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Database: UniProt
Entry: A0A182N8C4_9DIPT
LinkDB: A0A182N8C4_9DIPT
Original site: A0A182N8C4_9DIPT 
ID   A0A182N8C4_9DIPT        Unreviewed;      1638 AA.
AC   A0A182N8C4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
OS   Anopheles dirus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR003898-PA, ECO:0000313|Proteomes:UP000075884};
RN   [1] {ECO:0000313|Proteomes:UP000075884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles dirus WRAIR2.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ADIR003898-PA}
RP   IDENTIFICATION.
RC   STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR003898-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00005446}.
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DR   STRING; 7168.A0A182N8C4; -.
DR   EnsemblMetazoa; ADIR003898-RA; ADIR003898-PA; ADIR003898.
DR   VEuPathDB; VectorBase:ADIR003898; -.
DR   OrthoDB; 5474026at2759; -.
DR   Proteomes; UP000075884; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   CDD; cd18018; DEXHc_RecQ4-like; 1.
DR   CDD; cd22289; RecQL4_SLD2_NTD; 1.
DR   Gene3D; 1.10.10.1460; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR021110; DNA_rep_checkpnt_protein.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001878; Znf_CCHC.
DR   NCBIfam; TIGR00614; recQ_fam; 1.
DR   PANTHER; PTHR13710:SF108; ATP-DEPENDENT DNA HELICASE Q4; 1.
DR   PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF11719; Drc1-Sld2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          717..732
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          906..1083
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1105..1278
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          146..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          186..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..336
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..425
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..525
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        792..813
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1638 AA;  182243 MW;  6DB370A2DF64E9CF CRC64;
     MEDHAFRAKY QKCKYRVKQW EKEFKNKNGR VPSKLDIRDS PREIKNSYKM YYQLKTSLLK
     DTLLDALDDD DDFDGSLISQ ECSFSQDVSD VSGMLTSGTI LNESALLDRS SSMSSLLTKP
     IGGTSTGNSS TVFAAEQVDK HNLTAWQDEK NRKPKPVAEM QKESETPKPV TMKTMQLMPQ
     SSLLLPKRNP RKSMSRNSFG PAVQGASGLS DTGGSKIVLP DLETLLTAKS KELENIAPKV
     EPPLLLTASE PINQLDERWL KRQSGGTADN STVHVNANHQ STTNFGLRNV NLASIASSAS
     FGMSSLSVSE KPDATDVGQS RQEERTGVQN TAYDRAMHSD SDGVIENSED ESAKTSPGMM
     HIAKKRKIFT SINRSPVERS ESKLSSPKLV PEMLAQNDRR DVENQDPSKE MVPEPEHEHG
     STPMVPKKRS SKKTPKAKTK QETKKLVEKV KTTVVPRSRS TRSNARKVAT YKEPTIGDME
     EESAHGFSSD DEDKDPDYKE QIEQCDESIK HESEEEVERT KSPPAKQTRS ARPVAPPKQT
     RVRRTTKKFS AISPKLSPGS SKPVVKAKKG KKPTQRKIDV DEEAERLEEP QEYVPEFGLD
     RLKSIPRVDI NELARDAKIA DSFILGAAGR PELKGSVGGK KAAAAGAKDT ALRKKMAAGK
     LNENFVRIDL RKKVFVKGKK TINYSRYKKA QWKAKKVAAL SGPDMDMRGC DGGVLTCFQC
     GGTGHMAFQC KKPIEDKLLP HDPDATEDSA FPTLEEAAAM ASDRTAVVHS SRMENLPAVA
     NPTWKMDGDK EEDGAAEEEE EAKEASIDPE DFEDEIEPDA VETRILSPPA PATQTTSTYI
     GHKIPEDFLK KSGLLEVTVS GGFKGTIEPL YRAQPGGAFP PTPSEVFEAL RMFGHESFRH
     GQERAVMRVL CGMSTLVTLS TGAGKSLCYQ LPAYLYRQKG NCITLVISPL VSLMEDQVHG
     MPDFLNAHCL HTNQTPKIRD RTMQAITAGE VDVLLISPEA VVAGEKSTGF GSLLRQLPPI
     AFACIDEAHC VSQWSHNFRP SYLMICKVLK EKLGVKTILG LTATATVQTR QSIVSHLAIP
     DGLQGIISDI PLPDNLLLTV SRDANRDAAL VELLQSDRFR ALQSIIVYCT RRDDCERVAT
     FIRTCFQDAA RARAAEANAN KRKRLNYVAE PYHAGMPASR RRTIQNAFMG GELRIVVATI
     AFGMGINKAD IRAIIHYNMP KNFESYVQEV GRAGRDGLLS HCHLFLDNKG NDRNELRRFI
     YANSIDRHVI RKLLQKIFVP CACAKILTNK NLAKELRQEL EAVNGIDWDA EFFEAESQPT
     ATNGQSRHTG NRKRLCPGHE ICFSIESTVQ QLDIPEENIA TFLCYLELDE QRYIQALSPA
     YTLCKVMSYG GVRPLRQAAK ECPPLAMAFA LDLKRGISHA ASTAIEFPVI DVASAIGWDS
     GVVKYQLKNL EWTMVNNVRK RSPLSVNFTD LGFRVRAPGD LSDDELDRTL DALYERVTHQ
     ERTQLSQLQY ISQALNSVCF NSIGPVCRED CPTGPSDKLK TIVREYFLTD ISKENIEIIP
     EPDDTTDEQL IADIRTTIYR YPENNFTGRA IARLFHGVQS PNYPALVWSR SNFWRAYTKT
     DFNRIVRLAN AEIVRIRT
//
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