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Database: UniProt
Entry: A0A1M6FYK2_9FLAO
LinkDB: A0A1M6FYK2_9FLAO
Original site: A0A1M6FYK2_9FLAO 
ID   A0A1M6FYK2_9FLAO        Unreviewed;       277 AA.
AC   A0A1M6FYK2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=SAMN05216261_2556 {ECO:0000313|EMBL:SHJ02722.1};
OS   Algibacter luteus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Algibacter.
OX   NCBI_TaxID=1178825 {ECO:0000313|EMBL:SHJ02722.1, ECO:0000313|Proteomes:UP000184396};
RN   [1] {ECO:0000313|EMBL:SHJ02722.1, ECO:0000313|Proteomes:UP000184396}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12213 {ECO:0000313|EMBL:SHJ02722.1,
RC   ECO:0000313|Proteomes:UP000184396};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FQYK01000006; SHJ02722.1; -; Genomic_DNA.
DR   RefSeq; WP_019388788.1; NZ_FQYK01000006.1.
DR   AlphaFoldDB; A0A1M6FYK2; -.
DR   STRING; 1178825.SAMN05216261_2556; -.
DR   eggNOG; COG2264; Bacteria.
DR   OrthoDB; 9785995at2; -.
DR   Proteomes; UP000184396; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0008276; F:protein methyltransferase activity; IEA:UniProtKB-UniRule.
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   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:SHJ02722.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184396};
KW   Ribonucleoprotein {ECO:0000313|EMBL:SHJ02722.1};
KW   Ribosomal protein {ECO:0000313|EMBL:SHJ02722.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:SHJ02722.1}.
FT   BINDING         130
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         151
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         173
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         214
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
SQ   SEQUENCE   277 AA;  31886 MW;  3FCA78A734737B11 CRC64;
     MSNTIYIGYN FKVQPLQPAV EILIAELGYA GFESFVENED GVTAYIQKEE WNQDILEDVQ
     ILNSKEFNIA YTFEDIEQTN WNAEWEKNFN PIVVDDTCAV RAPFHEKFNV QYDIIIEPKM
     SFGTGHHETT HMMIQHILKN DFKDKSVLDM GCGTGVLAIL AELKGAKPID AIDYDNWCYL
     NSLENVERNN CKHITVIEGD ASVLKNKYDI IIANINRNIL LQDMATYISC LNKNGMLFLS
     GFYDDDVALI TSECEKHLLK FEEKLERNNW VSLKFLN
//
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