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   03-AUG-2022, entry version 59.
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}.
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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   CTD; 444061; -.
DR   Xenbase; XB-GENE-988094; smyd5.L.
DR   OrthoDB; 1001347at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 444061; Expressed in neurula embryo and 19 other tissues.
DR   GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0034773; P:histone H4-K20 trimethylation; ISS:UniProtKB.
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; 2.170.270.10; -; 1.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR044422; SMYD5_SET.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF82199; SSF82199; 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