ID   MCRAM_METJA             Reviewed;         415 AA.
AC   Q58251;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=[Methyl-coenzyme M reductase subunit alpha]-arginine C-methyltransferase {ECO:0000250|UniProtKB:Q8THG6};
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q8THG6};
GN   OrderedLocusNames=MJ0841;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- FUNCTION: Radical SAM methyltransferase that is responsible for the
CC       C(5)-methylation of 'Arg-274' of the methyl-coenzyme M reductase (MCR)
CC       subunit alpha McrA. This post-translational methylation, despite being
CC       not essential in vivo, plays a role for the stability and structural
CC       integrity of MCR. {ECO:0000250|UniProtKB:Q8THG6}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:Q8THG6};
CC       Note=Binds at least 1 [4Fe-4S] cluster. This cluster is coordinated
CC       with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000250|UniProtKB:Q8THG6};
CC   -!- PATHWAY: Protein modification. {ECO:0000250|UniProtKB:Q8THG6}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. MCR alpha subunit
CC       C-methyltransferase family. {ECO:0000305}.
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DR   EMBL; L77117; AAB98846.1; -; Genomic_DNA.
DR   PIR; A64405; A64405.
DR   RefSeq; WP_010870355.1; NC_000909.1.
DR   AlphaFoldDB; Q58251; -.
DR   STRING; 243232.MJ_0841; -.
DR   DNASU; 1451729; -.
DR   EnsemblBacteria; AAB98846; AAB98846; MJ_0841.
DR   GeneID; 1451729; -.
DR   KEGG; mja:MJ_0841; -.
DR   eggNOG; arCOG00950; Archaea.
DR   HOGENOM; CLU_668380_0_0_2; -.
DR   InParanoid; Q58251; -.
DR   OMA; IHLGYTS; -.
DR   OrthoDB; 21265at2157; -.
DR   PhylomeDB; Q58251; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR017672; MA_4551-like.
DR   InterPro; IPR007197; rSAM.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   TIGRFAMs; TIGR03278; methan_mark_10; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..415
FT                   /note="[Methyl-coenzyme M reductase subunit alpha]-arginine
FT                   C-methyltransferase"
FT                   /id="PRO_0000107078"
FT   DOMAIN          2..256
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         18
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:Q8THG6"
FT   BINDING         22
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:Q8THG6"
FT   BINDING         25
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:Q8THG6"
SQ   SEQUENCE   415 AA;  46721 MW;  0F67E63793A587F1 CRC64;
     MKEANLLIDL RGEPGINCNG FCKFCYFRKV NKNNPQPFGC RYCQFTVGCD YCMYSVREIN
     GDFIPLPFAL MELQSSLLFK RYSKVNLTAG GDVSCYPQLE ELCKAINNIG LKIHLGYTSG
     KGFDNVEIAK NLVDYGVDEV TFSVFSTNPK LRKEWMNDKN AETALKCLRY FCENCEVHCA
     IIVIPGVNDG EELKKTVSDL VDWGANAVIL MRFANSEEQG LILGNAPLIE GIKPHSVEEF
     KNIVDEIHNE FGDYIRVTGT PLHDPVAGTP FALAKEENSH ILERLKDKIN GEATIITGNV
     AYPFLKKIFD ETSVNVVKVN KDIADLITAK DLEKLDLKDV KETVFIPPKA FVHDRVAEEI
     LRRDGVDRIV VRGVEQLTLD GEVSGIYTRE EALKFEIEAF EELIGMINFF GMKKQ