ID   A0A2Y9NEU0_DELLE        Unreviewed;       649 AA.
AC   A0A2Y9NEU0;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364117};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU364117};
GN   Name=RECQL {ECO:0000313|RefSeq:XP_022433444.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022433444.1};
RN   [1] {ECO:0000313|RefSeq:XP_022433444.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022433444.1};
RG   RefSeq;
RL   Submitted (NOV-2023) 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=3.6.4.12;
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   RefSeq; XP_022433444.1; XM_022577736.1.
DR   AlphaFoldDB; A0A2Y9NEU0; -.
DR   STRING; 9749.A0A2Y9NEU0; -.
DR   Ensembl; ENSDLET00000003882; ENSDLEP00000003433; ENSDLEG00000002715.
DR   KEGG; dle:111176831; -.
DR   InParanoid; A0A2Y9NEU0; -.
DR   OrthoDB; 5474026at2759; -.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:1990814; F:DNA/DNA annealing activity; IEA:Ensembl.
DR   GO; GO:0036121; F:double-stranded DNA helicase activity; IEA:Ensembl.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0031297; P:replication fork processing; IEA:Ensembl.
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:UP000248483}.
FT   DOMAIN          100..275
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          300..451
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          599..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          11..45
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        606..622
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   649 AA;  73696 MW;  D79414C3EE37D111 CRC64;
     MASISALSEE LDSITSELHA VDIQIQELLE RQQELIQKKN VLTKRLKQCL ENSDAGESSE
     CDSSPASWNK EDFPWSGKVK DVLQNVFKLQ KFRSLQLETI NVTMSGKEVF LVMPTGGGKS
     LCYQLPALCS DGFTLVICPL ISLMEDQLMV LKQLGISATM LNASSSKEHV KWVHAEMVNK
     NSKLKLIYVT PEKIAKSKMF MSRLEKAYEA RRFTRIAVDE VHCCSQWGHD FRPDYKALGI
     LKRQFPNASL IGLTATATSH VLKDAQKILC VEKCFTFTAS FNRPNLYYEV RQKPSNTEDF
     IEDIVKLING RYKGQSGIIY CFSQKDSEQV TVSLQKLGIP AGAYHANMEP EDKTKVHRRW
     SANEIQVVVA TVAFGMGIDK PDVRFVIHHS MSKSMENYYQ ESGRAGRDDM KADCILYYGF
     GDIFRISSMV VMENVGQQKL YEMVSYCQNI SNCRRVLIAQ HFDEVWSPET CNKMCDNCCK
     EISFERKNIT AYCRDLIKIL KQAEELKEKL TPLKLIDSWM GKGAAKLRVA GVAPPALPRE
     DLEKIIAHFL IRQYLKEDYS FTAYATISYL KIGPKANLLN NEEHVITMQV KKPMQSCFRA
     ESPQSCHSEG ADKKRKEKTP SNFQKKSVNT LQQPDCKITG AKKRKIDNA
//