GenomeNet

Database: UniProt
Entry: W5JCG0_ANODA
LinkDB: W5JCG0_ANODA
Original site: W5JCG0_ANODA 
ID   W5JCG0_ANODA            Unreviewed;      2184 AA.
AC   W5JCG0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=AND_007863 {ECO:0000313|EMBL:ETN60514.1};
OS   Anopheles darlingi (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN60514.1};
RN   [1] {ECO:0000313|EMBL:ETN60514.1, ECO:0000313|Proteomes:UP000000673}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA   Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT   "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT   the genome of the newly sequenced Anopheles darlingi.";
RL   BMC Genomics 11:529-529(2010).
RN   [2] {ECO:0000313|EMBL:ETN60514.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ETN60514.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23761445;
RA   Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I., Loreto E.L.,
RA   Zaha A., Teixeira S.M., Wespiser A.R., Almeida E Silva A.,
RA   Schlindwein A.D., Pacheco A.C., Silva A.L., Graveley B.R., Walenz B.P.,
RA   Lima Bde A., Ribeiro C.A., Nunes-Silva C.G., de Carvalho C.R., Soares C.M.,
RA   de Menezes C.B., Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M.,
RA   Golenbock D., Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA   Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M., Guimaraes G.M.,
RA   Goldman G.H., Padilha I.Q., Batista Jda S., Ferro J.A., Ribeiro J.M.,
RA   Fietto J.L., Dabbas K.M., Cerdeira L., Agnez-Lima L.F., Brocchi M.,
RA   de Carvalho M.O., Teixeira Mde M., Diniz Maia Mde M., Goldman M.H.,
RA   Cruz Schneider M.P., Felipe M.S., Hungria M., Nicolas M.F., Pereira M.,
RA   Montes M.A., Cantao M.E., Vincentz M., Rafael M.S., Silverman N.,
RA   Stoco P.H., Souza R.C., Vicentini R., Gazzinelli R.T., Neves Rde O.,
RA   Silva R., Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P.,
RA   Camargo E.P., de Vasconcelos A.T.;
RT   "The genome of Anopheles darlingi, the main neotropical malaria vector.";
RL   Nucleic Acids Res. 41:7387-7400(2013).
RN   [4] {ECO:0000313|EnsemblMetazoa:ADAC007863-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
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; ADMH02001919; ETN60514.1; -; Genomic_DNA.
DR   STRING; 43151.W5JCG0; -.
DR   EnsemblMetazoa; ADAC007863-RA; ADAC007863-PA; ADAC007863.
DR   VEuPathDB; VectorBase:ADAC007863; -.
DR   VEuPathDB; VectorBase:ADAR2_006199; -.
DR   eggNOG; KOG0384; Eukaryota.
DR   HOGENOM; CLU_000315_8_1_1; -.
DR   OMA; NFLMPNK; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000000673; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProt.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18666; CD1_tandem_CHD1-2_like; 1.
DR   CDD; cd17993; DEXHc_CHD1_2; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 2.40.50.40; -; 2.
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; IPR002464; DNA/RNA_helicase_DEAH_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:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 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; 1.
DR   PROSITE; PS50013; CHROMO_2; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000673};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          412..507
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          533..596
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          637..807
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          934..1085
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1166..1197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1209..1286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1588..1629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1737..2184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          390..417
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..185
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..234
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..258
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..317
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..384
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1237..1254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1263..1286
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1849..1871
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1881..1911
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1914..1970
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1986..2084
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2184 AA;  242555 MW;  4D7E13A9D0BB0D17 CRC64;
     MSQTKEDKSD SENESSSDSK SGSSSESESE SGSASSSSSS SDNENEAQNS SLNTSNPGDT
     SGTTNNTSTN SDAKGAIAEN GLSDRHRGHQ NHTVVPGLRR SDGEEEENNR VRNNLAERTV
     DGNERSRSTD ASGSDSDESA EGDGGKGNQQ NSDSDNSASK PSNTSRQTDD DDDDDDDEDD
     EDEDSASAVR INGPQQSIIP TAAAAIAASP DIDEDDDDED DDEDDDDDAG RDEEDGDEDH
     HSSKSSYDEQ DYAANQLRRK SARKKAVAAA RKRPTTQPAS KTTKKKKSTN SSRWKSDTSD
     ESDGSDGDSE DSVRYNRRKA AAAAAASKKR AATTAAASKA KAKKKKRSGA YSSDDASNSD
     DDRKRSATRR KTAVSYKEAS GDEPTDSDDL LEVDQEAEEA AAAAAAEEEK AETIERIIGQ
     RRGRKGATGA ITTVYAIEEN GDPNEGATSG KLASGELEEQ YLIKWSGWSY LHCTWESEET
     LKEQKVKGLK KLENYVKREA TLQHWRRYQA GPEDIDYYEC QQELQQDLLK SYYNVERIIA
     QAAKAEGGEG SDYLCKWESL PYSDSTWEDA SLLRKKWQKK VVEFHEREES RCTPSKYSKA
     IHDRPKFRHL KTQPEYLGED RGLKLRDYQM DGLNWLILTW CKKNSVILAD EMGLGKTIQT
     ICFLYYLFKS QQLYGPFLCV VPLSTMPAWQ REFAIWAPEM NFVTYLGDVQ SREMIRQYEW
     CFDRTKKLKF NAILTTYEIL LKDKTFLGSI SWASLLVDEA HRLKNDDSLL YKALKEFDTN
     HRLLITGTPL QNSLKELWAL LHFIMPQRFE TWDSFERNYG NDKSYTELHK ELEPYILRRV
     KKDVEKSLPA KVEQILRVEM TSIQRQYYRW ILTRNFDALR KGLKGSANTF LNIVIELKKC
     CNHAMLTRPV EFDAQVNQDD VLQQLLKGSG KLVLLDKLLC RLKETGHRVL IFSQMVRMLD
     ILAEYLQKRH FSYQRLDGSI KGELRRQALD HFNAEGSTDF CFLLSTRAGG LGINLATADT
     VIIFDSDWNP QNDLQAQARA HRIGQKNQVN IYRLVTARSV EENIVERAKK KMVLDHLVIQ
     RMDTTGRTVL DKNGGSNTSN PFNKEELSAI LKFGTEELFK EEEDGDEELV CDIDEILRRA
     ETRDEAPGMP GDELLSAFNV TTFDFDEDKV GGKPITTPST GKERGGEAGG DDAKDWDEII
     PKSYRELVEA EERDREIQDL YLPPRRLATK QSDTAADGKG SKGRNRRKGE EDSDDDSDAS
     VGLGGDEDGK TKRSRGRPSN KEKITGFTDA ELRRLIKSYK KFPAPLKRLE AIACDAELQE
     KPLSDLRRVA QLLHERCVQT MKEIARETEN EKHLAPSAAA AAAAAADGKR KCARAAYSSK
     IGGASFNVKT MMQCVDELQP LDEAIPADPH ERARWQLSFK TRPSHFDVDW NEEDDARLLR
     GIYQFGIGSW EAMKMDPSLG LSEKILSNDA NRKPQGKHLQ SRAEYLLKVL RKTLELKRGP
     SKPRKQRKPK DTKVAALMHH PIAAASPLAS GTESSVGCSI AATIAAVAAG EDVSMGGATA
     CGGGMATAAS SMNNRTITVK IRQQQRQAAA AAAAAGTAGN AKEKKKSKKD KQKESKKDKK
     KNTGPMHFTA NNEPCALNIL GDLDPTVFNE CKEKMRPVKK ALKTLDNPDE TLSQEEQLRQ
     TRDCLLSIGN QINLCLGEYR DPEKAKEWRS NLWYFVSKFT EFDARKLFKL YKHALKRSEG
     GGTSGDGGGS AGECSREATD GAASSSTPAI GSSPMKDGKD TTRNHHQHHH HHQSSGGIPP
     PTSPGYGSLG KIKKLSSSSK KDNGHSYERT PGDSPLNAHG SVDGAAGGGG DKSEEERSRS
     RRERKEKKRL QLLSGIGGPI VSESAVQQRS RYMAATGTTG PCSSSGGGAN DHGSDSGGKD
     EGSSMHSKRR LEEGEYDENS KEYKRLHGDS RNHRDKKWDE YGDRDRMRNV APRSGGPSTP
     QGGRGYPDAR DDRGTYLPDP SMDRWRDSSR YGSVSDHKRD RYDGYGSRHT PTGGYHRDRE
     RERDRDWERA DRDRDRDRER DRSDRERDRD RGDRSFKDKR RHGPSGVGSY PNSHYGIPPA
     GYYPPSDSSA YRSYPVGVYP SGQRPSPGAP LPAVVPGVGI TGSGAGGSAS GGVPVGGLPS
     SDYIDNRRGE YDRRPPPAAP NNQS
//
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