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}.
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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