ID A0A384BUS3_URSMA Unreviewed; 611 AA.
AC A0A384BUS3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 2.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=KAT7 {ECO:0000313|RefSeq:XP_008686333.2};
OS Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008686333.2};
RN [1] {ECO:0000313|RefSeq:XP_008686333.2}
RP IDENTIFICATION.
RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008686333.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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DR RefSeq; XP_008686333.2; XM_008688111.2.
DR SMR; A0A384BUS3; -.
DR STRING; 29073.ENSUMAP00000021124; -.
DR KEGG; umr:103660491; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000261680; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 4.10.320.30; -; 1.
DR Gene3D; 3.30.60.60; N-acetyl transferase-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR InterPro; IPR002515; Znf_C2H2C.
DR InterPro; IPR036060; Znf_C2H2C_sf.
DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF210; HISTONE ACETYLTRANSFERASE KAT7; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF01530; zf-C2HC; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF103637; CCHHC domain; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS51802; ZF_CCHHC; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000261680};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01143}.
FT DOMAIN 332..607
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 508
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 611 AA; 70642 MW; 8368E7C4F07D8D7C CRC64;
MPRRKRNAGS SSDGTEDSDF STDLEHTDSS ESDGTSRRSA RVTRSSARLS QSSQDSSPVR
NLQSFGTEEP AYSTRRVTRS QQQPTPVTPK KYPLRQTRSS GSETEQVVDF SDRETKNTAD
HDESPPRTPT GNAPSSESDI DISSPNVSHD ESIAKDMSLK DSGSDLSHRP KRRRFHESYN
FNMKCPTPGC NSLGHLTGKH ERHFSISGCP LYHNLSADEC KVRAQSRDKQ IEERMLSHRQ
DDNNRHATRH QAPTERQLRY KEKVAELRKK RNSGLSKEQK EKYMEHRQTY GNTREPLLEN
LTSEYDLDLF RRAQARASED LEKLRLQGQI TEGSNMIKTI AFGRYELDTW YHSPYPEEYA
RLGRLYMCEF CLKYMKSQTI LRRHMAKCVW KHPPGDEIYR KGSISVFEVD GKKNKIYCQN
LCLLAKLFLD HKTLYYDVEP FLFYVMTEAD NTGCHLIGYF SKEKNSFLNY NVSCILTMPQ
YMRQGYGKML IDFSYLLSKV EEKVGSPERP LSDLGLISYR SYWKEVLLRY LHNFQGKEIS
IKEISQETAV NPVDIVSTLQ ALQMLKYWKG KHLVLKRQDL IDEWIAKEAK RSNSNKTMDP
SCLKWTPPKG T
//
