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Database: UniProt
Entry: V9EC20_PHYPR
LinkDB: V9EC20_PHYPR
Original site: V9EC20_PHYPR 
ID   V9EC20_PHYPR            Unreviewed;       997 AA.
AC   V9EC20;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=DNA replication ATP-dependent helicase/nuclease {ECO:0000256|RuleBase:RU367041};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU367041};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU367041};
GN   ORFNames=F443_17232 {ECO:0000313|EMBL:ETI36674.1};
OS   Phytophthora parasitica P1569.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI36674.1, ECO:0000313|Proteomes:UP000018721};
RN   [1] {ECO:0000313|EMBL:ETI36674.1, ECO:0000313|Proteomes:UP000018721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1569 {ECO:0000313|EMBL:ETI36674.1,
RC   ECO:0000313|Proteomes:UP000018721};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica P1569.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Key enzyme involved in DNA replication and DNA repair.
CC       Involved in Okazaki fragments processing by cleaving long flaps that
CC       escape FEN1: flaps that are longer than 27 nucleotides are coated by
CC       replication protein A complex (RPA), leading to recruit DNA2 which
CC       cleaves the flap until it is too short to bind RPA and becomes a
CC       substrate for FEN1. Also involved in 5'-end resection of DNA during
CC       double-strand break (DSB) repair by mediating the cleavage of 5'-ssDNA.
CC       {ECO:0000256|RuleBase:RU367041}.
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|ARBA:ARBA00001665,
CC         ECO:0000256|RuleBase:RU367041};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367041}.
CC       Chromosome {ECO:0000256|RuleBase:RU367041}.
CC   -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007913, ECO:0000256|RuleBase:RU367041}.
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:ETI36674.1}.
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DR   EMBL; ANIZ01002999; ETI36674.1; -; Genomic_DNA.
DR   AlphaFoldDB; V9EC20; -.
DR   EnsemblProtists; ETI36674; ETI36674; F443_17232.
DR   eggNOG; KOG1805; Eukaryota.
DR   HOGENOM; CLU_001666_2_0_1; -.
DR   OrthoDB; 170190at2759; -.
DR   Proteomes; UP000018721; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0017116; F:single-stranded DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IEA:UniProtKB-UniRule.
DR   CDD; cd18041; DEXXQc_DNA2; 1.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 3.90.320.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR026851; Dna2/JHS1_DEXXQ-box.
DR   InterPro; IPR045055; DNA2/NAM7-like.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR014808; DNA_replication_fac_Dna2_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
DR   InterPro; IPR047187; SF1_C_Upf1.
DR   PANTHER; PTHR10887:SF433; DNA REPLICATION ATP-DEPENDENT HELICASE_NUCLEASE DNA2; 1.
DR   PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR   Pfam; PF13086; AAA_11; 2.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF08696; Dna2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU367041};
KW   ATP-binding {ECO:0000256|RuleBase:RU367041};
KW   Chromosome {ECO:0000256|RuleBase:RU367041};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU367041};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU367041};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU367041};
KW   DNA-binding {ECO:0000256|RuleBase:RU367041};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU367041};
KW   Hydrolase {ECO:0000256|RuleBase:RU367041};
KW   Iron {ECO:0000256|RuleBase:RU367041};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU367041};
KW   Metal-binding {ECO:0000256|RuleBase:RU367041};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268,
KW   ECO:0000256|RuleBase:RU367041}; Nuclease {ECO:0000256|RuleBase:RU367041};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU367041};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367041};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018721}.
FT   DOMAIN          16..47
FT                   /note="DNA replication factor Dna2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08696"
FT   DOMAIN          477..576
FT                   /note="DNA2/NAM7 helicase helicase"
FT                   /evidence="ECO:0000259|Pfam:PF13086"
FT   DOMAIN          586..649
FT                   /note="DNA2/NAM7 helicase helicase"
FT                   /evidence="ECO:0000259|Pfam:PF13086"
FT   DOMAIN          658..885
FT                   /note="DNA2/NAM7 helicase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13087"
FT   REGION          928..950
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   997 AA;  110220 MW;  57E0E53F99B01771 CRC64;
     MAGSGTPLNE IPPKNGSKAR VTRILSTEEM MWSIKWGLKG ATDASVEGTI VNPGGKNGER
     TGSVVLPLEL KTGSKKYAGV EHQGQVILYT LLLNERYRQR CQDGLLIYVP PIETNRITAM
     ATHVRGLIMT RNNFASAIAK VKSIGGSTSA QVFPPMIRNR RECERCFQVD ECVLHHAATE
     NGTEDSSGLG ELFTLMTKHL GEADLNYFKH WNHLIDLEQQ HAEKNLRALW LQVGWKREKA
     QEGSTCIASL KMVSDSPALS ESGAKRTLRF VRDRRKRRDT GDSEVNSQPT SFADVRFRVD
     ERVILSAESL DGKNLLVHVS RATVRKIEHG LITIESRQSI PLIVKSGQSV VGKEYTWRLD
     KDSIMSGLRR AKENLVQLFI GPPPEVVSAG TALVNRPELQ VRMDSMVSAG NNGNGDHKVS
     GTGDTRRRNL IVHLARPHFK PCRVTDVITQ RCRDCAKDDH DGSVAAHGQS LLDAFYELNI
     DQQRAVQRVL SSLDYALVLG MPGTGKTATI AYTVRVLLFL GFSVLVTSYT HSAVDNLLLK
     LLDYKTPMLR IGNAAQVHPM IADFTLDRQA ELEGISSVRT MEAKMVNAQL VGCTCLSVNN
     HVLFAKRRFD FCIVDEATQI TQPIVLSALR CADTFVLVGD HYQLPPLVAN AQARKEGMDV
     SLFRRLAEAH PEATQQLSYQ YRMNRDIMLL ANRLVYGDKL KCGSFKVASN HLKPRWQRQD
     TIAQKSVWPM RVLTNNQGVM FLDTDAMGEA TSERSSTTQL GSSGRRRMEN VVEAQVIAGF
     VELLVLGSVP PDEIAVISPF RSQVALIHQH LTAVAAFRRA GGSDWIHSIE VSTIDKYQGK
     DKGVVLVSFV RCNEEKHVGE LLTDWRRINV ALTRAKQKLL LVGSESTLSG GSALFHVLSG
     VIKEQQWGLK LPRDAVETLR QFAVSVAAPI EPDPEQGTTP GPRSSRATDN VKVSILQRST
     GGNGDIESLV PNVSSVPLCS RRPAQMKPIS RDIFGEM
//
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