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 27-MAR-2024, entry version 83.
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.ENSGALP00000057344; -.
DR PaxDb; 9031-ENSGALP00000025878; -.
DR Ensembl; ENSGALT00000108478; ENSGALP00000075029; ENSGALG00000022920.
DR Ensembl; ENSGALT00015029677; ENSGALP00015017191; ENSGALG00015012193.
DR GeneID; 422951; -.
DR KEGG; gga:422951; -.
DR CTD; 10322; -.
DR VEuPathDB; HostDB:geneid_422951; -.
DR eggNOG; KOG2084; Eukaryota.
DR HOGENOM; CLU_054216_0_0_1; -.
DR InParanoid; Q5ZIZ2; -.
DR OMA; LMAMYQQ; -.
DR OrthoDB; 56553at2759; -.
DR PhylomeDB; Q5ZIZ2; -.
DR PRO; PR:Q5ZIZ2; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000022920; Expressed in brain and 13 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; 2.
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..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
//
