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Database: UniProt
Entry: A0A2U1PQP0_ARTAN
LinkDB: A0A2U1PQP0_ARTAN
Original site: A0A2U1PQP0_ARTAN 
ID   A0A2U1PQP0_ARTAN        Unreviewed;       960 AA.
AC   A0A2U1PQP0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN   ORFNames=CTI12_AA123990 {ECO:0000313|EMBL:PWA88079.1};
OS   Artemisia annua (Sweet wormwood).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC   Artemisiinae; Artemisia.
OX   NCBI_TaxID=35608 {ECO:0000313|EMBL:PWA88079.1, ECO:0000313|Proteomes:UP000245207};
RN   [1] {ECO:0000313|EMBL:PWA88079.1, ECO:0000313|Proteomes:UP000245207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Huhao1 {ECO:0000313|Proteomes:UP000245207};
RC   TISSUE=Leaf {ECO:0000313|EMBL:PWA88079.1};
RX   PubMed=29703587; DOI=10.1016/j.molp.2018.03.015;
RA   Shen Q., Zhang L., Liao Z., Wang S., Yan T., Shi P., Liu M., Fu X., Pan Q.,
RA   Wang Y., Lv Z., Lu X., Zhang F., Jiang W., Ma Y., Chen M., Hao X., Li L.,
RA   Tang Y., Lv G., Zhou Y., Sun X., Brodelius P.E., Rose J.K.C., Tang K.;
RT   "The genome of Artemisia annua provides insight into the evolution of
RT   Asteraceae family and artemisinin biosynthesis.";
RL   Mol. Plant 11:776-788(2018).
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:PWA88079.1}.
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DR   EMBL; PKPP01000849; PWA88079.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1PQP0; -.
DR   STRING; 35608.A0A2U1PQP0; -.
DR   Proteomes; UP000245207; 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; DNA BINDING PROTEIN-LIKE; 1.
DR   PANTHER; PTHR45786:SF7; OS12G0539700 PROTEIN; 1.
DR   Pfam; PF14214; Helitron_like_N; 1.
DR   Pfam; PF05970; PIF1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU363044};
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:UP000245207}.
FT   DOMAIN          307..473
FT                   /note="Helitron helicase-like"
FT                   /evidence="ECO:0000259|Pfam:PF14214"
FT   REGION          59..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   960 AA;  109989 MW;  4DC3C896127ADEAC CRC64;
     MSQGSQEQNK GIPSLSGMLH NSLLIYSKTF VSQHGRLQSY CGLKLTEFGG AITGEASTTL
     DTSTNLPLSQ MPSTSKSPFE YKKRRSSGPS YLRATRKTQE RAAFSSSDNS VNTGRGPYTF
     RINGQSYHRI GSLLPAQGTQ PKYAQLYFFD TGREVKNRIG AFIGKENAEG VDEKIVARLI
     KMFDQSSSIA KAFRMARDWC ESQNSAKFEL HLLSGRSATR QYNAPTVPEI AALITNDFGD
     GIPTRDIIIS NKNEGLKRIS ELHPEYMALQ YPLLFPYGED GFHEKIQYHN NTGTRKTKRD
     CVTMKEYYSY VIQQRNNQGT TLLRGGRLFQ QYLVDAFTAV EEQRLKWTRK NQDTLRVDLY
     HNLCDAVTRG DTSAAGIGKR IILPRTFIGS PRYMMQNYQD AMAICRTYGN PDLFITFTAN
     PKWPEIAEML KHIPGQKGID RPEVATRLFK IKLTEMLDDL TKHHIFGQTR AVMRLNYHLP
     NQNAVTIRDS ENLPALIQRE GIDITMFTDW FELNKRDTNA KSYTYAEIPM HYVWHEKDKM
     WKERKTQKSI GRIHYSHPAS GERYYLRMLL NIVRGPESFE KLMTVNDRLC STFKEACFAY
     GLLNDDTEWK HAISEASVWA FGPQLRDMFV TILLFCDVSR PIKLWEENWQ ILSEDILHKK
     RKIFKYPELQ LTDEQLQNYC LIEIQELLNR NGKSLAEFKD LPLPNPKLLT KLDNHLIREA
     LDYDMKKSGT GKTFLYKTII SRLRSERLIV LAVASSGIAS LLLPGGRTAH SRFVIPLELL
     ENSTCGIKQN THMAELMQEV KLIIWDEAPM TQKYAFEALD KTLKDILGFH DPDCRNRIFG
     GVTVLLGGDF RQVLPVIPKG SRADIVQSCI NQSDLWKHCK VFTLTRSMRV NEYTENGQID
     TCKQDFNKWV LAVGDGTVPA KCKEATRLTT TIYEEHRKPI HSVYTEYATA VQKNKPKICY
//
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