位置:首页 > 蛋白库 > RKM5_CANGA
RKM5_CANGA
ID   RKM5_CANGA              Reviewed;         352 AA.
AC   Q6FJQ5;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Ribosomal lysine N-methyltransferase 5 {ECO:0000250|UniProtKB:Q12367};
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q12367};
GN   Name=RKM5; OrderedLocusNames=CAGL0M04411g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC       methyltransferase that methylates 60S ribosomal protein L1.
CC       {ECO:0000250|UniProtKB:Q12367}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RKM5 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR380959; CAG62515.1; -; Genomic_DNA.
DR   RefSeq; XP_449539.1; XM_449539.1.
DR   AlphaFoldDB; Q6FJQ5; -.
DR   STRING; 5478.XP_449539.1; -.
DR   EnsemblFungi; CAG62515; CAG62515; CAGL0M04411g.
DR   GeneID; 2891548; -.
DR   KEGG; cgr:CAGL0M04411g; -.
DR   CGD; CAL0137451; CAGL0M04411g.
DR   VEuPathDB; FungiDB:CAGL0M04411g; -.
DR   eggNOG; KOG1018; Eukaryota.
DR   HOGENOM; CLU_051532_0_0_1; -.
DR   InParanoid; Q6FJQ5; -.
DR   OMA; TIMFIAW; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0006479; P:protein methylation; IEA:EnsemblFungi.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR14614; PTHR14614; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..352
FT                   /note="Ribosomal lysine N-methyltransferase 5"
FT                   /id="PRO_0000411041"
FT   BINDING         107
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         161..163
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         183
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         244
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         274
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
SQ   SEQUENCE   352 AA;  40185 MW;  36019934B5BECDCE CRC64;
     MPFSLVRIDE DDVLEYVFER YTAINSDADS IRQDLGIQDS KSTTLNIEIA PPKSLINDTN
     ITKKGKKKKG NKSSSDYDFY SFEIKQNVTS LHSTRDNDNS TTGYVLWSLT PVFCEWLLYN
     EQASPLHRAQ MVNICSLEKK IIHDIEFPSL LNEDTTVIEL GSGISSVLPI LCSNFVGTYI
     CTDQRGILNG LKQNIANNLD LVNKRTIVSE TLDISNIQEQ PTNSDDETIP IKPTTQLEVA
     ILDWETFPKS IKSGSSNILT DFVKPHGTIF LLALDVIYNE YLINPFLHTL HSIMFYYKNQ
     REIVALVGIH LRSDDIVQEF LEKVTTEFPF KLHVVDDPQW SHSRYDIYYI TL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024