PRMA_DICNV
ID PRMA_DICNV Reviewed; 294 AA.
AC A5EVX5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Ribosomal protein L11 methyltransferase {ECO:0000255|HAMAP-Rule:MF_00735};
DE Short=L11 Mtase {ECO:0000255|HAMAP-Rule:MF_00735};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00735};
GN Name=prmA {ECO:0000255|HAMAP-Rule:MF_00735}; OrderedLocusNames=DNO_0422;
OS Dichelobacter nodosus (strain VCS1703A).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales;
OC Cardiobacteriaceae; Dichelobacter.
OX NCBI_TaxID=246195;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VCS1703A;
RX PubMed=17468768; DOI=10.1038/nbt1302;
RA Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q.,
RA Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D.,
RA McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T.,
RA Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., Adler B.,
RA Songer J.G., Rood J.I., Paulsen I.T.;
RT "Genome sequence and identification of candidate vaccine antigens from the
RT animal pathogen Dichelobacter nodosus.";
RL Nat. Biotechnol. 25:569-575(2007).
CC -!- FUNCTION: Methylates ribosomal protein L11. {ECO:0000255|HAMAP-
CC Rule:MF_00735}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:54192, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:13826, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00735};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00735}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. PrmA family.
CC {ECO:0000255|HAMAP-Rule:MF_00735}.
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DR EMBL; CP000513; ABQ14174.1; -; Genomic_DNA.
DR RefSeq; WP_012030760.1; NC_009446.1.
DR AlphaFoldDB; A5EVX5; -.
DR SMR; A5EVX5; -.
DR STRING; 246195.DNO_0422; -.
DR EnsemblBacteria; ABQ14174; ABQ14174; DNO_0422.
DR KEGG; dno:DNO_0422; -.
DR eggNOG; COG2264; Bacteria.
DR HOGENOM; CLU_049382_4_1_6; -.
DR OMA; EFFFIFP; -.
DR OrthoDB; 1712450at2; -.
DR Proteomes; UP000000248; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008276; F:protein methyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00735; Methyltr_PrmA; 1.
DR InterPro; IPR004498; Ribosomal_PrmA_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PIRSF; PIRSF000401; RPL11_MTase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00406; prmA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..294
FT /note="Ribosomal protein L11 methyltransferase"
FT /id="PRO_1000046020"
FT BINDING 147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 169
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 191
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
FT BINDING 231
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00735"
SQ SEQUENCE 294 AA; 32700 MW; C38B0F7DA3BDA258 CRC64;
MTQRHWLELT LIADNDDDVL LLETALECAG AVAVTYQAAN EEEIFEPEIG TTPMWSKTGV
TGLFPLDTDP NAVIELLMQA LGEDYPIAQH LLPESDWTRA WLEHFQPIAF GNHFWVAASE
HVIEEHDAKV LRLDPGLAFG TGTHPSTAMC LHYLVNHAAL HGKTVYDYGC GSGILGIAAA
MMGAKAVYQT DIDPQALTAS YENAQKNQVA EKIFLCEQPD LAPAVDLLVA NILLEPLCAL
RAQFEKHLHA QSVMIFSGLL ERQQQKLEQA YQDHYRIERI NCRAGWILLR LTSL