ID A0A368XBI5_9BACI Unreviewed; 312 AA.
AC A0A368XBI5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=DFR57_11150 {ECO:0000313|EMBL:RCW65322.1};
OS Saliterribacillus persicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Saliterribacillus.
OX NCBI_TaxID=930114 {ECO:0000313|EMBL:RCW65322.1, ECO:0000313|Proteomes:UP000252585};
RN [1] {ECO:0000313|EMBL:RCW65322.1, ECO:0000313|Proteomes:UP000252585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27696 {ECO:0000313|EMBL:RCW65322.1,
RC ECO:0000313|Proteomes:UP000252585};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-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}.
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:RCW65322.1}.
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DR EMBL; QPJJ01000011; RCW65322.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368XBI5; -.
DR OrthoDB; 9785995at2; -.
DR Proteomes; UP000252585; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00735};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00735,
KW ECO:0000313|EMBL:RCW65322.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000252585};
KW Ribonucleoprotein {ECO:0000313|EMBL:RCW65322.1};
KW Ribosomal protein {ECO:0000313|EMBL:RCW65322.1};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:RCW65322.1}.
FT COILED 206..233
FT /evidence="ECO:0000256|SAM:Coils"
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 312 AA; 34653 MW; B7A3DA9A817F1819 CRC64;
MKWTELCIHT TNEAIEPISN IFHEAGASGV VIEDQSELDV QREDTYGEIY ELDPNDYPDE
GVLLKAYLPV NSFLGETVAE IKQAINNLLL YDIDLGRNSI TLSEVNEEDW ATAWKKYYKP
VKISERITIT PTWEDYQRVS SDELIIELDP GMAFGTGTHP TTVLSIQALE QYVKSNDTIL
DVGCGSGVLS IASALLGAQE IFAYDLDEVA VKSAKLNAKV NKVEKKIHVK QNNLLNNVTT
KADVIVANIL AEIILRFEKD AFSCLKSGGI FITSGIIQAK KDQVKSGLIN AGFEILEINQ
MEDWISIIAR RP
//