ID A0A3Q1FTZ2_9TELE Unreviewed; 2231 AA.
AC A0A3Q1FTZ2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184, ECO:0000256|RuleBase:RU361211};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184, ECO:0000256|RuleBase:RU361211};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000010090.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000010090.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000256|ARBA:ARBA00000780,
CC ECO:0000256|RuleBase:RU361211};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU361211}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107, ECO:0000256|RuleBase:RU361211}.
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DR Ensembl; ENSAPOT00000000534.1; ENSAPOP00000010090.1; ENSAPOG00000012511.1.
DR GeneTree; ENSGT00940000156962; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd04301; NAT_SF; 1.
DR CDD; cd15618; PHD1_MOZ_MORF; 1.
DR CDD; cd15527; PHD2_KAT6A_6B; 1.
DR Gene3D; 3.40.630.30; -; 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; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR048589; SAMD1-like_WH.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF26; HISTONE ACETYLTRANSFERASE KAT6A; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF21524; SAMD1_WH; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00526; H15; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51504; H15; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|RuleBase:RU361211};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 116..195
FT /note="H15"
FT /evidence="ECO:0000259|PROSITE:PS51504"
FT DOMAIN 230..289
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 286..337
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 518..792
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 66..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..1608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1643..1965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2021..2052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..379
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..818
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..893
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1037
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1069
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1191
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1346
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1391..1422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1469..1483
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1494..1509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1531..1567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1582..1598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1709..1783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1793..1865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1866..1882
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1883..1918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1919..1937
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2030..2044
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 694
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 2231 AA; 245368 MW; 7817587A1AAC7707 CRC64;
MVKLANPMYT QWILEAIKKV KKQKQRPSEE RICNAVSMSH GLDRKTVLEQ LELSVKDGTI
LKVTNKGLNS YKDPDNPGRL ALPKPKGGGG GGGGGGSSSS GGGGGGSSHS HSGKKPGLDW
NKLIKRALEG LHEPGGSSLK NIERFLKCQA DVAAYLSGSG SMGPGLFHQQ LRVALKRAVA
HGRVVKQGPL FQLISRSSSQ DDGTGTVSLE SLPPVRLLPH EKDKPVAEPI PICSFCLGTK
EQNRDKKPEE LISCADCGNS GHPSCLKFSP ELTARVKALW WQCIECKTCS SCQDQGKNAD
NMLFCDSCDR GFHMECCDPP LTRMPKGMWI CQICQPRKKG KKLLHEKAAQ IKRRYNAPLG
RPKNRPGRPF KKLGGRGRRK RSASANSSSS SSCEGYPGDD RLLFSMRDDD DLSHSSLRFN
NKTKGLIDAL TKFFTPSPEG RKARQEVVDY SQQCRIRKKA NRKGEGDDRG DNQEGSDWRD
EDEKLPGHEN LTEKDIELFR HIQELALQKV GVTGPPDPQM RCPSVIEFGK FEIQTWYSSP
YPQEYSRLPK LYLCEFCLRY MKSRSILYQH MKKCSWFHPP ANEIYRKDDV SVFEVDGNVS
TIYCQNLCLL AKLFLDHKTL YYDVEPFLFY VLTQNDSKGC HLVGYFSKEK HCQQKYNVSC
IMILPQYQRK GYGRFLIDFS YLLSKQEGQP GSPEKPLSDL GRLSYMAYWR SVVLECLHEV
RDQQITIRQL SKLTGICPQD ITTTLHSLTM LEQRGDRLVL VRRDKLVTTH MARLKARPRQ
LEVDPECLRW TPVIVTNTVV SDADGDDDEE EDDDELDEDN RKEIKPSHKV PPMSWHMRQM
KARDEEEEEE EEEERKGFLG FPISQSSPTS PPIRCPPPVP EPPRPPPPTN GERRPRGRPP
KNWPWGKVKD SARVGRPSKI RPMEDEDDED DERAEGGKTT GSGSSPPSLF SLDRQADSTA
FRSLDMARHP SITPTRRGRP PRKKRGPKPR LTEGPGEGLT QLPGISRLNE SPPVRKSCFS
ESSEEEEDDD DDEDDEERRA CSPPILTKPA MGLKCKKPLR KRRFRQRSHP HSSVVTETIS
ETTEVLDEPF VDSDSERPMP RLEEETPLGH PLRRYPPARS ALRLSDPAPK RSRHSNLTDS
EEDDITPVLK PVAALPAAPS ETLVANPEVP VKKKKGWPKG KSRKPLHWKK RGPGKPPSGG
PNQRAAAESQ VQSGDPQPPK IKMKPGRKPR SWYLQRAQEE AERQEQERRR LLEQQMDKDP
QLLQTDDHNS KRIGRTNTDR DNKQKDSDEE DDYLPKPVEQ KVPKRRGRPP KNRALHQPPQ
PAPKPPPTSE PEEEEEDDDE EETERTWEED KPSRPPSRPL LSPSSSSSTS GPRAPQSRIN
RRTAATPGSG SRRSEDHDAD DEGDGHLEDK SNSSKKRKSQ DSEDDDDDED EEEDNASHAN
SPPVKEEPQG GEAFLDMENS VARDYVSKQE EEEEEEEEAE EEVQEAKCQP SSADPQQEER
RRREQEESAA AAAAVETVTA MSVPTEPMEL QPLHPDDKDV TLLMEPQHTH PHSHPHQHSD
FKEELAHHHP HHPHHHSNEL DLETMQAVQS LTQGEAQDEE TEPQPHHGAY QDCEETLAAC
RTLQSYSHTG EAEEEALTLV EECGASQHSS PLPNPPVPPL PSQSVRSVNS PGLPSGIVDT
TPAGQRGGTP GPTGAGASGG GAGGGYTQIT PEHPSSLSAP SQQNMETSPM MDVPSVSDHS
QQVVDSGFSD LGSIESTTEN YDNPSSYDST MGGGGNGTGN GGNGGGMSAG VVAGASTASS
SSVSSSSSSA TPSSSSQSNS CSFVPAPSLT SSTGSGSSQL GMGSCSLIQQ TGPGPNSGPS
ASNVGSAVPQ PPPPPPPSNT PSCGIKSPQS CGVIERPPST NQQQQQQSQK KVPQQQQQQA
PNPQPPPSAP PPPPQQALSQ CSMGNGFAST PMIMEIPESG SGGGGRTLYE RMGQDFGTGG
YPQPSATFSL AKLQQLTNTI MDPHAMPYSH SASVTSYATS VSLSNPGLAP SPHTPLPQGQ
PTMTPPPNLS SGSMNLGSLQ LQCNMPATNI GLGPPPHTQR LQGQMTTVKG HISIRSKATQ
QLAPAPHQQQ LYSRSSGAVA MQGTPRTLAV QRGMMPNLMP TSAYSSMNMP LNAMSGGYRM
PQPMMNSGYH SNPAYMNQPA QYPMQMQMGM MGGQGYPQQP MQPNHHGNMM YTGPSHHSYA
GVPKQSPYMS R
//
