ID   A0A183MS46_9TREM        Unreviewed;       426 AA.
AC   A0A183MS46;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=SMRZ_LOCUS18871 {ECO:0000313|EMBL:VDP29477.1};
OS   Schistosoma margrebowiei.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=48269 {ECO:0000313|WBParaSite:SMRZ_0001887201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMRZ_0001887201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP29477.1, ECO:0000313|Proteomes:UP000277204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zambia {ECO:0000313|EMBL:VDP29477.1,
RC   ECO:0000313|Proteomes:UP000277204};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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. DECD subfamily.
CC       {ECO:0000256|ARBA:ARBA00038213}.
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DR   EMBL; UZAI01017784; VDP29477.1; -; Genomic_DNA.
DR   STRING; 48269.A0A183MS46; -.
DR   WBParaSite; SMRG1_25220.2; SMRG1_25220.2; SMRG1_25220.
DR   WBParaSite; SMRZ_0001887201-mRNA-1; SMRZ_0001887201-mRNA-1; SMRZ_0001887201.
DR   Proteomes; UP000050790; Unassembled WGS sequence.
DR   Proteomes; UP000277204; 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; cd17950; DEADc_DDX39; 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; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR   PANTHER; PTHR47958:SF104; ATP-DEPENDENT RNA HELICASE WM6; 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   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};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000277204}.
FT   DOMAIN          43..71
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          74..248
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          260..421
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           43..71
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        1..16
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   426 AA;  49089 MW;  AD8FAC9E9CB80B17 CRC64;
     MADEAELLDY EDEEQETVQE ARPNGEATAK KGVKGAYVTI HSSGFRDFIL KPELLRAIVD
     CGFEHPSEVQ HECIPQAILS MDVLCQAKSG MGKTAVFVIA TLQQLDPEGE ANTTVLVLCH
     TRELAFQISK EYERFSKYMP KIKVGVFFGG MPIRKDIETL TKSPVHIVVG TPGRILDLVR
     SKTLKLQHVK HFIIDECDKM LDTLDMRRDV QEIFRMTPHQ KQVMMFSATM SKEIRPVCRN
     FMQDPLEIFI ENDSKLTLHG LRQHYVKVKE NEKNRKLFEL LDELQFNQVI IFVKSVQRCM
     ALAQLLVDQN FPAIAMHRNM AQEERLERYQ AFKNFQKRLL VATNLFGRGM DIERVNIVFN
     YDMPEDSDTY LHRVARAGRF GTKGLAITFI SDEVDAKVLN EVQNRFEVNI SELPDVMEIS
     SYMEDR
//