ID W5MSG3_LEPOC Unreviewed; 419 AA.
AC W5MSG3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Histone-lysine N-trimethyltransferase SMYD5 {ECO:0000256|ARBA:ARBA00026238};
DE EC=2.1.1.372 {ECO:0000256|ARBA:ARBA00024057};
DE AltName: Full=SET and MYND domain-containing protein 5 {ECO:0000256|ARBA:ARBA00033038};
DE AltName: Full=[histone H4]-lysine20 N-trimethyltransferase SMYD5 {ECO:0000256|ARBA:ARBA00029994};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000011322.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000011322.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00023940};
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DR EMBL; AHAT01015459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MSG3; -.
DR STRING; 7918.ENSLOCP00000011322; -.
DR Ensembl; ENSLOCT00000011337.1; ENSLOCP00000011322.1; ENSLOCG00000009281.1.
DR eggNOG; KOG2084; Eukaryota.
DR GeneTree; ENSGT00510000047420; -.
DR InParanoid; W5MSG3; -.
DR OMA; LMAMYQQ; -.
DR Proteomes; UP000018468; Linkage group LG4.
DR Bgee; ENSLOCG00000009281; Expressed in ovary and 13 other cell types or tissues.
DR GO; GO:0042799; F:histone H4K20 methyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060216; P:definitive hemopoiesis; IEA:Ensembl.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IBA:GO_Central.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IEA:Ensembl.
DR GO; GO:0060215; P:primitive hemopoiesis; IEA:Ensembl.
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 InterPro; IPR002893; Znf_MYND.
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 Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 20..356
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 386..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..419
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 419 AA; 47256 MW; F0DA3D5C0DC9D775 CRC64;
MAAPSGDMFS FCSEPGKVGG LVEVRFIDKV KGRGLFAKKA ICKGENIFIE RPLVSAQFLW
NALYKYRAPA CEYCLRSLET AEENARRLSG NASLLLPHPE QCSIRPELHQ ACPRCQVMYC
STECRRAALE QYHQVLCLGQ SRDDLEHPLN KLQEAWRSMH YPPETASIML MARMVAIVKQ
VEAQDKGHWL SIFSQLCSRT ASEQEEQIAH KLLGEKFQGQ LESLRNLFTA ALYDDHLSRW
FSPEGFRSLF ALVGTNGQGI GTSSLSQWVH GCDALELPVQ PREQLDAYID QLYKDIETET
GDFLNCEGSG LFLLQSSCNH SCFPNAEASF PDNNFLLHLT ALSDITAGEE ICISYLDCCQ
RERSRHSRHK ILRENYLFVC SCPKCHSQAD DPDVTSEEEE EEGDGETEGD DLEDEMTDV
//
