DNA2_XENTR
ID DNA2_XENTR Reviewed; 1048 AA.
AC F6QXW0;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 63.
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 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
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 by mediating the
CC cleavage of 5'-ssDNA, while the 3'-ssDNA cleavage is prevented by the
CC presence of RPA. Also involved in DNA replication checkpoint
CC independently of Okazaki fragments processing. Possesses different
CC enzymatic activities, such as single-stranded DNA (ssDNA)-dependent
CC ATPase, 5'-3' helicase and endonuclease activities. While the ATPase
CC and endonuclease activities are well-defined and play a key role in
CC 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Mitochondrion
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
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DR EMBL; AAMC01051984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01051985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01051986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F6QXW0; -.
DR SMR; F6QXW0; -.
DR STRING; 8364.ENSXETP00000016310; -.
DR PaxDb; F6QXW0; -.
DR eggNOG; KOG1805; Eukaryota.
DR HOGENOM; CLU_001666_2_0_1; -.
DR InParanoid; F6QXW0; -.
DR OMA; NYCEAAI; -.
DR TreeFam; TF314903; -.
DR Proteomes; UP000008143; Genome assembly.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; 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-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: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: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; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF08696; Dna2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; DNA damage; DNA repair; DNA replication; DNA-binding;
KW Endonuclease; Helicase; Hydrolase; Iron; Iron-sulfur; Metal-binding;
KW Mitochondrion; Multifunctional enzyme; Nuclease; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..1048
FT /note="DNA replication ATP-dependent helicase/nuclease
FT DNA2"
FT /id="PRO_0000419467"
FT REGION 86..521
FT /note="Nuclease activity"
FT /evidence="ECO:0000250"
FT REGION 522..1048
FT /note="Helicase activity"
FT /evidence="ECO:0000250"
FT REGION 683..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..700
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 142
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 395
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 649..656
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1048 AA; 118558 MW; 49BDCEC35E9FC942 CRC64;
MEPVSAECQL PPEDDLLEMM MEQSFTEPEE KSKDKSTRKI IPKTKLCRGL NNRYCVLNVK
EVYAQGEEKH LTITASQEGD DLELCILKDD WVALHIKPGD IIHLEGNCAF DNTWTISRDT
GYLILYPDLL ISGTSIANGI RCLRRSVLSE KFKVCDKGSR QMLIGTMLHD IFQRATTRGF
TDSVLQELAH HTVHGPKYLK EMYQLKLNQT DVMGEVQEYL PSFAKWAIDF MTHPLNQHQI
NVTRPTAGDP TEATKVSEFL DIEENIWSPR FGLKGKIDVT ARVKIHQKSK SHLKIMPLEL
KTGKESNSIE HRSQVVLYTL LSQERREDPE AGLLLYLKTG NMYSVPGNRL DRRELLKIRN
ELSYYLTNVV HKSDNGSKEI TLASLPALIA DRQACKFCSQ MRNCALYSRS VEQQIENCYI
PAEMIPVVQK ETEHLNKDHL QYFRLWYLMC TLEGNSKDSK MGRKNIWMMS SSEREEDGQC
IGNLIRTGPV QTISDGQHLH SFQRKSGTVP ATNLMSGDRV VVSGEDKFLA LSSGYIKEVK
HNNITCILDR SLGKLPEDLL FRLDHEEGGG GLESHLGNLS RLMENSPVSD KLRKLIIDFS
KPNFVQHLSS VLPSDAKDIV ANILKGLNKP QKQAMKRVLL SKDYTLIVGM PGTGKTTTIC
TLVSTLHLKT CTSCLVDDHR EAAGTHRSHR HSKGTVNLGK QKRQHRVTST TSSTSAKCRS
KTEPAVSAEN KKLQKLISGS HVCIMVNGHK TFSQNNYIIF FDNILLLKKL PLHYMCAFAL
IHHQCFKGCV KSVSLVRELG MSESLFKRLE RNQEAVVQLT VQYRMNSQIM ALSNKLVYEG
RLECASDRVS NAVVKLPHIK TLLLELEFRE SQESMWIKDV LEPSNPVCFL NTEKIPALET
EEKGGISNWI EAKLVFCLTK LFLKAGCRPS DIGIIAPYRQ QLKVISNYFN SLSASAVEVN
TVDKYQGRDK SVIIVSFVRS NIDGKLGDLL KDWRRLNVAL TRAKHKLIML GCVPTLSRFL
CLEQLICHLK SKNHIYDLPA GAHEHMPV
