(data stored in SCRATCH9089 zone)

SWISSPROT: PRMC_PASMU

ID   PRMC_PASMU              Reviewed;         298 AA.
AC   Q9CN82;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 112.
DE   RecName: Full=Release factor glutamine methyltransferase {ECO:0000255|HAMAP-Rule:MF_02126};
DE            Short=RF MTase {ECO:0000255|HAMAP-Rule:MF_02126};
DE            EC=2.1.1.297 {ECO:0000255|HAMAP-Rule:MF_02126};
DE   AltName: Full=M.PmuHemKP;
DE   AltName: Full=N5-glutamine methyltransferase PrmC {ECO:0000255|HAMAP-Rule:MF_02126};
DE   AltName: Full=Protein-(glutamine-N5) MTase PrmC {ECO:0000255|HAMAP-Rule:MF_02126};
DE   AltName: Full=Protein-glutamine N-methyltransferase PrmC {ECO:0000255|HAMAP-Rule:MF_02126};
GN   Name=prmC {ECO:0000255|HAMAP-Rule:MF_02126}; Synonyms=hemK;
GN   OrderedLocusNames=PM0556;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Methylates the class 1 translation termination release
CC       factors RF1/PrfA and RF2/PrfB on the glutamine residue of the
CC       universally conserved GGQ motif. {ECO:0000255|HAMAP-Rule:MF_02126}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-
CC         methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release
CC         factor] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42896, Rhea:RHEA-
CC         COMP:10271, Rhea:RHEA-COMP:10272, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:61891; EC=2.1.1.297; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02126};
CC   -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC       family. PrmC subfamily. {ECO:0000255|HAMAP-Rule:MF_02126}.
DR   EMBL; AE004439; AAK02640.1; -; Genomic_DNA.
DR   RefSeq; WP_010906722.1; NC_002663.1.
DR   SMR; Q9CN82; -.
DR   PRIDE; Q9CN82; -.
DR   EnsemblBacteria; AAK02640; AAK02640; PM0556.
DR   KEGG; pmu:PM0556; -.
DR   PATRIC; fig|272843.6.peg.563; -.
DR   eggNOG; ENOG4105EQY; Bacteria.
DR   eggNOG; COG2890; LUCA.
DR   HOGENOM; HOG000076274; -.
DR   KO; K02493; -.
DR   OMA; HVLIPRP; -.
DR   BioCyc; PMUL272843:G1FZ8-587-MONOMER; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0102559; F:protein-(glutamine-N5) methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0018364; P:peptidyl-glutamine methylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02126; RF_methyltr_PrmC; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR004556; HemK-like.
DR   InterPro; IPR025714; Methyltranfer_dom.
DR   InterPro; IPR040758; PrmC_N.
DR   InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF13847; Methyltransf_31; 1.
DR   Pfam; PF17827; PrmC_N; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00536; hemK_fam; 1.
DR   TIGRFAMs; TIGR03534; RF_mod_PrmC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q9CN82.
DR   SWISS-2DPAGE; Q9CN82.
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..298
FT                   /note="Release factor glutamine methyltransferase"
FT                   /id="PRO_0000157167"
FT   REGION          131..135
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT   REGION          205..208
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT   BINDING         162
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT   BINDING         189
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT   BINDING         205
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
SQ   SEQUENCE   298 AA;  33428 MW;  07624CC6EA2CC2D8 CRC64;
     MTYQEWRQFA EHVLMKNKEN DPFLDVKSES VLLLQTVTKR SKASILAFSE TVLTEVELQQ
     LAQLLMRRAK GEPIAYILGE KAFWSLSLKV SEHTLIPRPD TEVLVEHALD FAKQRVTSAH
     VSGELSILDL GTGTGAIALA LAAELTPLTQ KCGINLNILG VDRIAEAVAL AKDNAKQNEL
     KVNFLQSVWF DALNPEIRFD LIVSNPPYID KNDPHLTQGD VRFEPLSALV AAEEGYADIR
     HIIEQAPLFL KPQGALLLEH GWQQAEKVRS IFQKNLWHNV ATLKDYSGNE RVTLGCWR
//

If you have problems or comments...

PBIL Back to PBIL home page