ID S8AHV7_DACHA Unreviewed; 1697 AA.
AC S8AHV7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=H072_5379 {ECO:0000313|EMBL:EPS40726.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS40726.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS40726.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS40726.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPS40726.1}.
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DR EMBL; AQGS01000282; EPS40726.1; -; Genomic_DNA.
DR RefSeq; XP_011111259.1; XM_011112957.1.
DR STRING; 1284197.S8AHV7; -.
DR eggNOG; KOG1805; Eukaryota.
DR HOGENOM; CLU_001666_2_1_1; -.
DR OMA; WEADIAK; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000015100; 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:UP000015100}.
FT DOMAIN 608..808
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 1175..1263
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1274..1343
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1351..1572
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 1..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1655..1689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..510
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1697 AA; 187674 MW; 15A607FDF4BD7292 CRC64;
MSKRTTSFLD QDHSAAPRPE NRLGFRRYNT NNGVPKPLAG QPLKKTNSEP VSVSAKTKEK
LGSFAHKSAA PVRKQSVEVK HISKAAEPQD DISKLPAAPI DSSPPVFRKE NLKPDPKTSL
QGDQSTVTKA NKAGSKTAPD SNLSISRGTN DIPSTPQHRY ALNDLLTQAN MTPSVTISNE
ETSPEDRVSW KNSPKKSQGQ PDGTPLRRGK GRAAMHKKRA RSSSPVDSPR ASKRVGTQLA
FDISSSALKT PMANPFEDAW TRRLQEHPSA GVSTVKGESI FDGSSPRAPT DIGDSPSALR
RSFSAPAKRL KLGEPRTGEA ANPEGKNPLS TLKLARRGGL PGRNPTNDRV SSLLAKLKDT
KVTALQKSET APPALYSSPN SLSGRFDDAT SSIQVQVTPP VVETGPWGRE TSAAPSRRSN
SVKPSSDSNK VTKGVSLAVA PCQEPKSDDY GLDDDDDEEM FELVESTSRS VQPRCDATQG
ENNEVVSEAQ DEEMDDYGLD DLDDDDDAWE ADIAKAVGSS GTSKPPSKNK FKTPVKASPE
VSLPKQHKPT VASPSSDDYG SDFDPDEVVK DAKSRVIQRF VVLDVFEDDY ISSSGDTKPE
KALRVEDERT RTERRVLLRQ SWMDCDVREG DVVNVIGAFD DETCIIDNTQ NMLILHPDIL
LSATAVADSF DCIRLATLKE RVKAISDASE WSVYGNILHE LFQAALSAND FSSAFLEKEI
NRILSAQMQN LYAVRVTPGT AMDHLRTKLP PLQEWAKSFV SARPQHDAIA KGHRAPDSNL
AIRKVLDVEE HIWSPKFGLK GNMDVTVEIE IQDLKGSRTL TAPLELKTGR NTKNMTHRAQ
TMLYTLLMSD RYDIESLCGI LYYTETSETL RIPNLTDELR GLMIGRNHLA RFIYSKLDLP
PMLQDKRTCG RCYAKTSCFV YHRTMENGTV ESSGVGDIFA KETAHLNQTH ADFFSKWEIL
LSKEEKDMEK FRKELWVMTS EQREAAGRCF SDLSMIPESA PTSNDVASKI NRFNYRFVKR
EPPSSFSFLE SQIGVGEPIV ISDEEGHFAL AKGYVTKVSS KWIMVAVDRR LHNSRVRQPG
FHETKNQIFS AIMEILEDGT TRYGAPVSSQ EAQTSYRLDK DEFSNGMALI RNNLVELVKA
NGNPRLRELI VELAPPVYNV TSTAYPLPSA SQGKINVDQK NAIEKVMSAQ DYALVLGMPG
TGKTTTIAHI IRALVHQGKS VLLTSYTHTA VDNILLKIKD DPIKVLRLGV GSKIHPEVQK
FAVLANAPKK SFEEIQDALH SPQVVATTCL SINHIVFTER VFDYCIVDEA SQITLPVCVG
PIRMAKKFVL VGDHFQLPPL VRSQEAKAGG LDVSLFKLLS DSHPDSVVNL EHQYRMCEEI
MTLSNYLIYE GRLKCGTERI AHSSLAIPDI GALDNFHKAS STPLAKTVCG DAGAPCWIRD
LLQEDVKARF LDTDLVSAPE ERKGDRIYNP TEAELTRQLV EGFLHCGVDA NEIGVVSVYR
SQIKAIQHLL HHHQSVEMHT ADKFQGRDKD CIIISLVRSN DKENVGELLK DWRRINVAFT
RAKTKLLIIG SKSTLKTNDL LGKFVDMMEE RKWVYTLPSQ AHLLHNVPIP VTQVTQRSPG
KGNAAVLSQR QRMLLAYNSE NKPKVQKSLL DMLGKKGEDS KGEKESTTEG PRQGTVGQRS
LLGSRPVLRD IMNEING
//
