RFTRM_RICPR
ID RFTRM_RICPR Reviewed; 518 AA.
AC Q9ZCB3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=M.RprHemKP;
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=RP847;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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; AJ235273; CAA15271.1; -; Genomic_DNA.
DR PIR; G71646; G71646.
DR RefSeq; NP_221195.1; NC_000963.1.
DR RefSeq; WP_004599678.1; NC_000963.1.
DR AlphaFoldDB; Q9ZCB3; -.
DR SMR; Q9ZCB3; -.
DR STRING; 272947.RP847; -.
DR EnsemblBacteria; CAA15271; CAA15271; CAA15271.
DR GeneID; 57569970; -.
DR KEGG; rpr:RP847; -.
DR PATRIC; fig|272947.5.peg.885; -.
DR eggNOG; COG0220; Bacteria.
DR eggNOG; COG2890; Bacteria.
DR HOGENOM; CLU_018398_3_3_5; -.
DR OMA; DDISENC; -.
DR Proteomes; UP000002480; 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; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..518
FT /note="Bifunctional methyltransferase"
FT /id="PRO_0000157174"
FT REGION 1..302
FT /note="RF MTase"
FT REGION 1..300
FT /note="HemK"
FT REGION 301..518
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT REGION 305..518
FT /note="tRNA MTase"
FT ACT_SITE 421
FT /evidence="ECO:0000250"
FT BINDING 140..144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 207..210
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 372
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 399
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 421
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 457
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 518 AA; 59564 MW; C66BB8DB273704A1 CRC64;
MQYSIKQILS NANDKLNKIG INLPGLEARI LLQHVTNKPI EHLLIKLNEQ LSEAEIEAFE
KLLERRLAHE PIAYIIGVKE FYSREFIVNK HVLIPRIDTE VLVDVVIGLV VSRNNLHMFS
KLKSLDSVLT TQSYNILELG TGSGCIAISL LCELPNTNII ATDISVDAIK VAKSNSIKYN
VTDRIQIIHS NWFEKLDKQK FDFIVSNPPY ISHTEKLKMA IETINYEPSI ALFAEEDGLE
AYSIIAKNAK QFLKPNGKII LEIGFSQAAK VSKIFLNYGY NIDYIYRDLQ SHNRVIEISP
INLNRSYARR IGKSLSKMQQ KLLDNELPKY LFSKEKFKSE KRKVFLEIGF GMGEHLINQA
KINPDTLFIG VEVYLNGVAN VLKHSAQHNI TNFLLFPNNL DLILNDLPNN SLDGIYILFP
DPWIKNKKKK KRIFNKERLK ILQNKLKNNG NLVFASDIEN YFYEAMALIR QNGNFEIIHN
DDYLQPHDNY IITKYHQKAI NANRTAKFMI LQHALTDH
