ID A0A094KDC8_ANTCR Unreviewed; 1813 AA.
AC A0A094KDC8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
DE Flags: Fragment;
GN ORFNames=N321_00697 {ECO:0000313|EMBL:KFZ56605.1};
OS Antrostomus carolinensis (Chuck-will's-widow) (Caprimulgus carolinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Caprimulgiformes;
OC Caprimulgidae; Antrostomus.
OX NCBI_TaxID=279965 {ECO:0000313|EMBL:KFZ56605.1, ECO:0000313|Proteomes:UP000053620};
RN [1] {ECO:0000313|EMBL:KFZ56605.1, ECO:0000313|Proteomes:UP000053620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N321 {ECO:0000313|EMBL:KFZ56605.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KL347273; KFZ56605.1; -; Genomic_DNA.
DR Proteomes; UP000053620; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:UniProt.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:UniProt.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:UniProt.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd05495; Bromo_cbp_like; 1.
DR CDD; cd15557; PHD_CBP_p300; 1.
DR CDD; cd15802; RING_CBP-p300; 1.
DR CDD; cd02337; ZZ_CBP; 1.
DR Gene3D; 2.10.110.40; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 1.10.246.20; Coactivator CBP, KIX domain; 1.
DR Gene3D; 1.20.1020.10; TAZ domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR003101; KIX_dom.
DR InterPro; IPR036529; KIX_dom_sf.
DR InterPro; IPR010303; RING_CBP-p300.
DR InterPro; IPR038547; RING_CBP-p300_sf.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000197; Znf_TAZ.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR13808; CBP/P300-RELATED; 1.
DR PANTHER; PTHR13808:SF34; CREB-BINDING PROTEIN; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF02172; KIX; 1.
DR Pfam; PF06001; RING_CBP-p300; 1.
DR Pfam; PF02135; zf-TAZ; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00551; ZnF_TAZ; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF47040; Kix domain of CBP (creb binding protein); 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF57933; TAZ domain; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS50952; KIX; 1.
DR PROSITE; PS50134; ZF_TAZ; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00203}; Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053620};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00203};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 123..209
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 362..441
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 890..962
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1110..1487
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1489..1537
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1552..1633
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 123..209
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1552..1633
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 217..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1343..1402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1661..1813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..675
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..852
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1389
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1661..1682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1683..1703
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1704..1726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1727..1741
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1751..1766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1780..1813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFZ56605.1"
FT NON_TER 1813
FT /evidence="ECO:0000313|EMBL:KFZ56605.1"
SQ SEQUENCE 1813 AA; 200071 MW; A994BD1BA41C7CE6 CRC64;
APAMQGNAGS VLAETLTQVS PQMAGHTGLN TAQTGAMTKM GMTGNTSPFG QPFSQTGGQQ
MGATGVNPQL PNKPGMANSL SPFPADIKST PVTSVPNMSQ MQTQVQQVGI VPTQAMATGP
TADPEKRKLI QQQLVLLLHA HKCQRREQAN GEVRACALPH CRTMKNVLNH MTHCQAGKAC
QVAHCASSRQ IISHWKNCTR HDCPVCLPLK NASDKRNQQP LLGSPAGGIQ NSIGSVGTGQ
QNTPSLSNPN PIDPSSMQRA YAALGLPYGN QPQTQLQPQV QGQQQAQPQA HQQMRTINAL
GANQMNLPAG GITTDQQTSL ISETALPTSL GTNNPLMNDG TNSGNVGNLS SMPTAAPPSS
TGVRKAWHEH VTQDLRNHLV HKLVQAIFPT PDPAALKDRR MENLVAYARK VEGDMYESAN
SRDEYYHLLA EKIYKIQKEL EEKRRSRLHK QGMLGNQTAL QTPGPQPPGI SQVAAAMGQA
QPVRPPNGPM SMPTVPISRM QVSQGMNQFN PMSIGNVQMP QAPMGPRAAS PMNHPVQMNN
MGAVPAMAMS PSRMPQPQNM MGAHSNNMMG QAPTQNQFLP QNQFPASSGA MNVNNVGMGQ
STAQAGVAQG QVPSAALPNS MNMLGPQSGQ LPCPPVTQPP LHQTTPPVST AAGMPPIQHQ
TPAGMTPPQP AAPTQPSTPV SSSGQTPTPT PGSVPNATQT QSTPTGQTAA QAQVTPQPQT
PVQPQSVPTP QPSQQQPTSV QAQPPGTPLS QAAASIDNRV PTPASVASAD TNSQQLGPDA
PMLESKSEVK TEETEPETSE TQVEAKTEVE EDLQGSSQTK EESDGTELKQ EPMEIEEKKP
EVKVDAKEEE ESSTNGTTSQ STSPSQPRKK IFKPEELRQA LMPTLEALYR QDPESLPFRQ
PVDPQLLGIP DYFDIVKNPM DLSTIKRKLD TGQYQEPWQY VDDVWLMFNN AWLYNRKTSR
VYKFCTKLAE VFEQEIDPVM QSLGYCCGRK YEFSPQTLCC YGKQLCTIPR DAAYYSYQNR
YHFCEKCFTE IQGENVTLGD DPSQPQTTIS KDQFEKKKND TLDPEPFVDC KECGRKMHQI
CVLHYDIIWP SGFVCDNCLK KTGRTRKENK FSAKRLQTTR LGNHLEDRVN KFLRRQNHPE
AGEVFVRVVA SSDKTVEVKP GMKSRFVDSG EMSESFPYRT KALFAFEEID GVDVCFFGMH
VQEYGSDCPP PNTRRVYISY LDSIHFFRPR CLRTAVYHEI LIGYLEYVKK LGYVTGHIWA
CPPSEGDDYI FHCHPPDQKI PKPKRLQEWY KKMLDKAFAE RIIHDYKDIF KQATEDRLTS
AKELPYFEGD FWPNVLEESI KELEQEEEER KKEESTAASE TTEGSQGDSK NAKKKNNKKT
NKNKSSISRA NKKKPSMPNV SNDLSQKLYA TMEKHKEVFF VIHLHAGPVI NTLPPIVDPD
PLLSCDLMDG RDAFLTLARD KHWEFSSLRR SKWSTLCMLV ELHTQGQDRF VYTCNECKHH
VETRWHCTVC EDYDLCINCY NTKSHDHKMV KWGLGLDDES NSQGEQQSKS PQESRRLSIQ
RCIQSLVHAC QCRNANCSLP SCQKMKRVVQ HTKGCKRKTN GGCPVCKQLI ALCCYHAKHC
QENKCPVPFC LNIKHKLRQQ QIQHRLQQAQ LMRRRMATMN TRNVPQQSLP SPTSATPGTP
TQQPSTPQTP QPPPQPQPSP VSMSPAGFPS VSRTQPPTTV STGKPANPVS APPPPAQPPP
AAVEAARQIE REAAQQQQQL YRGNNINNGL PPGRPGLVNP TVGSVNQMQP VSMNVPRPNP
VSGPVMSNMQ PGQ
//
