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Database: UniProt
Entry: A0A2Y9A2Z8_9RHOB
LinkDB: A0A2Y9A2Z8_9RHOB
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ID   A0A2Y9A2Z8_9RHOB        Unreviewed;       290 AA.
AC   A0A2Y9A2Z8;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=BCF38_101940 {ECO:0000313|EMBL:PWJ22526.1},
GN   SAMN05421539_101940 {ECO:0000313|EMBL:SSA38804.1};
OS   Jannaschia seohaensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=475081 {ECO:0000313|EMBL:SSA38804.1, ECO:0000313|Proteomes:UP000251571};
RN   [1] {ECO:0000313|EMBL:SSA38804.1, ECO:0000313|Proteomes:UP000251571}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25227 {ECO:0000313|EMBL:SSA38804.1,
RC   ECO:0000313|Proteomes:UP000251571};
RA   Cai Z.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PWJ22526.1, ECO:0000313|Proteomes:UP000245839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25227 {ECO:0000313|EMBL:PWJ22526.1,
RC   ECO:0000313|Proteomes:UP000245839};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-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; QGDJ01000001; PWJ22526.1; -; Genomic_DNA.
DR   EMBL; UETC01000001; SSA38804.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Y9A2Z8; -.
DR   OrthoDB; 9785995at2; -.
DR   Proteomes; UP000245839; Unassembled WGS sequence.
DR   Proteomes; UP000251571; Unassembled WGS sequence.
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:0032259; P:methylation; IEA:UniProtKB-KW.
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:SSA38804.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245839};
KW   Ribonucleoprotein {ECO:0000313|EMBL:SSA38804.1};
KW   Ribosomal protein {ECO:0000313|EMBL:SSA38804.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:SSA38804.1}.
FT   BINDING         137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         161
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         184
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         229
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
SQ   SEQUENCE   290 AA;  30395 MW;  D906CF015F561E0B CRC64;
     MSDTITPASW TALTTLPGKE SAEALGEMLE EQLAPDGVGV FEMEDGSGLW EVGAYFAEAP
     DETALAILAA AHGARPFTVS EIPPTDWVAH VRRELQPVEA GRFFVYGSHD ADRVPEGRVA
     LLIEAAMAFG TGHHGTTQGC LLAFEALIEE GIAPDTVADI GAGTAVLAMA AKRIFPQASV
     IASDIDVVAV EVAEANLAVN GMAGEVACIE AAGFDHPDLA GPFDLIFANI LKGPLIELAP
     DMARAARGHV ILSGLLNPQA EEVIAAYESA GFGLVRRVEL GDWTTLTLRR
//
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