ID G4WLH1_9EURY Unreviewed; 150 AA.
AC G4WLH1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 22-FEB-2023, entry version 15.
DE SubName: Full=Methyl coenzyme reductase subunit A {ECO:0000313|EMBL:AEP93559.1};
DE Flags: Fragment;
GN Name=mcrA {ECO:0000313|EMBL:AEP93559.1};
OS uncultured methanogenic archaeon.
OC Archaea; Euryarchaeota; environmental samples.
OX NCBI_TaxID=198240 {ECO:0000313|EMBL:AEP93559.1};
RN [1] {ECO:0000313|EMBL:AEP93559.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22869718; DOI=10.1073/pnas.1206632109;
RA Ver Eecke H.C., Butterfield D.A., Huber J.A., Lilley M.D., Olson E.J.,
RA Roe K.K., Evans L.J., Merkel A.Y., Cantin H.V., Holden J.F.;
RT "Hydrogen-limited growth of hyperthermophilic methanogens at deep-sea
RT hydrothermal vents.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:13674-13679(2012).
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DR EMBL; HQ635529; AEP93559.1; -; Genomic_DNA.
DR AlphaFoldDB; G4WLH1; -.
DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:InterPro.
DR GO; GO:0015948; P:methanogenesis; IEA:InterPro.
DR Gene3D; 1.20.840.10; Methyl-coenzyme M reductase, alpha/beta subunit, C-terminal; 1.
DR InterPro; IPR008924; Me_CoM_Rdtase_asu/bsu_C.
DR InterPro; IPR009047; Me_CoM_Rdtase_asu_C.
DR Pfam; PF02249; MCR_alpha; 1.
DR SUPFAM; SSF48081; Methyl-coenzyme M reductase alpha and beta chain C-terminal domain; 1.
PE 4: Predicted;
FT DOMAIN 1..115
FT /note="Methyl-coenzyme M reductase alpha subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02249"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEP93559.1"
FT NON_TER 150
FT /evidence="ECO:0000313|EMBL:AEP93559.1"
SQ SEQUENCE 150 AA; 16046 MW; DD962CCA714A95BA CRC64;
GFTQYATAAY TNDIVDDDLY WGAEYAKDKY GAIPGNAPAN IDTVKDISTE TTLYSLESYE
KYPTTLEDHF GGSQRATVVA IAAGGATALA TGHSNAGLSA WYLSMYLHKE AHGRLGFYGY
DLQDQCGATN VFSVASDEGC VGELRGANYP
//
