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 27-MAR-2024, entry version 120. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.gene:17555916; -. 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 OrthoDB; 9800643at2; -. 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(46)-N7)-methyltransferase activity; IEA:UniProtKB-UniRule. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 NCBIfam; TIGR00536; hemK_fam; 1. DR NCBIfam; TIGR03534; RF_mod_PrmC; 1. DR NCBIfam; TIGR00091; tRNA (guanosine(46)-N7)-methyltransferase TrmB; 1. DR PANTHER; PTHR18895; HEMK METHYLTRANSFERASE; 1. DR PANTHER; PTHR18895:SF74; MTRF1L RELEASE FACTOR GLUTAMINE METHYLTRANSFERASE; 1. DR Pfam; PF02390; Methyltransf_4; 1. DR Pfam; PF05175; MTS; 1. DR Pfam; PF17827; PrmC_N; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2. 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 //