ID   G0MYV8_CAEBE            Unreviewed;       617 AA.
AC   G0MYV8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364117};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU364117};
GN   ORFNames=CAEBREN_03628 {ECO:0000313|EMBL:EGT47797.1};
OS   Caenorhabditis brenneri (Nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN   [1] {ECO:0000313|Proteomes:UP000008068}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG   Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA   Wilson R.K.;
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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=3.6.4.12;
CC         Evidence={ECO:0000256|RuleBase:RU364117};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364117}.
CC   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00005446, ECO:0000256|RuleBase:RU364117}.
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DR   EMBL; GL379821; EGT47797.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0MYV8; -.
DR   STRING; 135651.G0MYV8; -.
DR   EnsemblMetazoa; CBN03628.1; CBN03628.1; WBGene00142353.
DR   eggNOG; KOG0353; Eukaryota.
DR   HOGENOM; CLU_001103_12_5_1; -.
DR   InParanoid; G0MYV8; -.
DR   OMA; FKLSTMV; -.
DR   Proteomes; UP000008068; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0032392; P:DNA geometric change; IEA:UniProt.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   CDD; cd18015; DEXHc_RecQ1; 1.
DR   CDD; cd18794; SF2_C_RecQ; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032284; RecQ_Zn-bd.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; TIGR00614; recQ_fam; 1.
DR   PANTHER; PTHR13710:SF72; ATP-DEPENDENT DNA HELICASE Q1; 1.
DR   PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF16124; RecQ_Zn_bind; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364117};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU364117};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364117};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU364117}; Nucleus {ECO:0000256|RuleBase:RU364117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008068}.
FT   DOMAIN          95..270
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          298..443
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          588..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          6..47
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        588..610
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   617 AA;  69559 MW;  5B7040ACEE4044F8 CRC64;
     MGEVLLSKLS TELADIDGEI EQIDNKIGEL RRKKTQLVQK KQAIERKIEL KTHEDSDVVV
     DRWDRDGFSW SDEANKILKD RFHLESFRPL QRAAINAVMS KEDAVVILST GGGKSLCYQL
     PALLTKGLTL VVSPLISLVE DQILQLRKLN IDASCLNAST SKEETKRVED AITNKDSQFR
     LLYVTPEKLA KSKRMMNKLE KSLSVGFLKL IAIDEVHCCS QWGHDFRTDY AFLNVLKRQF
     KGVPILGLTA TATSNVLDDV KDMLGIQAAL VFRAGFNRSN LKYEVISKKS SDEECAEEIA
     HVINTQFSGQ TGIVYCLSRN DCEKMATLLK TKGIRAKHYH AYMEPSEKSS SHQNWISGKI
     QVIVATVAFG MGIDKPDVRF VIHHTIPKSI ENYYQESGRA GRDGLPATCI LYFKLSDVFK
     QSSMVQQDRT GLSNLYNIVR YASDSSTCRR VKMAEHFEEA WEPSWCQKQC DVCQRATSSE
     LKSTDVSKET KIAVQIIEDN LNAVKDGSGR ITGNKLLDLL SKKLAGSRNR VFCEKLILFL
     LLESYLQEDF HYTVYSVISY VVVGSKWSVY KGGEILMPLY SNELGLSETK SRKRKAGSSS
     NEKRVEAEDD EVVFLDD
//