RKM5_VANPO
ID RKM5_VANPO Reviewed; 324 AA.
AC A7TTV0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Ribosomal lysine N-methyltransferase 5 {ECO:0000250|UniProtKB:Q12367};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q12367};
GN Name=RKM5; ORFNames=Kpol_152p1;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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 -!- SEQUENCE CAUTION:
CC Sequence=EDO14306.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; DS480632; EDO14306.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001642164.1; XM_001642114.1.
DR AlphaFoldDB; A7TTV0; -.
DR STRING; 436907.A7TTV0; -.
DR EnsemblFungi; EDO14306; EDO14306; Kpol_152p1.
DR GeneID; 5542277; -.
DR KEGG; vpo:Kpol_152p1; -.
DR eggNOG; KOG1018; Eukaryota.
DR HOGENOM; CLU_051532_0_0_1; -.
DR InParanoid; A7TTV0; -.
DR OrthoDB; 1346733at2759; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006479; P:protein methylation; IEA:UniProt.
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..324
FT /note="Ribosomal lysine N-methyltransferase 5"
FT /id="PRO_0000411044"
FT BINDING 90
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 140..142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 162
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 217
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 247
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
SQ SEQUENCE 324 AA; 36820 MW; 750044E3D0D15863 CRC64;
MSGLLQLDEE SLYDHIFERY TLLTSNNDSL KQDLGIVDRT VSKITIDIDQ FDFNNKKSNN
DFYSIEINQP ITSLNSSSVN NNSTTGYVVW STTPFFTRWL IFHSNASIFR NGGSIELIDQ
DDELKLPPMF SNSVGLLELG SGIAGILPVT LGNFVGSFIA TDQIGILSTL KTNILENLSQ
LNRKIVTSRS LNLNLDVDES TLLKRSLLSL ECLPLDWELF DIKDTTKLDP ALLSLFKEKE
TIYVLAMDVI YNEYLIESFL STIQNLKSLA FKFNVNLNCL IGIQLRSEEV TTLFLEKAII
DYEMKVYYIQ DNILESSRFS IYMI