UniProt: A0A2D0PLV7

Database: UniProt
Entry: A0A2D0PLV7_ICTPU

LinkDB:  A0A2D0PLV7_ICTPU 
Original site:  A0A2D0PLV7_ICTPU

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Ontology (13)   
   GO (13)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (5)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (2)   
   RefSeq(pep) (2)   
Protein domain (22)   
   InterPro (12)   
   Pfam (4)   
   PROSITE (3)   
   SMART (3)   
All databases (43)   

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ID   A0A2D0PLV7_ICTPU        Unreviewed;      2199 AA.
AC   A0A2D0PLV7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=kat6a {ECO:0000313|RefSeq:XP_017306984.1,
GN   ECO:0000313|RefSeq:XP_017306985.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017306984.1};
RN   [1] {ECO:0000313|RefSeq:XP_017306984.1, ECO:0000313|RefSeq:XP_017306985.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017306984.1,
RC   ECO:0000313|RefSeq:XP_017306985.1};
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_017306984.1; XM_017451495.3.
DR   RefSeq; XP_017306985.1; XM_017451496.3.
DR   STRING; 7998.ENSIPUP00000025984; -.
DR   Ensembl; ENSIPUT00000027057; ENSIPUP00000025984; ENSIPUG00000017536.
DR   GeneID; 108255509; -.
DR   KEGG; ipu:108255509; -.
DR   CTD; 7994; -.
DR   OrthoDB; 118560at2759; -.
DR   Proteomes; UP000221080; Chromosome 22.
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:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR   GO; GO:0001502; P:cartilage condensation; IEA:Ensembl.
DR   GO; GO:0010172; P:embryonic body morphogenesis; IEA:Ensembl.
DR   GO; GO:0009880; P:embryonic pattern specification; IEA:Ensembl.
DR   GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR   GO; GO:0014036; P:neural crest cell fate specification; IEA:Ensembl.
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; 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; 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; SM00384; AT_hook; 3.
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   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          97..177
FT                   /note="H15"
FT                   /evidence="ECO:0000259|PROSITE:PS51504"
FT   DOMAIN          212..271
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          268..319
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          530..804
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51726"
FT   REGION          65..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          363..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          810..1115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1127..1513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1540..1572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1629..1906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1994..2029
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2069..2089
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..381
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        452..501
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        814..830
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..863
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        864..888
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        916..937
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        938..954
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        999..1020
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1053..1068
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1089..1107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1132..1146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1178..1193
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1198..1223
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1235..1300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1339..1356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1394..1426
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1486..1509
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1547..1570
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1682..1812
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1833..1850
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1862..1880
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1881..1903
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        706
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ   SEQUENCE   2199 AA;  242533 MW;  26AD535E8747DC1E CRC64;
     MVKLANPLYT AWILEAIKKV KKQKQRPSEE RICNAVSTSH GLDRQTVLEQ LELSVQDGTV
     LKVSNKGLNS YKDPDNPGRL VPPKPKGGVS TGGSGASKKA ALDWNKLIRR ALEGLHESGG
     SSLRSIERFL KCQADVASQL TGTAAPRIFH QQLRLALKRA VGHGRVLKHG PLFRLASSND
     GSDAGDGRVA LESLPPVRPL PHEKDRPVAE PIPICSFCLG TKEQNRVKEP EELISCADCG
     NSGHPSCLKF SPELTARVKA LWWQCIECKT CSSCQDQGKN AENLLLCDSC DRGFHMECCD
     PPLTRMPKGM WICQICRPRK KGRNVLHEKA AQIKRRYNAP LSRQKGRHIN RCEILLWKKP
     GRPFKKLRGS GRGRRRRGPG ASHSRGSASP HSSSSSSCDG YLGEGYPGDD RLLFSRRDDE
     DESQGAARFN RKTKGLIDAL SKFFTPSPDG RKSRTESLDY AEQHRIRKKS GRKSDAHQRA
     GDNQDCSDDW KEDEEKLPGH ENLTEKDMEL FRHIQELALQ KVGVTGPPDP QMRCPAVIEF
     GKYEIQTWYS SPYPQEYSRL PKLYLCEFCL RYMKSRSILY QHMRKCTWFH PPANEIYRKD
     DVSVFEVDGN VSTIYCQNLC LLAKLFLDHK TLYYDVEPFL FYVLTQNDSK GCHLVGYFSK
     EKHCQQKYNV SCIMILPQYQ RKGYGRFLID FSYLLSKREG QPGSPEKPLS DLGRLSYMAY
     WRSVVLECLH EVRDRKLTIR RLSKITGICP QDITATLQNL NMLEHRGDRL ILVRREKLVS
     THMARLHARP RLLEVDPDCL RWTPVIVANP VVSDEDGDGD DDEDEEEDGE KENNKDMKSN
     RKSSPLPWNT RVDKEDNEEK KCFPTFPKNQ SSLPSSPIRN SLPSPEATPL QANGERRGRG
     RPPKNWPWGK VKDQPRPGPG RPRKTRPKED DDEEYPSQNK MTPVSLSPSP LFASEKEPNC
     TERLFGASRH SAIPPPRNRG RPARKRGGPK RRLNEESGDD VPSLTTAPRL SESPVPHSCS
     SESSEDDDDD DDYNEEMGTR SPPILTKPTL GLKSKKLPRK RRIRQRSHPH SSVVTETISE
     TTEVLDEPFV DSDSERPMPR LEEETPFGHS LRCYPPARKH LDSTLKMIRP TNLSESDEDD
     HTPVLKPVSG LRRPETAALE GEEPSTVTPE VPLKKKKGWP KGKSRKPQHW KKGPGRKPGS
     GTTNQVADTG LTAQSSEETP RQSVQSKPGR KRRNYYPQQT KDEGARAELD RSHLSQLQLE
     KPEDRTFKRR PLTSDFDCEK HKDSEEEGIF PQQTREQPKP RRRGRPPKKA NLEPPVSKPA
     PVSEPEEEEE EDQTWSEEKP SRSPSCNLSQ VSGPRVPQNR DGDMADQEED EEREDEDHNN
     SGSRRTGAIS GSGSRRSDDH DADDEGDGRL EEKSDSGKRR KNQDSEDDDD EELEDGEEEP
     SSPPRSPPVK EEPQSGEGFL DMQESGSREY IHKQEVVEDE DEEDEVREVK TRSVDSQDER
     RRRELEESAA AAAAVETVTS IAIPSDSPHM QSMDSKSDLL METGHPHANS EFKDELSHHP
     HDHHHSSELD LETVQAVQSL TQGEAQDEEA EPHGAYQDCE ETLAACRTLQ NYSHGEGEEE
     SLAMVEDCGA SQHSSPMPNP PMPPLASQSV RSVNSPGMTP GPLETGPGVS GPAGGNGGGY
     TQITPEHPSS LSAPSLQNME TSPMMDVPSV SDHSQQVVDS GFSDLGSIES TTENYDNPSS
     YDSTMGGGGG SGGNSGSGSS MSVTVAAVSS ASSSSSTPSS SSQGNSCSFV STPGMSSSSA
     SVGSQLAMGS CSLIQQAGPG PGPNGGPGST SGSTVPQPPP PPPPPSANTP GCGIKSPQSC
     VIERPPSASQ QQQQKKVPQQ QQPPNPQPQP APSAPPPPPP QQQALSQCSM GNSFASTPMI
     MEIPESAGSG GSGRSIYDRM GQDFGAGSYA QPSATFSLAK LQQLTNTIMD PHAMSYSHSA
     AVTSYATSAT LPNPSLAQLT SSPHPPLPQA QATMTPPPNL SSSSMNLGTS LIQCNMPGAN
     IGLPPPPHTQ RLQGQMATVK GHISIRSKAS QIQAGSPHQQ QIYGRSSMQG SPRTLAVQRG
     MMTNLMPTPA AYNSMNMNPL NAAMSAGYRM PQPMMNSGYH SNYMNQPAQY PMQMQMGMMG
     GQAYPQQPMQ PNHHGNMMYA GPSHHSYAGV PKQSPYMSR
//

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