ID   A0A164SWM0_9CRUS        Unreviewed;      1274 AA.
AC   A0A164SWM0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN   ORFNames=APZ42_025600 {ECO:0000313|EMBL:KZS10016.1};
OS   Daphnia magna.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS10016.1, ECO:0000313|Proteomes:UP000076858};
RN   [1] {ECO:0000313|EMBL:KZS10016.1, ECO:0000313|Proteomes:UP000076858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xinb3 {ECO:0000313|EMBL:KZS10016.1,
RC   ECO:0000313|Proteomes:UP000076858};
RC   TISSUE=Complete organism {ECO:0000313|EMBL:KZS10016.1};
RA   Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT   "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL   Submitted (MAR-2016) 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:RU363044};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU363044};
CC   -!- SIMILARITY: Belongs to the helicase family.
CC       {ECO:0000256|RuleBase:RU363044}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZS10016.1}.
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DR   EMBL; LRGB01001920; KZS10016.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A164SWM0; -.
DR   STRING; 35525.A0A164SWM0; -.
DR   Proteomes; UP000076858; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR010285; DNA_helicase_pif1-like.
DR   InterPro; IPR025476; Helitron_helicase-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45786:SF82; ATP-DEPENDENT DNA HELICASE; 1.
DR   PANTHER; PTHR45786; DNA BINDING PROTEIN-LIKE; 1.
DR   Pfam; PF14214; Helitron_like_N; 1.
DR   Pfam; PF05970; PIF1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU363044};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA damage {ECO:0000256|RuleBase:RU363044};
KW   DNA recombination {ECO:0000256|RuleBase:RU363044};
KW   DNA repair {ECO:0000256|RuleBase:RU363044};
KW   Helicase {ECO:0000256|RuleBase:RU363044};
KW   Hydrolase {ECO:0000256|RuleBase:RU363044};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU363044};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076858}.
FT   DOMAIN          594..691
FT                   /note="Helitron helicase-like"
FT                   /evidence="ECO:0000259|Pfam:PF14214"
FT   REGION          172..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          294..358
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        172..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1274 AA;  146618 MW;  D36B6A08C23834CA CRC64;
     MYPHSTLTSF KGYLFILAAL LEFLYSVLKS YNDDLKTYLE GVDDRQKLNN TRIFMVTKGL
     IWAFTGTTFC STKKDAKNIV LPSDSNTGLP HNSRVIFKAD RRLRKVARQR YTRNLLTDKS
     HQGVVANCLS LDGTSLDMAR LVSCRTPLFF RDWRYLHRAR LDILPLRGSS AVSHQEAQHR
     PRSPGNAASQ ASPQRDCKQS HPGQRLRPDV EYILSGSRVM WIMTNQGAWR MLTSERNDDI
     RSTLGIDARS WGAFQFKARL AAIQGSMEMM CAHFHYGAPK PEDEEIPLLH MYLVEETEEE
     AEILRDLNRE QTANYRRTEN EEETRERLEE NRLRMERLRE EQAENEEIIR AMNALEHAEI
     VPLETEEERT HHEEILAACN QAGLQRTHRL ACKTIVSEDH RPLHDCGAMD IICKECGAKH
     FKGERPQDKK FMQCCRKGKV ILQPPKECPQ PLAKLLQNNH PKWKNFMAKI RTYNSTHAFA
     SLGAMYHNMT PVGPDTTNPK YADLYFMDAA QAGEFRAISS RTEDARLIRG EGRRKRVTQG
     KFYSFLMSIR DYFNNFMVGG PLIQQSMVDS YVKIEANRIK YIREHQAELH VAHPRAMKKA
     YQDAMAISGK FGKPVFFLTF TCNPKWKEIV ANIPTHLSAS DRPDIVARVF NQKKNKLVND
     IEKRQVLGFA TARIHVIEFQ KRGLPHCHML IWIYKRDAPA TEKDVDETIC AEIPDKTTHL
     RLYNIVMAHM IREPRGSTNK QSPCMDGNIC TKRFPKKFMA ETIVNDNGYP TYRRRNTGIL
     SLKFDSHINL EYCASIVKNI FKYVYKGYDC IKMDKKVETF QQEAGDVPTV VWDEITSHLD
     AHYVSAPEAC WRIFKFPLSD RSHTICRLAV HLPREQSVFF LPCNEQHAAI NAATIDTNLT
     AYFMLNSEDD NARQHFYREI PHHYVFMKKI YSWKPRCRRS RIISRLYTVG VRQVERHCLR
     LLLINVKGAT SFEHLRTVDG LLYATFKSAA IALNLLEDDR AWSTTMEEAA VFQMPVQLRQ
     LYVDICLYCN PTDAATLFDA NLNHIMEDFI RSGHDANVAK NLTLKWIQDK LRLNNKTMEE
     FSLTVPDFHL INQLIEAQME RNDDNGQGKQ VIEVASTGIA LTLLLDGVTY HSQFKIYPPI
     TETTRSKIEE GTYNTQMIRN ASLIISGEAT MKTNHALDAI NHLFQTVMKN GVGPYGGKVL
     LLGGDFRQCL PVVRHGNRVQ NMRTTAGSQD YADWLIELGN GTLPQIPRLN NPDVIEIPQE
     IFLEKQGRRM QHHG
//