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Database: UniProt
Entry: V6MLP0_9BACL
LinkDB: V6MLP0_9BACL
Original site: V6MLP0_9BACL 
ID   V6MLP0_9BACL            Unreviewed;       313 AA.
AC   V6MLP0;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
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=T458_03625 {ECO:0000313|EMBL:EST56408.1};
OS   Brevibacillus panacihumi W25.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1408254 {ECO:0000313|EMBL:EST56408.1, ECO:0000313|Proteomes:UP000017973};
RN   [1] {ECO:0000313|EMBL:EST56408.1, ECO:0000313|Proteomes:UP000017973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W25 {ECO:0000313|EMBL:EST56408.1,
RC   ECO:0000313|Proteomes:UP000017973};
RX   PubMed=24459276;
RA   Wang X., Jin D., Zhou L., Wu L., An W., Chen Y., Zhao L.;
RT   "Draft Genome Sequence of Brevibacillus panacihumi Strain W25, a
RT   Halotolerant Hydrocarbon-Degrading Bacterium.";
RL   Genome Announc. 2:e01215-13(2014).
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:EST56408.1}.
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DR   EMBL; AYJU01000001; EST56408.1; -; Genomic_DNA.
DR   RefSeq; WP_023554795.1; NZ_KI629782.1.
DR   AlphaFoldDB; V6MLP0; -.
DR   STRING; 1408254.T458_03625; -.
DR   PATRIC; fig|1408254.3.peg.728; -.
DR   eggNOG; COG2264; Bacteria.
DR   HOGENOM; CLU_049382_0_1_9; -.
DR   OrthoDB; 9785995at2; -.
DR   Proteomes; UP000017973; 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:EST56408.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017973};
KW   Ribonucleoprotein {ECO:0000313|EMBL:EST56408.1};
KW   Ribosomal protein {ECO:0000313|EMBL:EST56408.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:EST56408.1}.
FT   BINDING         163
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         184
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         206
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         249
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
SQ   SEQUENCE   313 AA;  34718 MW;  4E573C7D82CEAAB3 CRC64;
     MNWSEISIHT TAEATEAVSS LLYELGANGV VIEDPEVLYR EWDTPFGEIY QLSPDDFPAE
     GVFVKAYLPV ESRDLLEVVE TLRGQLAELI EYGLDIGKAT IAVNDVHEDE WAHAWKKYYK
     PIHVTDRMTI KPVWEEYELK SPDEIIIEMD PGMAFGTGTH PTTILCLRAI EKYLSPGDRV
     YDVGTGTAIL SIAAVKLGAE HVLAMDLDEV AVRSAQANTE LNGVHESITV RQNNLLDGIE
     EQVEMVIANI LAEVIVRFTD DVYRVLKPGG TFIASGIIEA READVKEALT ASGLTIVETI
     FIDDWVAIVS KKR
//
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