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Database: UniProt
Entry: A0A094AWC1_9PEZI
LinkDB: A0A094AWC1_9PEZI
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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
//
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