ID   DHX35_CAEEL             Reviewed;         732 AA.
AC   Q9BKQ8;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Probable ATP-dependent RNA helicase DHX35 homolog;
DE            EC=3.6.4.13;
GN   Name=ddx-35 {ECO:0000312|WormBase:Y67D2.6};
GN   ORFNames=Y67D2.6 {ECO:0000312|WormBase:Y67D2.6};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000305}.
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DR   EMBL; FO081642; CCD73030.1; -; Genomic_DNA.
DR   RefSeq; NP_497420.1; NM_065019.3.
DR   AlphaFoldDB; Q9BKQ8; -.
DR   SMR; Q9BKQ8; -.
DR   BioGRID; 40564; 1.
DR   STRING; 6239.Y67D2.6; -.
DR   EPD; Q9BKQ8; -.
DR   PaxDb; Q9BKQ8; -.
DR   PeptideAtlas; Q9BKQ8; -.
DR   EnsemblMetazoa; Y67D2.6.1; Y67D2.6.1; WBGene00022056.
DR   GeneID; 175308; -.
DR   KEGG; cel:CELE_Y67D2.6; -.
DR   UCSC; Y67D2.6; c. elegans.
DR   CTD; 175308; -.
DR   WormBase; Y67D2.6; CE27311; WBGene00022056; ddx-35.
DR   eggNOG; KOG0922; Eukaryota.
DR   GeneTree; ENSGT00940000156142; -.
DR   HOGENOM; CLU_001832_5_11_1; -.
DR   InParanoid; Q9BKQ8; -.
DR   OMA; STEQQMY; -.
DR   OrthoDB; 354219at2759; -.
DR   PhylomeDB; Q9BKQ8; -.
DR   PRO; PR:Q9BKQ8; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00022056; Expressed in adult organism and 3 other tissues.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032502; P:developmental process; IEA:UniProt.
DR   GO; GO:0022414; P:reproductive process; IEA:UniProt.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..732
FT                   /note="Probable ATP-dependent RNA helicase DHX35 homolog"
FT                   /id="PRO_0000055170"
FT   DOMAIN          87..251
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          283..457
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           198..201
FT                   /note="DEAH box"
FT   COMPBIAS        1..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         100..107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   732 AA;  82544 MW;  E64171070E43BF41 CRC64;
     MSYHPGHGHR QEPRKGAGAR RGFARPDDSA DAPRTGPLIF EERSTENAGA APPIEEQLKV
     HNNPYASLNI QQQRIRLPIF KNRGHILYMC ERYRTIIIVG ETGCGKSTQV PQFLLEAGWA
     ADGRQIVITQ PRRVAVVTLA TRVAEEKDCI LGHDVGYTVR FDDVSDKDTK VKFMTDGLLL
     REILADPLLS KYSIIMIDEA HERSCNTDIL LGLLRKIIQI RNDLRIIVSS ATLDAELFKD
     FFEMNETGNS DKDTAGIISV EGRTHPVAVH HTKTSVPDYC QSAVDTVINI HKHENPGDIL
     VFLTGQDEVE DVCEKLRELA GNLKNCDRLW VVPCYGALPA REQMKAFDST PHGTRKVVVA
     TNIAEASITI PGICYVIDTG YVKLRAQHAA NGVETLMRVT VSKASAEQRA GRAGRIRPGK
     CYRLYPESEF ERFAEGTVPE IQRCQMASTI LQLKALGVQN VHRFHYLSPP PSWAMINGLE
     LLYALGAIDE TSQLTSPLGL QMAEFPLPPM HSKCLLKSAE FGCSTEMVTI VAMMQIQDVF
     ITPYRQRHQA DVIRKKFAVE EGDHMTMLNV FTKFVENGRS KKWCSDHFVN YRGLMRADNV
     RSQLVRLLKR FEIEKVSSRG LINCSENIRQ CLVTGFFSQA AQYHYTGKYM TVKESFPFNM
     YKGSSIMFKK DYPKWVIFTE VMQDSIRDVT VIEPEWLYEL APHYYEFGTE GELAEKRMRG
     PAATSAAADD DY