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Database: UniProt
Entry: A0A0T5P9R3_9RHOB
LinkDB: A0A0T5P9R3_9RHOB
Original site: A0A0T5P9R3_9RHOB 
ID   A0A0T5P9R3_9RHOB        Unreviewed;       291 AA.
AC   A0A0T5P9R3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Ribosomal protein L11 methyltransferase {ECO:0000256|HAMAP-Rule:MF_00735};
DE            Short=L11 Mtase {ECO:0000256|HAMAP-Rule:MF_00735};
DE            EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_00735};
GN   Name=prmA {ECO:0000256|HAMAP-Rule:MF_00735,
GN   ECO:0000313|EMBL:QEW24463.1};
GN   ORFNames=RIdsm_00242 {ECO:0000313|EMBL:QEW24463.1}, XM52_12305
GN   {ECO:0000313|EMBL:KRS17770.1};
OS   Roseovarius indicus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=540747 {ECO:0000313|EMBL:KRS17770.1, ECO:0000313|Proteomes:UP000051401};
RN   [1] {ECO:0000313|EMBL:KRS17770.1, ECO:0000313|Proteomes:UP000051401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B108 {ECO:0000313|EMBL:KRS17770.1,
RC   ECO:0000313|Proteomes:UP000051401};
RA   Li G., Lai Q., Shao Z., Yan P.;
RT   "The draft genome sequence of Roseovarius indicus B108T.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QEW24463.1, ECO:0000313|Proteomes:UP000325785}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26383 {ECO:0000313|EMBL:QEW24463.1,
RC   ECO:0000313|Proteomes:UP000325785};
RA   Vollmers J., Petersen J.;
RT   "Genetic Globetrotter - A new plasmid hitch-hiking vast phylogenetic and
RT   geographic distances.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Methylates ribosomal protein L11. {ECO:0000256|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:0000256|HAMAP-
CC         Rule:MF_00735};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00735}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. PrmA family.
CC       {ECO:0000256|ARBA:ARBA00009741, ECO:0000256|HAMAP-Rule:MF_00735}.
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DR   EMBL; LAXI01000006; KRS17770.1; -; Genomic_DNA.
DR   EMBL; CP031598; QEW24463.1; -; Genomic_DNA.
DR   RefSeq; WP_057816419.1; NZ_LAXI01000006.1.
DR   AlphaFoldDB; A0A0T5P9R3; -.
DR   STRING; 540747.SAMN04488031_10734; -.
DR   KEGG; rid:RIdsm_00242; -.
DR   PATRIC; fig|540747.5.peg.5440; -.
DR   OrthoDB; 9785995at2; -.
DR   Proteomes; UP000051401; Unassembled WGS sequence.
DR   Proteomes; UP000325785; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0008276; F:protein methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_00735; Methyltr_PrmA; 1.
DR   InterPro; IPR004498; Ribosomal_PrmA_MeTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR43648; ELECTRON TRANSFER FLAVOPROTEIN BETA SUBUNIT LYSINE METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43648:SF1; ELECTRON TRANSFER FLAVOPROTEIN BETA SUBUNIT LYSINE METHYLTRANSFERASE; 1.
DR   Pfam; PF06325; PrmA; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00735};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00735,
KW   ECO:0000313|EMBL:KRS17770.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051401};
KW   Ribonucleoprotein {ECO:0000313|EMBL:KRS17770.1};
KW   Ribosomal protein {ECO:0000313|EMBL:KRS17770.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:KRS17770.1}.
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         156
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         179
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         226
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
SQ   SEQUENCE   291 AA;  30260 MW;  5DFCC0927D7AE9DA CRC64;
     MPTYTALTTL SGKHAAEALG EDLERLTPEP TGIGTFEIED GSGLWEVGAY FDGAPDEAGL
     ALLAAIHDAK PFVVSELPDV DWVAKVRREL VPVEAGRFFV YGSHDADKVP SNSVPLLIEA
     SMAFGTGHHG TTQGCLRALD KLAAEGMTAT RVLDLGCGTA VLAMGAAHVW PDATILASDI
     DEVAVEVAEA NLAANGLAGR VACIEAEGLD NPDIAGKAPF DLIFANILKG PLIALAPAIT
     DALAPGGRVI LSGILNEQAD EVIEVYSAAG NSLVERSEIG EWTTTVLRKP V
//
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