GenomeNet

Database: UniProt
Entry: A0A0Q3LV93_AMAAE
LinkDB: A0A0Q3LV93_AMAAE
Original site: A0A0Q3LV93_AMAAE 
ID   A0A0Q3LV93_AMAAE        Unreviewed;      3005 AA.
AC   A0A0Q3LV93;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=E1A-binding protein p400 isoform X7 {ECO:0000313|EMBL:KQK74440.1};
GN   ORFNames=AAES_157896 {ECO:0000313|EMBL:KQK74440.1};
OS   Amazona aestiva (Blue-fronted Amazon parrot).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX   NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK74440.1, ECO:0000313|Proteomes:UP000051836};
RN   [1] {ECO:0000313|EMBL:KQK74440.1, ECO:0000313|Proteomes:UP000051836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FVVF132 {ECO:0000313|EMBL:KQK74440.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQK74440.1}.
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DR   EMBL; LMAW01003045; KQK74440.1; -; Genomic_DNA.
DR   STRING; 12930.A0A0Q3LV93; -.
DR   Proteomes; UP000051836; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
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; 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:UP000051836}.
FT   DOMAIN          793..865
FT                   /note="HSA"
FT                   /evidence="ECO:0000259|PROSITE:PS51204"
FT   DOMAIN          1098..1263
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1817..1974
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          2285..2346
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50090"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          84..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          536..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          689..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          914..965
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          991..1019
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2205..2227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2439..2477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2967..3005
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          838..901
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        102..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..266
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..340
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..581
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        914..939
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2446..2477
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2967..2992
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3005 AA;  331992 MW;  82FB38038A068153 CRC64;
     MHHGNGPQNA QRQLQRSRSF TGSEGEEQQA NLPQSPAASF APSASPSAPQ SPSYQIQQFI
     MSRSPVAGQN VNITLQNVGP VASGNQQITL TPLPIPNPTS PSFQFSPQQR RFEHGSPSYI
     QVTSPLPQQV QSQSPTQPNP VPVQTLPSVR AGTPGSGLGM CSQSPTRGFV DASVLVRQIS
     LSPSNGGHFV YQEGPGIAQI AQGAAAQVQL PSSGTPATVR ERRLSQPHSQ SGGTIHHLGP
     QSPVASGANM QSLTSPGHIT TTSLPPQISN IIQGQLMQQQ QQVLQGQQLG RPIGYDRTSG
     GLIAGVGGPS AFGMTSPPPP TSPSRASVPQ GLSSLPLTPT VNTTVKKQPK KLEEIPPANQ
     ETAQMRKQCL DHHHKQMEIL KETFKECLIE LFFLQHLQGN MMDFLAFKKK HCVPLQAYLR
     QNDLDLEEEE EEEQSEVIND EVKVVTGKDG QTGTPVAIAT QLPPNVSAAF SSQQQPFQQT
     HTGTPVTGTV NTIEIEAFKR QQALAPADSS KRPRIEVGRH GMVFQHPGVA SGVPLQQLMP
     TAQGGMPPTP QTVQLTGQKQ SQQQYDPSKG PPVQNAASLH TPPPQLPGRL QPANVPMTSL
     PAALQLSQQQ PQIVESPAQP QIQVKIQPQS VPLTSAPLPA PLQQQVPPAI HVQGQAPNQV
     SQPQATIQQQ TVTLTRPSVD PAQTSQRLTA NTLPPTSSVV PAAISGTAPP STYPVQTNRS
     SSATNKSLSP IASKPSGLAV AAAPKTQSPA QNAAVIPQDN SQDKLAEQVK LENQIHQRIA
     ELRKEGLWSP RRLPXLQEAP RPKSHWDYLL EEMQWMATDF AQERKWKMAT AKKMVRTVAR
     YHEEKKLNEE RAKREEQNKL RRIAASIARE IEYFWSNIEQ VVEIKLQIEF QEKRKKALNL
     KKISRKGRDT RTVEDLLLEK ESEMGSSSGR KRKASTSLTD EEVEDEEETI EEQEAKEGNI
     NHQTELSNLA KEAELPLEDL LKMYEGAFAE SFHWPQPKPD SEEDSSEEEX EDHISDRESP
     QKEVVLIDSL LSIDQYKCID RSSPPKKHMR DIAEVAAAAE MLLPKGSSRI TTAIKYNTPS
     LLYGPLREYQ KIGLDWLAKL YRKNLNGIXA DEAGLGKTVQ IIAFFAHLAC NEGNWGPHLV
     VVRSCNILKW ELELKRWCPG LKILLYFGSQ RELRAKRQEW TEPNSFNVCI TSYKQLFKGH
     PAFMKMRWKY LIVDEMQQIK SMTEKHWEAL FSLRSQHRLL LIDTPLHNTL MELWTMVHFL
     IPGISRPYLD FPVKAPNEEN QDYCHKLVIR LHRMIQPFIL RRSKRDVEKQ LTKKYEHVLK
     CRLSSRQKAM YEDVILQPGT QEALKSGHFI SVLHVLMQLQ RICNHPDLIN PRLSSTSYVS
     ETLEYRTASV VLSALEKDIW KESDLSLFDL IGMENKMTHY EAQMLPKQKV TRKLIEEIYS
     SPPPPARPNP VKLKPSRLFQ PVQYGQKPEG RTVVFPSTQV QRTVTTATVT QQAQVRGRSP
     IATVSSNQGG EVVKIAQLAS IAGAQGRIAQ PETPVTLQFQ GNKFTLSHSQ LRQLTAGQPL
     QLQGSVLQIV SAPGQQYLRP QGPVVMQTVS QAGAVQNALN ALGNQHQGGV PTSTAVAQQG
     RTAVTNLSSG DMGAALKPGP GLTHGQLQET YEEKNRLLKE RLDRIFSGNE RRCSRAPMYG
     RDLLSVCSLT DERKXSQPSS SQDNSWRWAG FVNCCLSSSA SGGPSSPLQE MILTLGQQQE
     SLKDVVNRAL LVLPAAVAAP PCMYVANPPP SYSHRLKLLK HSLKQKAAPH LHQLQRITTP
     HLLQFPDLRL VQYDSGKLEA LAVLLQKLKS EGRRVLILSQ MIXMLDILEL FLNFHFLTFV
     RIDEYANHEQ RQELMKIFNR DKRIFCAILS SHSRSTGVNL VEADTVVFYD NDLNPVMDAK
     AQEWCDRIGR CKDIHIYRLV SGNSVEEKLL KNGTKDLIRE VAAQGNDYSM AFLTQQTIQE
     LFEVHSPMED SGFRVKAEEF VVLSQEPSPA ENISPKVARP FIEALNSIEQ EDEESNDRVQ
     EIGRGPSIEP LISELCETKY NEEPSQLQEL VAVVDQLTPI EKYALNYLEL FHVSVDENEP
     RLNEMELKTA KKAWEVQHMX ELKAKEQKML WEDEEELLTY TREDAYNKEY VYEGPDGQTE
     IMPLWTPPTP PQDDNDIYID SVMCLMYDTT PIPESKLPPV YVRKERKRHK TDPSAAGRKK
     KQRHGETVIP PRSLFDRATP GMLKMRREGK EQKKNILLKQ QTQFAKPLPT LVKPAAEAGQ
     DNPEWLISED WALLQAVKQL LELPLNLAVV SPAHTPNWDL VSDVVNSCSR VYRSPKQCRN
     RYENVIIPRE EGKLMYEANP KKKTKSIYKT KNSRPLRTNQ IYAQDEGATH TQLYTNHFEM
     MKMIAGKRSP PIKPLGINYD KPLPPIQVAS LRAERIAKEK KALAEQQRAQ QQTGPQPQQQ
     QAGQQQAQQP AVQQAQAQPQ PQAQAQVVQQ PQAVVQTAVT TVANTAVLAG TIKTAVTGTS
     IQTATVSGNV IVNTVAGVPA ATFQPINKRL ASPVIPGTLT TSGGTATAQV VHTQQRTAAA
     PAASTELVTI ASTQGVRAVT SVTASAVVTT NLTPVQTQTR SLVTQVTPAT PTVQLSGKTI
     TPAHFQLLRQ QQQQAAQVQV PQIQAQAQAQ SPAQIKTVGK LSQEQLIKLQ KQKLQLPQQQ
     AAQQTQQGAQ QQTTQVQVQQ QQQTQQLTAV TAPRPGAVLT GTTVTNLQVA RLTRVPASQL
     QAQGQMQAQT PQAAQVALAK PPVVSVPAAV VSSAGVTTLP VTVAGISVAI GQPQKAAGGQ
     TVVAQPLHVQ QLLKLKHHQA AQQQKAIQPQ VAQGQAAVQQ KINAQQVTVQ TQQQTSQQQK
     VTYTTQPAIK TQFLTTPISQ TQKPGGTQQV QAQIQVQAQP QTVTLSQTTA GQQQVQVIPA
     TTATAQVVQQ KLIQQQVVTT ASPQIQAPGV QNPAQTPATS EAQNQQAKVQ MRTPTVRLKA
     PTKPS
//
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