ID V8NTA2_OPHHA Unreviewed; 1577 AA.
AC V8NTA2;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
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};
DE Flags: Fragment;
GN Name=Kat6a {ECO:0000313|EMBL:ETE64777.1};
GN ORFNames=L345_09453 {ECO:0000313|EMBL:ETE64777.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE64777.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE64777.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE64777.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE64777.1}.
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DR EMBL; AZIM01002113; ETE64777.1; -; Genomic_DNA.
DR Proteomes; UP000018936; Unassembled WGS sequence.
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; 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; PF00538; Linker_histone; 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; 1.
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.
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:UP000018936};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ETE64777.1};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 95..171
FT /note="H15"
FT /evidence="ECO:0000259|PROSITE:PS51504"
FT DOMAIN 482..756
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 314..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..809
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..868
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..893
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..934
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..989
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1067
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 658
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE64777.1"
SQ SEQUENCE 1577 AA; 176118 MW; 12444542BD6AB723 CRC64;
MVKLANPLYT EWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRKTVLEQ LELSVKDGTI
LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDGKPNVDWN KLIKRAIEGL AESSGSSLKN
IERYLKGQKD VSALFASGAP STFHQQLRLA IKRAVGHGRL LKDGPLYQLN TKAATHADGK
ESCESLSCLP PVSLLPHEKD KSCSFVALLT GRDEKRVSQL LNQSQSAVSA LVQKNKTEKR
NPRSSSLVPI AATADNMLFC DSCDRGFHME CCDPPLTRMP KGMWICQICR PRKKGRKLLQ
KKAAQIKRRY ANPIGRPKNR LKNQNATSKA PFSKVQTGPG RGRKRKTPLS SQSTCSSDGG
YLDQVDGLEF CGDASITLKF NKKTKGLIDG LTKFFTPSPD GRKARGEVVD YSQQYRIRRK
DNRKSSTSDW PTDNQDGWDG KQENEEWLLG GPDVMAEKDM ELFRDIQEQA LQKVGVTGAH
DPQVRCPSVI EFGKYEIHTW YSSPYPQEYS RLPKLYICEF CLKYMKSRTI LQQHTKKCGW
FHPPANEIYR KSNVSVFEVD GNVSTIYCQN LCLLAKLFLD HKTLYYDVEP FLFYVLTQND
MKGCHLVGYF SKEKHCQQKY NVSCIMILPQ YQRRGYGRFL IDFSYLLSKR EGQAGSPEKP
LSDLGRLSYM AYWKSVILEC LYHQNDKQIS IKKLSKLTGI CPQDITSTLH HLRMLDFRSD
QFVIVRREKL IQDHMAKLKL NTRPVVVDPE CLRWTPVIVS NSVVSEDEED DPEETEMEVP
QQLRERDIEV RMRGKPIPRK RRVRKRKHHN SSVVTETISE TTEVLDEPFE DSDSERPMPQ
LEPTFEMEDE EEEEEEEXXE EEEEEEEEEX RRRGGGGGGR RRGGGRGGRR GGGRKRIPGT
STPMKKKKGW PKGKSRKPIH WKKRPGRKPG FQLRRGKVRA PTSEETTDLM EPCSKSGRKM
KVQDEEELAE EKEELLPSAE ERKDEDGPPE VGDLGEEEDI MPAREARATS PVDSSNSPEM
DSKEPELEED VEKPQVLEDQ RPPSEEEQQE AEEPEHDQEE EEEEVAAVAN QHEDHDADDE
EDDGHLGSVK KDELEEQAEK EGLKEEPEVQ EPFLETSTQD NREEDAKNKS EGEGDSEEDP
VSHETSVGSD PVPGSEDDQE EEQHPKEGLM ELKEDEPIPH SELDLETVQA VQSLTQEEDN
HEHDVAYQDC EETLAACQNL QSYTQAEEDP QMPMVEDCQA SEHNSPISSV QSHPSQSVRS
VSSPSVPGAL ESSYTQISPE QGSLSAPSMQ NMETSPMMDV PSVSDHSQQV VDSGFSDLGS
IESTTENYEN PSSYDSTMGG SICGNASSQS SCSYGGLSSS SSLTQNSCVV TQQMAGMGSS
CSLLPRGSVQ PATNCNINIY ERLPSDFGAG GYSQPSATFS LAKLQQLTNT IMDPHAMPYS
HSSAVTSYAT SVSLSSTGLA QLAPSHPLAG AAQAQATMTP PPNLAPTTMN LTSPLLQCNM
STANLGIPHT QRLQGQMPVK GHISIRSNNL KGSLEGPQSS SCNSVDFLCP PEDGKAESLG
LPALVFSLEF LSMCRTL
//
