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Entry: A0A011NL38_9PROT
LinkDB: A0A011NL38_9PROT
Original site: A0A011NL38_9PROT 
ID   A0A011NL38_9PROT        Unreviewed;       296 AA.
AC   A0A011NL38;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
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:EXI65352.1};
GN   ORFNames=AW08_03272 {ECO:0000313|EMBL:EXI65352.1};
OS   Candidatus Accumulibacter adjunctus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=1454001 {ECO:0000313|EMBL:EXI65352.1, ECO:0000313|Proteomes:UP000020218};
RN   [1] {ECO:0000313|EMBL:EXI65352.1, ECO:0000313|Proteomes:UP000020218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-12 {ECO:0000313|Proteomes:UP000020218};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-2014) 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:EXI65352.1}.
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DR   EMBL; JFAX01000024; EXI65352.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A011NL38; -.
DR   STRING; 1454001.AW08_03272; -.
DR   PATRIC; fig|1454001.3.peg.3319; -.
DR   Proteomes; UP000020218; 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:EXI65352.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020218};
KW   Ribonucleoprotein {ECO:0000313|EMBL:EXI65352.1};
KW   Ribosomal protein {ECO:0000313|EMBL:EXI65352.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:EXI65352.1}.
FT   BINDING         151
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         172
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         194
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         233
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
SQ   SEQUENCE   296 AA;  31304 MW;  9734F871ED33C84C CRC64;
     MAWLSLSIRT DCLHAERLAD ALLEAGALAA SIEDADAGTA DEQPQFGEPG SISRPGWQRS
     LVVALLQPEA DARELLLRCG TQAGLTELPQ FSLEEVPEQD WVRLTQSQFE PIRVAQRLWI
     VPSWHTAPDP GAIVLVLDPG MAFGTGSHPT TRLCLEWLER SVGPGVSVLD YGCGSGVLAI
     AAGRLGAGEI VGVDIDPQAV VVARTNAEAN GVAARFQESA DRLSGQFDIV VANILANPLR
     VLAPALCGHL RAGGMLALSG ILVEQAEELI AAYKPHLTLT VVGTRDGWVC LAGSRN
//
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