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Database: UniProt
Entry: A0A176JAY4_9BACI
LinkDB: A0A176JAY4_9BACI
Original site: A0A176JAY4_9BACI 
ID   A0A176JAY4_9BACI        Unreviewed;       317 AA.
AC   A0A176JAY4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=AS29_002050 {ECO:0000313|EMBL:KZZ85987.1};
OS   Bacillus sp. SJS.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423321 {ECO:0000313|EMBL:KZZ85987.1, ECO:0000313|Proteomes:UP000028527};
RN   [1] {ECO:0000313|EMBL:KZZ85987.1, ECO:0000313|Proteomes:UP000028527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJS {ECO:0000313|EMBL:KZZ85987.1,
RC   ECO:0000313|Proteomes:UP000028527};
RA   Newman J.D., Stropko S.J., Pipes S.E.;
RT   "Bacillus sp. SJS genome.";
RL   Submitted (APR-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZZ85987.1}.
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DR   EMBL; JAQV02000004; KZZ85987.1; -; Genomic_DNA.
DR   RefSeq; WP_035405150.1; NZ_JAQV02000004.1.
DR   AlphaFoldDB; A0A176JAY4; -.
DR   STRING; 1423321.AS29_002050; -.
DR   eggNOG; COG2264; Bacteria.
DR   OrthoDB; 9785995at2; -.
DR   Proteomes; UP000028527; Unassembled WGS sequence.
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: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   NCBIfam; TIGR00406; prmA; 1.
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   PIRSF; PIRSF000401; RPL11_MTase; 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:KZZ85987.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028527};
KW   Ribonucleoprotein {ECO:0000313|EMBL:KZZ85987.1};
KW   Ribosomal protein {ECO:0000313|EMBL:KZZ85987.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:KZZ85987.1}.
FT   BINDING         162
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         183
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"
FT   BINDING         248
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
SQ   SEQUENCE   317 AA;  34871 MW;  C7EA1FA9CD0C5F64 CRC64;
     MKWSEISIHT TQEAVEPISN ILHEAGASGV VIEDQMDLLK ERESVYGEIY HLDPLDYPAE
     GVIIKAYLPM NSFLAETVEG ITNSIEGLSQ YGINLGSKQL KTSEVNEEDW ATAWKKYYHP
     VKISEKFTIV PTWEEYEPVH SDELIIELDP GMAFGTGTHP TTVLCIQALE RTVKKGDKVI
     DIGTGSGVLS IASALLGAEA VRAMDLDPVA VESARQNTVL NKVNGKVEVF QNDLLSGISE
     QADVIVANIL AEVILKFTDE AYNLVKEGGW FITSGIILNK KNDVRDALIK AGFEISETVV
     MEDWVAFIAR KSEQSAI
//
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