ID A0A183VY16_TRIRE Unreviewed; 433 AA.
AC A0A183VY16;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=TRE_LOCUS5372 {ECO:0000313|EMBL:VDQ01252.1};
OS Trichobilharzia regenti (Nasal bird schistosome).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Trichobilharzia.
OX NCBI_TaxID=157069 {ECO:0000313|WBParaSite:TRE_0000537601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TRE_0000537601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDQ01252.1, ECO:0000313|Proteomes:UP000280995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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|RuleBase:RU365068};
CC -!- DOMAIN: The helicase domain is involved in the stimulation of RELA
CC transcriptional activity. {ECO:0000256|RuleBase:RU365068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC {ECO:0000256|RuleBase:RU365068}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; UZAO01054432; VDQ01252.1; -; Genomic_DNA.
DR STRING; 157069.A0A183VY16; -.
DR WBParaSite; TRE_0000537601-mRNA-1; TRE_0000537601-mRNA-1; TRE_0000537601.
DR Proteomes; UP000280995; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd12873; SPRY_DDX1; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003877; SPRY_dom.
DR PANTHER; PTHR24031:SF307; ATP-DEPENDENT RNA HELICASE DDX1; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU365068};
KW Helicase {ECO:0000256|RuleBase:RU365068};
KW Hydrolase {ECO:0000256|RuleBase:RU365068};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU365068};
KW Reference proteome {ECO:0000313|Proteomes:UP000280995};
KW RNA-binding {ECO:0000256|RuleBase:RU365068};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 397..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..226
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT DOMAIN 228..407
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 433 AA; 47527 MW; 4F3531676094D1FA CRC64;
MGVLPELSKA VQEMDWILPT DIQSEAVPLI LGGGDVLMAA ETGSGKTGAF CLPVLQIVYE
TLKLLQSNKQ LNVYDRTEAM AIDSNGLLCQ SRDPGGWHGA RANRGVKNSG RYYYEAHVTD
EGLCRVGWST LNASHDVGTD AESFGFGGTG KMSHRRQFDS YGEPFGKGDT LGCFLDLDNG
AVSWSKNGKI FGKAYDIPAA LRSKGLFPSV CLKNAELKFN FGDSTFNFPP PNGWTAVSLC
SEANRVETTF KATVSAATSK PKPNAPLALI IEPSRELAEQ TFEQIKKFKR YLKDPSPREC
LLIGGANTKQ QMDELHSGVD IVVATPGRLD DLISTQSLLL SSCRFFVLDE CDGLLSAGYG
DMITRIHNQI PKATADGNRL QMIVCSATLH SMDVKRLAVS FCLDLWILLT FYFVKFLLSH
SSNVLKCKLY YYY
//