ID Q9U3F2_CAEEL Unreviewed; 1069 AA.
AC Q9U3F2;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 140.
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=dna-2 {ECO:0000313|EMBL:CAB54253.1,
GN ECO:0000313|WormBase:F43G6.1};
GN ORFNames=CELE_F43G6.1 {ECO:0000313|EMBL:CAB54253.1}, F43G6.1
GN {ECO:0000313|WormBase:F43G6.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAB54253.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAB54253.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAB54253.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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}.
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DR EMBL; BX284602; CAB54253.1; -; Genomic_DNA.
DR PIR; T22138; T22138.
DR RefSeq; NP_496516.1; NM_064115.3.
DR AlphaFoldDB; Q9U3F2; -.
DR SMR; Q9U3F2; -.
DR STRING; 6239.F43G6.1.1; -.
DR EPD; Q9U3F2; -.
DR PaxDb; 6239-F43G6-1a; -.
DR PeptideAtlas; Q9U3F2; -.
DR EnsemblMetazoa; F43G6.1.1; F43G6.1.1; WBGene00001016.
DR GeneID; 174809; -.
DR KEGG; cel:CELE_F43G6.1; -.
DR UCSC; F43G6.1a; c. elegans.
DR AGR; WB:WBGene00001016; -.
DR WormBase; F43G6.1; CE23725; WBGene00001016; dna-2.
DR eggNOG; KOG1805; Eukaryota.
DR GeneTree; ENSGT00940000165719; -.
DR HOGENOM; CLU_001666_2_0_1; -.
DR InParanoid; Q9U3F2; -.
DR OrthoDB; 170190at2759; -.
DR Reactome; R-CEL-69166; Removal of the Flap Intermediate.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001016; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IDA:WormBase.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
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:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IDA:WormBase.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IDA:WormBase.
DR GO; GO:0006259; P:DNA metabolic process; IDA:WormBase.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IEA:UniProtKB-UniRule.
DR GO; GO:0071932; P:replication fork reversal; IBA:GO_Central.
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; 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; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF08696; Dna2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 1: Evidence at protein level;
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 Coiled coil {ECO:0000256|SAM:Coils};
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 Proteomics identification {ECO:0007829|EPD:Q9U3F2,
KW ECO:0007829|PeptideAtlas:Q9U3F2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT DOMAIN 123..324
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 649..759
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 835..1043
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 433..468
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1069 AA; 120133 MW; 135A1921710734B6 CRC64;
MESRKRQLQN VNSESHEPKR LKEEFKGTEH DGDSVDSFEN FCPTASSPKE KISPRSRSER
IQLQECDDDD SFDAPVISSK PPALPKDSGV SGFPCLFDDK NVIHLTARKG EKRDDCLDLE
CIDKEGTTRI VYLQDHWSEM SIEAGSTINL IGAQAWGDRD FLVNDDVGIV ILNPDALVPC
TAVASATFCA RKTVLNDKFK FGNASNKAML LGTIMHEIFQ TAITSKKRPV MENDLMKIWN
KQAPKYAEEL VALSFTPSCL DAELQPYFSI ICGWINKHYP LSNSFFSKRE PLPSKSELLE
VYDIEENIWD SKLGLKGKID VTMRTKSRGG MESLELKTGK SSCSSEHTGQ VLLYCMMQSS
RYEQPIGPGN ILYLKDGASH CVTPRAADLL GVLQQRNKLS VHFEDPTTSN LPDPRQDSRF
CDKCDHKTMC SFYQKTEENF SKSNDKMKNF AENEMAHLEQ NHIEYAANWI RWISAEWKCE
RERMTSQNKD LWLKSVQERV EEGTCLSDLH PVSEEMSNSQ KIIISFSRKF LKSSNTPTFR
PGDVCLLSNK KHIAIGFALI DEVSDDQQIV KISTDKTIKS RYEAPFHLDK YTSMSTHSTT
LGNLVYLLQN DEIGKRLRNI LVDLLPPIIM DATGFNLTPA IKKIIIKAKL NNEQRKAVVH
ALATEDFMMV EGLPGSGKTT LISVLIQCLV ATNKKVLLAA FTHSAVDNIL TKLTKEVAAE
KILRLGSSSS IKDDIKKMTL KAKLENETSE EYYAAVRKVM KTTPIVACTC HHVPRELLFS
YRHFDVVIVD EASMVLEPLL LPVLATSNKF VLVGDCKQLT PLVVSRKAKQ EGAGISTMEK
LQQSHPGVVV SLTSQYRMNR EISVLSSKLF YENRLICGNE SVSRSSLDRT GDYIVAMDDG
SDHIRKALSG DIKDSCVFLD TQSTINSKMQ CEDGEGGGMC NDGEAKLISE LCQQFVMSGV
KPHEIGVMSA YRRQVDHIRG ILNSDELEVN TIDSYQGREK RVIIWSLTWT NNSTKKSELL
KDERRVNVAL TRARQKLVVV GCKNSAETIP VLFRFSQLIE NHISIPTQL
//
