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Database: UniProt
Entry: A0A0R3S245_9BILA
LinkDB: A0A0R3S245_9BILA
Original site: A0A0R3S245_9BILA 
ID   A0A0R3S245_9BILA        Unreviewed;       646 AA.
AC   A0A0R3S245;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
OS   Elaeophora elaphi.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX   NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000877001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EEL_0000877001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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. DDX41 subfamily.
CC       {ECO:0000256|ARBA:ARBA00023594}.
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DR   AlphaFoldDB; A0A0R3S245; -.
DR   STRING; 1147741.A0A0R3S245; -.
DR   WBParaSite; EEL_0000877001-mRNA-1; EEL_0000877001-mRNA-1; EEL_0000877001.
DR   Proteomes; UP000050640; Unplaced.
DR   GO; GO:0043186; C:P granule; IEA:UniProt.
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   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR   CDD; cd17951; DEADc_DDX41; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR044113; DEADc_DDX41.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR   PANTHER; PTHR47958:SF103; ATP-DEPENDENT RNA HELICASE DDX41-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000492}.
FT   DOMAIN          204..232
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          235..420
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          444..591
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          34..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          107..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           204..232
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        34..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   646 AA;  72448 MW;  750392E78F78E716 CRC64;
     MVIVDGVEGR AETSSDRNES ADVLLALQKY QAKRKQIEEE EARRRREGLL SDEEDASMDD
     VFIPARLRKK EKMHRRALLK QVLHAKGGAP DVDTEKEDLE FLERKRRKKE EEKKAEEAKK
     SLLEKHNELL ETEIGDRDSE KRKREEEQKL LESVAPGTAL MAVAEIARGV KYEESIKTSN
     EEHAAMRRKK GILVDGESVP PPIGSFIEMK FPPPVIKALR DKKIICPTVI QMQGIPVALS
     GRDMIGIAST GSGKTLTFAL PLIMFCLEQE VSLPFRHGEG PYGLIIVPSR ELAKQIHDVI
     ERLFENICDG TKFPRLRVGL CIGGLPISEQ ARVFERGVHV CVATPGRLSD LLSKKVFNLQ
     VCRYLVLDEA DRMLDMGFEE EIRTIFSFFK GQRQTLLFSA TMPRKIQNFA RSALVRAVIV
     NVGRAGAASL NVVQEIEYVR ADEKLTRILD CLQKTAPRVL IFAEKKSDVD NIYEYLLVKG
     VDVASLHGGK DQKDRHTGVD AFRRGEKDVL VATDVASKGL DFENIQHVIN FDMPEDIENY
     VHRIGRTGRS GRKGMATTFI NRRADMSVLQ DLRALLLEAG QELPLFLRDM GGPELELPSD
     SANADDKGCA YCSGLGHRIT NCPKLENVQT KTAAYLSRPD YGGEEI
//
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