ID A0A087QIC9_APTFO Unreviewed; 2399 AA.
AC A0A087QIC9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
DE Flags: Fragment;
GN ORFNames=AS27_07110 {ECO:0000313|EMBL:KFM00983.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM00983.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM00983.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM00983.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; KL225618; KFM00983.1; -; Genomic_DNA.
DR STRING; 9233.A0A087QIC9; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:InterPro.
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:0003713; F:transcription coactivator 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 GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd05495; Bromo_cbp_like; 1.
DR CDD; cd20910; NCBD_CREBBP-p300_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; 1.10.1630.10; Nuclear receptor coactivator, CREB-bp-like, interlocking 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; IPR009110; Nuc_rcpt_coact.
DR InterPro; IPR014744; Nuc_rcpt_coact_CREBbp.
DR InterPro; IPR037073; Nuc_rcpt_coact_CREBbp_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; PF09030; Creb_binding; 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; SSF69125; Nuclear receptor coactivator interlocking domain; 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 Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053286};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
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 322..408
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 561..640
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 1089..1161
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1309..1686
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1688..1736
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1751..1832
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 322..408
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1751..1832
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 46..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1237..1256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1542..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1860..1945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2079..2101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2169..2207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2251..2373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..874
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1051
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1542..1558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1574..1588
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1860..1881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1882..1902
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1903..1925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1926..1940
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2187..2207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2251..2307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2308..2335
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2352..2373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM00983.1"
FT NON_TER 2399
FT /evidence="ECO:0000313|EMBL:KFM00983.1"
SQ SEQUENCE 2399 AA; 261728 MW; 3D07DB58E02E94F5 CRC64;
DFGSLFDLEN DLPDELIPNG ELGLLNSSGN LVPDAASKHK QLSELLRGGS GSSLNPGIGN
VNSNSPVQQG VGSQVQGQPN SANIGNLGAM GKSPLNQGDS SASGLAKQAA STSGPTTPAS
QTLNSQAQKQ VGMVTSSPAT SQTGPGICMN TNFSQTHQSL LNSNSGHSLM NQPQQGQGQV
MNGSLGAAGR GRGAGMQYSA PAMQGNAGSV LAETLTQVSP QMAGHTGLNT AQTGAMTKMG
MTGSTSPFGQ PFSQTGGQQM GATGVNPQLP NKPGMANSLS PFPADIKSTP VTSVPNMSQM
QTQVQQVGIV PTQAMATGPT ADPEKRKLIQ QQLVLLLHAH KCQRREQANG EVRACALPHC
RTMKNVLNHM THCQAGKACQ VAHCASSRQI ISHWKNCTRH DCPVCLPLKN ASDKRNQQPL
LGSPAGGIQN SIGSVGTGQQ NTPSLSNPNP IDPSSMQRAY AALGLPYGNQ PQTQLQPQVQ
GQQPAQPQAH QQMRTINALG ANQMNLPAGG ITTDQQASLI SETALPTSLG TNNPLMNDGT
NSGNVGNLSS MPTAAPPSST GVRKAWHEHV TQDLRNHLVH KLVQAIFPTP DPAALKDRRM
ENLVAYARKV EGDMYESANS RDEYYHLLAE KIYKIQKELE EKRRSRLHKQ GMLGNQPALQ
TPGPQPPGIP QVAAAMGQAQ PVRPPNGPMS MPTVPISRMQ VSQGMNQFNP MSIGNVQMPQ
APMGPRAASP MNHPVQMNNM GAVPAMAMSP SRMPQPQNMM GAHSNNMMGQ APTQNQFLPQ
NQFPASSGAM NVNNVGMGQS TAQAGVAQGQ VPSAALPNSM NMLGPQSGQL PCPPVTQPPL
HQTTPPVSTA AGMPPIQHQT PTGMTPPQPA APTQPSTPVS SSGQTPTPTP GSVPNATQTQ
STPTGQTAAQ AQVTPQPQTP VQPQSVPTPQ PSQQQPTSVQ AQPPGTPLSQ AAASIDNRVP
TPASVASADT NSQQLGPDAP MLESKSEVKT EETEPETSET QVEAKTEVEE DLQGSSQTKE
ETDGTELKQE PMEIEEKKPE IKVDAKEEEE SGTNGTTSQS TSPSQPRKKI FKPEELRQAL
MPTLEALYRQ DPESLPFRQP VDPQLLGIPD YFDIVKNPMD LSTIKRKLDT GQYQEPWQYV
DDVWLMFNNA WLYNRKTSRV YKFCTKLAEV FEQEIDPVMQ SLGYCCGRKY EFSPQTLCCY
GKQLCTIPRD AAYYSYQNRY HFCEKCFTEI QGENVTLGDD PSQPQTTISK DQFEKKKNDT
LDPEPFVDCK ECGRKMHQIC VLHYDIIWPS GFVCDNCLKK TGRTRKENKF SAKRLQTTRL
GNHLEDRVNK FLRRQNHPEA GEVFVRVVAS SDKTVEVKPG MKSRFVDSGE MSESFPYRTK
ALFAFEEIDG VDVCFFGMHV QEYGSDCPPP NTRRVYISYL DSIHFFRPRC LRTAVYHEIL
IGYLEYVKKL GYVTGHIWAC PPSEGDDYIF HCHPPDQKIP KPKRLQEWYK KMLDKAFAER
IIHDYKDIFK QATEDRLTSA KELPYFEGDF WPNVLEESIK ELEQEEEERK KEESTAASET
TEESQGDSKN AKKKNNKKTN KNKSSISRAN KKKPSMPNVS NDLSQKLYAT MEKHKEVFFV
IHLHAGPVIN TLPPIVDPDP LLSCDLMDGR DAFLTLARDK HWEFSSLRRS KWSTLCMLVE
LHTQGQDRFV YTCNECKHHV ETRWHCTVCE DYDLCINCYN TKSHDHKMVK WGLGLDDESN
SQGEQQSKSP QESRRLSIQR CIQSLVHACQ CRNANCSLPS CQKMKRVVQH TKGCKRKTNG
GCPVCKQLIA LCCYHAKHCQ ENKCPVPFCL NIKHKLRQQQ IQHRLQQAQL MRRRMATMNT
RNVPQQSLPS PTSATPGTPT QQPSTPQTPQ PAPQPQPSPV SMSPAGFPSV SRTQPPTTVS
TGKPANPVSA PPPPAQPPPA AVEAARQIER EAAQQQQQLY RVNNINNGLP PGRPGLVNPT
VGSVNQMQQV SMNVPRPNPV SGPVMSNMQP GQWQMPGVQQ PPRSIPPNAL QDLLRTLKSP
SSPQQQQQVL NILKSNPQLM AAFIKQRTAK YVANQPGMQP QAGIQPQPGM QQPQTGMQQP
GMHAQAGLQN MNAMQAGVQR PSVPPQQQGI GAMNPQGQAI NIMNPGHNPS MANMSPQYRE
ILRRQLLQQQ QQQQQGGAGM AGGMAGHNQF QQPQGPGGYP QAMQQQRMQQ HISIQGGSMG
QMAQMGQLNQ MGQPGMGADG TPNIQQALQQ RILQQQQMKQ QIGSPGQPNP MSPQQHMLSG
QPQASHLPGQ QIATSLSNQV RSPAPVQSPR PQSQPPHSSP SPRIQPQPSP HHVSPQTGSP
HPGLAVTMAS SMDQGHLGNP EQSAMLPQLN TPNRSALSNE LSLVGDTTGD TLEKFVEGL
//
