ID A0A094AWC1_9PEZI Unreviewed; 1636 AA.
AC A0A094AWC1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=V493_03482 {ECO:0000313|EMBL:KFY27410.1};
OS Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY27410.1, ECO:0000313|Proteomes:UP000029327};
RN [1] {ECO:0000313|EMBL:KFY27410.1, ECO:0000313|Proteomes:UP000029327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFY27410.1}.
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DR EMBL; JPJV01001358; KFY27410.1; -; Genomic_DNA.
DR STRING; 1420906.A0A094AWC1; -.
DR HOGENOM; CLU_001666_2_1_1; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000029327; 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; 2.40.30.270; -; 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|ARBA:ARBA00023125, 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|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU367041};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU367041};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000029327}.
FT DOMAIN 556..757
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 764..868
FT /note="DUF83"
FT /evidence="ECO:0000259|Pfam:PF01930"
FT DOMAIN 928..1020
FT /note="DNA2 rift barrel"
FT /evidence="ECO:0000259|Pfam:PF21123"
FT DOMAIN 1122..1209
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1223..1290
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1298..1523
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1636 AA; 180839 MW; 304A1E8D43FD2D17 CRC64;
MPLQKSFSDT NHSTKRRPQW QRNKTYHAPQ TRHDLNPSEP ARGKPPIPIS AATKSKLEVF
QCNAQSKNRQ SSVDMSGRGA NPLVLEEDKE NTPLDVSEQG INQLSRNDFA KPSIETPATP
SSKLALPELI GMMDVGSMAQ LQLKTPDERV MWDHAINAED NNTTSYVAPR RGRKRPRSSS
PMSSPGNVSA HFAGNPETGD LQQLGAQAAH AGPGLDLWSG YAIGADKCTP RGAQNPLFAH
LMGNSSSPQS ANVKSFVSRE GTFKRSISCG TQFPKRRKVG VFEDHTATDV FMEPKKRALS
KPSRVSELLD GIKVAAVSPD KSAFSAGPSS SSPIPRSKGW SERKEMHQAS PLGAKDRHCT
GDAGIAEGEA PRLQLQPEEK YETIASQKSD STSSDYGDFD ADQFDESFLA VLESNQTSIQ
TSQSPATATH PEKRHINTQD SPIAATKPSI APPAEEEDEF ANSDEEMFAA DFEEILSKYD
TLPAAAEIEN QAGLRQGGLT EENGSIIKTV ADVADSDDEY GDDLDDTDFA VAEASATQAL
QESASCFSNV LIVQVENTKE YRTIRLRDGW IETPVTEKAA VHVIGNFVSG QCVIDDSQNL
LILHPDHLIS STVVADSFSC TRRAVLQDRV KATNDSSAPL VYGTILHEIF QAAMMANRWD
SPWLHDLIEK TATRHLEDLY TIKLQIPQAV EYLQSKMGEL QSWAEVFVTS KPHPEAIVKA
GNGETATMCV SKLLDVEEHV WSPMYGLKGN IDATVQVTMQ DAKSRRTLTV PFEVKTGKNA
NASHRAQTAL YNLLLSDRYD IDIAYGILYY METSETIRIP AIRHELRHMI MQRNELACFV
RERHAQLPPM LKRENLCNRC YAKTTCFIYH KLADDGDGET SGMKGKFDEV VKHLTPQHKE
FFLKWDDLLT KEEKESLKFR RELWTMLSSE REKLGRCFSN VIIEPGSAYE EQNNPKINRF
RYTLIRQDEA VNSSFLESQI TIGEPIVISD EKGHFALANG YVTHVRKHRI SVAVDRRLHN
ARIRRPGFDE ASNQVFASIM EVAGEGSPPE STEGKITEAP VRYRLDKDEF SNGMATVRNN
IIQIMADGPF MSRQIRSLVV DLEAPKFKSQ ATNYVLKDRE NINIDQRRAI EKVMSAQNYA
LVLGMPGTGK TTTIAHIIRA LVSQGKSVLL TSYTHTAVDN ILLKLRDDKI PILRLGAAAK
INTEVQEFAE LAAKPRTSFE ELERLWNDTP VVATTCLGVN HAIFNQRTFD YCIVDEASQI
TLPVCLGPIR MARTFVLVGD HNQLPPLVQN EAARTGGLDV SLFKLLSDAH PPAVVNLEHQ
YRMCAEVMAL SNELIYSGRL KCGTPEIAAR SISIPNMANL QTHHFSPSTM SRAGKTICAA
PAKGQCWIRD LLDPETKACF VNTDTLVPRP REEAKGNRIV NPTEATVCSQ LVQALLSVGV
PGSEIGVMTH YRSQLALLKH NLRSHQEVEM HTCDRFQGRD KEVVVISLVR SNEAGGIGEL
LRDWRRINVA FTRAKTKLLV VGSGSTLKGG EGGAEEMVGQ FVRLMERKAW VYDLPGTALD
SHCFDDAATQ ASGSAAATPE KGVWKQLDLK AARKPKLGGR GIGGENFKGP KKAVINERAL
FAGKPVLRDI MNEALQ
//