ID H5TAU1_9ALTE Unreviewed; 294 AA.
AC H5TAU1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
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:GAB55418.1};
GN ORFNames=GPUN_1294 {ECO:0000313|EMBL:GAB55418.1};
OS Glaciecola punicea ACAM 611.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Glaciecola.
OX NCBI_TaxID=1121923 {ECO:0000313|EMBL:GAB55418.1, ECO:0000313|Proteomes:UP000053586};
RN [1] {ECO:0000313|EMBL:GAB55418.1, ECO:0000313|Proteomes:UP000053586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB55418.1,
RC ECO:0000313|Proteomes:UP000053586};
RX PubMed=22628500; DOI=10.1128/JB.00463-12;
RA Qin Q.-L., Xie B.-B., Shu Y.-L., Rong J.-C., Zhao D.-L., Zhang X.-Y.,
RA Chen X.-L., Zhou B.-C., Zhanga Y.-Z.;
RT "Genome sequence of proteorhodopsin-containing sea ice bacterium Glaciecola
RT punicea ACAM 611T.";
RL J. Bacteriol. 194:3267-3267(2012).
RN [2] {ECO:0000313|EMBL:GAB55418.1, ECO:0000313|Proteomes:UP000053586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB55418.1,
RC ECO:0000313|Proteomes:UP000053586};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(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:GAB55418.1}.
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DR EMBL; BAET01000012; GAB55418.1; -; Genomic_DNA.
DR RefSeq; WP_006004474.1; NZ_BAET01000012.1.
DR AlphaFoldDB; H5TAU1; -.
DR STRING; 56804.BAE46_06420; -.
DR eggNOG; COG2264; Bacteria.
DR OrthoDB; 9785995at2; -.
DR Proteomes; UP000053586; 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:GAB55418.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053586};
KW Ribonucleoprotein {ECO:0000313|EMBL:GAB55418.1};
KW Ribosomal protein {ECO:0000313|EMBL:GAB55418.1};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:GAB55418.1}.
FT BINDING 145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT BINDING 166
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT BINDING 188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT BINDING 229
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
SQ SEQUENCE 294 AA; 33087 MW; A58A9B1DCEAFAB86 CRC64;
MAWQQIKINV EADHAEALAD FFTELNAQAV TFVDAKDTPM YEPKPGQILL WPDTQVIALY
DAQEDLKPVI SAILKQYRFI DTNEIAVDQL EDKNWEREWM KDFHPMKFGK RLWICPSWHD
IPDINAVNIK LDPGLAFGTG THPTTRLCLE WLDSVDLVDK VLVDFGCGSG ILAIAALKLG
AKEVIGIDID PQALIASKDN AQRNSVEDRL SLYLPQNQPN LEADIVIANI LSAPLKELSD
TISNYCKNAG MLVMSGILQE QYESVVQVYE NQFIFDPATL EGEWVRLSAL KKKQ
//
