ID W5J7W9_ANODA Unreviewed; 1838 AA.
AC W5J7W9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=AND_008316 {ECO:0000313|EMBL:ETN60071.1};
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:ETN60071.1};
RN [1] {ECO:0000313|EMBL:ETN60071.1, 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:ETN60071.1}
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:ETN60071.1}
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:ADAC008316-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}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; ADMH02001988; ETN60071.1; -; Genomic_DNA.
DR STRING; 43151.W5J7W9; -.
DR EnsemblMetazoa; ADAC008316-RA; ADAC008316-PA; ADAC008316.
DR VEuPathDB; VectorBase:ADAC008316; -.
DR VEuPathDB; VectorBase:ADAR2_010972; -.
DR eggNOG; KOG1015; Eukaryota.
DR HOGENOM; CLU_237207_0_0_1; -.
DR OMA; CHTHIGT; -.
DR OrthoDB; 3269924at2759; -.
DR Proteomes; UP000000673; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd11726; ADDz_ATRX; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR025766; ADD.
DR InterPro; IPR041430; ADD_ATRX.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46357; TRANSCRIPTIONAL REGULATOR ATRX; 1.
DR PANTHER; PTHR46357:SF1; TRANSCRIPTIONAL REGULATOR ATRX; 1.
DR Pfam; PF17981; ADD_ATRX; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51533; ADD; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000000673};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 32..170
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT REGION 191..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1229..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1324..1363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1398..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1498..1523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1575..1689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1723..1750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1817..1838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1346..1363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1501..1523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1575..1592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1605..1633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1634..1656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1726..1746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1838 AA; 203017 MW; 243B10ECD63EAF4B CRC64;
MYEEHYDEDG FKLSFDDGVS KMDKRFFMRT FPNVSRIAER KVHCTSCHTH IGTAPISEAV
IRKHPVLGVT QCSDCHDFYN SGEFSKGEDG SELYCRWCGQ GGEVYCCSNC PFVFCKSCIT
KNLSRVCVQD VASNDNWSCF RCAPNILSHL RAQHWALVNY IQKQKKEIKK KNYNAQTIMA
MMKEDKTTCC ATKGKKSGSH GGSAKNAPKQ RTGSIPEASS SGTDSPKPST SKAATASTID
NDDSVPLAAL KKSKDPPSRK VVPAQVLLRQ PQIILNSVLA QKDKPQRRSE EETTESANRS
LPDRKKQQAM DQLDRIAGNK RVKEDHRAEK RQHESPKVPK SEDQAEEKSS AKKAKLSNDE
VVCTPDIMGL LSPVVEITPL APILRKARVS EKVYSSGREK GVSGTSTAAK PFSIDDLPTT
VSVQYGYRSK TKPTGNQPVP ANDIRSMHHK LQQYLGTKDP PATPKSSKLP LPMPVPSANR
GTQAPVYHII NGFRVDLHLA SQQSTYRLPD GKLIQVRKQK NSQHESVPNS NESDEAQDQN
KARSSARSTT NSSNCSYTVT SLPSALSNAS QTEEIPKGKR MFSVHQTLPK GHPQLANNNI
KHTQPHLLVT NQRMPVKQLR FQQLPSQQQQ PQQTPRLARE QQQSAVQQQQ SPVQQQELQL
SPQELQQSAL LQPQQQQPRP KSKQMKQKST LRPLLPAGTL LLRPQSELQQ QPFQQSQVQQ
QPFQQSQVQQ QPFQQSQVQQ QSFQQSQVQQ QPFQQSQMQQ QPFQQSQVQQ PQLQPHIILH
SPFQQQIQHE QQLLQQQMKQ REQSLQQQMQ QQPMQQFRIQ HSNPLPAQQI LRLPPYLEIS
TYQPPNPTGQ QNMLGLPLPS SMIPQQQMQP QPFQRPQPQQ PQIIVTAITP SAQQRKRGRP
SNKNHPPAAM NSSGAAVTAN NVTPIVRPPL LNTLRDMVNG PHQNSQVGRG KKEFEAKLLV
GAETCHQIMS KIATLTGSQS FKKIRHLRDL KELYLHMSYL LTYGVRRLQG LQEQCIEDVH
ALGFDNASEF LRTDVATNVN APEEADKSGQ GEANPEDDED DDCEIIEQRA TVIEVDSDDD
EGSQAAQPDQ ATNTSTQESV QLAARFEIVG GEQGNYDFRP IASPLAGGGE STATSSSNTQ
STGADNNSQR QNLERTAPPE GEVVVDQTNA SEPTNATKPS ECHLGNSSAS ASREQAPNDS
NELVELIELN EANDGGTDAQ CAHVNQEVEA RDRVSDGANE KAASTVEQDA STSKGNESLS
GSELLEQLDS LMDQGLLDDP KILATDTGIS DVSKEAAELF EICPKEVSEL LNNQMVDTMV
EQEQNNQTNQ EDVEKNDETK VVEEANKKQT TTNISSANNE SNLTLETTEV VDSSNQADGA
AIIVADKTNA CPSVELEIAT EDSKTEEKDQ SGESTVPQKS GANSLLEKQD ISVEGKDKED
SLKQSAGITN LDFAEQERKT LECGNEKDRM QSDDNAMSEM VGEKDSVDST IAIDSVADVD
MQDVSNRDEK VEQHSEGRTG DVEMKDVSNT MLDKGEIVND SNILKQNSVA SSVLICSEDL
ELQSIVPLED TNKAVEMKDK SSPNKRKEVI SIVSKPENNL EGEESQKPAD NQAQQMENTV
AQQQQTNENC SDARIRSTGK EESFSKAKIT VENPVKESED IDEETVDDFS EKSVEHLNDD
SMPGGSTIVP SVESSITLKA DKTIVLSCNT STKDDEMEIS EVKNAQPDDN VDTLSTGSSE
GFRSPETILS DSFLFDDPRV GMSGEGSKME ETNINEEASI STVGEASQEA NTVVETSAVL
DEQNIVNEDL ISLESISNEA WEDSEQDLTQ DGVNKKTE
//
