ID A0A1G9MSQ7_9FIRM Unreviewed; 312 AA.
AC A0A1G9MSQ7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-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=SAMN04488502_101790 {ECO:0000313|EMBL:SDL77336.1};
OS Dendrosporobacter quercicolus.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Dendrosporobacter.
OX NCBI_TaxID=146817 {ECO:0000313|EMBL:SDL77336.1, ECO:0000313|Proteomes:UP000214880};
RN [1] {ECO:0000313|EMBL:SDL77336.1, ECO:0000313|Proteomes:UP000214880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1736 {ECO:0000313|EMBL:SDL77336.1,
RC ECO:0000313|Proteomes:UP000214880};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FNHB01000001; SDL77336.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9MSQ7; -.
DR STRING; 146817.SAMN04488502_101790; -.
DR OrthoDB; 9785995at2; -.
DR Proteomes; UP000214880; 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: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:SDL77336.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000214880};
KW Ribonucleoprotein {ECO:0000313|EMBL:SDL77336.1};
KW Ribosomal protein {ECO:0000313|EMBL:SDL77336.1};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:SDL77336.1}.
FT BINDING 160
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT BINDING 181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT BINDING 203
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT BINDING 246
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
SQ SEQUENCE 312 AA; 33871 MW; 0E821707C4E04AC2 CRC64;
MKWAEISIQT THEATEAIAD IFHELGSSGV VIEDPELVNA YRRSGAWDYC DIPEQTNLEV
VTVKAYLPVD EQLDDKLKVF EEQVNELANH HLDKGQGSIQ CQEINEEDWA SSWKDYFHTV
KIGERIVIKP SWEKYEQTEN DLVIELDPGM AFGTGTHHTT AMCIRYLEEV VEPGSTIFDI
GTGSGILAVA AAKLGAASVQ AVDLDGVAVR VATENAAINQ VNEIVDIHTG NLLTGLFGQA
DVIIANIIAD VIIQLVEDIP GRLTDNGVLI ASGIIAERLS DVTAAVIANH LTVDKVMEEG
GWVAMLVRKG GG
//
