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
//