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Database: UniProt
Entry: A6GR84_9BURK
LinkDB: A6GR84_9BURK
Original site: A6GR84_9BURK 
ID   A6GR84_9BURK            Unreviewed;       304 AA.
AC   A6GR84;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, 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   ECO:0000313|EMBL:EDM83357.1};
GN   ORFNames=LMED105_07143 {ECO:0000313|EMBL:EDM83357.1};
OS   Limnobacter sp. MED105.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Limnobacter.
OX   NCBI_TaxID=391597 {ECO:0000313|EMBL:EDM83357.1, ECO:0000313|Proteomes:UP000010322};
RN   [1] {ECO:0000313|EMBL:EDM83357.1, ECO:0000313|Proteomes:UP000010322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED105 {ECO:0000313|EMBL:EDM83357.1,
RC   ECO:0000313|Proteomes:UP000010322};
RA   Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) 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:EDM83357.1}.
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DR   EMBL; ABCT01000008; EDM83357.1; -; Genomic_DNA.
DR   RefSeq; WP_008250524.1; NZ_ABCT01000008.1.
DR   AlphaFoldDB; A6GR84; -.
DR   STRING; 391597.LMED105_07143; -.
DR   OrthoDB; 9785995at2; -.
DR   Proteomes; UP000010322; 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:EDM83357.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010322};
KW   Ribonucleoprotein {ECO:0000313|EMBL:EDM83357.1};
KW   Ribosomal protein {ECO:0000313|EMBL:EDM83357.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:EDM83357.1}.
FT   BINDING         156
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         177
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         199
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         239
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
SQ   SEQUENCE   304 AA;  32887 MW;  9CD45ACA8F813564 CRC64;
     MNPQATPLIQ AKLTLPFEQA DEVSDLLMEL GALAVSLEDA NADSEDEQPL FGEPGMEPES
     AAWNLNHVVA LFRNKAEGEQ IFGEIPAELL GEAEIDYTEV PQVDWVRLTQ SQFDPIPISA
     RLWIVPSWHE PQNIDDRINL VLDPGLAFGT GSHPTTALCL RWLSEFPLKG QSVLDYGCGS
     GILGIAALKL GASEAIGVDI DPQAVDSTAY NAGNNGVEMP CGLPDFPLAK RQFPVVVANI
     LSNPLKVLAP SLCNHVEAGG QLVLSGVLAR QAEEVISHYR QWINLAVWAE RDGWVCLHGQ
     KAAD
//
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