ID H0ZCP3_TAEGU Unreviewed; 3030 AA.
AC H0ZCP3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=E1A binding protein p400 {ECO:0000313|Ensembl:ENSTGUP00000008354.2};
GN Name=EP400 {ECO:0000313|Ensembl:ENSTGUP00000008354.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000008354.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000008354.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000008354.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR STRING; 59729.ENSTGUP00000008354; -.
DR Ensembl; ENSTGUT00000008441.2; ENSTGUP00000008354.2; ENSTGUG00000008078.2.
DR GeneTree; ENSGT00940000154764; -.
DR HOGENOM; CLU_000397_0_0_1; -.
DR InParanoid; H0ZCP3; -.
DR OMA; YGEDCRG; -.
DR TreeFam; TF106424; -.
DR Proteomes; UP000007754; Chromosome 15.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0000786; C:nucleosome; IEA:Ensembl.
DR GO; GO:0000812; C:Swr1 complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR031575; EP400_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR46459:SF1; E1A-BINDING PROTEIN P400; 1.
DR PANTHER; PTHR46459; E1A-BINDING PROTEIN P400-RELATED; 1.
DR Pfam; PF15790; EP400_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007754}.
FT DOMAIN 787..859
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 1080..1245
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1878..2035
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2346..2407
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1517..1551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2265..2288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2503..2542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2989..3030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 832..895
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 102..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1551
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2989..3017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3030 AA; 333949 MW; B95551EDBA0EC914 CRC64;
MHHGNGPQNA QRQLQRSRSF TGSEGEEQQA NLPQSPAASF APSASPSAPQ SPSYQIQQFI
MSRSPVAGQN VNITLQNVGP VASGNQQITL TPLPLPNPTS PSFQFSPQQR RFEHGSPSYI
QVTSPLPQQV QSQSPTQPNP VQALPSVRAG TPGPGLGMCS QSPTRGFVDA SVLVRQISLS
PSNGGHFVYQ EGPGIAQIAQ GAAAQVQLPS SGPPATVRER RLSQPHSQSG GTIHHLGPQS
PVASGANMQS LTSPGHITTT SLPPQISNII QGQLMQQQQQ VLQGQQLSRP IGFDRTSGGL
IAGVGGPSAF GMTSPPPPTS PSRATVPQGL SSLPLTPTAN TAVKKQPKKL EEIPPANQET
AQMRKLCLDH HHKQMEILKE TFKECLIELF FLQHLQGNMM DFLAFKKKHC VPLQAYLRQN
DLDLEEEEEE EQSEVINDEV KVVTGKDGQT GTPVAIATQL PPNVSAAFSS QQQPFQQTHT
GTPATGTVST IEIEAFKRQQ QALAPADSSK RPRIEVGRHG MVFQHPGVAS GVPLQQLMPT
AQGGMPPTPQ PVQLTGQKQS QQQYDPSKGP PVQNAASLHT PPPQLPARLQ PANVPMASLP
AALQLPQQQP QLVEPPAQPQ IQVKIQPQSV PLTAAPLPAP LQQQVPPAIH VQGQAPSQVS
QPQTVTLTRP SADPAQSSQR LAANPLPPTS SIAPAAIPGT TPPSPYPLQT NRTSPATNKS
LSPIASKPPG LAVAAAAPKT QSPAQNAAVL PQENSQDKLA EQVKLENQIH QRIAELRKEG
LWSPRRLPKL QEAPRPKSHW DYLLEEMQWM ATDFAQERKW KMATAKKMVR TVARYHEEKK
LNEERAKREE QNKLRRIAAS IAREIEYFWS NIEQVVEIKL QIEFQEKRKK ALNLKRFSRK
GNCFPFNKKH SLNSDDIVLY NITQFEDEEE TIEEQEAKEG NINHQTELSN LAKEAELPLE
DLVKMYEGAF AENFHWPQPK PDSEEESSEE EMEDHMSDRE SPQKEVVLID SLLSIDQYKS
MDRSSPPKKH MRDIAEVAAA AEMLLPKGSS RITTAIKYNT PSLLYGSLRE YQKIGLDWLA
KLYRKNLNGI LADEAGLGKT VQIIAFFAHL ACNEGNWGPH LVVVRSCNIL KWELELKRWC
PGLKILLYFG SQRELRAKRQ EWTEPNSFNV CITSYKQLFK GHPAFMKMRW KYLIVDEMQQ
IKNMTEKHWE AIFSLRSQHR LLLIDTPLHN TLMELWTMVH FLIPGISRPY LDFPVKAPNE
ENQDYCHKLV IRLHRMIQPF ILRRSKRDVE KQLTKKYEHV LKCRLSSRQK AMYEDVILQP
GTQEALKSGH FISVLHVLMQ LQRICNHPDL INPRLSSSSY VSETLEYRTA SLVLRALERD
IWKESDLSLF DLIGMEDKMT HYEAQMLPKQ KVTRKLIEEI YSSPPPPARP NPVKLKPSRL
FQPVQYGQKP EGRTVVFPST QVQRTVTTAT VTQQGQVRGR SPIATVSSNQ AAAAQFQTTQ
ASTSAPRHQP AATFTTATSA ANPVKPRGQT SAPAPQPGQP QPQPQPPPHT IQQSVLPQRL
VLTSQAQARL PSGEVVKIAQ LASIAGAQGR IAQPETPVTL QFQGNKFTLS HSQLRQLTAG
QPLQLQGSVL QIVSAPGQQY LRPQGPVVMQ TVSQAGTVQN ALNALGNQHQ AGGPTSTAVT
QQVCIPGRAT VTNLPSGDMG AVLKPAPLHG QSQEKNRLLK ERLDRIFCGN ERRCARAPVY
GRDVLSVCSL AGDTKASQLP SSEGNSWRWA GFVNCCLSSS ACGGPSNPLQ EMILGLVQQQ
ESLKDLVNRA LFVLPAAVAA PPCFYVANPP PSYSHRLKLL KHSLRQKAAP HLHQLQQLTT
PHLLQFPDLR LVQYDSGKLE ALAVLLQKLK SEGRRVLILS QMILMLDILE LFLNFHFLTF
VRIDEYANQE QRQELMKIFN RDKRIFCAIL SSHSRSTGVN LVEADTVVFY DNDLNPVMDA
KAQEWCDRIG RCKDIHIYRL VSGNSVEEKL LKNGTKDLIR EVAAQGNDYS MAFLTQQTIQ
ELFEVHSPME DSGFRVKAEE FVVLSQEPSP AENISPKVAR PFIEALNSIE REDEESNDHI
QEIGSESSLE PLISELCETK YIEEPSQLQE LVAVVDQLTP IEKYALNYLE LFHGSVDDNE
PRLSEMELKT AKKAWEVQHM KELKEREQKM LWEDEEELLT YTREDAYNKE YVYEGPDGQT
EIMPLWTPPT PPQDDNDIYI DSVMCLMYDT TPIPESKLPP VYVRKERKRH KTDPSAAGRK
KKQRHGETVI PPRSLFDRAT PGMLKMRREG KEQKKNILLK QQTQFAKPLP TLVKPATEAG
QDNPEWLISE DWALLQAVKQ LLELPLNLAV VSPAHTPNWD LVSDVVNSCS RVYRSPKQCR
NRYENVIIPR EEGKTKNSRP LRTNQIYAQD EGATHTQLYT NHFEMMKMIA GKRSPPIKPL
LGMNPFQKNP KHASVLAESG INYDKPLPPI QVASLRAERI AKEKKALAEQ QRAQQQTGPQ
PQQPQAGQQP PQQPPVQQAQ AQPQAQAQAQ VVQQPQAVVQ TAVTTVANTA VLVRKGELGA
SDVVTSVLLC AGTIKTAVTG TSIQTATVSG NVIVNTVAGV PAATFQPINK RLASPVIPGT
LTTSGGTTTA QVVHSQPRAA AAPAASTELV TIASTQGVRA VTSVTASAVV TTNLTPVQTQ
TRSLVTQVTP GNNPQLIKLQ KQKLQLPQQQ AAQQTQQGAQ QQTAQVQVQQ QQQTQQLTAV
TAPRPGAVLT GTTVTNLQVA RLTRVPASQL QAQGQIQGQT PQAAQVALAK PPVVSVPAAV
VSSAGVTTLP VTVAGISVAI GQPQKAAGQT VVAQPLHVQQ LLKLKHHQAA QQQKAIQPQV
AQGQATVQQK TQQQTSQQQK VTYATQPAIK TQFLTTPISQ TQKPGGTQQV QAQIQVQVTQ
VQAQPQTVTL SQTTAGQQQV QVIPATTATA QVVQQKLIQQ QVVTTASPQV QAPGVQNPAQ
TPAAPEAQSQ QAKVQMRTPT VRLKAPTKPS
//
