ID   Y928_METJA              Reviewed;         197 AA.
AC   Q58338;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Putative protein N5-glutamine methyltransferase MJ0928 {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000305};
DE   AltName: Full=M.MjaHemkP;
GN   OrderedLocusNames=MJ0928;
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: Putative protein methyltransferase using S-adenosyl-L-
CC       methionine as the methyl donor. May methylate a Gln residue in target
CC       proteins (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutaminyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC         N(5)-methyl-L-glutaminyl-[protein] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:57452, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14895,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30011, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61891; Evidence={ECO:0000305};
CC   -!- SIMILARITY: Belongs to the eukaryotic/archaeal PrmC-related family.
CC       {ECO:0000305}.
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; L77117; AAB98930.1; -; Genomic_DNA.
DR   PIR; H64415; H64415.
DR   RefSeq; WP_010870442.1; NC_000909.1.
DR   AlphaFoldDB; Q58338; -.
DR   SMR; Q58338; -.
DR   STRING; 243232.MJ_0928; -.
DR   EnsemblBacteria; AAB98930; AAB98930; MJ_0928.
DR   GeneID; 1451817; -.
DR   KEGG; mja:MJ_0928; -.
DR   eggNOG; arCOG00109; Archaea.
DR   HOGENOM; CLU_018398_6_2_2; -.
DR   InParanoid; Q58338; -.
DR   OMA; EWDDWME; -.
DR   OrthoDB; 72076at2157; -.
DR   PhylomeDB; Q58338; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0035657; C:eRF1 methyltransferase complex; IBA:GO_Central.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008276; F:protein methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR004557; PrmC-related.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   Pfam; PF05175; MTS; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00537; hemK_rel_arch; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..197
FT                   /note="Putative protein N5-glutamine methyltransferase
FT                   MJ0928"
FT                   /id="PRO_0000157177"
FT   BINDING         42..46
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         64
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         105..108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   197 AA;  22057 MW;  2AE2377FE86EB217 CRC64;
     MIIEIEGIKL KLHPEVYEPA EDSILLLKNL VDVKNKDVLE IGVGTGLISI ACAKKGAKKI
     VGVDINPYAV KLAKENAKLN NVNISFFESD LFENVTGKFD VILFNPPYLP TSEDEKIDSY
     LNFAFDGGKD GREILDRFIY ELPNYLKKGG VVQILQSSLT GEKETINKLK PLGFKVEISA
     RLKVPFEELM VINAWRL