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Database: UniProt
Entry: A0A1W6SLV1_9PROT
LinkDB: A0A1W6SLV1_9PROT
Original site: A0A1W6SLV1_9PROT 
ID   A0A1W6SLV1_9PROT        Unreviewed;       305 AA.
AC   A0A1W6SLV1;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=EBAPG3_002690 {ECO:0000313|EMBL:ARO86765.1};
OS   Nitrosospira lacus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=1288494 {ECO:0000313|EMBL:ARO86765.1, ECO:0000313|Proteomes:UP000012179};
RN   [1] {ECO:0000313|EMBL:ARO86765.1, ECO:0000313|Proteomes:UP000012179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APG3 {ECO:0000313|EMBL:ARO86765.1,
RC   ECO:0000313|Proteomes:UP000012179};
RX   PubMed=25336720; DOI=10.1099/ijs.0.070789-0;
RA   Urakawa H., Garcia J.C., Nielsen J.L., Le V.Q., Kozlowski J.A., Stein L.Y.,
RA   Lim C.K., Pommerening-Roser A., Martens-Habbena W., Stahl D.A., Klotz M.G.;
RT   "Nitrosospira lacus sp. nov., a psychrotolerant, ammonia-oxidizing
RT   bacterium from sandy lake sediment.";
RL   Int. J. Syst. Evol. Microbiol. 65:242-250(2015).
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; CP021106; ARO86765.1; -; Genomic_DNA.
DR   RefSeq; WP_004175916.1; NZ_CP021106.3.
DR   AlphaFoldDB; A0A1W6SLV1; -.
DR   KEGG; nlc:EBAPG3_002690; -.
DR   eggNOG; COG2264; Bacteria.
DR   OrthoDB; 9785995at2; -.
DR   Proteomes; UP000012179; Chromosome.
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   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00735};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00735,
KW   ECO:0000313|EMBL:ARO86765.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012179};
KW   Ribonucleoprotein {ECO:0000313|EMBL:ARO86765.1};
KW   Ribosomal protein {ECO:0000313|EMBL:ARO86765.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00735};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00735, ECO:0000313|EMBL:ARO86765.1}.
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         172
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         194
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
FT   BINDING         242
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00735"
SQ   SEQUENCE   305 AA;  33004 MW;  073CACCCECD3ECDA CRC64;
     MSWISLTLET DDLHAEILSD AMLELGALST DIHDAAAGTE REQPLFDEPG ELAGEIWSMS
     ELTALFEADA DIASIVQAAA QAAQLPTPPA YHLALVEEQD WVRITQSQFD PIQISSRLWI
     VPTWHRAPDP AAINLALDPG LAFGTGSHPT TQLCLAWLDE NLQGGEDLLD YGCGSGILAI
     AASKLGARYV VGVDIDAQAV AASRENALLN QCDETAIEFH AAHLATWEDS AREAWADVVL
     ANILANPLIM LAPILTRAVR PGGHIVLSGI LVEQAEEVRH AYREWCNMHV ADVREGWVLL
     TGIRT
//
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