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Database: UniProt
Entry: D4K2F7_9FIRM
LinkDB: D4K2F7_9FIRM
Original site: D4K2F7_9FIRM 
ID   D4K2F7_9FIRM            Unreviewed;       304 AA.
AC   D4K2F7;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
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=FP2_32270 {ECO:0000313|EMBL:CBL00456.1};
OS   Faecalibacterium prausnitzii L2-6.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Faecalibacterium.
OX   NCBI_TaxID=718252 {ECO:0000313|EMBL:CBL00456.1, ECO:0000313|Proteomes:UP000008804};
RN   [1] {ECO:0000313|EMBL:CBL00456.1, ECO:0000313|Proteomes:UP000008804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-6 {ECO:0000313|Proteomes:UP000008804};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Faecalibacterium prausnitzii L2/6.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL00456.1, ECO:0000313|Proteomes:UP000008804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-6 {ECO:0000313|Proteomes:UP000008804};
RA   Pajon A.;
RL   Submitted (MAR-2010) 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; FP929045; CBL00456.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4K2F7; -.
DR   STRING; 718252.FP2_32270; -.
DR   KEGG; fpr:FP2_32270; -.
DR   PATRIC; fig|718252.3.peg.1428; -.
DR   eggNOG; COG2264; Bacteria.
DR   HOGENOM; CLU_049382_0_1_9; -.
DR   Proteomes; UP000008804; 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; 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:CBL00456.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008804};
KW   Ribonucleoprotein {ECO:0000313|EMBL:CBL00456.1};
KW   Ribosomal protein {ECO:0000313|EMBL:CBL00456.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:CBL00456.1}.
FT   BINDING         154
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         175
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         197
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         240
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
SQ   SEQUENCE   304 AA;  32530 MW;  54D9E3041CB07FCA CRC64;
     MEWTDIRLTV SKTDAEAAEA VATMIAEGGI YIEDYSDIEE QVEQIAHVDL IEQELLDKPR
     DTVIIHMYLE PGASPVETLA LIAARMEAAG IPYTSETEGV EQEDWQNGWR KYYHPMDVGQ
     RLAIVPSWQD YDTDRVKLIL DPGLAFGTGG HETTNLCLEV LDERVKGGER VLDIGTGSGI
     LAIAALKLGA AVAEGVDIDP VAVRTAGENA ALNGVADKLT VLVGDLSDKA SGKYDIITAN
     IVANAIMSLA PAVPGLMADD AVFIASGIID SRKDEVIAAL EAAGLAVLEV KEKRGWECIV
     CKKA
//
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