ID A0A182NF41_9DIPT Unreviewed; 897 AA.
AC A0A182NF41;
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=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
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:ADIR006263-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:ADIR006263-PA}
RP IDENTIFICATION.
RC STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR006263-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
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DR AlphaFoldDB; A0A182NF41; -.
DR STRING; 7168.A0A182NF41; -.
DR EnsemblMetazoa; ADIR006263-RA; ADIR006263-PA; ADIR006263.
DR VEuPathDB; VectorBase:ADIR006263; -.
DR OrthoDB; 5488182at2759; -.
DR Proteomes; UP000075884; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; 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:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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 InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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 PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 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 SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 263..427
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 452..625
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 897 AA; 103165 MW; FDA9F8253551A51F CRC64;
MSNHSTNRTI IPPPSDDSSS DSEEDARRRD LKARDEFAQR LKKRDEARTR NVAASSGSRA
YAEAAKRLRL ESEDKDKLIP QLRVESRRKY LEKRKDDKVV ELEADIRDDE YLFPEADITE
RERQDRAHKK RLLQIAQEHE KARDLERVQR YHMPKDTKQG ETEAYVEVDE RERVPHSEQK
KWEAERLASA TYQFGAKDAS KMAQQEAYDL LLEDQIDFVE VFKMDGTKEQ DRKPELTERE
KKRQTIAETQ KSLPIYAYKE DLIRAIKDHQ ILIVEGETGS GKTTQIPQYL YEAGFTNEGK
KIGCTQPRRV AAMSVAARVA EEMNVKLGNE VGYSIRFEDN TSERTVIKYM TDGTLHREFL
SEPDLASYSV MIIDEAHERT LHTDILFGLV KDVARFRKDL KLLISSATLD VEKFCEFFDN
APKFRIPGRR YSVDIFYTKA PEADYIEACV VTVLQIHATQ PLGDILVFLT GQEEIETCQE
MLQERMKRLG SKVRELLILP IYANLPSDMQ AKIFEPTPAN ARKVVLATNI AETSLTIDNI
IYVIDPGFAK QNNFNARTGM ETLLVVPISK ASANQRAGRA GRVAPGKCFR LYTAWAYQNE
LEENTVPEIQ RINLGNAVLM LKALGINDLL KFDFLDPPPQ QMLIMALEQL YALGALNHHG
ELTRLGRRMA EFPVDPMMAK MLLGSERYRC SEEAVTIAAM LSVNGAIFYR PKDKIIHADT
ARKNFDHREG DHLSLLQVYG QWAEAGYGTQ WCYENFIQYR SMRRARDVRD QLVGLMQRVE
IEMVSAGERD TVGVRKAITS GYFYHVARLS RSGHYRTVKH NQTVTIHPNS ALFEDLPRWL
LYHELVFTTK EFMRAVIPIE SKWLLEVAPH YYKAKDLEDS TNMKMPKTVG RTMRTDA
//
