RFTRM_RICFE
ID RFTRM_RICFE Reviewed; 527 AA.
AC Q4UJU4;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Bifunctional methyltransferase;
DE Includes:
DE RecName: Full=Release factor glutamine methyltransferase;
DE Short=RF MTase;
DE EC=2.1.1.297;
DE AltName: Full=N5-glutamine methyltransferase PrmC;
DE AltName: Full=Protein-(glutamine-N5) MTase PrmC;
DE AltName: Full=Protein-glutamine N-methyltransferase PrmC;
DE Includes:
DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase;
DE EC=2.1.1.33;
DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase;
DE AltName: Full=tRNA(m7G46)-methyltransferase;
GN Name=prmC/trmB; Synonyms=hemK; OrderedLocusNames=RF_1344;
OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=315456;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1525 / URRWXCal2;
RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA Parinello H., Claverie J.-M., Raoult D.;
RT "The genome sequence of Rickettsia felis identifies the first putative
RT conjugative plasmid in an obligate intracellular parasite.";
RL PLoS Biol. 3:1-12(2005).
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:0000250}.
CC -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46
CC (m7G46) in tRNA. {ECO:0000250}.
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;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-
CC methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42708, Rhea:RHEA-COMP:10188, Rhea:RHEA-COMP:10189,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; EC=2.1.1.33;
CC -!- SIMILARITY: In the C-terminal section; belongs to the class I-like SAM-
CC binding methyltransferase superfamily. TrmB family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the protein N5-
CC glutamine methyltransferase family. PrmC subfamily. {ECO:0000305}.
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DR EMBL; CP000053; AAY62195.1; -; Genomic_DNA.
DR RefSeq; WP_011271644.1; NC_007109.1.
DR AlphaFoldDB; Q4UJU4; -.
DR SMR; Q4UJU4; -.
DR STRING; 315456.RF_1344; -.
DR EnsemblBacteria; AAY62195; AAY62195; RF_1344.
DR KEGG; rfe:RF_1344; -.
DR eggNOG; COG0220; Bacteria.
DR eggNOG; COG2890; Bacteria.
DR HOGENOM; CLU_018398_3_3_5; -.
DR OMA; DDISENC; -.
DR OrthoDB; 301685at2; -.
DR Proteomes; UP000008548; 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:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0018364; P:peptidyl-glutamine methylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 2.
DR HAMAP; MF_02126; RF_methyltr_PrmC; 1.
DR HAMAP; MF_01057; tRNA_methyltr_TrmB; 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 InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR Pfam; PF02390; Methyltransf_4; 1.
DR Pfam; PF05175; MTS; 1.
DR Pfam; PF17827; PrmC_N; 1.
DR SUPFAM; SSF53335; SSF53335; 2.
DR TIGRFAMs; TIGR00536; hemK_fam; 1.
DR TIGRFAMs; TIGR03534; RF_mod_PrmC; 1.
DR TIGRFAMs; TIGR00091; TIGR00091; 1.
DR PROSITE; PS51625; SAM_MT_TRMB; 1.
PE 3: Inferred from homology;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..527
FT /note="Bifunctional methyltransferase"
FT /id="PRO_0000229298"
FT REGION 1..311
FT /note="RF MTase"
FT REGION 1..309
FT /note="HemK"
FT REGION 310..527
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT REGION 314..527
FT /note="tRNA MTase"
FT ACT_SITE 430
FT /evidence="ECO:0000250"
FT BINDING 149..153
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 216..219
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 381
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 408
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 434
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 466
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 527 AA; 60400 MW; 33F7BD26BBCC46E3 CRC64;
MQYSIKQVLS KASDKLNKIG ISSSQLEARI LLRYVINKPI EYLLINLDEQ LNEVEIEAFE
KLLERRLKHE PIAYIIGIKE FYSREFIVNK HVLIPRADTE VLVDVCVHKS SLRATKRSVA
ISGILSKIAS STPMASSRND EYTKILELGT GSGCIAISLL CELPNARVVA TDISLDAIEV
ARNNALKYHV TDRIQIIHSN WFENLGKQKF DVIVSNPPYI STDEKPEMAL ETLNHEPYIA
LFAEEDGLQA YRIIAENAKK FLKPNGKIVL EIGFKQEEAV TQIFLSNGYN IESVYKDLQG
HSRVILFSPI NLNRSYARRI GKSLSGLQQN LLDNELPKYL FSKEKLIDEK RKIFLEIGFG
MGEHFINQAK MNPDALFIGV EVYLNGVANV LKLASEQNIT NFLLFPNNLD FILNDLPNNS
LDGIYILFPD PWIKNKQKKK RIFNKERLKI LQDKLKDNGN LVFASDIENY FYEAIELIEQ
NSNFKIMNKN NYLKPHDNYV ITKYHQKAIK ANRIPRFIIL QHVSGDH
