PRMC_RHILO
ID PRMC_RHILO Reviewed; 290 AA.
AC Q98G94;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 1.
DT 03-AUG-2022, 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.MloHemKP;
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=mll3434;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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}.
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DR EMBL; BA000012; BAB50322.1; -; Genomic_DNA.
DR RefSeq; WP_010911668.1; NC_002678.2.
DR AlphaFoldDB; Q98G94; -.
DR SMR; Q98G94; -.
DR STRING; 266835.14023717; -.
DR EnsemblBacteria; BAB50322; BAB50322; BAB50322.
DR KEGG; mlo:mll3434; -.
DR PATRIC; fig|266835.9.peg.2732; -.
DR eggNOG; COG2890; Bacteria.
DR HOGENOM; CLU_018398_3_1_5; -.
DR OMA; FDARYWE; -.
DR OrthoDB; 1816476at2; -.
DR Proteomes; UP000000552; 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 Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_02126; RF_methyltr_PrmC; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004556; HemK-like.
DR InterPro; IPR040758; PrmC_N.
DR InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR Pfam; PF05175; MTS; 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;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..290
FT /note="Release factor glutamine methyltransferase"
FT /id="PRO_0000157168"
FT BINDING 130..134
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT BINDING 153
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT BINDING 182
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT BINDING 196..199
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
FT BINDING 196
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02126"
SQ SEQUENCE 290 AA; 30689 MW; C0DCE5E1B330EB14 CRC64;
MADPLPEALG PLLREARARL VAAGVGDPAL DARLIVEHFS GTTRTQAIAD PERTIDSNAI
AAIDAALGRR AGGEPVHRIL GYREFYGLRL SLSPETLEPR PDTETLVEAV LPFVKAMAAR
EGTCRILDLG TGTGAIALAL LSAVPAATAT GVDISAGALA TAARNAGELG LGGRFTTVQS
DWFEKVSGRY HVIAANPPYI PTRDIGNLQD EVRDFDPRLA LDGGVDGLNP YRIIAAEAAR
FLEAESRIAV EIGHTQRDEV TDIFKAAGYA SVAALRDLGG NDRVLVFQWG
