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Database: UniProt
Entry: A0A093ERS4_TYTAL
LinkDB: A0A093ERS4_TYTAL
Original site: A0A093ERS4_TYTAL 
ID   A0A093ERS4_TYTAL        Unreviewed;      1804 AA.
AC   A0A093ERS4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE   Flags: Fragment;
GN   ORFNames=N341_03308 {ECO:0000313|EMBL:KFV43128.1};
OS   Tyto alba (Barn owl).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX   NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV43128.1, ECO:0000313|Proteomes:UP000054190};
RN   [1] {ECO:0000313|EMBL:KFV43128.1, ECO:0000313|Proteomes:UP000054190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV43128.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KK370088; KFV43128.1; -; Genomic_DNA.
DR   Proteomes; UP000054190; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   CDD; cd18666; CD1_tandem_CHD1-2_like; 1.
DR   CDD; cd18661; CD2_tandem_CHD1-2_like; 1.
DR   CDD; cd18054; DEXHc_CHD2; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 2.40.50.40; -; 2.
DR   Gene3D; 6.10.140.1440; -; 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; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR040793; CDH1_2_SANT_HL1.
DR   InterPro; IPR025260; CHD1-like_C.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR023779; Chromodomain_CS.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623:SF19; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 2; 1.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   Pfam; PF18375; CDH1_2_SANT_HL1; 1.
DR   Pfam; PF13907; CHD1-like_C; 1.
DR   Pfam; PF00385; Chromo; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01176; DUF4208; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00598; CHROMO_1; 2.
DR   PROSITE; PS50013; CHROMO_2; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000313|EMBL:KFV43128.1};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KFV43128.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054190};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          236..328
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          353..430
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          470..640
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          769..920
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1004..1101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1304..1437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1530..1622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1651..1804
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..175
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..210
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..226
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1014..1044
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1054..1101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1325..1410
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1531..1552
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1561..1586
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1598..1620
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1662..1676
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1677..1726
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1752..1766
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1775..1790
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV43128.1"
FT   NON_TER         1804
FT                   /evidence="ECO:0000313|EMBL:KFV43128.1"
SQ   SEQUENCE   1804 AA;  209115 MW;  DA90FB455F9D268D CRC64;
     SHSASEEASG SDSASQSESE QGSDSNSSSE SSESQSESES ESTGSKSQQT PPETKEKPAS
     KKERIADVKK MWEEYPDVYG VRRSNRSRQE PSRFNIKDEA SSESENESPK RRGQKQMKKA
     EVSGEEEDED GGEQGTSGES EPEPKKVKAR RPAQRRTVAK TTVKKPHKPQ RGKKRKKQVS
     SEDDDDDEDD ETPKRQTRRR AAKNVSYKED DDFETDSDDL IEMTGEGADE QQDNSETIEK
     VLDIRLGKKG ATGASTTVYA TEANGNPSAD FDPEKDEGEV QYLIKWKGWS YIHSTWESEE
     SLQQQKVKGL KKLENFKKKE EEIKQWLGKV SPEDVEYFNC QQELASELNK QYQIVERVIA
     VKTSKSATGH SDFPANSRKT SSNDPEYLCK WMGLPYAECS WEDEALISKK FQHCIDSFNN
     RNNSKTIPTR DCKVLKQRPR FVALKKQPSY IGGENLELRD YQLEGLNWLA HSWCKNNSVI
     LADEMGLGKT IQTISFLSYL FHQHQLYGPF LVVVPLSTLT SWQREFEVWA PEINVVVYIG
     DLMSRNMIRE YEWIHAQSKR LKFNALITTY EILLKDKAVL GSINWAFLGV DEAHRLKNDD
     SLLYKTLIDF KSNHRLLITG TPLQNSLKEL WSLLHFIMPE KFEFWEDFEE DHGKGRENGY
     QSLHKVLEPF LLRRVKKDVE KSLPAKVEQI LRVEMSALQK QYYKWILTRN YKALSKGTRG
     STSGFLNIVM ELKKCCNHCY LIKPPEENER ENGLETLQSL IRSSGKLILL DKLLTRLRER
     GNRVLIFSQM VRMLDILAEY LTIKHYPFQR LDGSIKGEIR KQALDHFNAD GSEDFCFLLS
     TRAGGLGINL ASADTVVIFD SDWNPQNDLQ AQARAHRIGQ KKQVNIYRLV TKGTVEEEII
     ERAKKKMVLD HLVIQRMDTT GRTVLDNNSG RSNSNPFNKE ELTAILKFGA EDLFKELEGE
     ESEPQEMDID EILRLAETRE NEVSTSATDE LLSQFKVANF ATMEEEETEL DERSQKDWDD
     IIPEEQRKKV EEEERQKELE EIYMLPRIRS STKKAQTNDS ESDAETKRRL QRSSGSESET
     DDTDDEKRPK RRGRPRSVRK DTVEGFTDAE IRRFIKAYKK FGLPLERLEC IARDAELVDK
     SVADLKRLGE LIHNSCVSAM QEYEEQLKEN PGEGKGPGKR RGPTIKISGV QVNVKSIIQH
     EEEFEMLHKS IPTDPEERKK YRLTCRVKAA HFDVDWGVEE DSRLLVGIYE HGYGNWELIK
     TDPELKLSDK ILPVETDKKP QGKQLQTRVD YLLKLLKKDL DKKENMKDGE EGKLKKRKPR
     VKKENKAPKV KDEHGNELSS PRHSDNQSEE GEVKEDGLEK SPVKKKQKKK ENKENKEKQT
     TTKKEKESDK EKKKTKDKKE KPKGGESKSG SKGKRSQGPV HITAGSEPIP IGEDEDDDLD
     QETFSVCKER MRPVKKALKQ LDKPDKGLTV QEQLEHTRNC LLKIGDRISE CLKAYTDQDH
     IKLWRRNLWI FVSKFTEFDA RKLHKLYKMA HKKRSQEEEE QKKKEDMSSM KKPFRPEPSG
     SSRDSVMSQS HVPHNPHSQK IHLPPSHAQQ QMHGHPRDNY GHPNKRHFSN TDRGEWQRDR
     KFNYGGNSNQ MWGGERHHQY EQHWYKDHHY GDRRSRGEPH RSSGNYRPNN LSRKRPYEQY
     NSDRDHRGHR DYYDRHHHDS KRRRSDEFRP QNYHQQDFRR MSDHRPPMGY HGQGPSDHYR
     SFHTDKLGDY KQPLPPPHPA VSDPRSPPSQ KSPHDSKSPL DHRSPLDRSL EQKNNPDYNW
     NMRK
//
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