ID A0A1Q9J0F3_9FIRM Unreviewed; 275 AA. AC A0A1Q9J0F3; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 03-AUG-2022, entry version 19. DE RecName: Full=Release factor glutamine methyltransferase {ECO:0000256|HAMAP-Rule:MF_02126}; DE Short=RF MTase {ECO:0000256|HAMAP-Rule:MF_02126}; DE EC=2.1.1.297 {ECO:0000256|HAMAP-Rule:MF_02126}; DE AltName: Full=N5-glutamine methyltransferase PrmC {ECO:0000256|HAMAP-Rule:MF_02126}; DE AltName: Full=Protein-(glutamine-N5) MTase PrmC {ECO:0000256|HAMAP-Rule:MF_02126}; DE AltName: Full=Protein-glutamine N-methyltransferase PrmC {ECO:0000256|HAMAP-Rule:MF_02126}; GN Name=prmC {ECO:0000256|HAMAP-Rule:MF_02126}; GN ORFNames=BIV16_14510 {ECO:0000313|EMBL:OLR38305.1}; OS Roseburia sp. 831b. OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae; OC Roseburia; unclassified Roseburia. OX NCBI_TaxID=1261635 {ECO:0000313|EMBL:OLR38305.1, ECO:0000313|Proteomes:UP000186530}; RN [1] {ECO:0000313|EMBL:OLR38305.1, ECO:0000313|Proteomes:UP000186530} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=831b {ECO:0000313|EMBL:OLR38305.1, RC ECO:0000313|Proteomes:UP000186530}; RX PubMed=27613689; RA Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.; RT "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate RT Transferases and Their Diversity in the Proximal Colon of Swine."; RL Appl. Environ. Microbiol. 82:6788-6798(2016). 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:0000256|ARBA:ARBA00002551, CC ECO:0000256|HAMAP-Rule:MF_02126}. 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 Evidence={ECO:0000256|ARBA:ARBA00000932, ECO:0000256|HAMAP- CC Rule:MF_02126}; CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase CC family. PrmC subfamily. {ECO:0000256|HAMAP-Rule:MF_02126}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02126}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OLR38305.1}. 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; MJHW01000010; OLR38305.1; -; Genomic_DNA. DR RefSeq; WP_075681612.1; NZ_MJHW01000010.1. DR STRING; 1261635.BIV16_14510; -. DR EnsemblBacteria; OLR38305; OLR38305; BIV16_14510. DR Proteomes; UP000186530; Unassembled WGS sequence. 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:0018364; P:peptidyl-glutamine methylation; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_02126; RF_methyltr_PrmC; 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 Pfam; PF05175; MTS; 1. DR Pfam; PF17827; PrmC_N; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00536; hemK_fam; 1. DR TIGRFAMs; TIGR03534; RF_mod_PrmC; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 3: Inferred from homology; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP- KW Rule:MF_02126}; Reference proteome {ECO:0000313|Proteomes:UP000186530}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP- KW Rule:MF_02126}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_02126}. FT DOMAIN 5..75 FT /note="PrmC_N" FT /evidence="ECO:0000259|Pfam:PF17827" FT DOMAIN 100..185 FT /note="MTS" FT /evidence="ECO:0000259|Pfam:PF05175" FT REGION 182..185 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126" FT BINDING 141 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126" FT BINDING 182 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126" SQ SEQUENCE 275 AA; 30876 MW; 1FAF3B3113012E41 CRC64; MTYQEAVKNG EKVLNLAGIA DAKVDAWLLF EMACKVDRQF YYLHMGEDIT MEQQKEYEIV LKKRTEHIPL QYIVGEQEFM GLKFKVNSSV LIPRQDTETL VEEALKKIQP DMKVLDMCTG SGCIIISIIK NVPSAEGYAV DISKQALNVA KENAKSNEVP VNFERSDLFD NVTGVYDVIV SNPPYIPTAE IPKLMPEVGS FEPLEALDGK EDGLFFYRKI VAECGSHLKD GGYLLFEIGC EQANDVTTML RETGFYEVQV VKDLAGLDRV VIGRK //