ID A0A1A9W114_9MUSC Unreviewed; 2219 AA.
AC A0A1A9W114;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
OS Glossina brevipalpis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=37001 {ECO:0000313|EnsemblMetazoa:GBRI002426-PA, ECO:0000313|Proteomes:UP000091820};
RN [1] {ECO:0000313|Proteomes:UP000091820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000091820};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GBRI002426-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GBRI002426-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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}.
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DR STRING; 37001.A0A1A9W114; -.
DR EnsemblMetazoa; GBRI002426-RA; GBRI002426-PA; GBRI002426.
DR VEuPathDB; VectorBase:GBRI002426; -.
DR OrthoDB; 3135277at2759; -.
DR Proteomes; UP000091820; Unassembled WGS sequence.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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; cd15489; PHD_SF; 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; IPR019786; Zinc_finger_PHD-type_CS.
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:SF102; HISTONE ACETYLTRANSFERASE; 1.
DR Pfam; PF00538; Linker_histone; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF21524; SAMD1_WH; 1.
DR Pfam; PF17772; zf-MYST; 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; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
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 88..160
FT /note="H15"
FT /evidence="ECO:0000259|PROSITE:PS51504"
FT DOMAIN 180..248
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 797..1078
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 306..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1486..1590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1701..1815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1895..1929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1962..2050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2143..2219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..453
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..492
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1486..1580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1701..1716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1731..1772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1784..1805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 973
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 2219 AA; 247647 MW; 0698E13007B3A81A CRC64;
MFDSTQEISL EVWQQWILDA ISKIRSQKQR PSVQRICQAI GTHHKFHEDI VAEKLEQIVE
TGAVIKVYNK GLHSYKAPMA KRVIRVEKNT NLCKVVARAV HDLGECEGSS IKSIENYIQK
FNTIEMIGDA DYKTVIKQSI KKAVEAGFLI QEGKLYKKGR SLTTPRNSNA SADVPVQIGN
DVCKHCSGNA QKNLNGIPEP LSSCKQCGIS LHTTCANIAA KCKTQSFVLL YMLVTKGTSW
YCENCVKCNV CGKGNKGPCL LQCFVCQKNY HLSCLDTIPD KKPKHPYRCS TCLKLNTDVF
RMVKGKDSQK KMVMSKQRTT NTSSPRQQAA NTSSPSNRAN NVTCTSSATP TSSPEKFWPT
GRQQRGSNSK TPIKSQAVMF ENHPSTTAMA RARNMNAEET LKQQLSAYHE AAASLKNRNS
RKRTLSNLSS SSSSSDSDDE QNNGDEDQDN DDTTSSDSCS STTSSGSDSS ESSSDSSDCD
DNDDDNDDDD YDSEHSDSKS NMMLSQIFKK QKCEGLLSAT LKNKQQQQNI AHGGLQQHHQ
PQKEEEWGFA AVAKSHADIF SQNNNNNNNN NAGKDSNKEI KTVKKRINEQ FAASTKDNKN
NTLVNHSQQQ QQQQQQKQQQ NISTTPVKAS SNSTKSSLSE QKTSMMIKYK PKPHQVITEG
LNKKSNQQPI QKKAVLLKSM PLEKKDSHKA PEEEDDEEIP YLSQKNVIKY KLLEDITSAK
CQEKPCETVA NKEPEERKPW EVDTDENPFD SQPLPNGVTQ ADVDVYKRIR ERAKLAITGA
LESPSKLIAK PALVHSQPDR CPGSIEIGKW HIETWYSSPF PQEYARLTKL YLCEFCLKYT
KSRSVLDRHQ NKCTWKQPPG TEIYRHQDLS VFEVDGNINK IYCQNLCLLA KLFLDHKTLY
YDVEPFLFYV LTKNDNKGCH LVGYFSKEKH CAQKYNVSCI LTMPQFQRQG FGRFLIDFSY
LLSREEGQLG TPEKPLSDLG RLSYFSYWKS IILEYMYDHR NDEKITFHEI AMETGLTVSD
IALALELLNF IKLRKNEHDI RYQINIKVDW QNVMSHQERL RRRNNRILIE SERLRWSPLL
SNLKNSSLDQ SGGRQSLSPR KNNLQKFDDN KKELKEKTYK KETMGKCKPI GRVGKHKAEI
KEKVPEPIKE TLEYGKKGAE MKNRTGNYKS VNGQEKTGNL FPELKGINDT KRIANVTTTP
TTKRKRAYSS PSTAPIDVAL KVPDVKKQKP ENHNEESMDL EPPLEEIKAT ENTKKQSEEN
TKVEVTENHK VVSASSSRAQ RLANRKQSTP QPLKRKHEET TETTTSAEIL QPKSGEEPKP
KEDTIKKFSD LNEEGAKETS KSLKITNEMD NVKQNSPEAQ VEPKQVDKRV PNLFPKLRAK
NSGKINDETN NDVDTDIKES SKEQENQIEV AKTELQPSEV ITQTASATPP IKLEPVPQQL
TAIPNSVIKS TEAEDKVLEA VAKKTKKTSY QENDLDRMKT EAVSLPTLIP TQATSPSNNE
VNKEDVTPVG VISQNITNSV ISDKEQSKSQ QIQENSSAES TKENEKSVLT PASVLTSSAQ
ISTTSPISET SEQINETVKT SAIKSHDDVK EKLENPLKLT AAASPSITPI TTPNNVDIKQ
SLPLHKPENC ELKQESISPV NTAESAVKTS SLSVDIPVRQ EPVITRNETK LNVSPKLPEK
INESKASPDA IQPKTEIKLS THTTGIVSNQ NKVEPPQITI PKVEPQLAKK ESPTITKSPA
KVISTATATE KTSTNHSSSS SSSLSSGGGS VGGVGLNMNP EKSIHDTKQT KSQKSKDKSE
PSKSSSELKN QKSLHGLSAR EKQGQNMLMA QTQALKAFHG SLQIKEEDRM LQTMTSSAAA
AAAHEKLHFK PAEHITNQID LNKIAPQFQI NQLPNYPTSQ YWHNQSTNNN NNQKNRSMTN
QQASSSKYHG AQHVAVAAAA AAAAGVLTSL QQQQQQQQQQ QQTACQKSKN EQNINQNNAN
NSAGASSASN TNDDNKMKSS NTAQNPSQQQ AATTTVTPEM TSPMVYSNNN NESSSANNNN
NNNNNNMHHY ECGLSVPMGM DSPASIASDI TQNSSDVVAA NPTVHMQQQQ QQPQQFSNCS
LQNQTNNTPM HMAIHTSHIQ QQQQQQQQTG MNINQAQTLN NMTSNQHSSQ QQQNRKLNQN
ENSASTSGSV QRSSTPKLMR NTSSANSHRQ SKQQQQQQQQ QQQQQQALNN NLSQQQQQQ
//
