ID A0A0V0WD08_9BILA Unreviewed; 994 AA.
AC A0A0V0WD08;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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};
DE Flags: Fragment;
GN Name=dna2 {ECO:0000313|EMBL:KRX73725.1};
GN ORFNames=T06_1828 {ECO:0000313|EMBL:KRX73725.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX73725.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX73725.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX73725.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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}.
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:KRX73725.1}.
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DR EMBL; JYDK01000166; KRX73725.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WD08; -.
DR Proteomes; UP000054673; 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: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; 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:UP000054673}.
FT DOMAIN 90..287
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 576..671
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 679..748
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 755..966
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX73725.1"
SQ SEQUENCE 994 AA; 112937 MW; 647B9E40CCD9BA18 CRC64;
YLTSLIHSTN PSLKDVYERR YTRKTKSDSH YVKRSSLFFD FFASTMQNPQ GVFDDSFEEL
ISGMDDNFNT VSPFNLLQEE NSTLLRCVDS GGTAKRVWLE EYWSDGLFKE GDKVRAFLPK
NLSEMDEFHI SNKSGAVILN PGSVVGVNRI SNGHFCMRKS VLMEIFKGFD KPGLKTQVGI
IAHKMFQRAV KESITDEDTL RKMIVEISKQ VEFTLNQYYH DIDPAAVNSE LQTFVKDIAK
FVQNCVSNRN PLPGVVPSTV IDRVLAVEEE MISEKFGFRG SIDMTMGVKV DAEQKSTLMP
FELKTGKVSS YGDHIAQVML YCLLLSSNNH ESCERGLLYY CGGDELKAVD MKMNELNGLL
RMRNEVTYYL HRFFDNPEAC DLLLPGPIKN MKMCQKCPQM LNCCLRQKIC DEAFVRDSPW
DAMLEAELWH LDKKDLQYVR RWTTWLRMEG IEERMRGRRN SNIDYDEEEE HSTEECGIAM
SVQQFKENSR ILTLAPLSNV DLIRMFTPYD QVLLNGIGER TLPIFATIIT VGLQHIDVQF
SRNRKRQLII DLDEPHFKIS LCSEIVQKMK LFCKGLNAEQ KFAIVKTMLA DDYALIKGFP
GSGKSSTVIA MIRTFISNGN SVLVCAYTNS AVDNILLKLK AHITDMLRLG PSFIVHPDIR
QFTLEAIFAN KEPGLDEVSE ILGSTLLVGC TCTTATMHPL LRKRTFNLCI IDEATLATEA
MSIGPLLAAE KFVLVGDPLQ LKPLIQSERA RKQGMDISLF SKLEQKYPHA VVTLKLQYRM
NREICKLSNQ MFYNGELVAA NDEVANAFLN VTVDDDVAEE PWVRRCLSSL PEHAVVFLDT
SNCKDNSATR QGIAHVENKL EVDLVVKLCQ TFLKSGLDDD EIGVMSIFKT QVECIRRSLK
SSGSNGIEVN TVDQYQGKDK DVIIVSFVWT KELKRKLNTT CYLLKNARRV NVALTRARKK
LILIGHYNDL KADNPVFENL HNILSETQIF PLML
//
