ID I0JTR8_9EURY Unreviewed; 157 AA.
AC I0JTR8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 22-FEB-2023, entry version 13.
DE SubName: Full=Methyl coenzyme M reductase alpha subunit {ECO:0000313|EMBL:CCG47735.1};
DE Flags: Fragment;
GN Name=mcrA {ECO:0000313|EMBL:CCG47735.1};
OS uncultured methanogenic archaeon.
OC Archaea; Euryarchaeota; environmental samples.
OX NCBI_TaxID=198240 {ECO:0000313|EMBL:CCG47735.1};
RN [1] {ECO:0000313|EMBL:CCG47735.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22492456; DOI=10.1128/AEM.00133-12;
RA Franchini A.G., Zeyer J.;
RT "Freeze-coring method for characterization of microbial community structure
RT and function in wetland soils at high spatial resolution.";
RL Appl. Environ. Microbiol. 78:4501-4504(2012).
RN [2] {ECO:0000313|EMBL:CCG47735.1}
RP NUCLEOTIDE SEQUENCE.
RA Franchini A.;
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; HE774286; CCG47735.1; -; Genomic_DNA.
DR AlphaFoldDB; I0JTR8; -.
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..117
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:CCG47735.1"
FT NON_TER 157
FT /evidence="ECO:0000313|EMBL:CCG47735.1"
SQ SEQUENCE 157 AA; 17133 MW; 2AD122434844C028 CRC64;
GGVGFTQYAT AAYTDNILED YTYWAADLIK TKYGGLCKSK PTMELVNKLG TEINSYALEQ
YERYPAAMES HFGGSQRATV AAAATGIGVA VATANANAGV NAWYLSMLQH RERLGRLGFY
GYDLQDMCGA SNSLSYRSDE GLPHELRGPN YPNYAMN
//
