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Database: UniProt
Entry: A0A1B9FXS2_9TREE
LinkDB: A0A1B9FXS2_9TREE
Original site: A0A1B9FXS2_9TREE 
ID   A0A1B9FXS2_9TREE        Unreviewed;      1348 AA.
AC   A0A1B9FXS2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
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   ORFNames=I302_06555 {ECO:0000313|EMBL:OCF23572.1};
OS   Kwoniella bestiolae CBS 10118.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Kwoniella.
OX   NCBI_TaxID=1296100 {ECO:0000313|EMBL:OCF23572.1, ECO:0000313|Proteomes:UP000092730};
RN   [1] {ECO:0000313|EMBL:OCF23572.1, ECO:0000313|Proteomes:UP000092730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10118 {ECO:0000313|EMBL:OCF23572.1,
RC   ECO:0000313|Proteomes:UP000092730};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA   Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Cryptococcus bestiolae CBS10118.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000092730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10118 {ECO:0000313|Proteomes:UP000092730};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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; KI894023; OCF23572.1; -; Genomic_DNA.
DR   RefSeq; XP_019044642.1; XM_019193165.1.
DR   STRING; 1296100.A0A1B9FXS2; -.
DR   GeneID; 30210954; -.
DR   VEuPathDB; FungiDB:I302_06555; -.
DR   OrthoDB; 170190at2759; -.
DR   Proteomes; UP000092730; Unassembled WGS sequence.
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; cd22318; DNA2_N-like; 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; 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; 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:UP000092730}.
FT   DOMAIN          272..483
FT                   /note="DNA replication factor Dna2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08696"
FT   DOMAIN          857..955
FT                   /note="DNA2/NAM7 helicase helicase"
FT                   /evidence="ECO:0000259|Pfam:PF13086"
FT   DOMAIN          959..1024
FT                   /note="DNA2/NAM7 helicase helicase"
FT                   /evidence="ECO:0000259|Pfam:PF13086"
FT   DOMAIN          1034..1248
FT                   /note="DNA2/NAM7 helicase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13087"
FT   REGION          1..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..88
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1348 AA;  150894 MW;  D3C021650244FB49 CRC64;
     MTSTPFRPKS RSRTDETHSS SKRPRLSSSK PAPTIKNEPT QDEKALMDDL MAGLDASMFD
     GMTSSPIRPK SNRGSQASPI QSQQRREHAK PLSPVRNRHI NNSPRKLKSH KSPIKEKARN
     AFAPSLVKVK SPVKVKKEQV SPPRHVPEVI VKQEIEVELD QKVISLKQEI QTKPDLADED
     LYDFDFDLND LSAFEEDLLG LPELKTRYPV PNPARPPPPP GYTSTPWSRC IVNAVSTGLR
     FTNGVVPSLE GFERDDEGGT SFGKTLIVTS TETEIKRIVH LKDQWSNLHI KKNDIINIIS
     PALSKQSFTG PIVLTLKDPS TFLIHHPDLM LTMTSIANAI PCPRKPILQS LIKAPGPPSK
     AVLYGNLLHS LLQGALLEQS FDADSTFKRI DTELKKEERR LEIWSTGMGT MDVREEIGMR
     AGRGFEVFGD KWVGDQPGIE GELHTSPGDN PSLLAINGLH EVEEDIWSPK WGLKGKVDAS
     VQARIIRDPS KPHEAEEHVA PLEIKTGRSV GVMAHRAQTM LYTLLMEDRY GVPVPAGLLY
     YSQLDSILRV EAKSNEIRAL IIARNELADW LSKKRRVPKA PPPTTDDLVK KVEDVEEAFL
     PPTIDHTKEC RSCYAVDSCM LYRKTIDNVH PDPDDPIAEL YDEKTGHMTQ KDADFYKKWD
     TLLTVEEQDI GRYRSQLWTM TAKEREKTGR CFGDMIISSY SNDLGKSLAK IHRHAYTFKR
     APHAGTQISQ TSLLSGHIAK GDPVSLSIEP DLLCLSRGFV LDLTAESITI GVTYVIDVEA
     LLKRTGRSHA LSEGEGKVVF RIDKDEMASG MMRMRNNLAS LFYAKSGDEA RRRLIVNLAE
     PEFESSWVPY DEDIPNHLNE DQRNAMKKVM SARDYALILG MPGTGKTTTI AEIINLLVKQ
     GKSVLLTSYT HSAVDTILMK LVNAEFGILR LGNIDKVHPD VQHLTLEAME QSTNMEQLEK
     RLMNPPVVAA TCLAIDHPLF FKRKFDYCIV DEASQITLPT CIGPLRMADK FVLVGDHFQL
     PPIVRHPEAR RGGLDVSLFK LLSSAHPQAV CDLSMQYRMN EDIMLLSNRL VYEGKLKCGN
     EQVAKRGLVL KERKRCEGIF DCGDSEGHKE CWVQDLLEES AKCIFVDTDG LPAPDSRVGD
     LVQNETEARL VQQLATALTD SGLHQEDLAI ITPYRQQIKL LSSLLKPDLP RVEILTADKS
     QGRDKDCILI SLVRSNEGGN IGDLLKDWRR INVSFTRAKK KLIIFGSAKT LSQDNLLNGF
     LELMGSKNWI RRLGRGDDMI HQSRKIKMDA QETALIPMEK EEPVKGEKEV DQESKILKKK
     DGKGRKVIRA GSDVLVKGAF GKEILGME
//
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