RFTRM_RICTY
ID RFTRM_RICTY Reviewed; 518 AA.
AC Q68VR6;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=RT0836;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU04290.1; -; Genomic_DNA.
DR RefSeq; WP_011191264.1; NC_006142.1.
DR AlphaFoldDB; Q68VR6; -.
DR SMR; Q68VR6; -.
DR STRING; 257363.RT0836; -.
DR EnsemblBacteria; AAU04290; AAU04290; RT0836.
DR KEGG; rty:RT0836; -.
DR eggNOG; COG0220; Bacteria.
DR eggNOG; COG2890; Bacteria.
DR HOGENOM; CLU_018398_3_3_5; -.
DR OMA; DDISENC; -.
DR OrthoDB; 301685at2; -.
DR Proteomes; UP000000604; 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..518
FT /note="Bifunctional methyltransferase"
FT /id="PRO_0000229299"
FT REGION 1..302
FT /note="RF MTase"
FT REGION 1..300
FT /note="HemK"
FT /evidence="ECO:0000250"
FT REGION 301..518
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT /evidence="ECO:0000250"
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; 59700 MW; 0DE0F08E4E220130 CRC64;
MQYSIKQILN NANDKLNKIG INLPELEARI LLQHVTNKPI EHLLIKLNEQ LSEAEIEAFE
KLLERRLEHE PIAYITGIKE FYSREFIVNK HVLIPRIDTE ILIDVVIGLV VSRNDLNTCS
KLKSLDSVKT IQHYNILELG TGSGCIAISL LCELPNTSVI ATDISVDAIK VAKSNTIKHN
VTDRIQIIHS NWFEKLNKQK FDLIVSNPPY ISHSEKLEMA IETINYEPHI ALFAEEDGLE
AYSIIAKNAK QFLKPNGKII LEIGFSQAEK VCQIFLNYGY NIDHIYQDLQ SHNRVIEISP
INLNRSYARR IGKSLSKMQQ KLLDNELPKY LFSKEKFASE KRKIFLEIGF GMGEHFINQA
KINPDTLFIG VEVYLNGVAN VLKHAAQHNI MNFLLFPNNL DLILNDLPNN SLDGIYILFP
DPWIKNKKKK KRILNKERLN ILQNKLKNNG NLVFASDIEN YFYETITLIR QNGNFEIIHN
DDYLKPHDNY IITKYHQKAI NENRTAKFMI LQHALTGH
