ID   Q93413_CAEEL            Unreviewed;      1119 AA.
AC   Q93413;
DT   01-FEB-1997, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 3.
DT   27-MAR-2024, entry version 182.
DE   SubName: Full=Helicase ATP-binding domain-containing protein {ECO:0000313|EMBL:CAB02082.3};
GN   Name=drh-3 {ECO:0000313|EMBL:CAB02082.3,
GN   ECO:0000313|WormBase:D2005.5};
GN   ORFNames=CELE_D2005.5 {ECO:0000313|EMBL:CAB02082.3}, D2005.5
GN   {ECO:0000313|WormBase:D2005.5};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000313|EMBL:CAB02082.3, ECO:0000313|Proteomes:UP000001940};
RN   [1] {ECO:0000313|EMBL:CAB02082.3, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CAB02082.3,
RC   ECO:0000313|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RA   Sulson J.E., Waterston R.;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0007829|PDB:6M6Q, ECO:0007829|PDB:6M6R}
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 939-1108 IN COMPLEX WITH ZN(2+).
RX   PubMed=34403472; DOI=10.1093/nar/gkab712;
RA   Li K., Zheng J., Wirawan M., Trinh N.M., Fedorova O., Griffin P.R.,
RA   Pyle A.M., Luo D.;
RT   "Insights into the structure and RNA-binding specificity of Caenorhabditis
RT   elegans Dicer-related helicase 3 (DRH-3).";
RL   Nucleic Acids Res. 49:9978-9991(2021).
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:ARBA00029316};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000256|ARBA:ARBA00029316};
CC   -!- INTERACTION:
CC       Q93413; Q95XS0: eri-5; NbExp=3; IntAct=EBI-866549, EBI-866573;
CC       Q93413; G5ECM1: rrf-1; NbExp=2; IntAct=EBI-866549, EBI-7692364;
CC   -!- SIMILARITY: Belongs to the helicase family. RLR subfamily.
CC       {ECO:0000256|ARBA:ARBA00006866}.
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DR   EMBL; BX284601; CAB02082.3; -; Genomic_DNA.
DR   PIR; T20332; T20332.
DR   RefSeq; NP_492161.3; NM_059760.5.
DR   PDB; 6M6Q; X-ray; 2.80 A; A/B=1-335.
DR   PDB; 6M6R; X-ray; 1.89 A; A=939-1108.
DR   PDB; 6M6S; X-ray; 1.60 A; A/B=939-1108.
DR   AlphaFoldDB; Q93413; -.
DR   SMR; Q93413; -.
DR   DIP; DIP-35120N; -.
DR   IntAct; Q93413; 3.
DR   MINT; Q93413; -.
DR   STRING; 6239.D2005.5.1; -.
DR   EPD; Q93413; -.
DR   PaxDb; 6239-D2005-5; -.
DR   PeptideAtlas; Q93413; -.
DR   EnsemblMetazoa; D2005.5.1; D2005.5.1; WBGene00008400.
DR   GeneID; 172546; -.
DR   KEGG; cel:CELE_D2005.5; -.
DR   UCSC; D2005.5; c. elegans.
DR   AGR; WB:WBGene00008400; -.
DR   WormBase; D2005.5; CE36120; WBGene00008400; drh-3.
DR   eggNOG; KOG0354; Eukaryota.
DR   GeneTree; ENSGT00940000153173; -.
DR   HOGENOM; CLU_297035_0_0_1; -.
DR   InParanoid; Q93413; -.
DR   OMA; SSMRIAC; -.
DR   OrthoDB; 342391at2759; -.
DR   PhylomeDB; Q93413; -.
DR   Reactome; R-CEL-1169408; ISG15 antiviral mechanism.
DR   Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR   Reactome; R-CEL-936440; Negative regulators of DDX58/IFIH1 signaling.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00008400; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0000794; C:condensed nuclear chromosome; IDA:WormBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR   GO; GO:0070090; C:metaphase plate; IDA:WormBase.
DR   GO; GO:0043186; C:P granule; IDA:WormBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IDA:WormBase.
DR   GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IDA:WormBase.
DR   GO; GO:0003725; F:double-stranded RNA binding; IDA:WormBase.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070063; F:RNA polymerase binding; IPI:WormBase.
DR   GO; GO:0003727; F:single-stranded RNA binding; IDA:WormBase.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:1903863; P:P granule assembly; IMP:WormBase.
DR   GO; GO:0035194; P:regulatory ncRNA-mediated post-transcriptional gene silencing; IMP:WormBase.
DR   GO; GO:0030422; P:siRNA processing; IMP:WormBase.
DR   CDD; cd15804; RLR_C; 1.
DR   Gene3D; 1.20.1320.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 2.170.150.30; RIG-I-like receptor, C-terminal regulatory domain; 1.
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; IPR038557; RLR_C_sf.
DR   InterPro; IPR021673; RLR_CTR.
DR   PANTHER; PTHR14074:SF16; ANTIVIRAL INNATE IMMUNE RESPONSE RECEPTOR RIG-I; 1.
DR   PANTHER; PTHR14074; HELICASE WITH DEATH DOMAIN-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF11648; RIG-I_C-RD; 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; PS51789; RLR_CTR; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:6M6Q, ECO:0007829|PDB:6M6R};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:CAB02082.3};
KW   Helicase {ECO:0000313|EMBL:CAB02082.3};
KW   Hydrolase {ECO:0000313|EMBL:CAB02082.3};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW   Metal-binding {ECO:0007829|PDB:6M6R, ECO:0007829|PDB:6M6S};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Proteomics identification {ECO:0007829|EPD:Q93413,
KW   ECO:0007829|PeptideAtlas:Q93413};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW   Zinc {ECO:0007829|PDB:6M6R, ECO:0007829|PDB:6M6S}.
FT   DOMAIN          379..558
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          731..915
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          938..1066
FT                   /note="RLR CTR"
FT                   /evidence="ECO:0000259|PROSITE:PS51789"
FT   BINDING         952
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:6M6R, ECO:0007829|PDB:6M6S"
FT   BINDING         955
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:6M6R, ECO:0007829|PDB:6M6S"
FT   BINDING         1007
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:6M6R, ECO:0007829|PDB:6M6S"
FT   BINDING         1010
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:6M6R, ECO:0007829|PDB:6M6S"
SQ   SEQUENCE   1119 AA;  129096 MW;  EDBDA9994166DF5A CRC64;
     MQPTAIRLED YDKSKLRLPF ESPYFPAYFR LLKWKFLDVC VESTRNNDIG YFKLFESLFP
     PGKLEEIARM IIDEPTPVSH DPDMIKIRNA DLDVKIRKQA ETYVTLRHAH QQKVQRRRFS
     ECFLNTVLFD EKGLRIADEV MFNYDKELYG YSHWEDLPDG WLTAETFKNK FYDEEEVTNN
     PFGYQKLDRV AGAARGMIIM KHLKSNPRCV SETTILAFEV FNKGNHQLST DLVEDLLTEG
     PAFELKIENG EEKKYAVKKW SLHKTLTMFL AIIGFKSNDK KEKNEHEEWY YGFIDAMKND
     PANRAALYFL DKNWPEELEE REKERDRIRL TLLKSQRTNE EAVGEDVCTT IRPQPKDSGY
     NPDAVVTELV LRTYQEELVQ PALEGKNCVI VAPTGSGKTE VAIYAALKHI EERTSQGKPS
     RVVLLVPKIP LVGQQKDRFL KYCNGMYEVN GFHGSESSVS GTGRRDEVIA THVSVMTPQI
     LINMLQSVRQ NERLYVSDFS MMIFDEVHKA AKNHPYVLIN QMVQEWKYEK PQIIGLTASL
     SVKVDGQKDE NQMLNDIYNM LALINAPHLS TITRQSSIDE LNEHVGKPDD SVELCLPAKE
     NILRDYIERY LNHAHGKFLE ELASMSKSTG RNNTIPPNMI NTFKKNQPKN YEYYDSLLQG
     IIQELNKLNV PEKWNSQTWA KYMKVYLEAR GIVDLMPAMV AFKYMEKAIG KLNESHSETV
     EYSTFIKDHD TLKQTIQSVE PEIVLRLKNT LTNQFHVAPE SRVIIFVTQR STAQRVSDFL
     NESKVLDQFG NYGEQMVGYV LGTNKQGAVQ QTSQEQQLTL DKFNNGRLKV IVATSVVEEG
     LDVTACNLII KYNCSSGSAI QLVQQRGRAR AKNSRSVLLS VKSSINETET NALISEKYMR
     LCVKKITENG EKQLAAEVKR VAELNAAERK RNLEEQLNLR LRHENKIYKL MCSNCSKEFC
     KSIYIKKVFS NYMVFDPSVW RFLHVESKRK VSKYLSEDNQ PLSDIKCFHC KLDVGRAYKI
     RGTYLPQLSV KALTFVQESD YSSMTKAKWS DVEQDLFYIS EAIEDDFRIM LNALSDTEEN
     IEKKIVLDLD SRQHNKQLEM KRFHIQQEPP TKGVAPEAQ
//