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Database: UniProt
Entry: A0A091S9Q8_NESNO
LinkDB: A0A091S9Q8_NESNO
Original site: A0A091S9Q8_NESNO 
ID   A0A091S9Q8_NESNO        Unreviewed;      2307 AA.
AC   A0A091S9Q8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE   Flags: Fragment;
GN   ORFNames=N333_11170 {ECO:0000313|EMBL:KFQ54042.1};
OS   Nestor notabilis (Kea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Nestor.
OX   NCBI_TaxID=176057 {ECO:0000313|EMBL:KFQ54042.1, ECO:0000313|Proteomes:UP000053840};
RN   [1] {ECO:0000313|EMBL:KFQ54042.1, ECO:0000313|Proteomes:UP000053840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N333 {ECO:0000313|EMBL:KFQ54042.1};
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   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007025}.
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DR   EMBL; KK945562; KFQ54042.1; -; Genomic_DNA.
DR   Proteomes; UP000053840; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18668; CD1_tandem_CHD5-9_like; 1.
DR   CDD; cd18663; CD2_tandem_CHD5-9_like; 1.
DR   CDD; cd18059; DEXHc_CHD7; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 2.40.50.40; -; 2.
DR   Gene3D; 3.40.5.120; -; 2.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
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; IPR006576; BRK_domain.
DR   InterPro; IPR037259; BRK_sf.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
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; PTHR46850; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 9; 1.
DR   PANTHER; PTHR46850:SF3; DNA HELICASE; 1.
DR   Pfam; PF07533; BRK; 2.
DR   Pfam; PF00385; Chromo; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00592; BRK; 2.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF160481; BRK domain-like; 2.
DR   SUPFAM; SSF54160; Chromo domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50013; CHROMO_2; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000313|EMBL:KFQ54042.1};
KW   Helicase {ECO:0000313|EMBL:KFQ54042.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053840};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          101..168
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          183..248
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          281..455
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          595..765
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          877..902
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1137..1199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1444..1583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2121..2196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2242..2307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        877..900
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1153..1192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1444..1465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1466..1536
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1554..1572
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2136..2160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2161..2196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2246..2280
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2283..2307
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ54042.1"
FT   NON_TER         2307
FT                   /evidence="ECO:0000313|EMBL:KFQ54042.1"
SQ   SEQUENCE   2307 AA;  260875 MW;  322BD1EB81CF17FA CRC64;
     SNKKPDSETS AAKKKGNKGK EGSENSDLEK TPPPSPHPED EDDPGVQKRR SSRQVKRKRY
     TEDLEFKISD EEADDADAAG RDSPSNTSQS EQQESADAEG PVVEKIMSSR SVKKKMENGE
     EVEVEEFYVK YKNFSYLHCQ WASVEELDKD KRIQQKIKRF KAKQGQNKFL SEIDDELFNP
     DYVEVDRILD FSRSTDDNGE PVTHYLVKWC SLPYEDSTWE LKQDIDQAKI EEFEKLMSRE
     PEMERVERPP ADDWKKSESS REYKNNNKLR EYQLEGVNWL LFNWYNTRNC ILADEMGLGK
     TIQSITFLYE IYLKGIHGPF LVIAPLSTIP NWEREFRTWT ELNVVVYHGS QASRRTIQLY
     EMYFKDPQGR VIKGSYKFHA IITTFEMILT DCPELRNIPW RCVVIDEAHR LKNRNCKLLE
     GLKMMDLEHK VLLTGTPLQN TVEELFSLLH FLEPGRFPSE TTFMQEFGDL KTEEQVQKLQ
     AILKPMMLRR LKEDVEKNLA PKEETIIEVE LTNIQKKYYR AILEKNFTFL SKGGGQANVP
     NLLNTMMELR KCCNHPYLIN GAEEKILEEF KETHNADSPD FQLQAMIQAA GKLVLIDKLL
     PKLKAGGHRV LIFSQMVRCL DILEDYLIQR RYPYERIDGR VRGNLRQAAI DRFSRPDSDR
     FVFLLCTRAG GLGINLTAAD TCIIFDSDWN PQNDLQAQAR CHRIGQSKSV KIYRLITRNS
     YEREMFDKAS LKLGLDKAVL QSMSGRENAT NGVQQLSKKE IEDLLRKGAY GALMDEEDEG
     SKFCEEDIDQ ILLRRTHTIT IESEGKGSTF AKASFVASGN RTDISLDDPN FWQKWAKKAE
     LDIDALNGRN NLVIDTPRVR KQTRLYSAVK EDELMEFSDL ESDSEEKPST KPRRPQDKSQ
     GYARSECFRV EKNLLVYGWG RWTDILSHGR YKRQLTEQDV ETICRTILVY CLNHYKGDEN
     IKSFIWDLIT PTADGQTRAL VNHSGLSAPV PRGRKGKKVK AQSSQPMLQD ADWLTTCNPD
     VLFQEDSYRK HLKHHCNKVL LRVRMLYYLR QEVIGDQADK ILEGADSSEI DVWIPEPFHA
     EVPADWWDKE ADKSLLIGVF KHGYEKYNSM RADPALCFLE RVGMPDAKAI AAEQRGTDML
     ADGGDGGEFD REDEDPEYKP TRTPFKDEID EFANSPPEDK EESVEIHPNK HGESNSELGQ
     LYWPNTSTLT TRLRRLITAY QRSYKRQQMR QEALMKTDRR RRRPREEVRA LEAEREAIIT
     EKRQKWTRRE EADFYRVVST FGIIFDPVKH QFDWNQFRAF ARLDKKSDES LEKYFNGFVN
     MCRRVCRMPV KPDDEPPDLS TMIEERASRT LYRIELLRKI REQVLHHPQL GERLKLCQPS
     LDLPEWWECG KHDKDLLIGA AKHGVSRTDY HILNDPELSF LEAHKNFAQN RGTGNANTVS
     SVNPLGAGCS QTPPIVPSTP IQEEKITEQT ESKVEGSENP AAKEKSDIKE ETDTADKDTK
     PDCDAEAEPG SVKCELKDIE MNTDVDPKSI SEKGSEEDEE EKMDDDDKSE ESSQPEAGAV
     SQGKNFDEES NASMSTARDE TRDGFYMEDG DASVVQLLHE RTFAFSFWPK DRVMINRLDN
     ICEAVLKGKW PVNRRQMFDF QGLIPGYTPT AVDSPLQKRS FAELSMVGQA SASGSEDITV
     SPQLSKEDAL NLSVPRQRRR RRRKIEIEAE RAAKRRNLME MVAQLRESQV VSENGQEKVV
     DLSKASREAA SSTSNFSSVT SKFILPNVST PVSDAFKTQM ELLQAGLSRT PTRHLLNGSL
     IDGEPPMKRR RGRRKNVEGL DLLFMSNKRT SLTVEDAEVT KAFEEDMEAL PARNIPSPGQ
     LDPDTRIPVI NLEDGTRLVG EDAPKNKDLV EWLKLHPTYT VDMPSYVPKS ADVLFSPFQK
     PKQKRHRCRN PNKLDINTLT GEERVPVVNK RNGKKMGGAM APPMKDLPRW LEENPEFAVA
     PDWTDIVKQS GFVPESMFDR LLTGPVVREE GASRRGRRPK SEIAKAAAAA AAVASTSGIN
     PLLMNSLFAG MDLTSLQNLQ NLQSLQLAGL MGFPPGLATA AAAGGDAKNP AAMLPLMLPG
     MAGLPNMFGL SGLLNNPITA TTGNATTASG QGETEDGASK AEEKKNENEE ENKDSEKSTD
     TVSATDSANG SVSAATAATT ATATTTTTTN TGLPTNPLAF NPFLLSTMAP GLFYPSMFLP
     PGLGGLTLPG FPALAGLQNA VGSNEEKATD KTEGTAFKDE ENLEGSDAEE SLDKTADSSV
     LEDEIAQGEE LDSLDGGEEI ENNENDE
//
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