ID B5RV45_DEBHA Unreviewed; 1531 AA.
AC B5RV45;
DT 04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
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 OrderedLocusNames=DEHA2G06820g {ECO:0000313|EMBL:CAR65924.1};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAR65924.1, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAR65924.1, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382139; CAR65924.1; -; Genomic_DNA.
DR RefSeq; XP_002770589.1; XM_002770543.1.
DR STRING; 284592.B5RV45; -.
DR GeneID; 8999137; -.
DR KEGG; dha:DEHA2G06820g; -.
DR VEuPathDB; FungiDB:DEHA2G06820g; -.
DR eggNOG; KOG1805; Eukaryota.
DR HOGENOM; CLU_001666_2_1_1; -.
DR InParanoid; B5RV45; -.
DR OMA; QCATQEL; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000000599; Chromosome G.
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: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: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; 2.
DR InterPro; IPR022765; Dna2/Cas4_DUF83.
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; PF01930; Cas_Cas4; 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:UP000000599}.
FT DOMAIN 511..709
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 714..818
FT /note="DUF83"
FT /evidence="ECO:0000259|Pfam:PF01930"
FT DOMAIN 1058..1156
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1169..1228
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1238..1453
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1531 AA; 173712 MW; BC0178BCF1ED8BBE CRC64;
MTDKRQGITS PPISKAVKKM RPNEAGSNYK ENIDDVNKVR KIPAKTTYFF QPSNTLAYRN
SGSKETKDKM GDSGSAAHVL KESDTNAISS TNANSSAQQI KTPSKTYENY EKFIQEQQSS
DDSFDGIRWR ASPRKAISKG VNGVPSSPLK NTVSPRKRGD ESKSSSTLVN EQANSVLSKY
GAGFHNIQSQ TPTMNRTHSD ISSSESVHKK FINAQHSPSL TRTKSFGMDN LVSSKTMSML
QRFERPNSKS ATPKTAASFS NSTSLNSWID KFDKSNSKAE TSPCALDLET IASSANEIIQ
SAQHPNHHNE HELKCDTSAS VQETVVTQEV LNGIDFSDDF SDSGLMTSPN KPEESAKLEP
VPVDSDDPFS SDDEVVLTAI RTQSRKLEDK SQSQSIDEED SEDPFSDDDV KFSQLDTKIE
TRPSSSSQKY LTTQQKSDNR HAESFQNDVK RLENLQSIDK SISDNDINDA KLSYSRPDLQ
RFQIKSILNN TYKVQNRIRN QAILIVVDGK LEESKLILRG EYLQLDFQIN DVIHLILTDP
SHPKLIDDTH NLLIWNPDIL VSATTVSQQM GCPRKSVLIN RLSFPGESSI PLIVGIIIHE
IFQACFHTEN WSMDYMIGLM ELEIQSKLLQ IYSIGNEVNK VKTEIQNQLP YLETWFKTYF
KKPLSSNTSI PTNHGNQKVM FAANKALDIE ENIWSPMFGL KGKVDVTLEG QLYDQSTNGK
FLLPMEIKTG REYISHHAQS SLYSLLFKDR YDMDVNMFLL VYTKERISKK YDISRTDLKS
LVNLRNRITK YFKSGTRELP ELIKQSQCDR CEVQQACMTI NKLVENGTAE ESGLPQDVYN
GLTFHLENDE NSRVFYNYWD NLITQEEGIM TNLKKDLWTL TAKERENTKG KALSDLIIKE
SNDNDDFQEK FFYTFERPNN PQSLQNSQLI KYDRIIISDQ EGHFAIAQGF ITAIRPSFIK
ITADRRIVNS NLKVDGFNET DNQTFQSVLH KNLNSQKQDK LYRIDKDDMF HGMGLARYNI
LNLFLKDGDS RRRESIVNLK EPKFMPSKLQ YDISSENFNS DQIGAFDKIL NTKDYSLILG
MPGTGKTTVI AQIIKLLVQN KKTVLLASYT HSAVDNILLK VKDYGIDILR VGSPLKVHKD
IRKYVAGFDT DKQIKNYDDF IATYMTPPVV AATCLGIGDI AFNLRTHFDY CIIDEASQVS
LPISIGPLRF CDKFILVGDH NQLPPLVQHP NPAIKQGLSR SLFKILSDTY PQSIAELTYQ
YRMCEEIMLL SNVLIYGGRL KCGTEKVAKQ SLYIPNPNMI EDQISPQYSL KLRKEDLWID
SILKPENKVI FINHDDVPGV ERTIGEKVEN LTEVDLIKQI VESLTMCGVK ESSIGVMSLY
RSQLRLLHRG LSHKPDVEVL TADQFQGRDK DCIIISLVRS NKDNKVGDLL KEWRRVNVAI
TRSKSKLIIL GSKSTLKSVK MLEAFMALIE SRGWMYDLPP YADKFYEFAF MESLSNPVRN
VKSKVNQNLT QDSRIINNNP LIRDIINDMT N
//
