ID A0A1V9Z2Q9_9STRA Unreviewed; 1316 AA.
AC A0A1V9Z2Q9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=ACHHYP_04055 {ECO:0000313|EMBL:OQR92100.1};
OS Achlya hypogyna.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Achlya.
OX NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR92100.1, ECO:0000313|Proteomes:UP000243579};
RN [1] {ECO:0000313|EMBL:OQR92100.1, ECO:0000313|Proteomes:UP000243579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR92100.1,
RC ECO:0000313|Proteomes:UP000243579};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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:OQR92100.1}.
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DR EMBL; JNBR01000480; OQR92100.1; -; Genomic_DNA.
DR STRING; 1202772.A0A1V9Z2Q9; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000243579; 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:UP000243579}.
FT DOMAIN 294..485
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 849..945
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 950..1016
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1026..1227
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..194
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1316 AA; 142794 MW; 3AD6F1B85A09C51A CRC64;
MDPPAIFGRD DDTTGASPMK DDSMGVIWKE SPVEKKLLQP SGASNAHANA SELRGFVNSL
ITSPSPNKHQ SSKLKFKKKV VPDGVSRHIA FSPDRRDEPR TRPPTVPVPS PQAQAKRHKS
GDEDQHLLSI LQQMDDAYSD SPEKLGSVIP PAAPLTSTAQ SRPPAPTATP IHIPASTAVP
KAPPAVPTPA PPPALDDDLT DEAWDLLEQI EIQATQQHME RQREQSARVE ESPAEAPRVK
ERAGISPAVV AKAPVARLFP PAAKPRPTDY LRFVALEVHV DHNARRLQLR AMDEDTAMHD
VVLAEDWFDT PIAVGDTFNF IFTVQPPGPL IATNAQHLVI VHPDILVSPT NVTASLQCAR
LAMLQKSLSL NQPSGPKALV GTLKHDLFER ALNSGYHSIP YLVEQSQCII QASLLKCLES
GLTETQAAEE MRASFQDMSA WLSKLHAAGV VAGSSTLRLH DVLATEEPLW SIKYGLKGAV
DASVRLVRNG RPALLPLELK TGQKKFGFQD HQGQVLLYSL LLEERYGACA EGLLLYLLGP
ETILVPRVAP IVRALLQARN RHAVHVATYE TTSAYPPLLR RPRDCGYCFS AAECMLHHAS
EEKGTAATSG VHELFLQHTA HLTAAEQAYF AKWNRLLDVE FRASQTAVQQ LWRQTDAARV
EAGTCIAGLA LANVTPTTLQ VTAAMAFSAR DLKLQVDDRI IVSAESATAT LLHVAKGKIT
ALRADAVDIA LFAPIPRAVL KGDSVVGAQP HWRIDKDTLS SGLHQAKRNL TMLFVGPSPA
GITAGLHPSR PRTEREDELG DPKRRRLICR LEAPRFDHSR STLALLEAHA AAHPTAPPFA
PLYASFLAMN PDQQRAIENV LHAKDYALIL GMPGTGKTSA ITMCVRLLLH LGFSVLVTSY
THSAVDTLLL KLLDFNIPML RVGAKEQVHA RLQPHLLEAR VRSLSTTAAI EAELTGAQLV
GSTCLSTNHV LFAKRRFDYC IVDEASQITQ PVLLGALRSA DTFCLVGDHY QLPPLVTALK
AKAGGLDVSL FKRLGEAHPS ATVQLSFQYR MHRDIMLLCN ALVYNHQLQC GDTRRPPWPL
AAVAVAPWLQ RVVAANVVFV DTDASGFHEE RGAKGLVNPV EADAVGQIVR ALRQAGAADV
GVLSPFRAQV QLLEAQQAGV EVGSKHQRWL SGSVSTIDKY QGRDKDVVVV SFVRSNARAI
VGELLLDWRR INVALTRARH KLVLVGSPTT LAGSPVLKAL VDLVAAQRWV VPLPAGGVTG
YCARPPVDDA PRGAKRVFVH VGADEGDIEG PAAPRRATVR PCPPVSRNIL DESLGR
//
