ID A0A1Y1S8I7_9MICR Unreviewed; 941 AA.
AC A0A1Y1S8I7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 Name=DNA2 {ECO:0000313|EMBL:ORD94759.1};
GN ORFNames=ECANGB1_66 {ECO:0000313|EMBL:ORD94759.1};
OS Enterospora canceri.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC Enterospora.
OX NCBI_TaxID=1081671 {ECO:0000313|EMBL:ORD94759.1, ECO:0000313|Proteomes:UP000192639};
RN [1] {ECO:0000313|EMBL:ORD94759.1, ECO:0000313|Proteomes:UP000192639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB1 {ECO:0000313|EMBL:ORD94759.1,
RC ECO:0000313|Proteomes:UP000192639};
RX PubMed=28345194; DOI=10.1111/1462-2920.13734;
RA Wiredu Boakye D., Jaroenlak P., Prachumwat A., Williams T.A., Bateman K.S.,
RA Itsathitphaisarn O., Sritunyalucksana K., Paszkiewicz K.H., Moore K.A.,
RA Stentiford G.D., Williams B.A.;
RT "Decay of the glycolytic pathway and adaptation to intranuclear parasitism
RT within Enterocytozoonidae microsporidia.";
RL Environ. Microbiol. 19:2077-2089(2017).
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|RuleBase:RU367041};
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|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:ORD94759.1}.
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DR EMBL; LWDP01000010; ORD94759.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1S8I7; -.
DR VEuPathDB; MicrosporidiaDB:ECANGB1_66; -.
DR Proteomes; UP000192639; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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 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; 2.
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|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|RuleBase:RU367041};
KW DNA-binding {ECO:0000256|RuleBase:RU367041};
KW Helicase {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|RuleBase:RU367041};
KW Nuclease {ECO:0000256|RuleBase:RU367041};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367041};
KW Nucleus {ECO:0000256|RuleBase:RU367041};
KW Reference proteome {ECO:0000313|Proteomes:UP000192639}.
FT DOMAIN 142..294
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 624..697
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 710..773
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 780..829
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT DOMAIN 850..923
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
SQ SEQUENCE 941 AA; 108393 MW; 018A51749CC4B18E CRC64;
MVDKPKIVWE ETEFSECDIV TDENMHNTSK RHQTVNSLDE ISDITILDDF EGVELNSSCF
ESKEEDKDTF DSVIDNFNAS EPSALYFSSM EGCNLFTSQI DPAKLEHELN SNNKLANSNI
SRGSFVISRI RRVANDVVLE GDGSKVHVSG NWNIIDYEIG MKVTILHCGC CSHKQPLYRV
DNNQNLLFVE DDVLTISNFI SSFECINRPK TKVKVHEFEF EYQHSMIVIG LSIHEAIQRM
LVEKRVDTKF INEVLNSFCR ENAIRLYRCN ITETQLKNEA MKQIQNSIGF VNKIGSCDKI
EHWLFSNLFG LRGNIDFFNS KYVVELKTGK YTHVSHRAQV IFYTLMLAHE ENKEQKEKHP
LKTTRIPMIF YTQLYQTPVI QLIHAEVREL VIRRNRVATT KGIIACTCNE TETCALYNSI
MRLDKSHWLR MTLEELEKES SNLNLIKISE KKALNSTISF KCSDGIKNSL KKKDPIAFYT
KRLKFICKGS VSLFNENELV CDVQTKIDFS DAYYFTYEVD DLFYRFCKYS LLNIAYFSYF
GTKQQECANR FRMPGQEEDE LFDEENKRRR IQNTVLSQTP QMNPICTSEF TLKAVNQTMT
IPPKTAKSTT IPIPDMFKAE FFRLNKYQQH ALINALNCTD FSLIHGMPGT GKSTLIALLI
KILVFYNKKV LLVCYTHLAI NNLLGKLNDV RWFKANGSSA LDKMTVAGIR AHFDSFEVIA
GTCYSLGDAV FVNRRFDFCI TDEGSQISLL LNLIPISRSD RFVIVGDHLQ ISPIKGNRLS
LFEHLHYQYG SDELRTQYRM GEEIMKISNQ LFYQNRMVAG CNHNSSVKFI DTATRSIEET
LLGLDDGDTT VLCYFNCIVD QISRILKNRR IPVYTIDRFQ GSESDRIVII FDPILMNACQ
LCPRRLNVAL TRARSRLILV GNRAEMEKTV LFRELLELVV K
//
