Wayne J.M., Sharp R.J., Riley P.W.;
RT   "The mcrA gene as an alternative to 16S rRNA in the phylogenetic
RT   analysis of methanogen populations in landfill.";
RL   Microbiology 148:3521-3530(2002).
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF414046; AAL29295.1; -; Genomic_DNA.
DR   HSSP; P11558; 1HBN.
DR   SMR; Q977G2; 1-139.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     139    139
SQ   SEQUENCE   139 AA;  15325 MW;  CAB4B4D04B22FB49 CRC64;
     YTDNVLDDFS YFGKDYVEDK YGDLCSAPND MDTVLDVGSA VTFYSLEQYE EYPALLETHF
     GGSQRAAVVS AASGISTAFA TGNAQTGLSA WYLAQYLHKE QHSRLGFYGY DLQDQCGAAN
     VFAIRNDEGL PLELRGPNY
//

ID   Q9C4I3_9EURY   PRELIMINARY;   PRT;   157 AA.
AC   Q9C4I3;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   30-MAY-2006, entry version 16.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogen RS-MCR24.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosaetaceae; environmental samples.
OX   NCBI_TaxID=143073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21217833; PubMed=11321536;
RX   DOI=10.1046/j.1462-2920.2001.00179.x;
RA   Lueders T., Chin K.-J., Conrad R., Friedrich M.;
RT   "Molecular analyses of methyl-coenzyme M reductase alpha-subunit
RT   (mcrA) genes in rice field soil and enrichment cultures reveal the
RT   methanogenic phenotype of a novel archaeal lineage.";
RL   Environ. Microbiol. 3:194-204(2001).
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CC   -----------------------------------------------------------------------
DR   EMBL; AF313828; AAK16858.1; -; Genomic_DNA.
DR   HSSP; P07962; 1E6Y.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     157    157
SQ   SEQUENCE   157 AA;  16803 MW;  F5FCAD90BACC7FFC CRC64;
     GSYMSGGVGF TQYATAAYTN DVLDDFCYYG VDFAVDKLGG FAKAPKTLDV AKELGTEVTL
     YGMEQYEAYP TLLEDHFGGS QRASVLAAAS GITAAIASGH SQVGLAAWYL SMLLHKEGWG
     RLGFFGYDLQ GQCGPTNVFS YQSDEGNPVE MRGANYP
//

ID   Q8NKK4_9EURY   PRELIMINARY;   PRT;   239 AA.
AC   Q8NKK4;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   30-MAY-2006, entry version 13.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogenic archaeon.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=198240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Galand P.E., Saarnio S., Fritze H., Yrjala K.;
RT   "Depth related diversity of methanogen Archaea in Finnish oligotrophic
RT   fen.";
RL   FEMS Microbiol. Ecol. 42:441-449(2002).
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AJ489778; CAD34001.2; -; Genomic_DNA.
DR   HSSP; P07962; 1E6Y.
DR   SMR; Q8NKK4; 1-238.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   InterPro; IPR003183; MCR_alpha_N.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
FT   NON_TER       1      1
FT   NON_TER     239    239
SQ   SEQUENCE   239 AA;  25584 MW;  EFB2217B1B240F09 CRC64;
     FIAAYNMCAG EAAVADLAFA AKHASLVEMA SMLPARRARG PNEPGGLSFG FMADICQKDR
     IKPDDPVEVS LEVVAAGCML YDQIWLGSYM SGGVGFTQYA TAAYTDNILD DYSYYGNDYA
     KKYGANGKAP KTMDVVNDIA TEVTLYGIEQ YEKYPTTLED HFGGSQRATV LAAASGVAAA
     IATGNSNAGL SAWYLSMLLH KDAWGRLGFY GYDLQDQCGS TNVFSVRSDE GSPDELRGA
//

ID   Q8NKK9_9EURY   PRELIMINARY;   PRT;   239 AA.
AC   Q8NKK9;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   30-MAY-2006, entry version 13.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogenic archaeon.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=198240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Galand P.E., Saarnio S., Fritze H., Yrjala K.;
RT   "Depth related diversity of methanogen Archaea in Finnish oligotrophic
RT   fen.";
RL   FEMS Microbiol. Ecol. 42:441-449(2002).
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CC   -----------------------------------------------------------------------
DR   EMBL; AJ489773; CAD33996.2; -; Genomic_DNA.
DR   HSSP; P07962; 1E6Y.
DR   SMR; Q8NKK9; 1-238.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   InterPro; IPR003183; MCR_alpha_N.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
FT   NON_TER       1      1
FT   NON_TER     239    239
SQ   SEQUENCE   239 AA;  25669 MW;  4B9ABECE39E14B60 CRC64;
     FIAAYNMCAG EAAVADLAFA AKHASLVEMA NMLPARRARG PNEPGGLSFG FMADICRKDR
     IKPDDPVEVS LEVVAAGCML YDQIWLGSYM SGGVGFTQYA TAAYTDNILD DYSYYGNDYA
     KKYGANGKAP KTMDVVNDLA TEVTLYGIEQ YEKYPTTLED HFGGSQRATV LAAASGVTAA
     IATGNSNAGL SAWYLSMLLH KDAWGRLGFY GYDLQDQCGS TNVFSVRSDE GSPDELRGA
//

ID   O74030_METWO   PRELIMINARY;   PRT;   569 AA.
AC   O74030;
DT   01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1998, sequence version 1.
DT   30-MAY-2006, entry version 22.
DE   Tungsten formylmethanofuran dehydrogenase subunit fwdA.
GN   Name=fwdA;
OS   Methanobacterium wolfei.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=145261;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Hochheimer A., Hedderich R., Thauer R.K.;
RT   "The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium
RT   wolfei and Methanobacterium thermoautotrophicum: Induction of the
RT   molybdenum isoenzyme by molybdate and constitutive synthesis of the
RT   tungsten isoenzyme.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AJ009688; CAA08783.1; -; Genomic_DNA.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR012027; FwdA.
DR   InterPro; IPR011059; Metal-dep_hydro_comp.
DR   Pfam; PF07969; Amidohydro_3; 1.
DR   PIRSF; PIRSF006453; FwdA; 1.
SQ   SEQUENCE   569 AA;  62668 MW;  39C0351A7932E678 CRC64;
     MEYIIKNGFV YCPLNGVDGE KMDICVKDGK IVESVSDSAK VIDASGKIVM PGGVDPHSHI
     AGAKVNVGRM YRPEDSKRDA EKFKGGRAGS GFSVPSTFMT GYRYAQMGYT TAMEAAMPPL
     LARHTHEEFH DTPIIDHAAY PLFGNNWFVM EYLKEGDVDA CAAYASWLLR ATKGYTIKIV
     NPAGTEAWGW GGNVHGIYDP APYFDITPAE IIKGLAEVNE KLQLPHSIHL HCNDLGHPGN
     YETTLASFDV PKNIKPNPAT GSRDTVLYAT HVQFHSYGGT TWRDFLSEAP KIADYVNKND
     HIVIDVGQIT LDETTTMTAD GPMEYDLHSL NGLKWANCDV ELETGSGVVP FIYSARAPVP
     AVQWAIGMEL FLLIDNLEKV CLTTDSPNAG PFTRYPRVIA WLMSNKYRMN LIEGELHKWA
     QRKSTVATID REYTFSEIAQ ITRATSAKVL GLSDTKGHLG VGADADIAVY DINPETIDPS
     AEYMAIEEAF SRAACVLKDG GIVVKDGEVV ASPHGRTYWV DTQVDESIYS EVLANVESKF
     KQYYSVNFAN YPVQDDYLPK SAPVKGVML
//

ID   Q9C4J6_9EURY   PRELIMINARY;   PRT;   156 AA.
AC   Q9C4J6;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   30-MAY-2006, entry version 16.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogen RS-MCR09.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; environmental samples.
OX   NCBI_TaxID=143096;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21217833; PubMed=11321536;
RX   DOI=10.1046/j.1462-2920.2001.00179.x;
RA   Lueders T., Chin K.-J., Conrad R., Friedrich M.;
RT   "Molecular analyses of methyl-coenzyme M reductase alpha-subunit
RT   (mcrA) genes in rice field soil and enrichment cultures reveal the
RT   methanogenic phenotype of a novel archaeal lineage.";
RL   Environ. Microbiol. 3:194-204(2001).
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DR   EMBL; AF313815; AAK16845.1; -; Genomic_DNA.
DR   HSSP; P11558; 1HBN.
DR   SMR; Q9C4J6; 1-156.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     156    156
SQ   SEQUENCE   156 AA;  16957 MW;  9D40CDE824BF5950 CRC64;
     GSYMSGGVGF TQYATAAYTD NVLDDFTYFG QEYVEDKYGM TEAPNNMDTV LDVASEVNFY
     ALEQFEDYPA LLETIFGGSQ RASIVAAAAG CSTAFATGNA QTGLSGWYLS MYLHKEQHSR
     LGFYGYDLQD QCGASNVFSI RGDEGLPLEA RGANYP
//

ID   Q9C4J4_9EURY   PRELIMINARY;   PRT;   155 AA.
AC   Q9C4J4;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   30-MAY-2006, entry version 16.
DE   Methyl-coenzyme M reductase II alpha subunit (Fragment).
GN   Name=mrtA;
OS   uncultured methanogen RS-MCR11.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; environmental samples.
OX   NCBI_TaxID=143097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21217833; PubMed=11321536;
RX   DOI=10.1046/j.1462-2920.2001.00179.x;
RA   Lueders T., Chin K.-J., Conrad R., Friedrich M.;
RT   "Molecular analyses of methyl-coenzyme M reductase alpha-subunit
RT   (mcrA) genes in rice field soil and enrichment cultures reveal the
RT   methanogenic phenotype of a novel archaeal lineage.";
RL   Environ. Microbiol. 3:194-204(2001).
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DR   EMBL; AF313817; AAK16847.1; -; Genomic_DNA.
DR   HSSP; Q49605; 1E6V.
DR   SMR; Q9C4J4; 1-155.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     155    155
SQ   SEQUENCE   155 AA;  16792 MW;  43455219C74F304A CRC64;
     GAYMPGGVGF TQYATAAYTD DILDDFLYYG KEYVEDKFGI CQAKADMDVV KDISSEVTLY
     AMEQYEIPTL LESHFGGSQR AAVAAAAAGC STAFATGNSN AGINGWYLSQ ILHKEVHSRL
     GFYGYDLQDQ CGASNSLSVR SDEGLIHELR GPNYP
//

ID   Q9C4G7_9EURY   PRELIMINARY;   PRT;   156 AA.
AC   Q9C4G7;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   30-MAY-2006, entry version 15.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogen RS-MCR41.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=143118;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21217833; PubMed=11321536;
RX   DOI=10.1046/j.1462-2920.2001.00179.x;
RA   Lueders T., Chin K.-J., Conrad R., Friedrich M.;
RT   "Molecular analyses of methyl-coenzyme M reductase alpha-subunit
RT   (mcrA) genes in rice field soil and enrichment cultures reveal the
RT   methanogenic phenotype of a novel archaeal lineage.";
RL   Environ. Microbiol. 3:194-204(2001).
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DR   EMBL; AF313844; AAK16874.1; -; Genomic_DNA.
DR   HSSP; P11558; 1HBN.
DR   SMR; Q9C4G7; 1-156.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     156    156
SQ   SEQUENCE   156 AA;  17046 MW;  8410E6ADB309F0A7 CRC64;
     GSYMSGGVGF TQYATAAYTD DILDDFTYYG YDYAKGKYKI GQTKPTMDIV NDLGTEVTLY
     GIEQYEKYPT TLEDHFGGSQ RATVLAAASG VTTAMATGNS NAGLSAWYLS MYLHKEAWGR
     LGFFGYDLQD QCGATNVFSC RSDEGAIDEL RGPNYP
//

ID   Q8NKL6_9EURY   PRELIMINARY;   PRT;   239 AA.
AC   Q8NKL6;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   30-MAY-2006, entry version 12.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogenic archaeon.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=198240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Galand P.E., Saarnio S., Fritze H., Yrjala K.;
RT   "Depth related diversity of methanogen Archaea in Finnish oligotrophic
RT   fen.";
RL   FEMS Microbiol. Ecol. 42:441-449(2002).
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DR   EMBL; AJ489765; CAD33988.2; -; Genomic_DNA.
DR   HSSP; P07962; 1E6Y.
DR   SMR; Q8NKL6; 1-238.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   InterPro; IPR003183; MCR_alpha_N.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
FT   NON_TER       1      1
FT   NON_TER     239    239
SQ   SEQUENCE   239 AA;  25637 MW;  F32E0A0F95048BE3 CRC64;
     FIAAYNMCAG EAAVADLAFA AKHASLVEMA NMLPARRARG PNEPGGLSFG FMADMVQTDR
     IYPDDPVRSS LEVVAAGCML YDQIWLGSYM SGGVGFTQYA TAAYTDNILD DYSYYGNDYA
     KKYGEDGKAP ATMDVVNDLG TEVTLYGTEQ YEKYPTTLED HFGGSQRATV LAAASGVTAA
     IATGNSNAGL SAWYLSMLLH KDAWGRLGFY GYDLQDQCGS TNVFSVRSDE GAPDELRGA
//

ID   Q977S5_9CREN   PRELIMINARY;   PRT;   105 AA.
AC   Q977S5;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   30-MAY-2006, entry version 14.
DE   Rhodanese-related sulfurtransferase/oxidoreductase.
OS   uncultured crenarchaeote 4B7.
OC   Archaea; Crenarchaeota; Thermoprotei; marine archaeal group 1;
OC   environmental samples.
OX   NCBI_TaxID=44557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21633832; PubMed=11772643; DOI=10.1128/AEM.68.1.335-345.2002;
RA   Beja O., Koonin E.V., Aravind L., Taylor L.T., Seitz H., Stein J.L.,
RA   Bensen D.C., Feldman R.A., Swanson R.V., DeLong E.F.;
RT   "Comparative genomic analysis of archaeal genotypic variants in a
RT   single population and in two different oceanic provinces.";
RL   Appl. Environ. Microbiol. 68:335-345(2002).
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DR   EMBL; U40238; AAK66795.1; -; Genomic_DNA.
DR   GO; GO:0016740; F:transferase activity; IEA.
DR   InterPro; IPR001763; Rhodanese-like.
DR   Pfam; PF00581; Rhodanese; 1.
DR   SMART; SM00450; RHOD; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
KW   Transferase.
SQ   SEQUENCE   105 AA;  11534 MW;  4633DAA6005AD61B CRC64;
     MSIQYKLIMA ESISKDQLKQ EQGSFVIIDV REPDEISNGA IENSKNMSLG LAIRNAKKGQ
     IDDLKDKKIC VYCASGYRGN IAADELVKAG FSAVNLEGGY MAWTQ
//

ID   Q9C4F8_9EURY   PRELIMINARY;   PRT;   239 AA.
AC   Q9C4F8;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   30-MAY-2006, entry version 15.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogen RS-ME05.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; environmental samples.
OX   NCBI_TaxID=143081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21217833; PubMed=11321536;
RX   DOI=10.1046/j.1462-2920.2001.00179.x;
RA   Lueders T., Chin K.-J., Conrad R., Friedrich M.;
RT   "Molecular analyses of methyl-coenzyme M reductase alpha-subunit
RT   (mcrA) genes in rice field soil and enrichment cultures reveal the
RT   methanogenic phenotype of a novel archaeal lineage.";
RL   Environ. Microbiol. 3:194-204(2001).
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DR   EMBL; AF313853; AAK16883.1; -; Genomic_DNA.
DR   HSSP; P11558; 1HBN.
DR   SMR; Q9C4F8; 1-238.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   InterPro; IPR003183; MCR_alpha_N.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
FT   NON_TER       1      1
FT   NON_TER     239    239
SQ   SEQUENCE   239 AA;  25933 MW;  AE0DC2B140FAB645 CRC64;
     MISAYKQAAG EAATGDFAYA AKHAEVILMG NALPQRRARG ENEPGGIAFG FLADIVQTGR
     KYPBDPVRQT LDVVAAGAML YDQIWLGSYM SRGVGFTQYA TASYTDNVLD DFTYFGQEYV
     EDKYGMTEAP NNMDTVLDVA SEVNFYALEQ FEEYPALLET IFGGSQRASI VAAAAGCSTA
     FATGNAQTGL SGWYLSMYLH KEQHSRLGFY GYDLQDQCGA SNVFSIRGDE GLPLEARGA
//

ID   Q977L5_9CREN   PRELIMINARY;   PRT;   122 AA.
AC   Q977L5;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   30-MAY-2006, entry version 9.
DE   Rossmann-fold nucleotide-binding protein.
OS   uncultured crenarchaeote 74A4.
OC   Archaea; Crenarchaeota; Thermoprotei; marine archaeal group 1;
OC   environmental samples.
OX   NCBI_TaxID=166279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21633832; PubMed=11772643; DOI=10.1128/AEM.68.1.335-345.2002;
RA   Beja O., Koonin E.V., Aravind L., Taylor L.T., Seitz H., Stein J.L.,
RA   Bensen D.C., Feldman R.A., Swanson R.V., DeLong E.F.;
RT   "Comparative Genomic Analysis of Archaeal Genotypic Variants in a
RT   Single Population and in Two Different Oceanic Provinces.";
RL   Appl. Environ. Microbiol. 68:335-345(2002).
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DR   EMBL; AF393466; AAK96093.1; -; Genomic_DNA.
SQ   SEQUENCE   122 AA;  12806 MW;  942F6F9091E4CC24 CRC64;
     MNACSHGAKD GNGITVGILP QDDPKFANDY CDIVIPSGMG FTRDFLNALS ADGVIIVGGG
     SGTLSEVCAA YMSKKPMVAI RGIESSITPY IDGYVDHRKN VKIIGADTAK EAVEKILELI
     TA
//

ID   Q49114_9EURY   PRELIMINARY;   PRT;   163 AA.
AC   Q49114;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   30-MAY-2006, entry version 24.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrI;
OS   Methanohalobium evestigatum.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanohalobium.
OX   NCBI_TaxID=2322;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=96174929; PubMed=8590683;
RA   Springer E., Sachs M.S., Woese C.R., Boone D.R.;
RT   "Partial gene sequences for the A subunit of methyl-coenzyme M
RT   reductase (mcrI) as a phylogenetic tool for Methanosarcinaceae.";
RL   Int. J. Syst. Bacteriol. 45:554-559(1995).
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DR   EMBL; U22236; AAC43408.1; -; Genomic_DNA.
DR   HSSP; P07962; 1E6Y.
DR   SMR; Q49114; 1-163.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     163    163
SQ   SEQUENCE   163 AA;  17559 MW;  8D906F78370AC39D CRC64;
     GSYMSGGVGF TQYATAAYTN NILDDNLYYD IEYINDKYNN AGKPGADNKA PATMDVVKDI
     ATESTLYGLE NYEKYPTALE DHFGGSQRAT VLSAAAGSAT SIATGNSNAG LSAWYLSMYL
     HKEAHGRLGF FGFDLQDQCG AANVFSYQSD EGLPLELRGP NYP
//

ID   Q8NKW0_ACIAM   PRELIMINARY;   PRT;   179 AA.
AC   Q8NKW0;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   30-MAY-2006, entry version 15.
DE   Hypothetical protein.
OS   Acidianus ambivalens (Desulfurolobus ambivalens).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Acidianus.
OX   NCBI_TaxID=2283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM3772, and Lei 10;
RX   MEDLINE=22830413; PubMed=12949162; DOI=10.1099/mic.0.26455-0;
RA   Laska S., Lottspeich F., Kletzin A.;
RT   "Membrane-bound hydrogenase and sulfur reductase of the
RT   hyperthermophilic and acidophilic archaeon Acidianus ambivalens.";
RL   Microbiology 149:2357-2371(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM3772, and Lei 10;
RA   Laska S.;
RL   Thesis (2000), Institute of Microbiology and Genetics, Darmstadt
RL   University of Technology, Darmstadt, Germany.
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DR   EMBL; AJ320523; CAC86880.1; -; Genomic_DNA.
DR   GO; GO:0005488; F:binding; IEA.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR013105; TPR_2.
DR   InterPro; IPR013026; TPR_region.
DR   Pfam; PF00515; TPR_1; 1.
DR   Pfam; PF07719; TPR_2; 2.
DR   SMART; SM00028; TPR; 3.
DR   PROSITE; PS50005; TPR; 4.
DR   PROSITE; PS50293; TPR_REGION; 1.
KW   Hypothetical protein; Repeat; TPR repeat.
SQ   SEQUENCE   179 AA;  21241 MW;  57267A2E8FC4B26E CRC64;
     MSDIDIKINE YKRLIKIEPN NAWHHFHLGE ALEEKGELND AIEEYSRAVE LDPTFPDFHF
     KKAEALLKLS KFQEAVQVYD NAIRKDPKDA HLYHYFKGEI YEELGKYEEA LKEYNRAIEW
     SPNNSWYRQA KIYLLEKMNR LEDALKEVDE LIKIDSSAVN LELRKEILAK LKNNNNIKV
//

ID   Q50828_9EURY   PRELIMINARY;   PRT;   163 AA.
AC   Q50828;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   30-MAY-2006, entry version 25.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrI;
OS   Methanolobus vulcani.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanolobus.
OX   NCBI_TaxID=38026;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=96174929; PubMed=8590683;
RA   Springer E., Sachs M.S., Woese C.R., Boone D.R.;
RT   "Partial gene sequences for the A subunit of methyl-coenzyme M
RT   reductase (mcrI) as a phylogenetic tool for Methanosarcinaceae.";
RL   Int. J. Syst. Bacteriol. 45:554-559(1995).
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DR   EMBL; U22245; AAC43427.1; -; Genomic_DNA.
DR   HSSP; P07962; 1E6Y.
DR   SMR; Q50828; 1-163.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     163    163
SQ   SEQUENCE   163 AA;  17522 MW;  D0A88D74E71C032D CRC64;
     GSYMSGGVGF TQYATAAYCN NILDDNLYYN VDYINDKYDG AANKGTDNKV KASLDVVKDI
     ATESTIYGLE NYEKYPTTLE DHFGGSQRAT SLSAAAGSAV ALATGNGNAG LSGWYLCMYL
     HKEAHGRLGF FGYDLQDQCG ATNVLSYQSD EGLALELRGP NYP
//

ID   Q8NKM9_9CREN   PRELIMINARY;   PRT;   221 AA.
AC   Q8NKM9;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   30-MAY-2006, entry version 15.
DE   Putative phosphoserine phosphatase.
OS   uncultured crenarchaeote.
OC   Archaea; Crenarchaeota; environmental samples.
OX   NCBI_TaxID=29281;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=22252841; PubMed=12366755;
RX   DOI=10.1046/j.1462-2920.2002.00345.x;
RA   Quaiser A., Ochsenreiter T., Klenk H.P., Kletzin A., Treusch A.H.,
RA   Meurer G., Eck J., Sensen C.W., Schleper C.;
RT   "First insight into the genome of an uncultivated crenarchaeote from
RT   soil.";
RL   Environ. Microbiol. 4:603-611(2002).
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DR   EMBL; AJ496176; CAD42691.1; -; Genomic_DNA.
DR   GO; GO:0003824; F:catalytic activity; IEA.
DR   GO; GO:0016791; F:phosphoric monoester hydrolase activity; IEA.
DR   GO; GO:0008152; P:metabolism; IEA.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR006383; HAD-SF_hydro_IB_PSP-like.
DR   Pfam; PF00702; Hydrolase; 1.
DR   TIGRFAMs; TIGR01488; HAD-SF-IB; 1.
SQ   SEQUENCE   221 AA;  24742 MW;  88F6ED94D289722E CRC64;
     MLYPMEFKST LAVFDMDGTL IDGRLIEVLS KKFGLYAQVR HIQSDKSIPG YVKTQKIAAV
     IRGIEEREIE IALDSIPPAK NSQEVISLLK KKGFRIGIIT DSYSVAAQAL VNKLDLDFFY
     ANELKVDNGI VTGEINMPLG WEKIDCFCKN SVCKRYHMEI HAKKICADIK NTIAIGDTKG
     DLCMIKQAGI GIAYMPKDKY INETINKVNT PDMIGVLDFI E
//

ID   Q977G1_9EURY   PRELIMINARY;   PRT;   138 AA.
AC   Q977G1;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   30-MAY-2006, entry version 13.
DE   Methyl-coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   Methanosphaera stadtmanae.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=2317;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 3091;
RX   MEDLINE=22315376; PubMed=12427943;
RA   Luton P.E., Wayne J.M., Sharp R.J., Riley P.W.;
RT   "The mcrA gene as an alternative to 16S rRNA in the phylogenetic
RT   analysis of methanogen populations in landfill.";
RL   Microbiology 148:3521-3530(2002).
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DR   EMBL; AF414047; AAL29296.1; -; Genomic_DNA.
DR   HSSP; Q49605; 1E6V.
DR   SMR; Q977G1; 1-138.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     138    138
SQ   SEQUENCE   138 AA;  14930 MW;  D4A7A5D2426675C4 CRC64;
     YTDEILDDFI YYGKDYVEGK YGGLCQAEAT SEVVKDIASE VTLYGLEQYE IPAALEDHFG
     GSQRAAVLAA GAGCSVAFAT ANSNAGVNGW YLSQLLHKEG HSRLGFYGYD LQDQCGSSNS
     LSVRSDEGLI HELRGPNY
//

ID   Q8NKT2_ACIAM   PRELIMINARY;   PRT;   145 AA.
AC   Q8NKT2;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   30-MAY-2006, entry version 11.
DE   Molybdopterin biosynthesis protein (Fragment).
GN   Name=moeA;
OS   Acidianus ambivalens (Desulfurolobus ambivalens).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Acidianus.
OX   NCBI_TaxID=2283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Lei 10;
RX   MEDLINE=22830413; PubMed=12949162; DOI=10.1099/mic.0.26455-0;
RA   Laska S., Lottspeich F., Kletzin A.;
RT   "Membrane-bound hydrogenase and sulfur reductase of the
RT   hyperthermophilic and acidophilic archaeon Acidianus ambivalens.";
RL   Microbiology 149:2357-2371(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Lei 10;
RA   Laska S.;
RL   Thesis (2000), Department of Institute of Microbiology and Genetics,
RL   Darmstadt University of Technology, Darmstadt, Germany.
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DR   EMBL; AJ345004; CAC86942.1; -; Genomic_DNA.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthesis; IEA.
DR   InterPro; IPR001453; MPT_bd.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   ProDom; PD002460; MoCF_biosynth; 1.
FT   NON_TER       1      1
SQ   SEQUENCE   145 AA;  15661 MW;  7A6AC63B61AA3465 CRC64;
     VIKAKADKYG WGIVYKEIVP DDENKIVEAI KSAVNNGAEA VIVTGGTSVD ATDKTPIAIS
     KLGKIISYGL PIKPTTMSIV AMWDSIPIFG ISAGGIYYRD YNAIDVMFTR LMAGIIPRKE
     DIAMMGHGGL LPNFQPKMKL QSINS
//

ID   Q977L6_9CREN   PRELIMINARY;   PRT;   393 AA.
AC   Q977L6;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   30-MAY-2006, entry version 19.
DE   3-hydroxyacyl-CoA dehydrogenase.
OS   uncultured crenarchaeote 74A4.
OC   Archaea; Crenarchaeota; Thermoprotei; marine archaeal group 1;
OC   environmental samples.
OX   NCBI_TaxID=166279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21633832; PubMed=11772643; DOI=10.1128/AEM.68.1.335-345.2002;
RA   Beja O., Koonin E.V., Aravind L., Taylor L.T., Seitz H., Stein J.L.,
RA   Bensen D.C., Feldman R.A., Swanson R.V., DeLong E.F.;
RT   "Comparative Genomic Analysis of Archaeal Genotypic Variants in a
RT   Single Population and in Two Different Oceanic Provinces.";
RL   Appl. Environ. Microbiol. 68:335-345(2002).
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DR   EMBL; AF393466; AAK96092.1; -; Genomic_DNA.
DR   HSSP; Q16836; 1F0Y.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA.
DR   GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase (NAD+) a...; IEA.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA.
DR   GO; GO:0006631; P:fatty acid metabolism; IEA.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolism; IEA.
DR   InterPro; IPR006108; 3HC_DH_C.
DR   InterPro; IPR006176; 3HCDH_NAD_bd.
DR   InterPro; IPR008927; 6DGDH_C_like.
DR   InterPro; IPR000205; FAD/NAD(P)_BS.
DR   InterPro; IPR006168; NAD_Gly3P_DH.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   PRINTS; PR00077; GPDHDRGNASE.
SQ   SEQUENCE   393 AA;  44177 MW;  0384DDDD22E9B91E CRC64;
     MKKYVIKDTE FHQHMLVKNI TVLGSGVMGH GIAQVSATAG YNVVLRDIKQ EFLDKAMEKI
     KWSLDKLVSK EKITKEEADS IFSRIIPIVD LKEAVKNAEM IIEVVPEIME LKKKVYAELD
     AVAGPDVIFA SNTSTLPITE IANTTSRPEK FIGIHFFNPP QLMKLVEIIP GEKTTQAITD
     LTQEYVKSVN KQAVPSRKDV PGFIINRLFI PMVHEACYAQ DRTNATLEEI DSAVKFKLGF
     PMGIFELADF TGMDVIHKAT VEMHLRDKKV INPHPTIGKM FDEKKLGQKS GEGYYKYSDD
     KYERVALSEE LAEKFNPIQL VANILNNAAW LITNGASDIS EIEKAAQLGL GLKKPLFETA
     KEIGIKNIVD ELNRLEKEHG EFYKPDPLLI SML
//

ID   Q9C4S0_METAC   PRELIMINARY;   PRT;   310 AA.
AC   Q9C4S0;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   30-MAY-2006, entry version 14.
DE   Hypothetical protein (Fragment).
OS   Methanosarcina acetivorans.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C2A;
RX   PubMed=15882413; DOI=10.1111/j.1365-2958.2005.04616.x;
RA   Pritchett M.A., Metcalf W.W.;
RT   "Genetic, physiological and biochemical characterization of multiple
RT   methanol methyltransferase isozymes in Methanosarcina acetivorans
RT   C2A.";
RL   Mol. Microbiol. 56:1183-1194(2005).
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DR   EMBL; AF319042; AAK07602.1; -; Genomic_DNA.
DR   GO; GO:0003677; F:DNA binding; IEA.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA.
DR   GO; GO:0006260; P:DNA replication; IEA.
DR   InterPro; IPR004013; PHP_C.
DR   InterPro; IPR003141; PHP_N.
DR   Pfam; PF02811; PHP; 1.
DR   SMART; SM00481; POLIIIAc; 1.
KW   Hypothetical protein.
FT   NON_TER       1      1
SQ   SEQUENCE   310 AA;  35378 MW;  0E738DBCF3A7D5AC CRC64;
     QEGWKKVDLH VHSSCSYDVP PAKAMHPSVL FEKARAKGLD YVTFTDHDTV EAYNLLGWDR
     EGLVPGVEIS IKDPENIGHT LHVNVFELDS EEFGELEAIV NQEHDFKSFI RYLRLHDLPH
     IYNHPFWFAI GDRPNLRAVP ELIKQFPVIE YNMQDLTEKN LITAALARKY GKGLAATTDS
     HTGGMGAVYT LAKGDSFREY FDNIKNGRSY MVIEGGARRH LTKELNAWVE LVFSMDRNAR
     GEVGFTTNVK TFDRLIGFFA NGKIREFPRI NGLAMKFFQN FSRSGLPAYM YMRAEKPLIS
     RIEKVVNLTA
//

ID   Q7ZAF4_9EURY   PRELIMINARY;   PRT;   162 AA.
AC   Q7ZAF4;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   30-MAY-2006, entry version 13.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured Methanosarcinaceae archaeon.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; environmental samples.
OX   NCBI_TaxID=176230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Chin K.-J., Lueders T., Klose M., Conrad R.;
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY125612; AAN02179.1; -; Genomic_DNA.
DR   HSSP; P11558; 1HBN.
DR   SMR; Q7ZAF4; 1-162.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
FT   NON_TER       1      1
FT   NON_TER     162    162
SQ   SEQUENCE   162 AA;  17640 MW;  075472D65C69DF73 CRC64;
     GAYMSGGVGF TQYATAAYTD DILDDFVYYG YDYIKGKYGV AKAKCTMDVV NDIGTEVTLY
     GIEQYEKYPT TLEDHFGGSQ RATVLSAAAG SVTSMATGNA NAGLSAWYLS MYLHKEAWGR
     LGFFGYDLQD QCGATNVFSC RSDEGAIDEL RGPNYPNYAM NV
//

ID   Q7ZAF2_9EURY   PRELIMINARY;   PRT;   162 AA.
AC   Q7ZAF2;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   30-MAY-2006, entry version 12.
DE   Methyl-coenzyme M reductase II alpha subunit (Fragment).
GN   Name=mrtA;
OS   uncultured Methanobacteriaceae archaeon.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; environmental samples.
OX   NCBI_TaxID=176233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Chin K.-J., Lueders T., Klose M., Conrad R.;
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY125614; AAN02181.1; -; Genomic_DNA.
DR   HSSP; P11558; 1HBN.
DR   SMR; Q7ZAF2; 1-162.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
FT   NON_TER       1      1
FT   NON_TER     162    162
SQ   SEQUENCE   162 AA;  17577 MW;  6B661B485480F0B3 CRC64;
     GSYMSGGVGF TQYATAAYTD NVLDDFTYYG KEYVEDKYGM TEAPNTMETV LDVGSEVTFY
     ALEQFEEYPA LLETVFGGSQ RASIVAAAAG ASTGFATGNA QTGLSAWYLS MYLHKEQHSR
     LGFYGYDLQD QCGAANTFAI RGDEGLPLEA RGANYPNYAM NV
//

ID   Q7ZAD5_9EURY   PRELIMINARY;   PRT;   163 AA.
AC   Q7ZAD5;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   30-MAY-2006, entry version 13.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured Methanobacteriaceae archaeon.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; environmental samples.
OX   NCBI_TaxID=176233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Chin K.-J., Lueders T., Klose M., Conrad R.;
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY125640; AAN02207.1; -; Genomic_DNA.
DR   HSSP; P11558; 1HBN.
DR   SMR; Q7ZAD5; 1-163.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
FT   NON_TER       1      1
FT   NON_TER     163    163
SQ   SEQUENCE   163 AA;  17793 MW;  8CAB3E679B971E1F CRC64;
     LGSYMSGGVG FTQYATASYT DNVLDDFTYF GQEYVEDKYG MTEAPNNMDT VLDVASEVNF
     YALEQFEEYP ALLETIFGGS QRASIVAAAA GCSTAFATGN AQTGLSGWYL SMYLHKEQHS
     RLGFYGYDLQ DQCGASNVFS IRGDEGLPLE ARGANYPNYA MNV
//

ID   Q7ZAC4_9EURY   PRELIMINARY;   PRT;   162 AA.
AC   Q7ZAC4;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   30-MAY-2006, entry version 12.
DE   Methyl-coenzyme M reductase II alpha subunit (Fragment).
GN   Name=mrtA;
OS   uncultured Methanobacteriaceae archaeon.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; environmental samples.
OX   NCBI_TaxID=176233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Chin K.-J., Lueders T., Klose M., Conrad R.;
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY125659; AAN02226.1; -; Genomic_DNA.
DR   HSSP; P11558; 1HBN.
DR   SMR; Q7ZAC4; 1-162.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
FT   NON_TER       1      1
FT   NON_TER     162    162
SQ   SEQUENCE   162 AA;  17679 MW;  D7357D7790590D5F CRC64;
     GSYMSGGVGF TQYATASYTD NVLDDFTYFG QEYVEDKYGM TEAPNNMDTV LDVASEVNFY
     ALEQFEEYPA LLETIFGGSQ RASIVAAAAG CSTAFATGNA QTGLSGWYLS MYLHKEQHSR
     LGFYGYDLQD QCGASNVFSI RGDEGLPLEA RGANYPNYAM NV
//

ID   Q7ZAC2_9EURY   PRELIMINARY;   PRT;   162 AA.
AC   Q7ZAC2;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   30-MAY-2006, entry version 12.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured Methanosarcinaceae archaeon.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; environmental samples.
OX   NCBI_TaxID=176230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Chin K.-J., Lueders T., Klose M., Conrad R.;
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY125661; AAN02228.1; -; Genomic_DNA.
DR   HSSP; P11558; 1HBN.
DR   SMR; Q7ZAC2; 1-162.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
FT   NON_TER       1      1
FT   NON_TER     162    162
SQ   SEQUENCE   162 AA;  17641 MW;  7989F6A4E5B474E1 CRC64;
     GSYMSGGVGF TQYATAAYTD DILDDFCYYG YDYIKGKYGV AKAKCTMDVV NDIGSEVTLY
     GIEQYEKYPT TLEDHFGGSQ RATVLSAAAG VTTSIATGNA NAGLSAWYLS MYLHKEAWGR
     LGFFGYDLQD QCGATNVFSC RSDEGAIDEL RGPNYPNYAM NV
//

ID   Q7ZAC0_9EURY   PRELIMINARY;   PRT;   162 AA.
AC   Q7ZAC0;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   30-MAY-2006, entry version 12.
DE   Methyl-coenzyme M reductase II alpha subunit (Fragment).
GN   Name=mrtA;
OS   uncultured Methanobacteriaceae archaeon.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; environmental samples.
OX   NCBI_TaxID=176233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Chin K.-J., Lueders T., Klose M., Conrad R.;
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY125663; AAN02230.1; -; Genomic_DNA.
DR   HSSP; P11558; 1HBN.
DR   SMR; Q7ZAC0; 1-162.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
FT   NON_TER       1      1
FT   NON_TER     162    162
SQ   SEQUENCE   162 AA;  17593 MW;  B47E9015E1F4FFDB CRC64;
     GSYMSGGVGF TQYATAAYTD NVLDDFTYFG QEYVEDKYGM TEAPNTMETV LDVGSEVTFY
     ALEQFEDYPA LLETIFGGSQ RASIVAAAAG CSAGFATGNA QTGLSAWYLS MYLHKEQHSR
     LGFYGYDLQD QCGASNVFSI RGDEGLPLEA RGANYPNYAM NV
//

ID   Q7ZAB9_9EURY   PRELIMINARY;   PRT;   162 AA.
AC   Q7ZAB9;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   30-MAY-2006, entry version 12.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured Methanobacteriaceae archaeon.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; environmental samples.
OX   NCBI_TaxID=176233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Chin K.-J., Lueders T., Klose M., Conrad R.;
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY125665; AAN02232.1; -; Genomic_DNA.
DR   HSSP; P11558; 1HBN.
DR   SMR; Q7ZAB9; 1-162.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
FT   NON_TER       1      1
FT   NON_TER     162    162
SQ   SEQUENCE   162 AA;  17603 MW;  92756C77904C5818 CRC64;
     GSYMSGGVGF TQYATASYTD NVLDDFTYFG QEYVEDKYGM TEAPNNMDTV PDVASEVNFY
     ALEQFEEYPA LLETIFGGSQ RASIVAAAAG CSTAFATGNA QTGLSGWYLS MYLHKEQHSR
     LGSYGYDLQD QCGASNVFSI RGDEGLPLEA RGANYPNYAM NV
//

ID   Q7ZA90_9EURY   PRELIMINARY;   PRT;   147 AA.
AC   Q7ZA90;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   30-MAY-2006, entry version 13.
DE   Methyl-coenzyme M reductase II alpha subunit (Fragment).
GN   Name=mrtA;
OS   Methanothermobacter thermophilus.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=49341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 6529;
RA   Lausten T., Westermann P., Ahring B.K.;
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY289753; AAQ18239.1; -; Genomic_DNA.
DR   HSSP; Q49605; 1E6V.
DR   SMR; Q7ZA90; 1-147.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
FT   NON_TER       1      1
FT   NON_TER     147    147
SQ   SEQUENCE   147 AA;  15996 MW;  2B4EA5B0D40B0DAE CRC64;
     GGVGFTQYAT AAYTDDILDD FVYYGMEYVD DKYGICGTKP TMDVVRDIST EVTLYSLEQY
     EEYPTLLEDH FGGSQRAAVA AAAAGCSTAF ATGNSNAGIN GWYLSQILHK EAHSRLGFYG
     YDLQDQCGAS NSLSIRSDEG LIHELRG
//

ID   Q7ZA87_9EURY   PRELIMINARY;   PRT;   147 AA.
AC   Q7ZA87;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   30-MAY-2006, entry version 13.
DE   Methyl-coenzyme M reductase II alpha subunit (Fragment).
GN   Name=mrtA;
OS   Methanothermobacter thermoflexus.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=49340;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 7268;
RA   Lausten T., Westermann P., Ahring B.K.;
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY303951; AAQ21199.1; -; Genomic_DNA.
DR   HSSP; Q49605; 1E6V.
DR   SMR; Q7ZA87; 1-147.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
FT   NON_TER       1      1
FT   NON_TER     147    147
SQ   SEQUENCE   147 AA;  16012 MW;  D0B87FB0D41DD7A0 CRC64;
     GGVGFTQYAT ASYTDDILDD FVYYGMEYVD DKYGICGTKP TMDVVRDIST EVTLYSLEQY
     EEYPTLLEDH FGGSQRAAVA AAAAGCSTAF ATGNSNAGIN GWYLSQILHK EAHSRLGFYG
     YDLQDQCGAS NSLSIRSDEG LIHELRG
//

ID   Q877F5_9EURY   PRELIMINARY;   PRT;   240 AA.
AC   Q877F5;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   30-MAY-2006, entry version 13.
DE   Methyl-coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   Methanomethylovorans hollandica.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanomethylovorans.
OX   NCBI_TaxID=101192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=22748895; PubMed=12866859; DOI=10.1078/072320203322346173;
RA   Simankova M.V., Kotsyurbenko O.R., Lueders T., Nozhevnikova A.N.,
RA   Wagner B., Conrad R., Friedrich M.W.;
RT   "Isolation and characterization of new strains of methanogens from
RT   cold terrestrial habitats.";
RL   Syst. Appl. Microbiol. 26:312-318(2003).
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DR   EMBL; AY260442; AAP20897.1; -; Genomic_DNA.
DR   HSSP; P07962; 1E6Y.
DR   SMR; Q877F5; 1-240.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   InterPro; IPR003183; MCR_alpha_N.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
FT   NON_TER       1      1
FT   NON_TER     240    240
SQ   SEQUENCE   240 AA;  25625 MW;  2C23726350D3BE77 CRC64;
     EAAVADLSYA AKHAGVISMG EMLPARRARG PNEPGGISFG HLSDIVQTSR VDPEDPAHVA
     LEVVGAGCML YDQIWLGSYM SGGVGFTQYA TAAYTNNILD DNLYYNVDYI NDKYNGAAKK
     GTDNKVKATL EVVKDIATES TLYGMENYEK YPTALEDHFG GSQRATVLSA AAGAATAIAT
     GNGNAGLSGW YLSMYLHKEG HGRLGFFGFD LQDQCGATNV LSYQSDEGLP VELRGPNYPN
//

ID   Q75NC6_9ARCH   PRELIMINARY;   PRT;   216 AA.
AC   Q75NC6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 12.
DE   Methyl-coenzyme M reductase (Fragment).
GN   Name=mcrA;
OS   uncultured archaeon.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=115547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15574947; DOI=10.1128/AEM.70.12.7445-7455.2004;
RA   Inagaki F., Tsunogai U., Suzuki M., Kosaka A., Machiyama H., Takai K.,
RA   Nunoura T., Nealson K.H., Horikoshi K.;
RT   "Characterization of C1-metabolizing prokaryotic communities in
RT   methane seep habitats at the Kuroshima Knoll, southern Ryukyu Arc, by
RT   analyzing pmoA, mmoX, mxaF, mcrA, and 16S rRNA genes.";
RL   Appl. Environ. Microbiol. 70:7445-7455(2004).
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DR   EMBL; AB176931; BAD16563.1; -; Genomic_DNA.
DR   SMR; Q75NC6; 1-216.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   InterPro; IPR003183; MCR_alpha_N.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
FT   NON_TER       1      1
FT   NON_TER     216    216
SQ   SEQUENCE   216 AA;  22858 MW;  D618DE46A9F2AF4B CRC64;
     AGEAAVADLA FGAKHAGLVS MSEMLPARRA RGPNEPGGLS FGYMADIVQT SRITPDDPCN
     VTLEVAGAAS MLYDQIWLGG YMSGGVGFTQ FASCVYTNDI LDDFLYWGAD YIVDKYGEYG
     KAEVSLGAIK DIATVVTLYG LENYEEYPTA LEDHFGGSQR ATVIAISAGG STALATGNSS
     AAMSAWHLSM YLHKEAWGRL GAFGYDQQDQ CGAANV
//

ID   Q70CN7_9EURY   PRELIMINARY;   PRT;   253 AA.
AC   Q70CN7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 9.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogenic archaeon.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=198240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Galand P.E., Juottonen H., Fritze H., Yrjala K.;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AJ586250; CAE51953.1; -; Genomic_DNA.
DR   SMR; Q70CN7; 2-253.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   InterPro; IPR003183; MCR_alpha_N.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
FT   NON_TER       1      1
FT   NON_TER     253    253
SQ   SEQUENCE   253 AA;  27113 MW;  2D29FDF761E13A32 CRC64;
     FFISAYSMCA GEAAVADLSF AAKHAALVSM GEMLPARRAR GPNEPGGLSF GHISDIIQTS
     RKAIDDPAKV ALEVVGAGCM LYDQIWLGSY MSGGVGFTQY ATAAYTDDIL DNNVYYNIDY
     INDKYKGAAK VGKDNKIKAT LDVVKDIATE STIYGIETYE KFPTALEDHF GGSQRATVLA
     AAAGVATAIA TANANAGLSA WYLSMYLHKE AWGRLGFFGY DLQDQCGATN VLSYQGDEGL
     PDELRGPNYP NYA
//

ID   Q704C6_THETE   PRELIMINARY;   PRT;   735 AA.
AC   Q704C6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 10.
DE   Trehalose-6-phosphate synthase-phosphatase.
GN   Name=tpsp;
OS   Thermoproteus tenax.
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales;
OC   Thermoproteaceae; Thermoproteus.
OX   NCBI_TaxID=2271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15028704; DOI=10.1128/JB.186.7.2179-2194.2004;
RA   Siebers B., Tjaden B., Michalke K., Doerr C., Ahmed H., Zaparty M.,
RA   Gordon P., Sensen C.W., Zibat A., Klenk H.-P., Schuster S.C.,
RA   Hensel R.;
RT   "Reconstruction of the central carbohydrate metabolism of
RT   Thermoproteus tenax using genomic and biochemical data.";
RL   J. Bacteriol. 186:2179-2194(2004).
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DR   EMBL; AJ621287; CAF18468.1; -; Genomic_DNA.
DR   GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (U...; IEA.
DR   GO; GO:0003824; F:catalytic activity; IEA.
DR   GO; GO:0008152; P:metabolism; IEA.
DR   GO; GO:0005992; P:trehalose biosynthesis; IEA.
DR   InterPro; IPR001830; Glyco_trans_20.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR012766; Trehalose_OtsA.
DR   InterPro; IPR003337; Trehalose_PPase.
DR   Pfam; PF00982; Glyco_transf_20; 1.
DR   Pfam; PF02358; Trehalose_PPase; 1.
DR   TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR   TIGRFAMs; TIGR00685; T6PP; 1.
DR   TIGRFAMs; TIGR02400; trehalose_OtsA; 1.
SQ   SEQUENCE   735 AA;  82040 MW;  AF7A68E3844804ED CRC64;
     MGGQVRLIVV SNRLPVTISP SGEIRESVGG LATAMKSFLG AVNGGRELGL EEVVWVGWSG
     VPSERESNDL RERLRGMGLE PVPLSSEEVE GFYEGFSNST LWPLFHGFSE YATYEEKHWR
     AYRGVNEKYA KAVVALARPG DLVWIHDYHL MLAPAIVREA AEVGVGFFLH IPFPPAELLQ
     LLPSEWRREI LEGLLGSDLV GFHTYEYSAN FSRSVVRFLG YKVEMGAIAV GHRRVRVGVF
     PIGIDFDRFY NSSQDPSVVE EMAKLREMLG RAKVVFSIDR LDYTKGVLRR VAAWERFLRE
     HPEWRGRAVF VLVVVPSRTG VPMYEEMKRQ IDREVGRING ELGELNWVPI VYLYRFIPSP
     TLMALYNIAD VALITPLRDG MNLVAKEFVA SKRDCRGVLI LSELAGASKE LAEALVINPN
     DVGGTAEAIA EALSMSEDEQ CRRIRAMQER LRMRDVVRWG TDFIYSLISA KSAREEVEKA
     LRYMEELSVD KLKSDFAKAK RRLLLLDYDG TLVPHYPYPH MAVPDGDLLE LLSRLAALPE
     TAVYVVSGRG RDFLDGWLGR LPVGLVAEHG FFLKHPGGEW KSLGKVDPSW RQYAKGIMED
     FASNVPGSFV EVKEAGIAWH YRNADETIAE KAVVELIDAL SNALAGSGLS ILRGKKVVEV
     RPAGYTKGTA AKMLLDELSP DFVFVAGDDE TDEGMFEVAP QSAYTVKVGP GPTLAKFRVG
     DYRGLRSLLE QLRPP
//

ID   Q704B9_THETE   PRELIMINARY;   PRT;   610 AA.
AC   Q704B9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 12.
DE   Glycogen phosphorylase (EC 2.4.1.1).
GN   Name=glgP;
OS   Thermoproteus tenax.
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales;
OC   Thermoproteaceae; Thermoproteus.
OX   NCBI_TaxID=2271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15028704; DOI=10.1128/JB.186.7.2179-2194.2004;
RA   Siebers B., Tjaden B., Michalke K., Doerr C., Ahmed H., Zaparty M.,
RA   Gordon P., Sensen C.W., Zibat A., Klenk H.-P., Schuster S.C.,
RA   Hensel R.;
RT   "Reconstruction of the central carbohydrate metabolism of
RT   Thermoproteus tenax using genomic and biochemical data.";
RL   J. Bacteriol. 186:2179-2194(2004).
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DR   EMBL; AJ621294; CAF18475.1; -; Genomic_DNA.
DR   GO; GO:0004645; F:phosphorylase activity; IEA.
DR   GO; GO:0016757; F:transferase activity, transferring glycosyl...; IEA.
DR   GO; GO:0009058; P:biosynthesis; IEA.
DR   GO; GO:0005975; P:carbohydrate metabolism; IEA.
DR   InterPro; IPR000173; GAP_DH.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   PANTHER; PTHR11468; Glyco_trans_35; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR   PROSITE; PS00071; GAPDH; UNKNOWN_1.
KW   Glycosyltransferase; Transferase.
SQ   SEQUENCE   610 AA;  68870 MW;  E136805C0AE3F9BD CRC64;
     MLPSPYPPVI GDLAATTNLP VLTFVKPVNG PAANMSLLCG ESGSVPGGSS SHNIFIASPL
     PPMKSLAIEA SSSCTTNFLL VRSTLRILPC HPGMDCLSIL IYHFYLRRVA RFGDIAFKLT
     MPPRAMIVSI TPELALDGSK NYAGGLGVLE GDKFYAAARL GVPYTVITLL YDRGYVEYTE
     QNGQLEPTEE DQSNFIKRLE LFRTCWTTVG GEEVEVAFYL YRLNTATAVF VKPLRPAWAA
     QATERLYIER TELERFRKYI ILAKAALRYI EKFIGWDRVK YVDLQEAYTA LVPLLKPDPR
     YRLVVHTPAP WGHPTFPSRF FRQELGFDLA MNPVVLTELG LAASSEGVVV SKKMVHFAAR
     TFPHHAHKIK AVTNAVEIPR WQHPAVADVK GPEELKAARA RVKEEALRAL GVRTDRPVIV
     WARRLTSYKR PHYMVQLIEE VNTDLFFILG GRAHPNDEYG RRIMAEFKRL AATRPNVLYI
     PSLYVEDMRK IIWAADIFTF TPFSGWEASG TSFMKAGING VPSVASRDGA VVEVVRDRYN
     GWLFGEDRTE LVSPDTPDID EREYAEFKQK VNEALDALAD GSYWEVAFNA YKTFREYYSM
     ERLFKEYGYL
//

ID   Q702A3_9CREN   PRELIMINARY;   PRT;   448 AA.
AC   Q702A3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 14.
DE   Putative molybdopterin biosynthesis protein.
OS   uncultured crenarchaeote.
OC   Archaea; Crenarchaeota; environmental samples.
OX   NCBI_TaxID=29281;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Treusch A.H., Kletzin A., Raddatz G., Ochsenreiter T., Quaiser A.,
RA   Meurer G., Schuster S.C., Schleper C.;
RT   "Characterization of Large-Insert DNA Libraries from Soil for
RT   Environmental Genomic Studies of Archaea.";
RL   Environ. Microbiol. 9:970-980(2004).
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DR   EMBL; AJ627421; CAF28721.1; -; Genomic_DNA.
DR   HSSP; P12282; 1JWA.
DR   GO; GO:0003824; F:catalytic activity; IEA.
DR   GO; GO:0006790; P:sulfur metabolism; IEA.
DR   InterPro; IPR000205; FAD/NAD(P)_BS.
DR   InterPro; IPR009036; MoeB.
DR   InterPro; IPR007901; MoeZ_MoeB.
DR   InterPro; IPR000594; ThiF_NAD_FAD_bd.
DR   InterPro; IPR003749; ThiS.
DR   Pfam; PF05237; MoeZ_MoeB; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   Pfam; PF02597; ThiS; 1.
SQ   SEQUENCE   448 AA;  49046 MW;  3FDED96767FCF5DA CRC64;
     MTNIEFVIPS VLTKGTGEKK IPLDATDLQD AFTKITEQLG EDFKRKVLDM NGKPRSLINI
     YINGKNMRFS NDGMATKLNS GDSIYILPAV AGGSELKNED LQRYSRQIML EEIGFVGLEK
     LRKAKVCVVG VGGIGNPVVT QLTAMGVGKL KIVDRDIIEI SNLHRQHLYT ENDLGKVKVE
     AAKERLEKIN SSVEIEALPN SVTKYTAESI IRGYDIVVDA LDSIDARYAL NDACIKLNIP
     LIYAGALGML GSVCTIIPNK TACLRCIFPA LAEDDMPTCS TEGVHPSILY LVGGIQVSEA
     VKIILGEKPT LENKLMYVDL NDLSLEKISV FRQEECPSCG TKRIDIDELE TKQLIIEELC
     GRDRGKRTYT VTPSHISSSL NLIGIEKNAE RLGYTIKTKG ELGLTIMSNN SDNLSISFMS
     SGAATIVGAK SEDEALSIYK SFVDDIKP
//

ID   Q6ZXB1_9EURY   PRELIMINARY;   PRT;   156 AA.
AC   Q6ZXB1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 9.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogenic archaeon.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=198240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15812059; DOI=10.1128/AEM.71.4.2195-2198.2005;
RA   Galand P.E., Fritze H., Conrad R., Yrjala K.;
RT   "Pathways for methanogenesis and diversity of methanogenic Archaea in
RT   three different boreal peatlands.";
RL   Appl. Environ. Microbiol. 71:2195-2198(2005).
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DR   EMBL; AJ704551; CAG28707.1; -; Genomic_DNA.
DR   SMR; Q6ZXB1; 1-155.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     156    156
SQ   SEQUENCE   156 AA;  16799 MW;  721FEB54E1886332 CRC64;
     GGVGFTQYAT AAYTDNILDD YSYYGNDYAK KYGADGKAPA TMDVVNDLGT EVTLYGIEQY
     EKYPTTLEDH FGGSQRATVL AAASGVTAAI ATGNSNAGLS AWYLSMLLHK DAWGRLGFYG
     YDLQDQCGST NTFSVRSDEG APDELRGANY PNYAMK
//

ID   Q6ZXA7_9EURY   PRELIMINARY;   PRT;   156 AA.
AC   Q6ZXA7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 9.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogenic archaeon.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=198240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15812059; DOI=10.1128/AEM.71.4.2195-2198.2005;
RA   Galand P.E., Fritze H., Conrad R., Yrjala K.;
RT   "Pathways for methanogenesis and diversity of methanogenic Archaea in
RT   three different boreal peatlands.";
RL   Appl. Environ. Microbiol. 71:2195-2198(2005).
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DR   EMBL; AJ704555; CAG28711.1; -; Genomic_DNA.
DR   SMR; Q6ZXA7; 1-156.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     156    156
SQ   SEQUENCE   156 AA;  16863 MW;  B2F9EBC5FE28283D CRC64;
     GGVGFTQYAT AAYTDNILDD YTEYGVDYIK KKHGGIGKAK CTQEVVSDIA TEVNLYGMKQ
     YEQYPTALES HFGGSQRASV LAAASGISVG LATANSNAGL NGWYLSMLMH KEGWSRLGFF
     GYDLQDQCGS ANCMSIRPDE GLLGELRGPN YPNYAM
//

ID   Q6V265_9EURY   PRELIMINARY;   PRT;   154 AA.
AC   Q6V265;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 8.
DE   Methyl coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   uncultured methanogenic archaeon.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=198240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Nercessian O.G., Bienvenu N., Moreira D., Prieur D., Jeanthon C.;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY354021; AAQ56610.1; -; Genomic_DNA.
DR   SMR; Q6V265; 1-154.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     154    154
SQ   SEQUENCE   154 AA;  16894 MW;  5E8D758B5BD5179D CRC64;
     GGVGFTQYAT AAYTDDILDD FCYYGLDYVE NKYGRNGTKP TMDVVEDIAT EVTLYALEQY
     DEYPTLLEDH FGGSQRAAVA AAAAGVSTCM ATGNSNAGVN AWYLSQIMHK EYHSRLGFYG
     YDLQDQCGAS NSLSIRNDES SPLELRGPNY PNYA
//

ID   Q6V263_9EURY   PRELIMINARY;   PRT;   154 AA.
AC   Q6V263;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 8.
DE   Methyl coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   uncultured methanogenic archaeon.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=198240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Nercessian O.G., Bienvenu N., Moreira D., Prieur D., Jeanthon C.;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY354023; AAQ56612.1; -; Genomic_DNA.
DR   SMR; Q6V263; 1-154.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     154    154
SQ   SEQUENCE   154 AA;  16689 MW;  1BD57F0837C60913 CRC64;
     GVGFTQYATA VYTDNILDGY VYYGLDYVED KYGLAEAEPD MDVVKDVATE VTLYGLEQYE
     RYPAAMETHF GGSQRAAVCA AAAGCSVAFA TGHAQAGVNG WYLSQILHKE AHGRLGFYGY
     DLQDQCGAAN SLSVRSDEGL PLELRGPNYP NYAM
//

ID   Q6V262_9EURY   PRELIMINARY;   PRT;   156 AA.
AC   Q6V262;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 8.
DE   Methyl coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   uncultured methanogenic archaeon.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=198240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Nercessian O.G., Bienvenu N., Moreira D., Prieur D., Jeanthon C.;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY354024; AAQ56613.1; -; Genomic_DNA.
DR   SMR; Q6V262; 1-155.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     156    156
SQ   SEQUENCE   156 AA;  16983 MW;  92FD931E6BBD8D5D CRC64;
     GGVGFTQYAT AVYTDNILDD YVYYGLEYVE DKYGLAEADP SMDVVKDVAT EVTLYGLEQY
     ERYPAAMETH FGGSQRAAVC AAATGCSVSF ATGHAQAGLN GWYLSQIMHK EGHGRLGFYG
     YDLQDQCGAA NTLSVRSDEG LPLELRGPNY PNYAMK
//

ID   Q6V253_9EURY   PRELIMINARY;   PRT;   154 AA.
AC   Q6V253;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 8.
DE   Methyl coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   Methanothermococcus okinawensis.
OC   Archaea; Euryarchaeota; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanothermococcus.
OX   NCBI_TaxID=155863;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 14208;
RA   Nercessian O.G., Bienvenu N., Moreira D., Prieur D., Jeanthon C.;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY354033; AAQ56622.1; -; Genomic_DNA.
DR   SMR; Q6V253; 1-154.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     154    154
SQ   SEQUENCE   154 AA;  16879 MW;  4C04E07CDA356AE5 CRC64;
     GGVGFTQYAT ATYTDDILDD FSYYGYDYVE KKYGINGTKP TMDVVEDIAT EVTLYGLEQY
     DEFPALLEDH FGGSQRAGVV AAASGISVCM ATGNSNAGVN GWYLSQILHK EYHSRLGFYG
     YDLQDQCGAS NSLSIRNDES SPLELRGPNY PNYA
//

ID   Q6TWD8_9EURY   PRELIMINARY;   PRT;   374 AA.
AC   Q6TWD8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 10.
DE   Methyl-coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   Methanobacterium aarhusense.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanobacterium.
OX   NCBI_TaxID=256826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H2-LR;
RA   Shlimon A.G., Friedrich M.W., Niemann H., Ramsing N.B., Finster K.;
RT   "Methanobacterium aarhusense sp. nov., a novel methanogen isolated
RT   from a marine sediment (Aarhus Bay, Denmark).";
RL   Int. J. Syst. Evol. Microbiol. 54:759-763(2004).
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DR   EMBL; AY386125; AAR27839.1; -; Genomic_DNA.
DR   SMR; Q6TWD8; 1-374.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   InterPro; IPR003183; MCR_alpha_N.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
FT   NON_TER       1      1
FT   NON_TER     374    374
SQ   SEQUENCE   374 AA;  40718 MW;  9F8E7CB126CA17D0 CRC64;
     VIVGLNTAHT VIEKRLGKEV TPETITHYLG NCNHAMPGAA VVQEHMVETN PSLVADSYVK
     IFTGNDEISD EVDQRFVINI NEEFPEEQAK VLKAEVGDGM WQVVKIPTIV SRTCDGGTTS
     RWSAMQIGMS MISAYKQAAG EAATGDFAYA AKHAEVVHMG TYLPVRRARG ENEPGGIAFG
     FLADICQSSR VNMDDPVRVA LDVVASGAML YDQIWLGSYM SGGVGFTQYA TAAYTDNILD
     DFTYYGKEYV EDKFGLCEAP NNMDTVLDVA SEVTFYGLEQ YEEYPALLET QFGGSQRAAV
     AAAAAACSTG FATGNAQTAL SGWYLSMYLH KEQHSRLGFY GYDLQDQCGA SNVFSIRGDE
     GLPLELRGAN YPNY
//

ID   Q6T569_9EURY   PRELIMINARY;   PRT;   239 AA.
AC   Q6T569;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 10.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured Methanobacteriales archaeon.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   environmental samples.
OX   NCBI_TaxID=194842;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=14871211; DOI=10.1111/j.1462-2920.2004.00568.x;
RA   Newberry C.J., Webster G., Cragg B.A., Parkes R.J., Weightman A.J.,
RA   Fry J.C.;
RT   "Diversity of prokaryotes and methanogenesis in deep subsurface
RT   sediments from the Nankai Trough, Ocean Drilling Program Leg 190.";
RL   Environ. Microbiol. 6:274-287(2004).
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DR   EMBL; AY436537; AAR36119.1; -; Genomic_DNA.
DR   SMR; Q6T569; 1-239.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   InterPro; IPR003183; MCR_alpha_N.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
FT   NON_TER       1      1
FT   NON_TER     239    239
SQ   SEQUENCE   239 AA;  25871 MW;  2737778B60BA4F85 CRC64;
     MISAYNQCAG EGATGDFAYA SKHAEVIHMG TYLPVRRARA ENEPGGIAFG FLADMVQSTR
     VNPDDPVRSA LDVVAAGAAL YDQIWLGSYM SGGVGFTQYA SAAHTDNILD DFLYYGKEYV
     EDKFGICEAP NNMDTVLDVG SEVTFYGLEQ YEEYPALLET QFGGSQRASV VSAAAGCATA
     FATGNSQTGL SAWYLSMYLH KEQHSRLGFY GYDLQDQCGA SNVFSIRNDE GLPVEMRGP
//

ID   Q6SIF9_9EURY   PRELIMINARY;   PRT;   160 AA.
AC   Q6SIF9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 12.
DE   Methyl-coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   uncultured euryarchaeote.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=114243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15528519; DOI=10.1128/AEM.70.11.6559-6568.2004;
RA   Castro H., Ogram A., Reddy K.R.;
RT   "Phylogenetic characterization of methanogenic assemblages in
RT   eutrophic and oligotrophic areas of the Florida Everglades.";
RL   Appl. Environ. Microbiol. 70:6559-6568(2004).
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DR   EMBL; AY458420; AAR24541.1; -; Genomic_DNA.
DR   SMR; Q6SIF9; 2-160.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     160    160
SQ   SEQUENCE   160 AA;  17731 MW;  BB46B7EBD0AEABC9 CRC64;
     DFTQYATAAY TDNILDDYTY YGMDYIKDKY KVDWKNPSEK GLAKANQDVI NDIATEVTLY
     GMEQYEQFPT ALETHFGGSQ RASVLAAASG LSTAIATGNS NAGLNGWYLS MLLHKEGWSR
     LGFYGYDLQD QCGSANTELF RADEGCVGEL RGANYPNYAM
//

ID   Q6SEI7_9EURY   PRELIMINARY;   PRT;   162 AA.
AC   Q6SEI7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 11.
DE   Methyl-coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   uncultured euryarchaeote.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=114243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15528519; DOI=10.1128/AEM.70.11.6559-6568.2004;
RA   Castro H., Ogram A., Reddy K.R.;
RT   "Phylogenetic characterization of methanogenic assemblages in
RT   eutrophic and oligotrophic areas of the Florida Everglades.";
RL   Appl. Environ. Microbiol. 70:6559-6568(2004).
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DR   EMBL; AY459319; AAR24561.1; -; Genomic_DNA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     162    162
SQ   SEQUENCE   162 AA;  18115 MW;  3FF9CD3C09CBC441 CRC64;
     WCRFTQYATA AYTDNILDEY TYYGMDYIKD KYKVDWKNPN DKDKVKPTQD IANDMATEVA
     LNGMEQYEQF PTLMEDHFGG SQRAGVLAAA CGLTASIATG NSNAGLNAWY LCMLLHKEGW
     SRLGFFGYDL QDQCGSANSL AIRPDEGAIG ELRGPNYPNY AM
//

ID   Q6SCJ1_9EURY   PRELIMINARY;   PRT;   156 AA.
AC   Q6SCJ1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 11.
DE   Methyl-coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   uncultured euryarchaeote.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=114243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15528519; DOI=10.1128/AEM.70.11.6559-6568.2004;
RA   Castro H., Ogram A., Reddy K.R.;
RT   "Phylogenetic characterization of methanogenic assemblages in
RT   eutrophic and oligotrophic areas of the Florida Everglades.";
RL   Appl. Environ. Microbiol. 70:6559-6568(2004).
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DR   EMBL; AY460215; AAR24565.1; -; Genomic_DNA.
DR   SMR; Q6SCJ1; 1-156.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     156    156
SQ   SEQUENCE   156 AA;  17088 MW;  427F985B2412A482 CRC64;
     GGVGFTQYAT AAYTDNVLDD YTYYGQDYVK DKYKGWTKAP QTQAAVNDIA TEVTLYGMEQ
     YENFPSLLED HFGGSQRASV LAAAAGLTCS MATANSNAGL NGWYLSMLLH KEGWSRLGFY
     GYDLQDQCGS ANCMAIRSDE GLITELRGAN YPNYAM
//

ID   Q6MZC9_9ARCH   PRELIMINARY;   PRT;   589 AA.
AC   Q6MZC9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 13.
DE   Adenine deaminase (EC 3.5.4.2).
GN   Name=adeC; ORFNames=C2_0013;
OS   uncultured archaeon.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=115547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=14685246; DOI=10.1038/nature02207;
RA   Krueger M., Meyerdierks A., Gloeckner F.O., Amann R., Widdel F.,
RA   Kube M., Reinhardt R., Kahnt J., Boecher R., Thauer R.K., Shima S.;
RT   "A conspicuous nickel protein in microbial mats that oxidise methane
RT   anaerobically.";
RL   Nature 426:878-881(2003).
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DR   EMBL; BX649197; CAE46371.1; -; Genomic_DNA.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA.
DR   GO; GO:0016787; F:hydrolase activity; IEA.
DR   GO; GO:0006146; P:adenine catabolism; IEA.
DR   InterPro; IPR006679; Adenine_deam.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR011550; Amidohydro_like.
DR   InterPro; IPR011059; Metal-dep_hydro_comp.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   ProDom; PD001248; Amidohydro_like; 1.
DR   TIGRFAMs; TIGR01178; ade; 1.
KW   Hydrolase.
SQ   SEQUENCE   589 AA;  64490 MW;  062BF973558662E9 CRC64;
     MASTNLLKMD PYLLIKFPKL KCQKMNALID IALGDKKADL VLKNVNLVNV CSGEIYETDI
     AIAHGLIAGL GRYEGRLEID AQDNYAVPGL IDGHTHIEMS MLSVREFAKA VVPRGTTAVV
     ADPHEIANVL GIAGIRALFD DARTTALKVF CMAPSCVPST DPSLGLETSG ATIDHTEIRK
     LLRMDGIIGL AEVMNYVGVI AKEEVVWEKI EIAKALKMPI DGHAPLLSGK ELNAYVVSGA
     GSDHENTTYE ESQEKLRLGM RVMVREGSVA KNLKKIVPLL RTVDTRNCML VTDGDRTPLD
     LKDEGYLDYV LRRAIEEGID PVKAVQMCTI NPAQWFKLDA EIGCIAPGKI ADIVLLKNLD
     TFEVEKVIVN GKPDFAQRSE YSFNYPQYRE SVRIMRVKPD EFVIEQEGAI KARIIGLIEG
     ELLTEELVEE ISGIEIARDI LEIGVLERHH YSGNMGLGFV KGFGLKIGAI ASTIAHDSHN
     IVVIGTDEED MALACNRLKD IGGGIVLCNG KEVTSELKLP IAGLMSDNGL DYVMRKQKEM
     DDNISEMGCK LPAPFIAISF LALPVIPKLK ITDKGLVDVA KREIVGVFL
//

ID   Q6JIA4_9EURY   PRELIMINARY;   PRT;   160 AA.
AC   Q6JIA4;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 11.
DE   Methyl-coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   uncultured euryarchaeote.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=114243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15528519; DOI=10.1128/AEM.70.11.6559-6568.2004;
RA   Castro H., Ogram A., Reddy K.R.;
RT   "Phylogenetic characterization of methanogenic assemblages in
RT   eutrophic and oligotrophic areas of the Florida Everglades.";
RL   Appl. Environ. Microbiol. 70:6559-6568(2004).
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DR   EMBL; AY458406; AAR22531.1; -; Genomic_DNA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     160    160
SQ   SEQUENCE   160 AA;  17857 MW;  45AAC1637FA4A82E CRC64;
     DFTQYATAAY TDNILDEYTY YGMDYIKDKY KVDWKNPNEK DKVKPTQDIV NDMATEVALN
     GMEQYEQFPT LMEDHFGGSQ RAGVLAAACG LTTSIATGNS NAGLNAWYLC MLLHKEGWSR
     LGFFGYDLQD QCGSANSLAI RPDEGAIGEL RGPNYPNYAM
//

ID   Q6JIA0_9EURY   PRELIMINARY;   PRT;   160 AA.
AC   Q6JIA0;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 11.
DE   Methyl-coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   uncultured euryarchaeote.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=114243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15528519; DOI=10.1128/AEM.70.11.6559-6568.2004;
RA   Castro H., Ogram A., Reddy K.R.;
RT   "Phylogenetic characterization of methanogenic assemblages in
RT   eutrophic and oligotrophic areas of the Florida Everglades.";
RL   Appl. Environ. Microbiol. 70:6559-6568(2004).
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DR   EMBL; AY458410; AAR22535.1; -; Genomic_DNA.
DR   SMR; Q6JIA0; 2-160.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     160    160
SQ   SEQUENCE   160 AA;  17638 MW;  41D7BC21326D12ED CRC64;
     DFTQYATAAY TDNILDDYTY YGMDYVKDKY KVDYKNPSEK GLAKSTQDVI NDIATEVTLY
     GMEQYEQFPT ALETHFGGSQ RASVLAAASG LSTAIATGNS NAGLNGWYLS MLLHKEGWSR
     LGFYGYDLQD QCGSANTESF RADEGAVGEL RGANYPNYAM
//

ID   Q6JI97_9EURY   PRELIMINARY;   PRT;   162 AA.
AC   Q6JI97;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 11.
DE   Methyl-coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   uncultured euryarchaeote.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=114243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15528519; DOI=10.1128/AEM.70.11.6559-6568.2004;
RA   Castro H., Ogram A., Reddy K.R.;
RT   "Phylogenetic characterization of methanogenic assemblages in
RT   eutrophic and oligotrophic areas of the Florida Everglades.";
RL   Appl. Environ. Microbiol. 70:6559-6568(2004).
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DR   EMBL; AY458413; AAR22538.1; -; Genomic_DNA.
DR   SMR; Q6JI97; 1-162.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     162    162
SQ   SEQUENCE   162 AA;  17550 MW;  9FE49DB657A17C6A CRC64;
     GGVGFTQYAT AAYTDDILDN NVYYDVDYIN QKYKGAAEVG KNNKIKATLD VVKDIATEST
     IYGIETYEKF PTALEDHFGG SQRATVLAAA AGVAIALATA NANAGLSGWY LSMYLHKEAW
     GRLGFFGYDL QDQCGATNVL SYQGDEGLPD ELRGPNYPNY AM
//

ID   Q6ITY5_9EURY   PRELIMINARY;   PRT;   156 AA.
AC   Q6ITY5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 9.
DE   Methyl-coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   uncultured Methanosaeta sp.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosaetaceae; Methanosaeta; environmental samples.
OX   NCBI_TaxID=183756;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15946291; DOI=10.1111/j.1462-2920.2004.00766.x;
RA   Banning N., Brock F., Fry J.C., Parkes R.J., Hornibrook E.R.,
RA   Weightman A.J.;
RT   "Investigation of the methanogen population structure and activity in
RT   a brackish lake sediment.";
RL   Environ. Microbiol. 7:947-960(2005).
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DR   EMBL; AY625582; AAT45704.1; -; Genomic_DNA.
DR   SMR; Q6ITY5; 1-156.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     156    156
SQ   SEQUENCE   156 AA;  16803 MW;  804C926EB4A05656 CRC64;
     GGVGFTQYAT AAYTNDVLDD FSYYACDYGV DKYGGWGEAP AVLDTSKDIA TETTLYAMEQ
     YEAFPTLLED HFGGSQRSAV MAAASAIGSA CLTGNSQSGL AGWYLSHLIH KDGWGRMGFF
     GYDLQDQCGP TNVFSYQGDE GSPLELRGAN YPNYAM
//

ID   Q6ITY2_9EURY   PRELIMINARY;   PRT;   163 AA.
AC   Q6ITY2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 9.
DE   Methyl-coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   uncultured Methanomicrobiales archaeon.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales;
OC   environmental samples.
OX   NCBI_TaxID=183760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15946291; DOI=10.1111/j.1462-2920.2004.00766.x;
RA   Banning N., Brock F., Fry J.C., Parkes R.J., Hornibrook E.R.,
RA   Weightman A.J.;
RT   "Investigation of the methanogen population structure and activity in
RT   a brackish lake sediment.";
RL   Environ. Microbiol. 7:947-960(2005).
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CC   -----------------------------------------------------------------------
DR   EMBL; AY625585; AAT45707.1; -; Genomic_DNA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     163    163
SQ   SEQUENCE   163 AA;  17935 MW;  C7854F3AF24865F5 CRC64;
     GGVGFTQYAT AAYTDNILDE YTYYGMDYIK QKYKVDWANP AEKDKVKPTQ DIVNDIATEV
     ALNGMEQYEQ YPTLMEDHFG GSQRAGVLAA ACGLTCSIAT GNSNAGLNGW YLCMLLHKEG
     WSRLGFFGYD LQDQCGSANS LAIRPDEGAI GEFRGPNYSN YAM
//

ID   Q6ITX6_9EURY   PRELIMINARY;   PRT;   163 AA.
AC   Q6ITX6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 9.
DE   Methyl-coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   uncultured Methanomicrobiales archaeon.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales;
OC   environmental samples.
OX   NCBI_TaxID=183760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15946291; DOI=10.1111/j.1462-2920.2004.00766.x;
RA   Banning N., Brock F., Fry J.C., Parkes R.J., Hornibrook E.R.,
RA   Weightman A.J.;
RT   "Investigation of the methanogen population structure and activity in
RT   a brackish lake sediment.";
RL   Environ. Microbiol. 7:947-960(2005).
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DR   EMBL; AY625591; AAT45713.1; -; Genomic_DNA.
DR   SMR; Q6ITX6; 1-163.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     163    163
SQ   SEQUENCE   163 AA;  17859 MW;  0B21BA1171B080C1 CRC64;
     GGVGFTQYAT AAYTDNILDD YTYYGMDYIK DKYKVDWKNP NEKGLAKSNQ DVINDIATEV
     TLYGMEQYEQ FPTALETHFG GSQRASVLAA ASGLSTAIAT GNSNAGLNGW YLSMLLHKEG
     WSRLGFFGYD LQDQCGSTNS LSVRPDEGAV GELRGPNYPN YAM
//

ID   Q6ITX0_9EURY   PRELIMINARY;   PRT;   211 AA.
AC   Q6ITX0;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   30-MAY-2006, entry version 10.
DE   Methyl-coenzyme M reductase alpha subunit (Fragment).
GN   Name=mcrA;
OS   uncultured Methanomicrobiales archaeon.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales;
OC   environmental samples.
OX   NCBI_TaxID=183760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15946291; DOI=10.1111/j.1462-2920.2004.00766.x;
RA   Banning N., Brock F., Fry J.C., Parkes R.J., Hornibrook E.R.,
RA   Weightman A.J.;
RT   "Investigation of the methanogen population structure and activity in
RT   a brackish lake sediment.";
RL   Environ. Microbiol. 7:947-960(2005).
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DR   EMBL; AY625597; AAT45719.1; -; Genomic_DNA.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   InterPro; IPR003183; MCR_alpha_N.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
FT   NON_TER       1      1
FT   NON_TER     211    211
SQ   SEQUENCE   211 AA;  22996 MW;  D6135CB3891F28BF CRC64;
     AAVADLAFAA KHAGVIQMGD ILPARRARGP NEPGGIKFGH FADMIQADRK YPNDPARATL
     EVVGAGAMLF DQIWLGSYMS GGVGFTQYAT AAYTDNILDD YTYYGMDYIK SKYKVNWQSP
     SEKDKVKATQ DVVNDIATEV NLYGMEQYEQ YPTALEDHFG GSQRASVLAA ASGISVSIAT
     GNSNAGLNGW YLSMLMHKEG WSRLGFFGYD L
//

ID   Q69GZ5_METVO   PRELIMINARY;   PRT;  1199 AA.
AC   Q69GZ5;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   30-MAY-2006, entry version 9.
DE   Chromosomal segregation protein.
GN   Name=SMC;
OS   Methanococcus voltae.
OC   Archaea; Euryarchaeota; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=2188;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PS;
RA   Feldman R., Overbeek R., Whitman W.;
RT   "Chromosomal segregation protein SMC.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY288521; AAQ22369.1; -; Genomic_DNA.
DR   GO; GO:0005694; C:chromosome; IEA.
DR   GO; GO:0005524; F:ATP binding; IEA.
DR   GO; GO:0016887; F:ATPase activity; IEA.
DR   GO; GO:0005525; F:GTP binding; IEA.
DR   GO; GO:0005515; F:protein binding; IEA.
DR   GO; GO:0051277; P:chromosome organization and biogenesis (sen...; IEA.
DR   InterPro; IPR003439; ABC_transp_like.
DR   InterPro; IPR005289; GTP_bd.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR003395; SMC_N.
DR   InterPro; IPR011891; SMC_prok_A.
DR   Pfam; PF06470; SMC_hinge; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   ProDom; PD000006; ABC_transporter; 1.
DR   TIGRFAMs; TIGR00650; MG442; 1.
DR   TIGRFAMs; TIGR02169; SMC_prok_A; 1.
SQ   SEQUENCE   1199 AA;  137830 MW;  6BB179C2979CAA1D CRC64;
     MISISEIHLK NFKSFKNTKL KIPDGFTAIL GPNGSGKSNT IDGICFVLGK TSAKSLRAGK
     FNQLITYHNG KRADYAEVTL FFDNINREIP IDSDKVGICR KVKLNGDNNY YVVWYEVEKQ
     NTKINTESSQ KKTSKASKVE KRRRMKKNEV LDLLSKISLI ADGPNIILQG DLLRIIDTSP
     NERRKILDEV SGVAEFDEKS EKAKKELSQA REYIEKIDIR INEVRANLEK LKKEKEDAEK
     YTVYNKKLKV TKYILTSKKV EFLKMVLDET KDEIEALKET KNCYIQDISN IDSEIIGLKV
     KINELVNELN EKGSEEVMEL HKSIKELEVN LNNDKNALEN AIDDLKHTLK MEESKNNDLN
     ETKEKINNIR IDTLKKEAEA KVLIKEIEKL NEERQNLEKK VEQSESQVKA LKNQESKLSE
     RINDTQKELY GLKNELNQLE NTLNNRTFDY QKNNETIENL TNQIAEFSDL EDTKKLYKEL
     EDIAVELEFS KKKLQEKITE RNDSQSKLDN LHSEYVKENA RIKTLKDMEN FSLDRAVKGV
     LDAKLPGVVD IAGNLAKTKG EYKTAIEVAG GARLNHIVVK KMDDGSRAIN YLKQKRLGRA
     TFLPMDRIKG MDAKDISDTG IIGKAIDLVE FDIKYTNVFK FIFGNTHIVD NLENAKKLSL
     KYKARFVTLE GEVIEPSGAM VGGNIRRNSA IKVDIDMKKL TNLSEDIKEL EQILSNVKDE
     IERLNNKINT CSTRKLELDN RLKIARDQEF KKEEITKSNN LKIKELNMLN SKIDDEISEL
     TDEKEILSQK VQNLDNKLSE VMGQRERIVN EIKSYENSEL SKRIKEIDHK IRENESSKNT
     LENEIKKGAI LVKEVLIPKI SELNSNIKSL ADKKNMFKNS VEIYKSNIES NSSILSDKRG
     KYEELTKGLK DLTDKKECYE LEIENLQNNK EELREKATDI DNQVNVINVD RAKYETRLEE
     EERKLYLCDT LENIEDISDE MIEETYSLEI DDLERNQALL ESSIKKLEPV NMRAIEDYDF
     INERYEELFG KRKEYEQEEG KYLQLISEVQ KRKKETFMKT YDRVAENYEQ IYGEIGGNGK
     LSLENEEDPF SGGLLIDASP MNKQLQNLDV MSGGEKSLTA LAFLFAIQRL NPSPFYVLDE
     VDAALDTKNA SLIGDMISNA SKESQFIVIS HREQMISKSN VMYGVCMENG LSKIVSVKL
//

ID   Q64EJ0_9ARCH   PRELIMINARY;   PRT;   169 AA.
AC   Q64EJ0;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   30-MAY-2006, entry version 7.
DE   Carbon monoxide dehydrogenase beta subunit.
GN   Name=cdhC; ORFNames=GZ11A10_42;
OS   uncultured archaeon GZfos11A10.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=285399;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15353801; DOI=10.1126/science.1100025;
RA   Hallam S.J., Putnam N., Preston C.M., Detter J.C., Rokhsar D.,
RA   Richardson P.M., DeLong E.F.;
RT   "Reverse methanogenesis: testing the hypothesis with environmental
RT   genomics.";
RL   Science 305:1457-1462(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Putnam N., Detter J.C., Richardson P.M., Rokhsar D.;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY714815; AAU82187.1; -; Genomic_DNA.
DR   GO; GO:0003824; F:catalytic activity; IEA.
DR   GO; GO:0008152; P:metabolism; IEA.
DR   InterPro; IPR003704; CO_DH_CoA_synth.
DR   Pfam; PF02552; CO_dh; 1.
DR   PIRSF; PIRSF006035; CO_dh_b_ACDS_e; 1.
DR   TIGRFAMs; TIGR00315; cdhB; 1.
SQ   SEQUENCE   169 AA;  18111 MW;  0D34595386D8A56A CRC64;
     MTRAYQCANV PGPHLGKVGT SASVASAIKR AKRPVLIVGS ELTNLDWALD LAKKQDIPVV
     ATAHVAGTMR EKGVDPDRVL GAIEITNLLK SPEWGGIRGE GQHDLAIFVD VKYYLEAQML
     STLKHFAPHI KTISLTKGHQ PNADQSLPNL SEKKLGKFLA GVVEGLAEG
//

ID   Q64EE9_9ARCH   PRELIMINARY;   PRT;   565 AA.
AC   Q64EE9;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   30-MAY-2006, entry version 11.
DE   Adenine deaminase.
GN   Name=adeC; ORFNames=GZ11H11_35;
OS   uncultured archaeon GZfos11H11.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=285398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15353801; DOI=10.1126/science.1100025;
RA   Hallam S.J., Putnam N., Preston C.M., Detter J.C., Rokhsar D.,
RA   Richardson P.M., DeLong E.F.;
RT   "Reverse methanogenesis: testing the hypothesis with environmental
RT   genomics.";
RL   Science 305:1457-1462(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Putnam N., Detter J.C., Richardson P.M., Rokhsar D.;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY714816; AAU82228.1; -; Genomic_DNA.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA.
DR   GO; GO:0016787; F:hydrolase activity; IEA.
DR   GO; GO:0006146; P:adenine catabolism; IEA.
DR   InterPro; IPR006679; Adenine_deam.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR011550; Amidohydro_like.
DR   InterPro; IPR011059; Metal-dep_hydro_comp.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   ProDom; PD001248; Amidohydro_like; 1.
DR   TIGRFAMs; TIGR01178; ade; 1.
SQ   SEQUENCE   565 AA;  61595 MW;  CE23ED0096F61E64 CRC64;
     MNDLVDIASG NKKADLVLKN ANLVNVCSGE IYETDIAIAH GLIAGLGRYE GRVEIDAQDN
     YAVPGLIDGH THIEMSMLSV REFAKAVVPR GTTAVVADPH EIANVLGIAG IRALLDDART
     TALKVFCMAP SCVPSTDPSL GLETSGATLD HREIRKLLQM DGIIGLAEVM NYVGVIAKEE
     EVWEKIEIAK ALKMPIDGHA PLLSGKELNA YVVSGAGSDH ENTTYEESRE KLRLGMRVMV
     REGSVAKNLK NIAPLLRTVD TRNCMLVTDG DRTPLDLKDE GYLDYVLRRA IEEGIDPVKA
     VQMCTINPAQ WFKLDNIIGC IAPGKIADIV LLKKLDTFEV EKVIVNGKPD FAQRSEYSFK
     YPQYRESVRI MRVKPDEFVI AQEGAIKARI IGLIEGELLT EELVEEISGI EIARDILEIG
     VLERHHYSGN MGLGFVKGFG LKTGAIASTI AHDSHNIVVI GTNEEDMALA CNRLKAIGGG
     IVLCNGKEVT SELKLPIAGL MSDKGLDYVM RKQKEMDDSI SEMGCKLPAP FIAISFLALP
     VIPKLKITDK GLVDVAKREI VAVFL
//

ID   Q64DQ6_9ARCH   PRELIMINARY;   PRT;   308 AA.
AC   Q64DQ6;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   30-MAY-2006, entry version 7.
DE   Dolichol-P-glucose synthetase.
GN   ORFNames=GZ17F1_42;
OS   uncultured archaeon GZfos17F1.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=285395;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15353801; DOI=10.1126/science.1100025;
RA   Hallam S.J., Putnam N., Preston C.M., Detter J.C., Rokhsar D.,
RA   Richardson P.M., DeLong E.F.;
RT   "Reverse methanogenesis: testing the hypothesis with environmental
RT   genomics.";
RL   Science 305:1457-1462(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Putnam N., Detter J.C., Richardson P.M., Rokhsar D.;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY714823; AAU82471.1; -; Genomic_DNA.
DR   InterPro; IPR005242; CHP374.
DR   Pfam; PF03706; UPF0104; 1.
DR   TIGRFAMs; TIGR00374; CHP374; 1.
SQ   SEQUENCE   308 AA;  33388 MW;  FC3342236818F92B CRC64;
     MTSILAILIL FLIASIIGRA DIIDELRTAS PALIALSIPV YLISWPLRGI RYQQILAEIG
     VKEDLNFLVG CIAVSQSANV FLPARIGDVA RAYLLKKVKN ISWITGLSSL VVERMFDIIA
     ITVIGGFAVL GLRGMLLDQW VTDVITIAGL ATVTVFGILV LFLKLRTTIG GVIDRFIREI
     ALVSTNPRAF AIVLTGSLLV WLVDTLTCFV ILNAFSEQIS LSMIPVIFLA IAVGNLTKIF
     PITPGSIGPY EAVLTGIFSL GGIDTAIGFA AAVLDHFVKN LVTLILGRVY LSRFDLSWSQ
     LVEQSEQQ
//

ID   Q64DQ1_9ARCH   PRELIMINARY;   PRT;   462 AA.
AC   Q64DQ1;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   30-MAY-2006, entry version 9.
DE   Tungsten formylmethanofuran dehydrogenase subunit A.
GN   Name=fwdA; ORFNames=GZ17G11_3;
OS   uncultured archaeon GZfos17G11.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=285394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15353801; DOI=10.1126/science.1100025;
RA   Hallam S.J., Putnam N., Preston C.M., Detter J.C., Rokhsar D.,
RA   Richardson P.M., DeLong E.F.;
RT   "Reverse methanogenesis: testing the hypothesis with environmental
RT   genomics.";
RL   Science 305:1457-1462(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Putnam N., Detter J.C., Richardson P.M., Rokhsar D.;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY714824; AAU82476.1; -; Genomic_DNA.
DR   GO; GO:0016787; F:hydrolase activity; IEA.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR011059; Metal-dep_hydro_comp.
DR   Pfam; PF01979; Amidohydro_1; 1.
SQ   SEQUENCE   462 AA;  52175 MW;  44E101B5EB9B5B27 CRC64;
     MAIQIRNGTV YDPANGIEGE KMDIFVDDGK IVDEIKPDEI IDATDKTVMA GGIDVHSHVA
     TYGLNLARFT FGFPTVGEIG YAYALMGYTH VNEPLMTLNT ASYVHHELSS IPLVDTSALI
     VLSLYDIDKE IREGDKASVK SALPLLLDLT KSIDIKIYDV RVRYAKKGFF YRDIDVTKCL
     KFFYELVEEP KILLRTYPEL LDEDTSVLRG FCMAHIGSGI GDDARYDAAI EILNKGGAVD
     LGIVSPYQDE AVNMRIGYRA ATEKFVSMDI GLEQPLIISE VDEKREGNNK SLRFALDALE
     YLPSSNISFS TDSPSGCLFS SYPKLFTWLL SRRNRKELMP DVEYSLYELA QITRTNPARQ
     LGLENKGHLG IGADADIAIY DMDENTGWRE LEKRLGNCSF LLKDGEAIIR EGKLNKERAR
     KKTFYFVPEV TEKAYESELI ERICNRRSFR AEHLRVDECF LH
//

ID   Q64DN6_9ARCH   PRELIMINARY;   PRT;   510 AA.
AC   Q64DN6;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   30-MAY-2006, entry version 8.
DE   Methyl coenzyme M reductase I subunit alpha.
GN   Name=mcrA; ORFNames=GZ18B6_1;
OS   uncultured archaeon GZfos18B6.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=285363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15353801; DOI=10.1126/science.1100025;
RA   Hallam S.J., Putnam N., Preston C.M., Detter J.C., Rokhsar D.,
RA   Richardson P.M., DeLong E.F.;
RT   "Reverse methanogenesis: testing the hypothesis with environmental
RT   genomics.";
RL   Science 305:1457-1462(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Putnam N., Detter J.C., Richardson P.M., Rokhsar D.;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY714825; AAU82491.1; -; Genomic_DNA.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   InterPro; IPR003183; MCR_alpha_N.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
SQ   SEQUENCE   510 AA;  56185 MW;  9716DE2F2CCC05F5 CRC64;
     MPQGQRFLMP YMMNHTDIMV NADDLHWINN AAMQQCWDDM KRGIVLGLDD AHGLLEARLG
     KEVTPDTISH YMEVLNHALP GGAVIQEHMV ETKPMLVNDS YAKIFTGDDD LADAVDRRFL
     LDINKEFAAG WEKPGEQADQ LKDAIGKKIW QVLWMPTVVG RMTDGGTMFR WVGMQVGMTM
     ISAYKLCAGE SVTGEFAYYA KHAAVVQLSN YMPVKRARAH NEPGGMPLGI NADSVRSNAL
     FPNDPIRNEL ESIAVAAMVY DQLWFGTYMS GGVGFTQYAS ATYTDNILED FCYKGCEIGL
     DYAGGEMASI KGDKLNMDIL EEIIRAENDY ALTQYEAYPT VAESHFGGSV RACCAAAGCG
     SAVACATGLA QPTLSAWSLS QLGHYERKGR LGFFGYDLQD QCTACGSYSY QSDEGMPFEM
     RGVNYPNYAM NVGHQSAYGG LVAGAHCANH DAWVLSPLWK VAFSDRDLPF DRGYVTREYG
     LGANREYTKV AGERDLIIAG YYGREPGAKL
//

ID   Q64C70_9ARCH   PRELIMINARY;   PRT;   561 AA.
AC   Q64C70;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   30-MAY-2006, entry version 8.
DE   Methyl coenzyme M reductase subunit alpha.
GN   Name=mcrA; ORFNames=GZ26B2_4;
OS   uncultured archaeon GZfos26B2.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=285406;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15353801; DOI=10.1126/science.1100025;
RA   Hallam S.J., Putnam N., Preston C.M., Detter J.C., Rokhsar D.,
RA   Richardson P.M., DeLong E.F.;
RT   "Reverse methanogenesis: testing the hypothesis with environmental
RT   genomics.";
RL   Science 305:1457-1462(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Putnam N., Detter J.C., Richardson P.M., Rokhsar D.;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY714839; AAU83007.1; -; Genomic_DNA.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   InterPro; IPR003183; MCR_alpha_N.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
SQ   SEQUENCE   561 AA;  61463 MW;  C30CF6E30A992C71 CRC64;
     MAYKYPSEKI FVEALKAKFA GLDLADQKTR YVRAGFVQNA RKREFQAAGM RVAEQRGIKQ
     YDVNVHLGGM TLGQRQLVPY KLSTQPDIVE GDDLHYVNNP AMQQMWDDMK RTIIVGMDLA
     HETLEKRLGK EVTPESIAGY MEAVNHTMPG AAIVQEHMVE THPGLVDDCY VKMFTGDDEL
     ADEIDSQYVI NINDLFDKEG QNEKIKAAIG KTTWQAIHIP TIVVRCCDGG NTSRWSAMQL
     GMSYIAAYNM CAGEAAVADL AFAAKHAAAV QMAEMLPARR ARSPNEPGGL SFGYCADMVQ
     KMRVKPDDPV LYTLEVVACG TMLYDQIWLG SYMSGGVGFT QYATAAYTND VLDDFTYYGY
     DYALNKFGPD GTAPNDLATA TDLATEVTLN GMECYEDYPT LLEDHFGGSQ RAGILAAASA
     CTTGIATGNA QVALSAWYMS MYVHKEGWGR LGFFGYDLQD QCGATNVCSY QGDEGCCLEL
     RGANYPNYAM NVGHQGEYAG FTGAAHAGAH DAYCCNPLIK VCFADPSLVF DFADIRKEYA
     RGAMRTFRPA GERSLVIPAG V
//

ID   Q64BR7_9ARCH   PRELIMINARY;   PRT;   332 AA.
AC   Q64BR7;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   30-MAY-2006, entry version 9.
DE   Ketol-acid reductoisomerase.
GN   ORFNames=GZ26G2_30;
OS   uncultured archaeon GZfos26G2.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=285389;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15353801; DOI=10.1126/science.1100025;
RA   Hallam S.J., Putnam N., Preston C.M., Detter J.C., Rokhsar D.,
RA   Richardson P.M., DeLong E.F.;
RT   "Reverse methanogenesis: testing the hypothesis with environmental
RT   genomics.";
RL   Science 305:1457-1462(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Putnam N., Detter J.C., Richardson P.M., Rokhsar D.;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY714843; AAU83160.1; -; Genomic_DNA.
DR   GO; GO:0016853; F:isomerase activity; IEA.
DR   GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA.
DR   GO; GO:0009082; P:branched chain family amino acid biosynthesis; IEA.
DR   InterPro; IPR013023; AcH_isomrdctse.
DR   InterPro; IPR000506; AcH_isomrdctse_C.
DR   InterPro; IPR013116; IlvN.
DR   Pfam; PF01450; IlvC; 1.
DR   Pfam; PF07991; IlvN; 1.
DR   TIGRFAMs; TIGR00465; ilvC; 1.
KW   Isomerase.
SQ   SEQUENCE   332 AA;  36857 MW;  D5904ACF0CB78E4D CRC64;
     MEILHDEDVD DSILRDKTIA VMGYGAQGDA QANCLKDSGI NVVIGETEIL GGNKNPSWEK
     AKEDGFEVLP IDKAAEKGDV VHILLPDEVQ PAIYENQIKP QLKAGKALCF SHGFNICFKR
     IVPPEDVDVI MVAPKAPGTE ERKAYLEGFG VPGLVAVKQN PSGEAREVAL AMTKAMHWTK
     AGILECTFEQ ETYEDLFGEQ CVLCGGLVEL MRNGFEVLVE AGYPPEMAYF ECVHEMKLIV
     DLVWQGGIKR MAEVISNTAE YGMWAVGHQI IGPEVKEKMK EALKRVENGE FANEWVDEYK
     RGIPFLKASR EKMGEHQVET VGAEIRKLFA QK
//

ID   Q64BA0_9ARCH   PRELIMINARY;   PRT;   215 AA.
AC   Q64BA0;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   30-MAY-2006, entry version 9.
DE   Tungsten formylmethanofuran dehydrogenase subunit A.
GN   Name=fwdA; ORFNames=GZ27E7_1;
OS   uncultured archaeon GZfos27E7.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=285383;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15353801; DOI=10.1126/science.1100025;
RA   Hallam S.J., Putnam N., Preston C.M., Detter J.C., Rokhsar D.,
RA   Richardson P.M., DeLong E.F.;
RT   "Reverse methanogenesis: testing the hypothesis with environmental
RT   genomics.";
RL   Science 305:1457-1462(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Putnam N., Detter J.C., Richardson P.M., Rokhsar D.;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY714847; AAU83327.1; -; Genomic_DNA.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR011059; Metal-dep_hydro_comp.
DR   Pfam; PF07969; Amidohydro_3; 1.
SQ   SEQUENCE   215 AA;  24158 MW;  23A47E5E6B10C395 CRC64;
     MYSGKSPVNT IQWAIGQELA LLVKDPWKVA LTTDHPNAGP FIGYPIIISM LMSKKRRDES
     AEDMHKVIFD RAIYPSIDRE YDLYEIAIIT RGMAAKALGL HEHGKGHLGV GADGDVAIYD
     MSPEERDAGK IQKAFLNTKY TIKGGQIVVK DGEVVATPDG KTYFVTPECD DTLTDEMMVK
     LKDKFDHYYS VTYNNYAVQD AYVPNPYEIK APWRS
//

ID   Q64AT2_9ARCH   PRELIMINARY;   PRT;   225 AA.
AC   Q64AT2;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   30-MAY-2006, entry version 6.
DE   Hypothetical protein.
GN   ORFNames=GZ29E12_7;
OS   uncultured archaeon GZfos29E12.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=285380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15353801; DOI=10.1126/science.1100025;
RA   Hallam S.J., Putnam N., Preston C.M., Detter J.C., Rokhsar D.,
RA   Richardson P.M., DeLong E.F.;
RT   "Reverse methanogenesis: testing the hypothesis with environmental
RT   genomics.";
RL   Science 305:1457-1462(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Putnam N., Detter J.C., Richardson P.M., Rokhsar D.;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY714851; AAU83495.1; -; Genomic_DNA.
DR   InterPro; IPR013216; Methyltransf_11.
DR   Pfam; PF08241; Methyltransf_11; 1.
KW   Hypothetical protein.
SQ   SEQUENCE   225 AA;  25282 MW;  A3479529FFAFADA0 CRC64;
     MGKIPIFEDG AEEYDKWFDE NPFAYKSEVL ALGKFIPKNS KGLEVGVGTG RFAAPMGIQM
     GVEPARAMAD IARKRGIEVY EAKAEELPFD NESFDFILMA TTICFLQNPM LALQESTRVI
     KSGGYIIIGM IDSDSFLGKA YESKKKDSKF YRYAHFYSVN QVLKWVRKLG YCHIKICQTI
     FKNPGKITAT EPVKDGSGRG GFVVISAQKD VRLDFHPDHV RRSLS
//

ID   Q64AN1_9ARCH   PRELIMINARY;   PRT;   568 AA.
AC   Q64AN1;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   30-MAY-2006, entry version 11.
DE   Adenine deaminase.
GN   Name=adeC; ORFNames=GZ30H9_33;
OS   uncultured archaeon GZfos30H9.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=285372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15353801; DOI=10.1126/science.1100025;
RA   Hallam S.J., Putnam N., Preston C.M., Detter J.C., Rokhsar D.,
RA   Richardson P.M., DeLong E.F.;
RT   "Reverse methanogenesis: testing the hypothesis with environmental
RT   genomics.";
RL   Science 305:1457-1462(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Putnam N., Detter J.C., Richardson P.M., Rokhsar D.;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY714852; AAU83546.1; -; Genomic_DNA.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA.
DR   GO; GO:0016787; F:hydrolase activity; IEA.
DR   GO; GO:0006146; P:adenine catabolism; IEA.
DR   InterPro; IPR006679; Adenine_deam.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR011550; Amidohydro_like.
DR   InterPro; IPR011059; Metal-dep_hydro_comp.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   ProDom; PD001248; Amidohydro_like; 1.
DR   TIGRFAMs; TIGR01178; ade; 1.
SQ   SEQUENCE   568 AA;  62160 MW;  182260FF0D5B4F01 CRC64;
     MTKMNDLVDI ALGNKKADLV LKNVNLVNVC SGEIYETDIA IAHDVIAGLG RYEGRLEIDA
     QDNYAVPGLI DGHTHIEMSM LSVREFAKAV VPRGTTAVVA DPHEIANVLG IAGIRALLDD
     ARTTALKVFC MAPSCVPSTD PSLGLETSGA MIDHTEIRKL LRMDGIIGLA EVMNYVGVIA
     KEEEVWEKIE IAKALKMPID GHAPLLSGKE LNAYVVSGAG SDHENTTYEE SEEKLRLGMR
     VMVREGSVAK NLKNIAPLLR TVDTRNCMLV TDGDRTPLDL KDEGYLDYVL RRAIEEGIDP
     VKAVQMCTIN PAQWFKLDAE IGCIAPGKIA DIVLLKKLDT FEVEKVIVNG KPDFAQRSEY
     SFNYPHYRES VRIMRVKPDE FVIEQEGAIK ARIIGLIEGE LQTEELVEEI SGIEIARDIL
     EICVLERHHY SGNMGLGFVK GFGLKTGAIA STIAHDSHNI VVIGTNEEDM AVACNRLKDI
     GGGIVLCNGE EVTSELKLPI AGLMSDNGLD YVMRKQKEMD DNISEMGCKL PAPFIAISFL
     ALPVIPKLKI TDKGLVDVAK REIVGVFL
//

ID   Q649Z7_9ARCH   PRELIMINARY;   PRT;   449 AA.
AC   Q649Z7;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   30-MAY-2006, entry version 8.
DE   Methyl coenzyme M reductase subunit beta.
GN   Name=mcrB; ORFNames=GZ33H6_29;
OS   uncultured archaeon GZfos33H6.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=285376;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15353801; DOI=10.1126/science.1100025;
RA   Hallam S.J., Putnam N., Preston C.M., Detter J.C., Rokhsar D.,
RA   Richardson P.M., DeLong E.F.;
RT   "Reverse methanogenesis: testing the hypothesis with environmental
RT   genomics.";
RL   Science 305:1457-1462(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Putnam N., Detter J.C., Richardson P.M., Rokhsar D.;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY714858; AAU83780.1; -; Genomic_DNA.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR003179; MCR_beta.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02241; MCR_beta; 1.
DR   Pfam; PF02783; MCR_beta_N; 1.
DR   PIRSF; PIRSF000263; Meth_CoM_rd_beta; 1.
SQ   SEQUENCE   449 AA;  48001 MW;  88711BD50CEBBFB9 CRC64;
     MYSMMCRVSE ISKEEKKNMA DEIDLYDDRG SVLAKGVPLQ AISPLKNAAM RKIVNLTIRT
     GAVDLAGLEK KLKTGAIAGR GMVIRGVAKD LPILDKASTI AGEVEEMLRI ESGDDTEVTL
     MSGEKRMLIQ VPTARILADY SVGLTAAMGA LTHAIIDVCD VSMWDAPYVH AAVWGMYPQN
     PDPADGAVKM LVDIPMKNEG PGFTLRNIPV NHLAATVRKR AIQGAALTMI LEEAAQFEMG
     NCMGPHERGH LLDLAYEGLN ANNLLYNLVK DNGKGTLADV VYGLVEKAKA DGVIKPKKKM
     GSGYVVYEAD DPQLWNAYAS AGLLAAVCVN CGAMRAGQSV PGCIMYYNVL LEHETGMPGV
     DYGMTQGASV SSSFFSHSIY GGGGPGVFYG NHIVTRHPKG QFIPCFCASM CLDADTMYFS
     PARTSALYGE VLGAIPEFAE PMKAVAGAV
//

ID   Q5W1H7_9EURY   PRELIMINARY;   PRT;   156 AA.
AC   Q5W1H7;
DT   07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   07-DEC-2004, sequence version 1.
DT   30-MAY-2006, entry version 8.
DE   Methyl-coenzyme M reductase, subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogenic archaeon.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=198240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Juottonen H., Galand P.E., Tuittila E.S., Laine J., Fritze H.,
RA   Yrjala K.;
RT   "Methanogen communities and Bacteria along an ecohydrological gradient
RT   in a northern raised bog complex.";
RL   Environ. Microbiol. 7:1547-1557(2005).
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DR   EMBL; AJ853818; CAH68737.1; -; Genomic_DNA.
DR   SMR; Q5W1H7; 1-156.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     156    156
SQ   SEQUENCE   156 AA;  16826 MW;  933E29E6D0D3479E CRC64;
     GGVGFTQYAT AAYTNDVLDD FCYYTVDYAN DKYGGFAKAP ATLEVAKDIA TESTLYSAEQ
     YESFPTLLED HFGGSQRASV MAAASGIGAA IASGHSQIGL AGWYLSMLLH KEAWGRLGFF
     GYDLQDQCGP TNVFSYQSDE GNPTELRGAN YPNYAM
//

ID   Q5W1G6_9EURY   PRELIMINARY;   PRT;   155 AA.
AC   Q5W1G6;
DT   07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   07-DEC-2004, sequence version 1.
DT   30-MAY-2006, entry version 8.
DE   Methyl-coenzyme M reductase, subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogenic archaeon.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=198240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Juottonen H., Galand P.E., Tuittila E.S., Laine J., Fritze H.,
RA   Yrjala K.;
RT   "Methanogen communities and Bacteria along an ecohydrological gradient
RT   in a northern raised bog complex.";
RL   Environ. Microbiol. 7:1547-1557(2005).
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DR   EMBL; AJ853829; CAH68748.1; -; Genomic_DNA.
DR   SMR; Q5W1G6; 1-155.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     155    155
SQ   SEQUENCE   155 AA;  16687 MW;  BFF954EC7783321D CRC64;
     GGVGFTQYAT AAYTDNILDD YSYYGNDYAK KYGADGKAPS TMDVVNDLGT EVTLYGIEQY
     EKYPTTLEDH FGGSQRATVL AAASGVTAAI ATGNSNAGLS AWYLSMLLHK DAWGRLGFYG
     YDLQDQCGST NTFSVRSDEG APDELRGANY PNYAM
//

ID   Q5W1G5_9EURY   PRELIMINARY;   PRT;   156 AA.
AC   Q5W1G5;
DT   07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   07-DEC-2004, sequence version 1.
DT   30-MAY-2006, entry version 8.
DE   Methyl-coenzyme M reductase, subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogenic archaeon.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=198240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Juottonen H., Galand P.E., Tuittila E.S., Laine J., Fritze H.,
RA   Yrjala K.;
RT   "Methanogen communities and Bacteria along an ecohydrological gradient
RT   in a northern raised bog complex.";
RL   Environ. Microbiol. 7:1547-1557(2005).
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DR   EMBL; AJ853830; CAH68749.1; -; Genomic_DNA.
DR   SMR; Q5W1G5; 1-156.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     156    156
SQ   SEQUENCE   156 AA;  16861 MW;  01CD98138E827CCC CRC64;
     GGVGFTQYAT AAYTDSILDD YCYYGLDYIK AKHGGLGKAK KTQEVLNDIA TEVTLYGMEQ
     YEQYPTTLES HFGGSQRASV LAAAAGISCA PATANSNAGL NGWYMSMLAH KEGWSRLGFF
     GYDLQDQCGS TNSMSIRPDE GCIGELRGPN YPNYAM
//

ID   Q5W1G4_9EURY   PRELIMINARY;   PRT;   156 AA.
AC   Q5W1G4;
DT   07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   07-DEC-2004, sequence version 1.
DT   30-MAY-2006, entry version 8.
DE   Methyl-coenzyme M reductase, subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogenic archaeon.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=198240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Juottonen H., Galand P.E., Tuittila E.S., Laine J., Fritze H.,
RA   Yrjala K.;
RT   "Methanogen communities and Bacteria along an ecohydrological gradient
RT   in a northern raised bog complex.";
RL   Environ. Microbiol. 7:1547-1557(2005).
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DR   EMBL; AJ853831; CAH68750.1; -; Genomic_DNA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     156    156
SQ   SEQUENCE   156 AA;  16855 MW;  7B44DA99BF5C1A14 CRC64;
     GGVGFTQYAT ATYTDNILDD MCYNIADYVK KKYGGFTKAK VSMDTILDVA TEATEYGLDQ
     YDMYPTLAET HFGGSQRTSV VSASAGVGVS LATGRAQAGV NGWYLSEILH KEIAGRLGFY
     GYDAQDQMGA ANSFAFRGDE GLPMELRGPN YPNYAM
//

ID   Q5TIW9_9EURY   PRELIMINARY;   PRT;   155 AA.
AC   Q5TIW9;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   30-MAY-2006, entry version 7.
DE   Methyl-coenzyme M reductase, subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogenic archaeon.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=198240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Juottonen H., Galand P.E., Tuittila E.S., Laine J., Fritze H.,
RA   Yrjala K.;
RT   "Methanogen communities and Bacteria along an ecohydrological gradient
RT   in a northern raised bog complex.";
RL   Environ. Microbiol. 7:1547-1557(2005).
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DR   EMBL; AJ862825; CAH89321.1; -; Genomic_DNA.
DR   SMR; Q5TIW9; 1-155.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     155    155
SQ   SEQUENCE   155 AA;  16685 MW;  A4EB54EB3E1D9469 CRC64;
     GGVGFTQYAT AAYTDNILDD YAYYGNDYAK KYGADGKAPA TMDVVNDLGT EVTLYGIEQY
     EKYPTTLEDH FGGSQRATVL AAASGVTTAI ATGNSNAGLS AWYLSMLLHK DAWGRLGFYG
     YDLQDQCGST NTFSVRSDEG APDELRGANY PNYAM
//

ID   Q5NVZ6_9ARCH   PRELIMINARY;   PRT;   400 AA.
AC   Q5NVZ6;
DT   04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT   04-JAN-2005, sequence version 1.
DT   30-MAY-2006, entry version 9.
DE   Eukaryotic type DNA primase, small subunit (EC 2.7.7.-).
GN   Name=priA; ORFNames=orf10;
OS   uncultured archaeon.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=115547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16329940; DOI=10.1016/j.femsec.2004.12.004;
RA   Erkel C., Kemnitz D., Kube M., Ricke P., Chin K.-J., Dedysh S.,
RA   Reinhardt R., Conrad R., Liesack W.;
RT   "Retrieval of first genome data for rice cluster I methanogens by a
RT   combination of cultivation and molecular techniques.";
RL   FEMS Microbiol. Ecol. 53:187-204(2005).
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DR   EMBL; CR626857; CAH04810.1; -; Genomic_DNA.
DR   GO; GO:0003896; F:DNA primase activity; IEA.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA.
DR   GO; GO:0016740; F:transferase activity; IEA.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA.
DR   InterPro; IPR002755; DNA_primase_S.
DR   PANTHER; PTHR10536; DNA_primase_S; 1.
DR   Pfam; PF01896; DNA_primase_S; 2.
DR   PIRSF; PIRSF005538; DNA_primase_S; 1.
DR   TIGRFAMs; TIGR00335; primase_sml; 1.
KW   Nucleotidyltransferase; Transferase.
SQ   SEQUENCE   400 AA;  45530 MW;  482EDC1DAB000E66 CRC64;
     MNDQTRAFLR ERFRDYYSRS KVFVPPGLAQ REWGFIFHEE TVGVAMRRHK AFNSEGELAD
     YLRSMPPAHA YHSAAYYRHP QAPTMQEKDW LGADLIFDLD ADHLPGVKNM TYGEMLDNVK
     VEIIRLIDEF LIDDLGFREK DMDIVFSGGR GYHVHVRDER VRTLKSPERR EIVDYLLGTG
     LEPDRMFIRT NQRIDTGTTS VAGVWLIRGF DSVPGGWDRR VARHIVEKLD QIGRLPDKDA
     KEALRAFSLE SKDVKRILHV ARDPASLQKI REKGLIELSG NLEGFFRSIL AGTIDQFKVS
     LAGKTDEPVT ADIKRLIRLP GSIHGGSSFR VTPLTRAQLE SFNPLEDAII FSDDPVRVLV
     TRPAVVEMKG KIYRVSEGVG RLPENVAMFL MCRGSADYEP
//

ID   Q5IEN3_9ARCH   PRELIMINARY;   PRT;   240 AA.
AC   Q5IEN3;
DT   15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2005, sequence version 1.
DT   30-MAY-2006, entry version 7.
DE   Methyl coenzyme-M reductase (Fragment).
GN   Name=mcrA;
OS   uncultured archaeon.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=115547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15746419; DOI=10.1126/science.1102556;
RA   Kelley D.S., Karson J.A., Fruh-Green G.L., Yoerger D.R., Shank T.M.,
RA   Butterfield D.A., Hayes J.M., Schrenk M.O., Olson E.J.,
RA   Proskurowski G., Jakuba M., Bradley A., Larson B., Ludwig K.,
RA   Glickson D., Buckman K., Bradley A.S., Brazelton W.J., Roe K.,
RA   Elend M.J., Delacour A., Bernasconi S.M., Lilley M.D., Baross J.A.,
RA   Summons R.E., Sylva S.P.;
RT   "A serpentinite-hosted ecosystem: the Lost City hydrothermal field.";
RL   Science 307:1428-1434(2005).
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DR   EMBL; AY760635; AAW31860.1; -; Genomic_DNA.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   InterPro; IPR003183; MCR_alpha_N.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
FT   NON_TER       1      1
FT   NON_TER     240    240
SQ   SEQUENCE   240 AA;  25826 MW;  A0C50445B5347CC7 CRC64;
     QIGMSFINAY KMCAGESATR EFAFMAKHAS VVQMANYMPV RRARATSELG GLPLGITCDM
     TRSPALFPND PVRAALESIA DGALLLDQLW FGTYMSGGVG FTQYASATYT DNILEDFCYK
     AEEIAIDMFG DHCAAEPTME NIEKLVRAES EYCLTQYEAY PTVAESHFGG SVRAACQSAG
     AAVAVACATG SADAALNGWA LAQLLHYASV GRLGFYGYDL QDQCTSSTSF SYRSDEGLPF
//

ID   Q5IEN2_9ARCH   PRELIMINARY;   PRT;   242 AA.
AC   Q5IEN2;
DT   15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2005, sequence version 1.
DT   30-MAY-2006, entry version 7.
DE   Methyl coenzyme-M reductase (Fragment).
GN   Name=mcrA;
OS   uncultured archaeon.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=115547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15746419; DOI=10.1126/science.1102556;
RA   Kelley D.S., Karson J.A., Fruh-Green G.L., Yoerger D.R., Shank T.M.,
RA   Butterfield D.A., Hayes J.M., Schrenk M.O., Olson E.J.,
RA   Proskurowski G., Jakuba M., Bradley A., Larson B., Ludwig K.,
RA   Glickson D., Buckman K., Bradley A.S., Brazelton W.J., Roe K.,
RA   Elend M.J., Delacour A., Bernasconi S.M., Lilley M.D., Baross J.A.,
RA   Summons R.E., Sylva S.P.;
RT   "A serpentinite-hosted ecosystem: the Lost City hydrothermal field.";
RL   Science 307:1428-1434(2005).
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DR   EMBL; AY760636; AAW31861.1; -; Genomic_DNA.
DR   SMR; Q5IEN2; 1-234.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   InterPro; IPR003183; MCR_alpha_N.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
FT   NON_TER       1      1
FT   NON_TER     242    242
SQ   SEQUENCE   242 AA;  26091 MW;  87DF2FF18E27E82D CRC64;
     SYSMCAGEAA VADLSYAAKH AGVIQMGDML PARRARSPNE PGGVSFGHLA DIIQTSRVKS
     DDPTKVALEV IGAGCMLYDQ IWLGSYMSGR VGFTQYATAA YTDNILDDNM YYMVDYINEK
     YNGAADKGVD NKVEATLDVV KDIATESTLY GLENYELYPT TLESHFGGSQ RATVLSAAAG
     CSTSLATGNG NAGLSGWYLS MYLHKEAHGR LGFYGYDLQD QCGAANVFSY QSDEDCLLNF
     VV
//

ID   Q5IEM9_9ARCH   PRELIMINARY;   PRT;   242 AA.
AC   Q5IEM9;
DT   15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2005, sequence version 1.
DT   30-MAY-2006, entry version 7.
DE   Methyl coenzyme-M reductase (Fragment).
GN   Name=mcrA;
OS   uncultured archaeon.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=115547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15746419; DOI=10.1126/science.1102556;
RA   Kelley D.S., Karson J.A., Fruh-Green G.L., Yoerger D.R., Shank T.M.,
RA   Butterfield D.A., Hayes J.M., Schrenk M.O., Olson E.J.,
RA   Proskurowski G., Jakuba M., Bradley A., Larson B., Ludwig K.,
RA   Glickson D., Buckman K., Bradley A.S., Brazelton W.J., Roe K.,
RA   Elend M.J., Delacour A., Bernasconi S.M., Lilley M.D., Baross J.A.,
RA   Summons R.E., Sylva S.P.;
RT   "A serpentinite-hosted ecosystem: the Lost City hydrothermal field.";
RL   Science 307:1428-1434(2005).
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DR   EMBL; AY760639; AAW31864.1; -; Genomic_DNA.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   InterPro; IPR003183; MCR_alpha_N.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
FT   NON_TER       1      1
FT   NON_TER     242    242
SQ   SEQUENCE   242 AA;  25984 MW;  26DB7A0FE1509985 CRC64;
     MSFINAYKMC AGESATGEFA FMAKHASVVQ MANYMPVRRA RATNELGGLP LGITCDMTRS
     PALFPNDPVR AALESIAVGA LLLDQLWFGT YMSGGVGFTQ YASATYTDNI LEDFCYKAEE
     IAIDMFGDHC AAEPTMENIE KLVRAESEYC LTQYEAYPTV AESHFGGSVR AACQSAGAAV
     AVACATGSAD AALNGWALAQ LLHYASVGRL GFYGYDLQDQ CTSSTSFSYR SDEGLPFEMR
     GA
//

ID   Q5EGK4_9EURY   PRELIMINARY;   PRT;   256 AA.
AC   Q5EGK4;
DT   15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2005, sequence version 1.
DT   30-MAY-2006, entry version 6.
DE   McrA (Fragment).
GN   Name=mcrA;
OS   uncultured methanogenic archaeon.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=198240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Kormas K.A., Meziti A., Dahlman A., de Lange G., Lykousis V.;
RT   "Molecular fingerprinting of methanogens in eastern Mediterranean Sea
RT   mud volcanoes.";
RL   Geochim. Cosmochim. Acta 69:A77-A77(2005).
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DR   EMBL; AY883171; AAW80300.1; -; Genomic_DNA.
DR   SMR; Q5EGK4; 1-256.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-c...; IEA.
DR   GO; GO:0015948; P:methanogenesis; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   InterPro; IPR003183; MCR_alpha_N.
DR   InterPro; IPR009024; MCR_fer_like.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
FT   NON_TER       1      1
FT   NON_TER     256    256
SQ   SEQUENCE   256 AA;  27697 MW;  37D4C4F5C8AE04C2 CRC64;
     AMQIGMSFIS SYHMCAGEAA VADLAFTAKH AGLVEMSEML PARRARGPNE PGGLSFGHMC
     DIVQTSRKFR DDPCKIALET CAAAMMLYDQ IWLGGYMSGG VGFTQYATSA YTNNTVDDNL
     YADTEYGWDT FGTSIGDCKA PSIDIIRDMG TWGALYGLEL YENYPTALED HFGGSQRATV
     ISTATGAACA ITTGNSNAGL SAWYLSMYLH KEAHGRLGFF GYDLQDQCGA TNVFSYQSDE
     GLLAEMRGAN YPNYAM
//

ID   Q573A6_9ARCH   PRELIMINARY;   PRT;   201 AA.
AC   Q573A6;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   30-MAY-2006, entry version 6.
DE   Methyl-coenzyme M reductase alpha subunit (EC 2.8.4.1) (Fragment).
GN   Name=mcrA;
OS   uncultured archaeon.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=115547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16034418; DOI=10.1038/nature03796;
RA   Webster G., Parkes J., Cragg B.A., Weightman A.J., Newberry C.J.,
RA   Ferdelman T., Kallmeyer J., Jorgensen J., Aiello B.B., Fry J.C.;
RT   "Deep sub-seafloor prokaryotes stimulated at interfaces over
RT   geological time.";
RL   Nature 436:390-394(2005).
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DR   EMBL; AJ867766; CAI30322.1; -; Genomic_DNA.
DR   SMR; Q573A6; 1-197.
DR   GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA.
DR   GO; GO:0016740; F:transferase activity; IEA.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
KW   Transferase.
FT   NON_TER       1      1
FT   NON_TER     201    201
SQ   SEQUENCE   201 AA;  21402 MW;  8D267F2311353444 CRC64;
     VSMGEMLPAR RARGPNEPGG LSFGHLSDII QASRVSKDPA KIALEVVGAG CMLYDQIWLG
     SYMSGGVGFT QYATAAYTDD ILDNNVYYDV DYINDKYNGA ANVGKDNKVK ASLDVVKDIA
     TESTLYGIET YEKFPTALED HFGGSQRATV LAAAAGVACS LATANANAGL SGWYLSMYLH
     KEAWGKLGSF GFDLQDQCGA P
//

ID   Q4U340_9ARCH   PRELIMINARY;   PRT;   613 AA.
AC   Q4U340;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   30-MAY-2006, entry version 5.
DE   Alpha glucosidase (Fragment).
OS   archaeon #33-9.
OC   Archaea.
OX   NCBI_TaxID=328513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=#33-9;
RA   Ng C.C., Shyu Y.T.;
RT   "Thermo-stable protein alpha glucosidase translated from cell-free
RT   expression system from thermophile.";
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; DQ017387; AAY42612.1; -; Genomic_DNA.
DR   GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA.
DR   GO; GO:0005976; P:polysaccharide metabolism; IEA.
DR   InterPro; IPR008928; 6hp_glycosidase.
DR   InterPro; IPR011613; Glyco_hydro_15_rel.
DR   InterPro; IPR012343; Glyco_trans_sub.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
FT   NON_TER       1      1
SQ   SEQUENCE   613 AA;  71334 MW;  32E033F5BF8C4D8B CRC64;
     RMLINFDEKG RIVDIYYPYI GMENQTSGNP IRLAIWDKDK NTISLDEEWE TTVLYLDEAN
     MVEIRSDIRK LGLSLLSYNF LDPDDPIYMS IIKVANNENN NRNIKIFFIH DINLYSNPFG
     DTAFYDPLSL SIVHYKSKRY LAFKVFTTTS IFSEYNVGKG DLIGDIYDGN LGLNGIENGD
     VNSSMGIEAN IDPNSYVNLY YVIVADRNLE DLRQKIRKIN FANVETSFTL TYMFWRNWLK
     KNKLFRNSLM QDIKRVYDVS LFVIRNHMDI NGSIIASSDF SFVKIYGDSY QYCWPRDAAI
     AAYALDLAGY KELALRHFQF ISNIVNSEGF LYHKYNPNTT LASSWHPWFY KGKRIYPIQE
     DETALEVWAI VSHYEKYEDI DEILPLYKKF VKPALKFMMS FMEEGLPKPS FDLWEERYGI
     HIYTVSTVYG ALTKGAKLAY DVGDEILSED LSDTSGLLKG MVLKRMTYNG RFIRRIDEEN
     NQDLTVDSSL YAPFFFGLVD ANDKIMINTI NEIENKLTVN GGVIRYENDM YQRRKKQPNP
     WIITTLWLAE YYATINDKNK ANEYIKWVIN RALPTGFLPE QVDPETFEPT SVTPLVWSHA
     EFIIAINKLL NHI
//

ID   Q4QXS4_9EURY   PRELIMINARY;   PRT;   154 AA.
AC   Q4QXS4;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   30-MAY-2006, entry version 6.
DE   Methyl-coenzyme M reductase subunit A (Fragment).
GN   Name=mcrA;
OS   uncultured methanogenic archaeon.
OC   Archaea; Euryarchaeota; environmental samples.
OX   NCBI_TaxID=198240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16329940; DOI=10.1016/j.femsec.2004.12.004;
RA   Erkel C., Kemnitz D., Kube M., Ricke P., Chin K.-J., Dedysh S.,
RA   Reinhardt R., Conrad R., Liesack W.;
RT   "Retrieval of first genome data for rice cluster I methanogens by a
RT   combination of cultivation and molecular techniques.";
RL   FEMS Microbiol. Ecol. 53:187-204(2005).
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DR   EMBL; AY683452; AAV85896.1; -; Genomic_DNA.
DR   SMR; Q4QXS4; 1-154.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     154    154
SQ   SEQUENCE   154 AA;  16794 MW;  E06374541C3AD2FC CRC64;
     GGVGFTQYAT AAYTDDILDD FCYYGYDYIK GKYGIAKAKP TMDVVNDIGT EVTLYGIEQY
     EKYPTTLEDH FGGSQRATVL SAAAGVTTSL ATGNANAGLS AWYLSMYLHK EAWGRLGFFG
     YDLQDQCGAT NVFSCRSDEG AIDELRGPNY PNYA
//

ID   Q49KC1_9ARCH   PRELIMINARY;   PRT;   176 AA.
AC   Q49KC1;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   30-MAY-2006, entry version 5.
DE   Methyl coenzyme M reductase (Fragment).
GN   Name=mcr;
OS   uncultured archaeon.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=115547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16085853; DOI=10.1128/AEM.71.8.4592-4601.2005;
RA   Dhillon A., Lever M., Lloyd K.G., Albert D.B., Sogin M.L., Teske A.;
RT   "Methanogen diversity evidenced by molecular characterization of
RT   methyl coenzyme M reductase A (mcrA) genes in hydrothermal sediments
RT   of the Guaymas Basin.";
RL   Appl. Environ. Microbiol. 71:4592-4601(2005).
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DR   EMBL; AY837766; AAX46041.1; -; Genomic_DNA.
DR   SMR; Q49KC1; 1-176.
DR   InterPro; IPR008924; MCR_a/b_chain_C.
DR   InterPro; IPR009047; MCR_alpha_C.
DR   Pfam; PF02249; MCR_alpha; 1.
FT   NON_TER       1      1
FT   NON_TER     176    176
SQ   SEQUENCE   176 AA;  19653 MW;  736595D964EAC724 CRC64;
     YDQIWLGSYM SGGVGFTQYA TAAYTDNILD DFTYYGMDYL HDKYKIDWKN PNPKDKVKAT
     QEVVNDIAAE VNLYSMEQYE QFPTMMEDHF GGSQRAAVLG AACGLTTSIA TGNSNAGLNG
     WYLSMLMHKD GWSRLGFFGY DLQDQCGSAN SLSIRPDEGC IGEFRGPNYP NYAMNV
//
