ID A0A218Z8Q3_9HELO Unreviewed; 1684 AA.
AC A0A218Z8Q3;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=B2J93_4534 {ECO:0000313|EMBL:OWP03970.1};
OS Marssonina coronariae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Dermateaceae; Marssonina.
OX NCBI_TaxID=503106 {ECO:0000313|EMBL:OWP03970.1, ECO:0000313|Proteomes:UP000242519};
RN [1] {ECO:0000313|EMBL:OWP03970.1, ECO:0000313|Proteomes:UP000242519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL1 {ECO:0000313|EMBL:OWP03970.1,
RC ECO:0000313|Proteomes:UP000242519};
RA Cheng Q.;
RT "Draft genome sequence of Marssonina coronaria NL1: causal agent of apple
RT blotch.";
RL Submitted (APR-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: 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:OWP03970.1}.
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DR EMBL; MZNU01000153; OWP03970.1; -; Genomic_DNA.
DR STRING; 503106.A0A218Z8Q3; -.
DR InParanoid; A0A218Z8Q3; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000242519; 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; 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:UP000242519}.
FT DOMAIN 583..779
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 788..889
FT /note="DUF83"
FT /evidence="ECO:0000259|Pfam:PF01930"
FT DOMAIN 1143..1231
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1251..1311
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1320..1546
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 1..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1623..1684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1623..1639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1684 AA; 187362 MW; 82DC15A3C457FE3F CRC64;
MPIQKSFSDQ NHSAQARQQQ PQQWNRVKSV GGAPKTNLDS KPLQEKQPVP VSTATKNKLS
VFNFGAQSTT KNASKSATSL PSYNEKENNE SKSRTKNAEE QKDKLPKVSQ DQPAIAARKF
APSTPAARLA LPDLLGMGDV RRPAQSVSPD ERIEWDKKDE VPGSGFGGVR RARKRARSSS
PTGSSPAQAL SSHPQVDPGS ELWGRYSHNG SNAPTPQGPS VPALAQLMHT LSPQPTKDAI
TPRSGRGFRR ANSCGNQFPK RRRTGGSEND DMFTEPAAIG PSKLAVLIES VTEGLSQAPG
VNTVHKRLDS YHVSHRRPPS GDKKESPTQR SRLKQNENTS VFCDQASNLE DSKENVLPPL
PENEDTDYGE FDDDELDAGL LEIVDAQDLG SIIPPDPPPQ RRTVSNTTSL IRQSPPPQWC
SITKAMATPT GLEANPPKLP KTSDFKGSPM KAEKDEFGDS DDDMFTEIAS QYDAPISVAN
RASMVARLSV GQAKQIRRVP SKAESDDEFG NDGLEDGDFE EAESTATQAF QQTGNSLLPT
TQKAAIQRYL VTNIIESEYE NAKGQKQREK ILILQIERLK IPKLVHLRGI WIGTPVTTKA
FVHVIGLFDS RGRCIVDDDV NLLILHPDHL ISSTVVADSF GCTRRAVLQD RVKATSDSSA
PLVYGTILHE IFQSAMLENR WDTEWLGELI EKLALRHLED LYIIKIEVSH AVEYLKSKMF
ELQCWSELFV SSQPNPQATV QAGNGETAIM CVSKLLDVEE HVWSPMYGLK GNIDATVQVT
MHDGNHKRTL TVPFEVKTGK NPSAAHRAQT ALYNLLLSDR YDVEIAYGIL YYMETSETIR
IPAIRHELRH MIMQRNELAC FVREKHTQLP PMLKKENMCN RCYAKVPCFI YHKLADDGNG
ETSGMKTKFD ELVQHLGPKH QEFFNKWDDL LTKEEKETLK FRRELWTMLS SEREKLGRCF
SDVVIEPGSA FEEQNNQKIN RYRYSLVKPD APCDFSFLDS QIAIGEPIVI SDEKGHFALA
NGFITHVRKR RVTVAVDRRL HNARIRQPGF DEFDNQVFAS IMEVAPEGAK DEDAEGKITK
EPTRYRLDKD EFSNGMATVR NNLIQTMADG PFGSRKIRGL VVDLHAPRFQ SKPTAFVVND
HENLNGDQRN AILKVMSAED YALVLGMPGT GKTTTIAHII KTLVSQGKTV LLTSYTHTAV
DNILLKLKDA KIPILRLGTI AKVAMEVQEF ATLAATTKSS FEEIRGAWHD PPIVATTCLG
INHAIFSERT FDYCIVDEAS QITLPVCLGP IRLAKTFILV GDHYQLPPLV ANEEARVGGL
DISLFKHLSD THPGSVVNLE HQYRMCEDVM SLSNTLIYDG QLKCGSQEVA DSTINIPFLE
NLKNHHYSPS TLSLAPRSIC AGAIKGRCWI RDLVDPATKV SFINTDPLLP LSREEAKGNR
IVNPTEASVC TQLVESLLSV GVPACNIGIM THYRSQLSLL KDSMRAHPKI EMHTADRFQG
RDKEVIILSL VRSNEAKSIG ELLKDWRRIN VAFTRAKTKL LVVGSKDTLM CKGPDESGEE
EMVSKFVRLM DEKRWMYDLP KDALESHLFE IGKTQTQTQG PGSGKAPGSQ WTAIKREEII
LQKEVAADPE RKRKGAGKEN SPPAAHMRGP PLGVLRQPKK RTYGQKPFKQ PRMSVLGDVL
AEFQ
//
