ID   A0A3B4V6Z6_SERDU        Unreviewed;       642 AA.
AC   A0A3B4V6Z6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364117};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU364117};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000026526.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000026526.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A3B4V6Z6; -.
DR   Ensembl; ENSSDUT00000026998.1; ENSSDUP00000026526.1; ENSSDUG00000019205.1.
DR   GeneTree; ENSGT00940000157013; -.
DR   OMA; CYEIPAY; -.
DR   Proteomes; UP000261420; Unplaced.
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; 2.
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}.
FT   DOMAIN          116..291
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          314..465
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          55..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          600..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          7..34
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        55..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   642 AA;  72240 MW;  C39C4E79A653582E CRC64;
     MDRSGGNDDV QAELDSVETE LELVELQITE LLQKQTELTS RKNALLQRLE EACDTAQPSS
     SSSSASLKSS RADPVMSKQE MQRYDGADFS WSKEVEQQLK DSFHLSKFRP LQLRAINLSL
     SGKDLFLVMP TGRGKSLCYQ LPAVCSKGFT LVVTPLVSLM EDQIMYLKSI DVSAVMLNAS
     SSKEHAKTVM AGMTDPKTPF KLVYVTPEKI AKSKLLMSRL EKGYNANLLS RIAVDEVHCC
     SQWGHDFRPD YKLLGILKRQ FPKVPLLGLT ATATSSVLKD CEKILCVSQP ITLTSSFNRT
     NLYYEVRIKD SDASISDVAS LINSRYKDQS GIVYVFSQKD AESVSSELQK RDILAYPYHA
     NMDPDDKSRV HRKWTSNKIR VVVATVAFGM GIDKPDVRFV IHHTISKSIE NYYQESGRAG
     RDDQPADCII YFGFSDIFRI STMVVMENVG QQKLLQMVDY CQNIDRCRRS LMAVHFDEVW
     DDEGCNQMCD TCRHAKDYTT VDITQHARQV VQILELAGSM DEKLTPLKLV EAWMGKGPAK
     RRKMIQTTTL SRLQAEAVIV RLLLQGYLRE DFSFTPYTTY FYMKLGRKAP LLKSQTHTLS
     MKMRTTESGS AGVKAAKTKE GKRSGQSAGD APVSKKMKTD FP
//