ID W5J7B2_ANODA Unreviewed; 1290 AA.
AC W5J7B2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=ATP-dependent RNA helicase {ECO:0000313|EMBL:ETN58755.1};
GN ORFNames=AND_009658 {ECO:0000313|EMBL:ETN58755.1};
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:ETN58755.1};
RN [1] {ECO:0000313|EMBL:ETN58755.1, 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:ETN58755.1}
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:ETN58755.1}
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:ADAC009658-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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DR EMBL; ADMH02002124; ETN58755.1; -; Genomic_DNA.
DR STRING; 43151.W5J7B2; -.
DR EnsemblMetazoa; ADAC009658-RA; ADAC009658-PA; ADAC009658.
DR VEuPathDB; VectorBase:ADAC009658; -.
DR VEuPathDB; VectorBase:ADAR2_010471; -.
DR eggNOG; KOG0920; Eukaryota.
DR HOGENOM; CLU_001832_4_1_1; -.
DR OMA; PERVYVQ; -.
DR OrthoDB; 1095660at2759; -.
DR Proteomes; UP000000673; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF145; ATP-DEPENDENT RNA HELICASE DHX29; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF05773; RWD; 1.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:ETN58755.1};
KW Hydrolase {ECO:0000313|EMBL:ETN58755.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000673};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 107..152
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 244..271
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 463..637
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 734..915
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 244..271
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 217..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1290 AA; 146656 MW; 6F922B5BAD5C1564 CRC64;
MDEESRQLVA DCFLRAIVDP RSSNTSNEPP PTKQPVKVEL QVLRLKDESQ TLIMDTLRAI
HGEHFQLGDI SKYVDQGNRL KKNFWQDRGN LVIQGGCDFS NVVRTGNSNE DKFRMYAAMK
LHSYGFHRTH CEEALDHHNG DIDRSLELLF SKYFPPPADM APPPEEYDEE ELSTLRADER
EALESIYDKL FVEKERNRVW QLKFKIDHLL VHSPSEMKKL AERERQQQEE ERRRKQEELA
KKKKAKKEPC WNYAKGKCRY GNRCYYSHGP DESSTSEGGK GEGKKLLDKT IEEDPNWFFL
EVRFPPGNRY PFERPILLLR TTCPDIPDQL CLRVNRRLVQ ETIELTRDGM PCIYTVADLL
QNDTEIGRFI ELDRYQFLDP KRSLFYVPDE DEGREGPGGE LPSHHQRGNT GRQTGPRTNM
EQVLKEDRNI VRKFLDKQAN AAYREMVKAR SNLPAWGKMN EILELLESNQ ILVISGETGC
GKSTQVPQFL LDDWLLQSSR LGPNAKLRHV EIVCTQPRRL SAIGVAERVA EERIEKVGNT
VGYQIRLETR TSSSTRLTFC TTGILMRRLQ SDPQLSSVTH VIVDEVHERS EESDFLLLIL
KQLLEKRSDL KVILMSATLN SNLFASYFGD IPVLDIPGRT FPVEQLFLED ILERSGFVLE
PDSPYCRKLR KADRELLLQE LEYADLQASE VPPAKSIRDE NLKLPETFSR YADYSKQTCK
TLCLMDPLRI NPELIERVLT YIVDDPSHGW PQEGSILIFL PGLAEIQTVH EALTSSRLFG
PRGERFVLIP LHSMLTNEEQ ALVFRKAPKG KRKIVLSTNI AETSITIDDC VFVIDCGQMK
EKHFDSNSNM ESLEMVWVSR ANALQRKGRA GRVMPGVCIH LFTKPRFTNH ILAQPVPEIH
RIPLEPLLLR VKTLPTLQER PISAVLGATI EPPSEENIEA AKKRLVDVGA LDLDEQLTAL
GHHLAALPVD VRIGKLMLFG AIFQCLDSVL TIAAILSYKS PFVAPFAKRD EADNRKRQLA
IANSDHLTML NAYRRWLVAA QRSRYAGQCF AEENYLSSKT LTTIGEMKYQ FLELLVSIGF
VPIDLSGRSR SKRQQVDDLA ALTGAELNVN GDNNRLLAAI LCAALYPNVA KVLTPEKSFV
SGAGGAVPYL PQASDLRFKT RGDGYVALHP SSVNAQVGFF GSPFLVYQEK VKTSRIFIRE
TTMVPLLPMV LFSGSDLQIE LHGGDFVILL GDGWLMLQTP THQVAEMMKF LRLELVKMLE
LKISDPLLNL LHHEHGKRII ATIVHLINKE
//
