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Database: UniProt
Entry: A0A1I7UZ62_9PELO
LinkDB: A0A1I7UZ62_9PELO
Original site: A0A1I7UZ62_9PELO 
ID   A0A1I7UZ62_9PELO        Unreviewed;       586 AA.
AC   A0A1I7UZ62;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=ATP-dependent RNA helicase DDX1 {ECO:0000256|ARBA:ARBA00014916};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE   AltName: Full=DEAD box protein 1 {ECO:0000256|ARBA:ARBA00032348};
OS   Caenorhabditis tropicalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold630.g20803.t1};
RN   [1] {ECO:0000313|WBParaSite:Csp11.Scaffold630.g20803.t1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) 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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic granule
CC       {ECO:0000256|ARBA:ARBA00004463}. Mitochondrion
CC       {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008765}.
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DR   AlphaFoldDB; A0A1I7UZ62; -.
DR   STRING; 1561998.A0A1I7UZ62; -.
DR   WBParaSite; Csp11.Scaffold630.g20803.t1; Csp11.Scaffold630.g20803.t1; Csp11.Scaffold630.g20803.
DR   Proteomes; UP000095282; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004527; F:exonuclease 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; cd18787; SF2_C_DEAD; 1.
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; 3.
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; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   InterPro; IPR003877; SPRY_dom.
DR   PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR   PANTHER; PTHR47958:SF186; ATP-DEPENDENT RNA HELICASE DDX1; 1.
DR   Pfam; PF00270; DEAD; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50188; B302_SPRY; 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   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          2..30
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          60..252
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   DOMAIN          257..424
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          494..586
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   MOTIF           2..30
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
SQ   SEQUENCE   586 AA;  64633 MW;  9200DB819FD7ED10 CRC64;
     MTAFEEFGII PELSDAIDSL NWTLPTAVQS EAIPAILGGA DALIAAETGS GKTGAFCLPI
     VQIVWERRKA AKSQATPTTS EVTPTFSPSD YCINREDRDV SLQIDRTGLN CEGRVGKEWH
     GARGRGGLVG GGKYYYEVTV TRDGLCRVGW ATLAASLKIG TDFESFGYGG TGKKSYGKVF
     DNYGTSFTTN DVLGCFLDLD DLKIWWSKNG EHFPTAYSID RKFRDSAHCL FPAVLCQNSG
     LSVNFGGGHA PFRHPPGNGF QAVAKAANIK WWTPEERDTV DLTTPLCVIL EPTRELVQQT
     FQNIQTFAGV LKEPEIRCIS LAAGESMSQI LRTLETGCDI VVGTPSRIVD LIQTGKLATK
     SLQFVVIDEI DQFLADKNGS AGQIATMFRA LPLVTQDGVI ACSATLHNHE VTRFADRHMN
     FPQWIDLKGA DCVSADVHHV VCHVDAAEDK QWIRQKHQPI HLEDDHIHDS DQIRPGTQDR
     ETLSLGTKIL KGIYVVRAIQ ALKMDKAIIF CRTKQQCDHM EHFLHQNNFT AACLHGDRSA
     EERQASLEGF RKGQMRFLVC TDVVARGLDV QGVPFGREFI IKTAEK
//
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