RFTRM_RICCN
ID RFTRM_RICCN Reviewed; 524 AA.
AC Q92G13;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
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.RcoHemKP;
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=RC1314;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(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: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; AE006914; AAL03852.1; -; Genomic_DNA.
DR PIR; B97864; B97864.
DR RefSeq; WP_010977871.1; NC_003103.1.
DR AlphaFoldDB; Q92G13; -.
DR SMR; Q92G13; -.
DR EnsemblBacteria; AAL03852; AAL03852; RC1314.
DR KEGG; rco:RC1314; -.
DR HOGENOM; CLU_018398_3_3_5; -.
DR OMA; DDISENC; -.
DR Proteomes; UP000000816; 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..524
FT /note="Bifunctional methyltransferase"
FT /id="PRO_0000157173"
FT REGION 1..308
FT /note="RF MTase"
FT REGION 1..306
FT /note="HemK"
FT REGION 307..524
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT REGION 311..524
FT /note="tRNA MTase"
FT ACT_SITE 427
FT /evidence="ECO:0000250"
FT BINDING 146..150
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 213..216
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 427
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 524 AA; 60079 MW; 3E574D6CF7DFDC28 CRC64;
MQCSIKQILS DATDKLNKIG ISSPQLEARI LLQHVINKPI EYLLINLDEQ LNEAKIEAFE
KLLARRLKHE PIVYITGVKE FYSREFIVNK HVLIPRSDTE VLVDVVFQCH SRESGNPEKK
QPNPCFRGND ISENCNDKFL NILELGTGSG CIAISLLCEL PNANVIATDI SLDAIDIIKS
NAAKYEVTDR IQIIHSNWFE NIETQKFDFI VSNPPYIAHS EKSEMAIETI NYEPSIALFA
EKDGLQAYFL IAENAKQFLK PNGKIILEIG FKQEEAVTQI FLDHGYNIES VYKDLQGHSR
VILFSPINLN RSYARRIGKS LSGVQKNLLD NKLPKYLFSK EKLVNEKRKV FLEIGFGMGE
HFINQAKMNP NALFIGIEVY LNGVANVLKL AGEQNITNFL LFPNNLDLIL NEIPSNSLDG
IYILFPDPWI KNKQKKKRIF NKERLKLLQD KLKDNGNLVF ASDIENYFYE AIELIQQNGN
FEIINKNDYL KPHDNYVITK YHQKAIKANR TPKFMILRHV LGDH
