ID A0A365N778_GIBIN Unreviewed; 1537 AA.
AC A0A365N778;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=FPRO05_01371 {ECO:0000313|EMBL:RBA16647.1};
OS Gibberella intermedia (Bulb rot disease fungus) (Fusarium proliferatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=948311 {ECO:0000313|EMBL:RBA16647.1, ECO:0000313|Proteomes:UP000251714};
RN [1] {ECO:0000313|EMBL:RBA16647.1, ECO:0000313|Proteomes:UP000251714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ITEM 2341 {ECO:0000313|EMBL:RBA16647.1,
RC ECO:0000313|Proteomes:UP000251714};
RA Almiman B.F., Shittu T.A., Muthumeenakshi S., Baroncelli R.,
RA Sreenivasaprasada S.;
RT "Genome sequence of the mycotoxigenic crop pathogen Fusarium proliferatum,
RT strain ITEM 2341 from Date Palm.";
RL Submitted (DEC-2017) 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: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC Nucleus {ECO:0000256|RuleBase:RU367041}. Chromosome
CC {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:RBA16647.1}.
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DR EMBL; PKMI01000017; RBA16647.1; -; Genomic_DNA.
DR Proteomes; UP000251714; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
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-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; 3.
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; IPR048459; DNA2_Rift.
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 Pfam; PF21123; Dna2_Rift; 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|ARBA:ARBA00022840, 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|ARBA:ARBA00022801, 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268,
KW ECO:0000256|RuleBase:RU367041}; Nuclease {ECO:0000256|RuleBase:RU367041};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU367041};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367041}.
FT DOMAIN 466..668
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 680..779
FT /note="DUF83"
FT /evidence="ECO:0000259|Pfam:PF01930"
FT DOMAIN 841..931
FT /note="DNA2 rift barrel"
FT /evidence="ECO:0000259|Pfam:PF21123"
FT DOMAIN 1033..1120
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1136..1201
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1209..1436
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 1..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1484..1511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1537 AA; 173039 MW; 2B1C028F96C7E092 CRC64;
MPLQKSYSDQ VGRTKRLPWQ RSRSNPVQQT PRPRALQPVS EVTKNKLNKF QYHPSNGESA
TESTENDQNV SNNRTKDDTT TTPATRLTWQ ELLEPAGGTE DDTTTSPNDR LLWDNRQDTL
YMPALSPMLN RKGRKRARSS SPVSSPVADK SNTPSVNVRK LAQALKSPHA DPTLELWDRY
SLNGIDNAVD GIVFATAIET NGWRIQSQTS NKLWLELAQK EKGGKINVSI NGPSDEPREE
PQDAPESPSP KKRRIYTTSS GSPRLSKTQA RSQTPAQHPA QQHVQVPARP PVQLPPPEPA
SSDYGDDDFD EFDDDTIMQL EASINTTQLE TNPQPDVAVA ENNPVSEIEH KTPGRFDRKL
DEFDDLDDDF FDEAEDLITA DSQQVSQAPA ATELDDLDDE FGDAFDGDFD FEAVELAATQ
AAQNCSGDSR KPRTIQRYLV TNVLEGEYTD QYGHARPEKI LLIQADNSKD IKTVHLRASW
FDTPAHADAY VHIIGDFSLR GQCIVDDGQN LLILHPDQLI SATVVADSFG CMRRAVLQDR
VKATSPPTPP LIYGTMLHEI FQEALLANKW DLPFLCAVID RITEKHVEDL YTIKVGIPSA
REHLQSKMTE LSYWAGAFVS FRPKEDAVVE DRNGKKANMA VTKLLDVEEH VWSPMYGLKG
NIDATVEVAM QDGNDIRTLT VPFEVKTGKH ANSNHMAQTA LYTLLLSDRY DIEIAYGILY
YMETSKTMRI PAIRHELRHM IMQRNQLACY VRERSVQLPP MLKSKHMCGK CYAKTSCFIY
HRLADDGDGD SSGMNEKFDE LVKHLTPHHQ QFFIKWENLL TKEEKESQKT KRELWTMTSV
EREKKSRCFA DVIIEEGSAS VDTDNPRINR YHYTFVKRVQ VSGFSFLESE LSVGEPIVVS
DEEGHFALAI GYVTAVKRQR ISVAVDRRLH NARIRQPGFD ERDNQIFASI MDVAHEGATQ
DEATGKIKEA PIRYRLDQDE FSNGMATVRN NLVQMMADDI VGSRQIRRLI VDLEAPRFKA
APTQYIVSDR DSLNVDQHRA IEKVMSAQDY ALVLGMPGTG KTTTIAHIIR ALTSQGKSVL
LTSHTHTAVD NILLKLKADK IPILRLGAPA KVHPDVQDFA ILAGHPMKSF DEIKNAWHGT
PIVATTCLGI NHSVFHERSF DYCIVDEASQ ITLPICAGPI RMARTFVLVG DHNQLPPVVK
NEEAREGGLD VSLFKLLSDT HPESVVNLEH QYRMCEDIMT LSNTLIYNGR LRCGTEQLRR
RKLEVPRMEA LMQRHYDASN INAATPRSFC AAPGPNRCWL YDLLDSETRV RFINTDTIQP
PVREEAQGKR IVNSAEVRIV SQLVDSLLTV GIPASEIGVM THYRAQLFML KDKLKMFSGV
EMHTTDRFQG RDKEVIVLSL VRSNEACNIG DLLKDWRRIN VAFTRAKTKL LVVGSKSTLK
GSGSDSMLSR FISLMEDRNW IYEMPANALE NHYFEDFGTQ ITATGPTQRI KSPRKKASGK
ENRRRSPKTA RISDKALLKG KLITRDILNE MTNGAYV
//
