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Y1784_ARCFU
ID   Y1784_ARCFU             Reviewed;         177 AA.
AC   O28490;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Putative protein N5-glutamine methyltransferase AF_1784 {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000305};
DE   AltName: Full=M.AfuHemKP;
GN   OrderedLocusNames=AF_1784;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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}.
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DR   EMBL; AE000782; AAB89463.1; -; Genomic_DNA.
DR   PIR; G69472; G69472.
DR   RefSeq; WP_010879280.1; NC_000917.1.
DR   AlphaFoldDB; O28490; -.
DR   SMR; O28490; -.
DR   STRING; 224325.AF_1784; -.
DR   EnsemblBacteria; AAB89463; AAB89463; AF_1784.
DR   GeneID; 24795527; -.
DR   KEGG; afu:AF_1784; -.
DR   eggNOG; arCOG00109; Archaea.
DR   HOGENOM; CLU_018398_6_2_2; -.
DR   OMA; EWDDWME; -.
DR   OrthoDB; 72076at2157; -.
DR   PhylomeDB; O28490; -.
DR   Proteomes; UP000002199; Chromosome.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProt.
DR   GO; GO:0044260; P:cellular macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0043412; P:macromolecule modification; IEA:UniProt.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
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..177
FT                   /note="Putative protein N5-glutamine methyltransferase
FT                   AF_1784"
FT                   /id="PRO_0000157175"
FT   BINDING         30..34
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         86..89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   177 AA;  20041 MW;  12143379B026BD81 CRC64;
     MIYEPAEDSE LLLEAALREL KPDDEVIEVG AGSGFVAERL KGKCKCILTT DISPFAAMEL
     RRKGLDVVMT DIAKGIRKKF SLVLFNPPYV ELEDELRRGD WLDVAIDGGK KGVKVIKKFL
     DSLDEIMAER GRAILIASSQ NEPDVFDLID ERGFRYEIVG ERGLFFEKLF AIKIWKE
 
 
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