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Database: UniProt
Entry: A0A0F7JLD9_9DEIO
LinkDB: A0A0F7JLD9_9DEIO
Original site: A0A0F7JLD9_9DEIO 
ID   A0A0F7JLD9_9DEIO        Unreviewed;       270 AA.
AC   A0A0F7JLD9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
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   ORFNames=SY84_00245 {ECO:0000313|EMBL:AKH15733.1};
OS   Deinococcus soli (ex Cha et al. 2016).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=1309411 {ECO:0000313|EMBL:AKH15733.1, ECO:0000313|Proteomes:UP000034024};
RN   [1] {ECO:0000313|EMBL:AKH15733.1, ECO:0000313|Proteomes:UP000034024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N5 {ECO:0000313|EMBL:AKH15733.1,
RC   ECO:0000313|Proteomes:UP000034024};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Deinococcus soli/N5/whole genome sequencing.";
RL   Submitted (JAN-2015) 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; CP011389; AKH15733.1; -; Genomic_DNA.
DR   RefSeq; WP_046842309.1; NZ_JAVDTP010000002.1.
DR   AlphaFoldDB; A0A0F7JLD9; -.
DR   KEGG; dch:SY84_00245; -.
DR   PATRIC; fig|1309411.5.peg.50; -.
DR   OrthoDB; 9785995at2; -.
DR   Proteomes; UP000034024; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0042054; F:histone methyltransferase activity; IEA:RHEA.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.20.5.1350; -; 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:AKH15733.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034024};
KW   Ribonucleoprotein {ECO:0000313|EMBL:AKH15733.1};
KW   Ribosomal protein {ECO:0000313|EMBL:AKH15733.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:AKH15733.1}.
FT   BINDING         112
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         133
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         155
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         205
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
SQ   SEQUENCE   270 AA;  28888 MW;  2D6FF8480AEEA805 CRC64;
     MLVYHLPGTF ETREDHLDLL WEAGATGLEE RAGLIRAYFD EETELPPLIR DGEWRLEADQ
     DWLAEFKANL RPVQAGRVTI VPPWLRAEIP AGQVGLVIEP GMAFGTGHHA TTRMAVEALS
     DLNLDGQTIL DVGTGSGVLA IAGALLGAEY ALGVDIDPIT IPIAEENARD NAVPEGRTAF
     MVGTLGDDLP GDVVADGVFD VLVANLYAEL HDLLAGAYVG HLRPGGPLIL TGILTTKLPL
     VQDALDREGF TDVQVRTDGE WALVTARAGE
//
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