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Database: UniProt
Entry: A0A183VY16_TRIRE
LinkDB: A0A183VY16_TRIRE
Original site: A0A183VY16_TRIRE 
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}.
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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
//
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