ID   MCRD_METFE              Reviewed;         131 AA.
AC   P12974;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Methyl-coenzyme M reductase operon protein D;
GN   Name=mcrD;
OS   Methanothermus fervidus.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanothermaceae; Methanothermus.
OX   NCBI_TaxID=2180;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3170483; DOI=10.1128/jb.170.10.4718-4726.1988;
RA   Weil C.F., Cram D.S., Sherf B.A., Reeve J.N.;
RT   "Structure and comparative analysis of the genes encoding component C of
RT   methyl coenzyme M reductase in the extremely thermophilic archaebacterium
RT   Methanothermus fervidus.";
RL   J. Bacteriol. 170:4718-4726(1988).
CC   -!- SUBUNIT: MCR is composed of three subunits: alpha, beta, and gamma. The
CC       function of proteins C and D is not known.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; J03375; AAA72194.1; -; Genomic_DNA.
DR   AlphaFoldDB; P12974; -.
DR   SMR; P12974; -.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR003901; Me_CoM_Rdtase_D.
DR   Pfam; PF02505; MCR_D; 1.
DR   PIRSF; PIRSF005636; McrD; 1.
DR   TIGRFAMs; TIGR03260; met_CoM_red_D; 1.
PE   4: Predicted;
KW   Methanogenesis.
FT   CHAIN           1..131
FT                   /note="Methyl-coenzyme M reductase operon protein D"
FT                   /id="PRO_0000147492"
SQ   SEQUENCE   131 AA;  15086 MW;  B7C6F746AB0C98AF CRC64;
     MDVEIFPHRL LSAETTEKLL NKLGEIEGIK RMIIQGQRLP AGEHPDRRVI NVKGQDIELK
     VKTGRIFVEI EDKKTMEKIK EVCDEVFPFK YELIPGTFFR RQKTVTDAIK FGKDVDKLPT
     ELVGMTDTVL D