ID A0A3B3X3G8_9TELE Unreviewed; 2114 AA.
AC A0A3B3X3G8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000009596.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000009596.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_014845490.1; XM_014990004.1.
DR STRING; 48701.ENSPMEP00000009596; -.
DR Ensembl; ENSPMET00000000525.1; ENSPMEP00000009596.1; ENSPMEG00000011459.1.
DR GeneID; 106919553; -.
DR KEGG; pmei:106919553; -.
DR CTD; 23522; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000261480; Unplaced.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
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; 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:SF73; HISTONE ACETYLTRANSFERASE KAT6B; 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; SM00526; H15; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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 103..176
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 711..985
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 346..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1568..1600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1720..1829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 990..1017
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 495..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1065
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1159
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1226
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1737..1755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1756..1770
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1771..1785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1800..1829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 887
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 2114 AA; 234559 MW; D611F3BF2D38467A CRC64;
MVKLANPLYT EWILEAIQKI KRQKQRPSEE RICHAVSTLH GLDKKIVLEQ LDLSVHDGSV
LKVTNKGSAS YKDPGNPGRI GSILPANAPL PSKESIWNSS DLRHIDWNKI LRRAIEGLDD
THGSSLKNIE RYLRNQDDLS EVVDNSAFRQ RLRLAAKRSV NNGRLLKNGP RYKLSHGSVE
GRNPRCPSAS PLVLSSVTLL PHEREQLRVD PIPICSFCLG TKESNRDKQP EELLSCADCG
SSGHPSCLKF SPELTSNVKR LRWQCIECKT CSSCRIQGKN ADEMLFCDSC DRGFHMECCD
PPLSRMPKGT WICQVCRPKE NGKKLLHRKA DEIKRRYAKP IGRPKNKLKQ RMSVTSGDGS
MVALGGRGSP GRGQKITVCS TPSSGHAASV KDARDRLTVA EPCCAVNASQ FTPSPPTTTT
PSLTPTSTPA TLTVNKKTKG LIDGLSKFFT PSPVGRRSRA VAIELSSRDK GTPKLSQRPE
PFAFAADAPH KITPTSSALP ATSTSPGLSS PPQVTSSSTS ANSPQSSSSQ SSVPSLGSLC
SSSQLKGLFD GLSHIYTTQG QSRKKRLPCY APPKRRPYKQ DLSQCLGKNE FSKNRFHPTS
AGSGRLRGPP FKMVSHFKCN PFLKNHRTLG RLKYRVRAHN GATSPEKGDL TDGRIKPENN
HGHLSTLHVK QEAQADLAAM SRDHVSEEDI ETFTRVQELA AQKTGSLTNT DFVRRPAVIE
FGKYEIQTWY SSPYPPEYSR LQKLYLCEFC LKYMRSKNIL QRHTKKCGWF HPPATEIYRK
DNLSVFEVDG NVSKLFCQNL CLLAKLFLDH KTLYYDVEPF LFYILTKNDE KGCHLVGYFS
KEKLCQQKYN VSCIMIMPQY QRQGFGRFLI DFSYLLTRQE GQAGSPEKPL SELGRLSYLA
YWKSVMLEHL YKHPDKHISV KGISRATGMC PHDIAATLQQ LGMIDRRDGR TVLVRREQLI
QRHMERLRAN PRKNEVDPDA LRWTPSTTLN AVLSEEEREA EMDAERLKEQ ASCWEKEERE
SYMMTHGSRQ PLTKVHCKIP YRTYERRPAP PWSRRVPRPE VVSDADDDSD GSPPILTKAH
ELLSAKRKSS AVLKKRGRKR KRINSSVTTE TISETTEVLN EPFDNSEDER PMPRLEHTSR
MGEMEDDEDD DDDDEEEEEM QKYKISALPM KRRRGRPRLE KNTRKDNLER WNEGPELVSK
RSSRPRPVKR KKGWPKGVKR GPPKWRLKNS FKLNLYTPPE TPLEAEQHHI RTEETKHIPD
QESFSGDEET KAGGSLDSPD VMQEGLHSEP PSPADHGSQT STSPEGSPVA SPVCSPALSV
EAPSPQPEDR TDSLEPPRDD KQDSGHDPDS PAKDMEDSSE RAQSPENGNE ESYEEEQRAR
IEDQNADDED ERHSKKAAPE GGTEESEQSS KDAPNVTQAF LDPKEDDSSE LSQQVSTESY
CEDVPVSAGE KLQDATPETT AETSPPAAAV ASIAPLDSDN PADSESEEES APSPGPNHPP
LPPVGRSALS PVLREDPPVC TEFDSETVQA VKSLTQESEG ETVFQNCAES QEPCRNLQTY
AHMAQSPQLT PLDDCPQSDH SSPLSSAQSH PSQSVRSVSS PAVSILESGY TQISPDHSAI
SVPSLHNMET SPMMDVPSVS DHSQQVVDSG FSDLGSIEST TENYENPSSY DSTMGGSICG
AGPSQNSCSY GTIPPSSCAV SQQMAAVNPG GCGMIQQNSL SSPPHCGVKS PQGCVVVERP
PSNSQHNQHS QHGQRSQHSQ HSRHVPPHNQ HSQHNQHAPH NQLSQHSQHS HHHNHHPQHN
QLSQHNQHAQ HGLHSQQQPP PMAQCSIPPN FTTTMQLADI PESGNPNFAL YERINPQGEY
GSGHYPQSSG LSLAKLQQFT NTFIDHPHSN PFNHAAPHPI TSYANNPSLS SQHSSLVSLP
QNPHRVPNPQ VQATMTPPPN LSSPSSMMLQ PNMGISRSQR VAHMPSKGHV SARSKSAPLS
HNHQQQMYAR PPQAVAMQAP SRTLAAMPRM NMSMNIMPAP GYNVNSMNMP SLNAMNGYGM
SQPMMNSGYH GNHAYMNQSP QYSMQMGMMG TQPYPQQSMQ APPHGNMVYP PAGHHGYMNT
GMSKQSLKGP LIRR
//
