ID   RKM5_ASHGO              Reviewed;         317 AA.
AC   Q750W3;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=AGL174W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016820; AAS54317.1; -; Genomic_DNA.
DR   RefSeq; NP_986493.1; NM_211555.1.
DR   AlphaFoldDB; Q750W3; -.
DR   STRING; 33169.AAS54317; -.
DR   EnsemblFungi; AAS54317; AAS54317; AGOS_AGL174W.
DR   GeneID; 4622786; -.
DR   KEGG; ago:AGOS_AGL174W; -.
DR   eggNOG; KOG1018; Eukaryota.
DR   HOGENOM; CLU_051532_0_0_1; -.
DR   InParanoid; Q750W3; -.
DR   OMA; ACDTIYN; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0018022; P:peptidyl-lysine methylation; IBA:GO_Central.
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..317
FT                   /note="Ribosomal lysine N-methyltransferase 5"
FT                   /id="PRO_0000411040"
FT   BINDING         87
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         141..143
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         163
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         214
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         237
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
SQ   SEQUENCE   317 AA;  35283 MW;  F3AD41AC1F6A8064 CRC64;
     MLQLCPLDED TLYTHVYERY VELDRHAETL AQDLGIHASD AETLVVDIAP AQPTKSSDTY
     SLTVSQSLAS LRSSTVNNNS TTGYVLWSGT PFFLCWLLYA PSAAPLRDGG RVPVTDSAAQ
     FLQLPPLFSA PARPVCVVEL GSGAAGVAAI VLANYVDRYL VSDQKAILKP LRANLLANIS
     EVSRRTVCSK QTPELSSNRR TPARCELELI ALDWERIATV PAALRPTDAA HVHVLALDVV
     YNDFLIPPLL TAIKRLLRWY ADEHAVKATA YVLVHLRAQD ILQTFLEHAI IDLRLRCYYM
     DEERLRSSRF ALYYVTL