ID   SMYD5_CHICK             Reviewed;         420 AA.
AC   Q5ZIZ2;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 76.
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; ORFNames=RCJMB04_22j23;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720642; CAG32301.1; -; mRNA.
DR   RefSeq; NP_001012912.1; NM_001012894.1.
DR   AlphaFoldDB; Q5ZIZ2; -.
DR   STRING; 9031.ENSGALP00000025878; -.
DR   Ensembl; ENSGALT00000072661; ENSGALP00000057344; ENSGALG00000022920.
DR   GeneID; 422951; -.
DR   KEGG; gga:422951; -.
DR   CTD; 10322; -.
DR   VEuPathDB; HostDB:geneid_422951; -.
DR   eggNOG; KOG2084; Eukaryota.
DR   GeneTree; ENSGT00510000047420; -.
DR   HOGENOM; CLU_054216_0_0_1; -.
DR   InParanoid; Q5ZIZ2; -.
DR   OMA; LMAMYQQ; -.
DR   OrthoDB; 1001347at2759; -.
DR   PhylomeDB; Q5ZIZ2; -.
DR   PRO; PR:Q5ZIZ2; -.
DR   Proteomes; UP000000539; Chromosome 4.
DR   Bgee; ENSGALG00000022920; Expressed in brain and 13 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; -; 2.
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..420
FT                   /note="Histone-lysine N-trimethyltransferase SMYD5"
FT                   /id="PRO_0000227790"
FT   DOMAIN          29..358
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   ZN_FING         104..142
FT                   /note="MYND-type"
FT   REGION          392..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..420
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         357
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
SQ   SEQUENCE   420 AA;  46968 MW;  1DE51D720257EB7B CRC64;
     MAAAAGDVRG AALGARPGLG AAAAAAAAAE ARFISSAKGK GLFATRSIRK GEAVFVEKPV
     VSSQFLWNAL YNYRACDHCL RALETAEENA QRLLGRSSLV LPHPEQCSIR KDLHQQCPRC
     QVTYCSAECR QAALEQYHQV LCLGPSRDDP THPLNKLQEA WRNMHYPPET SSIMLMARMV
     ATVKQAKDKD WWIKAFSQFC SKTANEEEEI AHKLLGDKFK GQLELLRLLF TEALYDEQLS
     RWFTPEGFRS LFALVGTNGQ GIGTSSLSQW VHACDALDLP MLQREELDAF IDQLYKDIEK
     ESGEFLNCEG SGLYMLQSCC NHSCIPNAET SFPDNNFLLY LTALEDIEAG EEICISYLDC
     CQRERSRHSR NKILRENYLF TCSCPKCLAQ ADDPDVTSDE EEEAEGETDD AELEDEMTDV