ID I2ECQ1_9EURY Unreviewed; 166 AA.
AC I2ECQ1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 22-FEB-2023, entry version 14.
DE SubName: Full=Methyl-coenzyme M reductase subunit A {ECO:0000313|EMBL:AFJ97448.1};
DE EC=2.8.4.1 {ECO:0000313|EMBL:AFJ97448.1};
DE Flags: Fragment;
GN Name=mcrA {ECO:0000313|EMBL:AFJ97448.1};
OS uncultured methanogenic archaeon.
OC Archaea; Euryarchaeota; environmental samples.
OX NCBI_TaxID=198240 {ECO:0000313|EMBL:AFJ97448.1};
RN [1] {ECO:0000313|EMBL:AFJ97448.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23584407; DOI=10.1016/j.biortech.2013.03.101;
RA Ma J., Zhao B., Frear C., Zhao Q., Yu L., Li X., Chen S.;
RT "Methanosarcina domination in anaerobic sequencing batch reactor at short
RT hydraulic retention time.";
RL Bioresour. Technol. 137:41-50(2013).
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DR EMBL; JQ697443; AFJ97448.1; -; Genomic_DNA.
DR AlphaFoldDB; I2ECQ1; -.
DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:UniProtKB-EC.
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;
KW Transferase {ECO:0000313|EMBL:AFJ97448.1}.
FT DOMAIN 1..124
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:AFJ97448.1"
FT NON_TER 166
FT /evidence="ECO:0000313|EMBL:AFJ97448.1"
SQ SEQUENCE 166 AA; 18397 MW; B220D1242DE45637 CRC64;
GGVGFTQYAT AAYTDNILDE FTYYGMDYLK DKYKIDYKAV DPAQKVKPTQ EIVNDIASEV
TLNAMEQYEQ FPTMMEDHFG GSQRAGVIAA ASGLSVGVAT ANSNAGLNAW YLSMLMHKEG
WSRLGFFGYD LQDQCGSTNS LSVRPDEGCI GEYRGPNYPN YRMKIT
//