DNA2_BOVIN
ID DNA2_BOVIN Reviewed; 1061 AA.
AC E1BMP7;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=DNA replication ATP-dependent helicase/nuclease DNA2;
DE AltName: Full=DNA replication ATP-dependent helicase-like homolog;
DE Includes:
DE RecName: Full=DNA replication nuclease DNA2;
DE EC=3.1.-.-;
DE Includes:
DE RecName: Full=DNA replication ATP-dependent helicase DNA2;
DE EC=3.6.4.12;
GN Name=DNA2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
CC -!- FUNCTION: Key enzyme involved in DNA replication and DNA repair in
CC nucleus and mitochondrion. Involved in Okazaki fragments processing by
CC cleaving long flaps that escape FEN1: flaps that are longer than 27
CC nucleotides are coated by replication protein A complex (RPA), leading
CC to recruit DNA2 which cleaves the flap until it is too short to bind
CC RPA and becomes a substrate for FEN1. Also involved in 5'-end resection
CC of DNA during double-strand break (DSB) repair: recruited by BLM and
CC mediates the cleavage of 5'-ssDNA, while the 3'-ssDNA cleavage is
CC prevented by the presence of RPA. Also involved in DNA replication
CC checkpoint independently of Okazaki fragments processing. Possesses
CC different enzymatic activities, such as single-stranded DNA (ssDNA)-
CC dependent ATPase, 5'-3' helicase and endonuclease activities. While the
CC ATPase and endonuclease activities are well-defined and play a key role
CC in Okazaki fragments processing and DSB repair, the 5'-3' DNA helicase
CC activity is subject to debate. According to various reports, the
CC helicase activity is weak and its function remains largely unclear.
CC Helicase activity may promote the motion of DNA2 on the flap, helping
CC the nuclease function (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- SUBUNIT: Interacts with BLM and WDHD1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Mitochondrion
CC {ECO:0000250}.
CC -!- PTM: Acetylated by EP300, leading to stimulate the 5'-3' endonuclease,
CC the 5'-3' helicase and DNA-dependent ATPase activities, possibly by
CC increasing DNA substrate affinity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
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DR EMBL; DAAA02061817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1BMP7; -.
DR SMR; E1BMP7; -.
DR STRING; 9913.ENSBTAP00000003395; -.
DR PaxDb; E1BMP7; -.
DR PRIDE; E1BMP7; -.
DR Ensembl; ENSBTAT00000003395; ENSBTAP00000003395; ENSBTAG00000002620.
DR VEuPathDB; HostDB:ENSBTAG00000002620; -.
DR VGNC; VGNC:28118; DNA2.
DR eggNOG; KOG1805; Eukaryota.
DR GeneTree; ENSGT00780000122010; -.
DR HOGENOM; CLU_001666_2_0_1; -.
DR InParanoid; E1BMP7; -.
DR OMA; NYCEAAI; -.
DR OrthoDB; 633768at2759; -.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000002620; Expressed in oocyte and 60 other tissues.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005760; C:gamma DNA polymerase complex; IEA:Ensembl.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0017108; F:5'-flap endonuclease activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0016890; F:site-specific endodeoxyribonuclease activity, specific for altered base; IEA:Ensembl.
DR GO; GO:0006284; P:base-excision repair; IEA:Ensembl.
DR GO; GO:0000729; P:DNA double-strand break processing; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0033567; P:DNA replication, Okazaki fragment processing; ISS:UniProtKB.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IEA:Ensembl.
DR GO; GO:0043504; P:mitochondrial DNA repair; IEA:Ensembl.
DR GO; GO:0006264; P:mitochondrial DNA replication; IEA:Ensembl.
DR GO; GO:1902990; P:mitotic telomere maintenance via semi-conservative replication; IEA:Ensembl.
DR GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
DR GO; GO:0071932; P:replication fork reversal; IBA:GO_Central.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 3.90.320.10; -; 1.
DR InterPro; IPR026851; Dna2.
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 PANTHER; PTHR10887; PTHR10887; 1.
DR PANTHER; PTHR10887:SF433; PTHR10887:SF433; 1.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF08696; Dna2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Acetylation; ATP-binding; DNA damage; DNA repair; DNA replication;
KW DNA-binding; Endonuclease; Helicase; Hydrolase; Iron; Iron-sulfur;
KW Metal-binding; Mitochondrion; Multifunctional enzyme; Nuclease;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1061
FT /note="DNA replication ATP-dependent helicase/nuclease
FT DNA2"
FT /id="PRO_0000419465"
FT REGION 82..519
FT /note="Nuclease activity"
FT /evidence="ECO:0000250"
FT REGION 520..1061
FT /note="Helicase activity"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 393
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 648..655
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1061 AA; 120485 MW; DCF931ED3F1D3CBF CRC64;
MERVDELELL MEKSFWQEAE PSAELFQKKK VEASFSKIVL SRGMDNRYLV LAVDIVQSEE
GNHEKHLIIT ASQSLEYKEL CILRNDWCSV PVEPGDIIHL EGDCISNTWI IDEDFGYLIL
YPDMLISGTS IASSIRCMRR AVLSETFRSS DPATRQMLIG TVLHEVFQKA VSDSFAPEKL
QELASQTIQE IRHLKEMYRL KLNQDEIKQE VEEYLPSFSK WAGDFMHKHT STDFPQMQLS
LPSDGSNSNS TCNIEVTNSL DIEESIWSPR FGLKGKIDVT VGVKIHRGCK TKYKIMPLEL
KTGKESNSIE HRSQLVLYTL LSQERRADPE AGLLLYLKTG QMYPVPAKHL DKRELLRLRN
QMAFSLFHRI NKSTGEKTEL APLPQIIEEQ QTCKYCSQMG NCALYSRAVE QQMEDSSVPT
SMWPKIKEET QHLKPIHLEY FSLWCLMLTL ESQSKDNKRN YQHIWLMPAS EMEESGSCIG
SLIRIEHVKT VCDGQYLHNF QRKNGAIPIT NLMAGDRIIL SGEERTLFAL SRGYVKEINS
TTVTCSLDRN LSGLPESTLF RLDQEEKNCD IDTPLGNLSK LMENTRASQK LRDLIIDFRE
PQFISYLSSV LPHEAKDTVA CILKGLNKPQ RQAMKKVLLS KDYTLIVGMP GTGKTTTICT
LVRILYACGF SVLLTSYTHS AVDNILLKLA KFKIGFLRLG QIQKVHPDIQ KFTEEEICRS
KSIKSLALLE ELYNSQLIVA TTCMGINHPI FSRKTFDFCI VDEASQISQP VCLGPLFFSR
RFVLVGDHQQ LPPLVLNREA RALGMSESLF KRLEQNKNAV VQLTVQYRMN SKIMSLSNKL
TYEGKLECGS DKVANAVINL PNFKDVKLEL EFYADYSENP WLIAAFEPNN PVCFLNTHKV
PAPEQVEKGG VSNIMEAKLV VFLTSVFIKA GCKPSDIGII APYRQQLKVI SDLLAQSSVG
MVEVNTVDRY QGRDKSIVVV SFVRSNEDGT LGELLKDWRR LNVAITRAKH KLILLGCVPS
LSRYPPLRKL LNHLNSEKLI IDLPSGEHES LFHLLGDFQR K
