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Database: UniProt
Entry: A0A0G4J5G1_PLABS
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ID   A0A0G4J5G1_PLABS        Unreviewed;      1041 AA.
AC   A0A0G4J5G1;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=PBRA_009125 {ECO:0000313|EMBL:CEP02541.1};
OS   Plasmodiophora brassicae (Clubroot disease agent).
OC   Eukaryota; Sar; Rhizaria; Endomyxa; Phytomyxea; Plasmodiophorida;
OC   Plasmodiophoridae; Plasmodiophora.
OX   NCBI_TaxID=37360 {ECO:0000313|EMBL:CEP02541.1, ECO:0000313|Proteomes:UP000039324};
RN   [1] {ECO:0000313|EMBL:CEP02541.1, ECO:0000313|Proteomes:UP000039324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E3 {ECO:0000313|EMBL:CEP02541.1};
RA   Chooi Y.-H.;
RL   Submitted (FEB-2015) 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}.
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DR   EMBL; CDSF01000131; CEP02541.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4J5G1; -.
DR   STRING; 37360.A0A0G4J5G1; -.
DR   EnsemblProtists; CEP02541; CEP02541; PBRA_009125.
DR   OMA; NYCEAAI; -.
DR   OrthoDB; 170190at2759; -.
DR   Proteomes; UP000039324; 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; 3.
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; 1.
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:UP000039324}.
FT   DOMAIN          47..246
FT                   /note="DNA replication factor Dna2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08696"
FT   DOMAIN          697..763
FT                   /note="DNA2/NAM7 helicase helicase"
FT                   /evidence="ECO:0000259|Pfam:PF13086"
FT   DOMAIN          773..981
FT                   /note="DNA2/NAM7 helicase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13087"
SQ   SEQUENCE   1041 AA;  116041 MW;  8E9702DD291E5D2D CRC64;
     MGLLDAEFDA ALVALGDLEL PAPCTRFLVL EAGVDSAGTV LRLFHEGHGA ERVCRVRGDW
     RECFIDVGDY VNVIGEAGSD GEYVVDNENN MIIVHPDRLV SGTRVGSSVA CMRRAVLSER
     VNAPSSSVKA IRGTLAHQLF QACLRSGNFS ERFARDQVAD VVRDAYLDLI LFEETEQDTV
     HYLTSLIPQL QAWSSTFCGR AASADSEVHF ADKRVSTRIV DVLDIEDQVL APRYGLQGKI
     DATVRAECRE LGPLSAAVPR VLPLELKTGK PRTADNAQLS LYTLLLSERY SPERVESGLL
     LYLTAQSVAM KGASRTGLVC SSVRMTRLVG IVHRHGELRQ LIIKRNIIAS YAVGSEMHGR
     SGALPALIDN DHYCRNCFQA DSCMLFRKAY ESSDDRDPHP LDDIVGHLNE NHMRYFRFWN
     QMIDLDSREA RQRQSRIWTE TSATCQAHGR CVSNVCLDSE QVIGEMFFCT FKASLDSTTN
     FTSLYFEEGD KVAISTEDGQ VGIATGFVVN VDERSVVVRI YNRRLSVRFQ HCRFRIDKDE
     YISRYANLRG NLVALCAQAP DSDRLRDLIV DLRSPLFDIE RDLSVSDDDL RAAYFNDLNE
     DQRKAVRHVM ATQDYALILG FPGTGKTTLI VFLVRLMVFL GQPVLLCCHT NTSLDNILQK
     LVPIGVPFIR LGIMNRIQRS LHDHTLEEQR FQSLQEAREF CASQPVVGCT CLGASQTMLG
     RRRFDWVICD EASQATEIAM LAPLRLGKRF VLVGDHYQLP PLVRDPVAKR SGMDTSLFLR
     LSEAHPHAVV QLKSQYRMNE AILSLSNSLI YSNALVCGTD KVASARLHLP APKRLPRVTV
     PGATFDWLGR ALDPERPVLF LNTDAVPAPD GHRGEQNETE AELVLALLDA LSGAGVPGSH
     IGVISPYRSQ LQLLRRRLGA RRGDVEVESV DKFQGRDKDV IIMSLVRSNP KNRVGELLQD
     WRRINVALTR SRYKLVLVGS QTTLRHSPIM AALIDVIHRQ HTVVDLPARA HLFYRQEEAD
     EGAGAAVPQA KRLRLGPPGD G
//
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