PRMB_XANCP
ID PRMB_XANCP Reviewed; 308 AA.
AC Q8P7Q8;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=50S ribosomal protein L3 glutamine methyltransferase {ECO:0000255|HAMAP-Rule:MF_02125};
DE Short=L3 MTase {ECO:0000255|HAMAP-Rule:MF_02125};
DE EC=2.1.1.298 {ECO:0000255|HAMAP-Rule:MF_02125};
DE AltName: Full=N5-glutamine methyltransferase PrmB {ECO:0000255|HAMAP-Rule:MF_02125};
GN Name=prmB {ECO:0000255|HAMAP-Rule:MF_02125}; OrderedLocusNames=XCC2553;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
CC -!- FUNCTION: Specifically methylates the 50S ribosomal protein L3 on a
CC specific glutamine residue. {ECO:0000255|HAMAP-Rule:MF_02125}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[ribosomal protein uL3] + S-adenosyl-L-methionine
CC = H(+) + N(5)-methyl-L-glutaminyl-[ribosomal protein uL3] + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:45020, Rhea:RHEA-COMP:11063,
CC Rhea:RHEA-COMP:11064, ChEBI:CHEBI:15378, ChEBI:CHEBI:30011,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61891;
CC EC=2.1.1.298; Evidence={ECO:0000255|HAMAP-Rule:MF_02125};
CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC family. PrmB subfamily. {ECO:0000255|HAMAP-Rule:MF_02125}.
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DR EMBL; AE008922; AAM41825.1; -; Genomic_DNA.
DR RefSeq; NP_637901.1; NC_003902.1.
DR RefSeq; WP_011037683.1; NC_003902.1.
DR AlphaFoldDB; Q8P7Q8; -.
DR SMR; Q8P7Q8; -.
DR STRING; 340.xcc-b100_1609; -.
DR EnsemblBacteria; AAM41825; AAM41825; XCC2553.
DR KEGG; xcc:XCC2553; -.
DR PATRIC; fig|190485.4.peg.2720; -.
DR eggNOG; COG2890; Bacteria.
DR HOGENOM; CLU_018398_5_1_6; -.
DR OMA; IYYGHGT; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro.
DR GO; GO:0018364; P:peptidyl-glutamine methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_02125; L3_methyltr_PrmB; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004556; HemK-like.
DR InterPro; IPR017127; Ribosome_L3_Gln-N5_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR Pfam; PF05175; MTS; 1.
DR PIRSF; PIRSF037167; Mtase_YfcB_prd; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00536; hemK_fam; 1.
DR TIGRFAMs; TIGR03533; L3_gln_methyl; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..308
FT /note="50S ribosomal protein L3 glutamine
FT methyltransferase"
FT /id="PRO_0000414184"
SQ SEQUENCE 308 AA; 33841 MW; A4CC8B64FB7F806E CRC64;
MTAAAADELH TIIDLIRYGT SRFNEAGLTF GHSYDNALDE ATQLVLHSLH LPHDLGPAYG
QARLLRAEKE RVLALFQRRV DERVPAAYLT GEAWFAGLSF KSDARALVPR SPIAELIEAG
FEPWLGGREV TRALDLCTGS GCIAIAMGHY NPHWDVDGVD ISDDALALAA ENKARLHADN
VSLLKSDLFT GLAGRQYDLI VTNPPYVTND ETDALPQEYS YEPELGLRAG DDGLDLVLKI
LRDAPQHLSE DGLLICEVGE SEQHLIKLLP EVDFAWVEFK VGQMGIFAVE CRELIAHSAR
ITELASAR