ID A2TI01_9EURY Unreviewed; 157 AA.
AC A2TI01;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 22-FEB-2023, entry version 22.
DE SubName: Full=Methyl-coenzyme M reductase {ECO:0000313|EMBL:ABM91127.1};
DE Flags: Fragment;
GN Name=mcrA {ECO:0000313|EMBL:ABM91127.1};
OS uncultured euryarchaeote.
OC Archaea; Euryarchaeota; environmental samples.
OX NCBI_TaxID=114243 {ECO:0000313|EMBL:ABM91127.1};
RN [1] {ECO:0000313|EMBL:ABM91127.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18177370; DOI=10.1111/j.1462-2920.2007.01459.x;
RA Smith J.M., Green S.J., Kelley C.A., Prufert-Bebout L., Bebout B.M.;
RT "Shifts in methanogen community structure and function associated with
RT long-term manipulation of sulfate and salinity in a hypersaline microbial
RT mat.";
RL Environ. Microbiol. 10:386-394(2008).
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DR EMBL; EF202621; ABM91127.1; -; Genomic_DNA.
DR AlphaFoldDB; A2TI01; -.
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..119
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:ABM91127.1"
FT NON_TER 157
FT /evidence="ECO:0000313|EMBL:ABM91127.1"
SQ SEQUENCE 157 AA; 17090 MW; 903223F609155991 CRC64;
FTQYATAAYC NNILDDNLYY DVDYINDKYD GAANKGTDNK VKADLDVVKD IATESTIYGL
ENYEKYPTTL EDHFGGPQRA TSLSAAAGSA VAIATGNGNA GLSGWYLCMY LHKEALGRLG
FFGYDLQDQC GATNVLSYQS DEGLALELRG PNYPNYA
//
