ID   A0A0K0DVI4_STRER        Unreviewed;      1118 AA.
AC   A0A0K0DVI4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
OS   Strongyloides stercoralis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000125100.1};
RN   [1] {ECO:0000313|WBParaSite:SSTP_0000125100.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-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=3.6.4.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001556};
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000256|ARBA:ARBA00008792}.
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DR   AlphaFoldDB; A0A0K0DVI4; -.
DR   STRING; 6248.A0A0K0DVI4; -.
DR   WBParaSite; SSTP_0000125100.1; SSTP_0000125100.1; SSTP_0000125100.
DR   Proteomes; UP000035681; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0022414; P:reproductive process; IEA:UniProt.
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; IPR003593; AAA+_ATPase.
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; 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:SF99; ATP-DEPENDENT RNA HELICASE DHX37-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00382; AAA; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035681}.
FT   DOMAIN          250..416
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          445..671
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          88..115
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1118 AA;  128275 MW;  303CABD2772289D5 CRC64;
     MDRKRKQDKE ENVNYIAPSN DTQYETSADV SNQILLPSKA KKKKVVETCA PTKKLSRKKV
     EMQQKYKEKK LASLSKTKKK QLARVAARKE EKINLENLFT ELQQYQLQND NLSLITNSMD
     AKRKKDVTKF PTKLKSNDKD TSKKWDIDDG RKQKDFFETD SSSSDEDVEE EMKEFFNKIN
     QKKENQVIKE KCSVDKSKEQ DHSNSEMKPK IDEKEDLSPI VGKKIIVNRL DSIQEQRSSL
     PIFAEEQEIV ESINNNKVTI ICGETGSGKT TQVPQFLYEA GYTSKGHLIG ITEPRRVAAM
     SMAARVGAEL NDSDLSSYQI RFEGNKNIKT RILFMTDGVL MRELQQDIML SKFSVIIIDE
     AHERSMYSDV LIGILSRIVP LRSKKGFPLK LIIMSATLQL EDFMQKHLFP TIVPKVIKVE
     TRQFPVTIHF EKTTPSDFCD AAFKKVCQIH EKLPPGAILV FVSGQLDVER IIKKLKERYP
     LKNKRRKFQH KNLKNTTDEG NLDIDEFGVN DAACFDGNLD NDEEITLVEN TVIHPPPSNS
     QPLYCLPLYS LLSTERQKRI FNPIPEKSRL CIVATNVAET SITIPNIKYV IDSGKEKRKE
     YDVVTGVNRF VISWCSQASA NQRSGRAGRV QAGHAYRLYS SAVFQGFDKF SIPEILNKPT
     DQLILHLKSM NIVKVIHFPF VTKPEADQLE VSEQKLVKMG ALSVELNGQL KEAKITKLGR
     TLAALPLSPE YGKVLVMANQ KNLFNYAITL AAILSVREPL ISLRSIKGKD NEDTMALIKE
     ELVKRYKLCS SGQSKLLGDI TLLLKLMGAA LYGKWNQKEC EKMGLRYKAF LEARKMRKQL
     ITLVNTNAEG MIDGGEINID DDLEPPTEIQ CKQLRQILVS CLPERIARKV EGSDNLNQND
     IPKGAYYCQK LEDYVFIDPS SIVYKIQPEY VLYQEIIQTN EKRLMTGCCV VDAEWISILA
     SEYCTFYPFE NKNSLSNKDE VEIYKYNEKL GTVVEEVKCF FSPHQWYLGI CERPLSVNIT
     LYKLFAYHIL EGNVLKPLKK YKEYLLAQPS SLLKNWAKLQ ERTEAFINKL VEREIHQKSK
     IISLWKNGEK EYLLEEYLMW LPESIHDKVT LEWPPYEE
//