ID A0A1S3NPG8_SALSA Unreviewed; 2246 AA.
AC A0A1S3NPG8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
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};
GN Name=LOC106580491 {ECO:0000313|RefSeq:XP_014017096.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014017096.1};
RN [1] {ECO:0000313|RefSeq:XP_014017096.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014017096.1};
RG RefSeq;
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 RefSeq; XP_014017096.1; XM_014161621.1.
DR STRING; 8030.ENSSSAP00000095768; -.
DR PaxDb; 8030-ENSSSAP00000095768; -.
DR GeneID; 106580491; -.
DR CTD; 7994; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000087266; Chromosome ssa20.
DR Bgee; ENSSSAG00000072653; Expressed in brain and 16 other cell types or tissues.
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; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
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; 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; 2.
DR Pfam; PF21524; SAMD1_WH; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00384; AT_hook; 4.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
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:UP000087266};
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 113..192
FT /note="H15"
FT /evidence="ECO:0000259|PROSITE:PS51504"
FT DOMAIN 226..285
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 282..333
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 521..795
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 70..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..1535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1567..1594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1664..1833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1858..1990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2038..2069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2111..2135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..384
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1038
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1071
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1198
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1570..1594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1718..1833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1858..1876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1891..1924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1925..1944
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2115..2135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 697
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 2246 AA; 247387 MW; 52AE91250DFFB89A CRC64;
MVKLANPMYT TWILEAIKKV KKQKQRPSEE RICNAVSMSH GLDRKTILEQ LELSVKDGTI
LKVSNKGLNS YKDPENPGRL AYPKPRLGSG GGGGGHHGHV GHGGSHHRSG KKPGLDWNKL
IKRSLEGLHE PGGSTLKSVE RFLKCQGDVA AYLSGSGSMG PGLFHQQLRV ALKRACAHGR
VAKNGPLFHL ISRSSQLDGT GTVALDSLPP VRLLPHEKDK PVAEPIPICS FCLGTTESNR
DKKPEELISC ADCGNSGHPS CLKFSPELTV RVKALWWQCI ECKTCSNCQD QGKNAENMLF
CDSCDRGFHM ECCDPPLMRM PKGMWICQIC QPRKKGRKLL HEKAAQIKRR YNAPLGRPKN
RPGRPFKKLR GPGGRGRRKG GRRSQGSSSP HSSSSSSCEG YPGDDRLLFS LREDSSEQGG
LRFNKKTKGL IDALTKFFTP SPDGRKAQHE VDYSQQYRIR KKAIRKEEGD DRTDNQDSSD
WREDEDKLPG HENLTEKDVE LFRHIQELAL QKVGVTGPPD PQMRCPSVIE FGKFEIQTWY
SSPYPQEYSR LPKLYLCEFC LRYVKSRSIL FQHMRKCAWF HPPANEIYRK DGVSVFEVDG
NVSTIYCQNL CLLAKLFLDH KTLYYDVEPF LFYVLTQNDS KGCHLVGYFS KEKHCQQKYN
VSCIMILPQY QRKGYGRFLI DFSYLLSKQE GQPGSPEKPL SDLGRLSYMA YWRSVVLECL
HEVRDRQLTI RRLSKITGIC PQDITATLHH LNMLEQRGER LVLVRKEKLV SSHMACLTAR
PRLLEVDPDC LRWTPVIVTN TVVSEEEEEE EGDDTCKEIK PSHKVSPLSW LVRGEEEEEE
EMMIKCFPGF PTSQSSPASS PVRCPPPVLD HRSPPPANGE RRGRGRPPKN WPWGKVKDGP
RTERRPGPGR PPKMRLEVQD FDEEEDRAEG TKISPTSGSS PPSLFSLDRQ LADSTGTFRP
LEMLGRHPAV PPPRSRGRPP RKKRGPKRRL SEGPGETLPQ LPLAPRLSDP PPVRRSCFSE
SSEEEEEEED DEDDDDEERG THSPPILTKP TLGLKCKKPL RKRRMRQRSH SHAHSSVVTE
TISETTEVLD EPFVDSDSER PMPRLEEESP LGHPLRCYPP ARPALRHTET PPKRAQRANL
TESEEDEPTP VLKPPSFLRN PESTASAETP AANPEAPVKK KKGWPKGKPR KPLHWKKRPG
RPPGSGAKQN AGDTSLTNSG DPPPPKIKMK PGRKPRSWYL QRAQEEAERQ EAERQRLSLG
GVQQLDKPLQ QLEDRACKRA SRATATDNDK HKDSDEEDDY LPKPVEQRIP KRRGRPPKNP
ALRQQPVPKQ PTVSEPEEEE ETERSWVEDK PSRPPSRSLL SPSSTGGPRA PQPSRPDTDR
VMADRDEEDE EREDEECATL GTSSRRTATT PGSGSRRSDD HDADDEGDGH LEDKSKSKKR
KSQDSEEEDE DDEEEPTSPA SSPPVKEEPQ GGECFLDMQG SVQARDSYVS KQEEDEEEDE
EAEELQEVKC RPLDAAQDER RRREAEESAA AAAAVETVTA ISVPSEPLEL QLLHPEDKTV
TLLMEPQHPH QHPDSFKEEL SHHHGSHHGQ HHHSNELDLE TVQAVQSLTQ GEAQDEEPES
HGVSHGAYQD CEETLAACRT LQSYSHAGEA EEETTHLALV EECGASQHSS PLPHTNPPMP
PLPSQSVRSI NSPAGMMESG LGQQRGGTPG PTGGTGATGG GGYTQITPEH PSSLSAPSQH
NMETSPMMDV PSVSDHSQQV VDSGFSDLGS IESTTENYDN PSSYDSTMGG GGNGGGNNGS
NHAAVAVAAS SSSSTGSSSS SSVTPSSQGS SCSFVPAPCL TSSSGAVTSQ LAMGSCSLIQ
QTGPGPNNGP GGNNGGNNSV PPPPPRPPSA NTHQGIKSPQ SCVIERLPSA SQQSQKKVQH
QPPQQQQAPH PPPSAPPTPH PPQQQQPLSQ CSMGNGFGST PMIMEIPESA SQGGGRSLYE
RMGQDFGAGG YPQPSATFSL AKLQQLTNTI MDPHAMPYSH SASVTSYATS VSLSNPGLAQ
LSPSPLPPLA QGQATMTPPP QLSSGSMNLG SLQLQCNMPS SNIGLPPPPH TQRLQGQMAT
VKGHISIRSK AQLAPAPSPH QQQLYGRSSG AVAMQGSPRT LAVQRGMMPN LMPTPAGYNT
MNMNQLNAMS AGYRMPQPMM NSGYHGNPPY MNQPAQYPMQ MQMGMMGGQG YPQQPMQPNH
HGNMMYTGPT HHSYAGVPKQ SPYMSR
//
