ID SMYD5_XENLA Reviewed; 421 AA.
AC Q6GPQ4;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Histone-lysine N-trimethyltransferase SMYD5;
DE EC=2.1.1.372 {ECO:0000250|UniProtKB:Q3TYX3};
DE AltName: Full=SET and MYND domain-containing protein 5;
DE AltName: Full=[histone H4]-lysine20 N-trimethyltransferase SMYD5;
GN Name=smyd5;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Histone methyltransferase that specifically trimethylates
CC 'Lys-20' of histone H4 to form trimethylated histone H4 lysine 20
CC (H4K20me3) which represents a specific tag for epigenetic
CC transcriptional repression. {ECO:0000250|UniProtKB:Q3TYX3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:64456, Rhea:RHEA-COMP:15554, Rhea:RHEA-
CC COMP:15998, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.372;
CC Evidence={ECO:0000250|UniProtKB:Q3TYX3};
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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; BC073058; AAH73058.1; -; mRNA.
DR RefSeq; NP_001085635.1; NM_001092166.1.
DR AlphaFoldDB; Q6GPQ4; -.
DR BioGRID; 102224; 1.
DR DNASU; 444061; -.
DR GeneID; 444061; -.
DR KEGG; xla:444061; -.
DR AGR; Xenbase:XB-GENE-988094; -.
DR CTD; 444061; -.
DR Xenbase; XB-GENE-988094; smyd5.L.
DR OrthoDB; 56553at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 444061; Expressed in neurula embryo and 19 other cell types or tissues.
DR GO; GO:0042799; F:histone H4K20 methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0140943; F:histone H4K20 trimethyltransferase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISS:UniProtKB.
DR GO; GO:2000736; P:regulation of stem cell differentiation; ISS:UniProtKB.
DR GO; GO:2000035; P:regulation of stem cell division; ISS:UniProtKB.
DR CDD; cd10521; SET_SMYD5; 1.
DR Gene3D; 1.10.220.160; -; 1.
DR Gene3D; 6.10.140.2220; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044422; SMYD5_SET.
DR PANTHER; PTHR46402:SF2; HISTONE-LYSINE N-TRIMETHYLTRANSFERASE SMYD5; 1.
DR PANTHER; PTHR46402; SET AND MYND DOMAIN-CONTAINING PROTEIN 5; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50280; SET; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..421
FT /note="Histone-lysine N-trimethyltransferase SMYD5"
FT /id="PRO_0000227791"
FT DOMAIN 20..351
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 97..135
FT /note="MYND-type"
FT REGION 386..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..421
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 350
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
SQ SEQUENCE 421 AA; 48219 MW; 9F5A1D8AC57961D1 CRC64;
MAASMCDVFA FCAEQEPARR TVEIRFVSSG KGKGLFAIRT IRKGETIFQE KPLVSSQFQW
NALYRYRACD HCLRSLETAE ENAQRLSGNA HVLLPYPELC TVRNGLHQQC PRCQVTYCSA
ECLKAAAEQY HQILCLETSR DNPAHPLNKL EEAWRNMHYP PETASIMLMA RMVGTIKQAQ
DKDWWLHLFS QFCNKTANEE EEIVHKLLGE KFKGQLDQLR RLFVDALYEE RMSRWFTPEG
FRSLFALVGT NGQGIGTSSL SQWVHACDAL ELPPRDREKL DALIDQLYKD IEKVTGEFLN
CEGSGLYLLQ SCCNHSCVPN AEASFPDNNF ILHLTALEDI QPGEEICISY LDCCQRDRSR
HSRQKILREN YLFMCSCPKC LAQADEPDIT SEEEEEEEEE DDAELEGEPE DAELEDEMTD
V
//
