ID Q6M931_NEUCS Unreviewed; 1735 AA.
AC Q6M931;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 79.
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=H4H7.170 {ECO:0000313|EMBL:CAF06129.1};
OS Neurospora crassa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=5141 {ECO:0000313|EMBL:CAF06129.1};
RN [1] {ECO:0000313|EMBL:CAF06129.1}
RP NUCLEOTIDE SEQUENCE.
RA Schulte U., Aign V., Hoheisel J., Brandt P., Fartmann B., Holland R.,
RA Nyakatura G., Mewes H.W., Mannhaupt G.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAF06129.1}
RP NUCLEOTIDE SEQUENCE.
RA German Neurospora genome project;
RL Submitted (JAN-2004) 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}.
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DR EMBL; BX908811; CAF06129.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:NCU04749; -.
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 545..747
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 766..867
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..1208
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1222..1290
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1298..1552
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 1..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1558..1590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1628..1709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..451
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1673..1692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1735 AA; 191808 MW; 41BDC996A1E5543C CRC64;
MPLKKSYSDA YAQPPKRGGW QRTRSNPPNK GPLQSLAPVS ESSKNKLQAF RSDDTSSKPP
PKSARPVKAA IDELQKENIN TTKSIPRKRP LPDSNDDEPS SDAKTPADRH SWKDLFGVPE
VITEEEDGEK SPGDRVDWRS GVPLQLPASP MIPKNGRRRA KSSSPASSPA TKLTTPHVAL
KRFAGASKTP HADPASDLWS RFSSNGNDTS PSNHKNPLFA QLMASSSPRP QSSDRSLRKS
VSCGSAWPKR RRTLCPEEQN RIVSQDTPRK KKSSLLSELL QSVDGEIDSS KTPSNAPAQQ
KKSPSPMKKS PSKRKITPQT VPDQNSSPSR KKAERQTTET DASKQPEKAS SDYGDDDFDF
DESTLLELDA SILGQGDGST LIASDAVSPA PRESSKTLVD NDEFGDLDDD IFDGVEDLVA
QVESATQKPA QRLSPRKRPS PKKRLSPRKR QSPKKLPQQV AGDEDDEFGD DFGNDFDFDA
VEMAATQRAS HAQDVSSHPS QKPRAIQRYL VTNVLESSYT DDRGRESPEK VESPFRQYIL
IVQADRTNSV RTIHLRGDWF DTPASVSAYV HIIGQFEDQG KCVLDNNQNM LILHPDQLIS
STVVADSFSC MRRAVLQDRV KATSDLTPAL VYGTILHEIF QEALVANKWD PAFLTNVINK
TLEKHLEDLY ILKVSMDDAK SHVQSKMPEL RSWAQLFVTS QPKPDAIVQG RNGDKATMCV
SKLLDVEEHV WSPMYGLKGN IDATVQVTMR DPPARGSSSK APTTKTLTVP FEVKTGKNVN
SNHQAQTALY NLLLSDRYDI EIVYGILYYM ETSQTLRIPA VRHEIRHMIM QRNQLACYIR
ERSVQLPPMK KNKNACGRCY AQTTCFIYHK LADDGDGETS AMNEKFDEVV HHLSPTHKAF
FLKWEELLTK EEKESQKLRR ELWTMISTER EKVGRCFANV IIEEGSAYEN HQQMGKTNRF
AYTFIKEKPA PGFSFLDSQL TVGEPIVISD EQGHFALALG YVTSVRKTRI AVAVDRRLHN
ARVRQPGFDE ADNQTFASIM QVPGSGGNAP EDREAGPVRY RLDKDEFSNG MATVRNNLVQ
IMADGVLGSR QIRSLVVDLE APRFKAVPTQ YILPSTASGQ GLNVDQKAAV EKVMSAQDYA
LVLGMPGTGK TTTIAHIIRA LVAQKKTVLL TSYTHTAVDN ILLKLKDDGI PILRLGPPVK
VHPEVPSFAT LAGVPKTSFS EIHEAWNDTP IVATTCLGIN HPVFAERIFD YCIVDEASQI
TLPICLGPIR MARKFVLVGD HNQLPPLVQN EEARLGGLDV SLFKLLSEKH PQSVVNLEHQ
YRMCEDIMTL SNTLIYNGRL KCGTEALRTT SLEIPDMDAL ATKHFDADSF LAHSQQHPLK
EGDKLSFCPS PTPTTCWLRD LLDPSARVRF INTDSLLPHS REEKSTRGQR IVNPLESRIV
CQLVDSLLTV GVPASEIGVM THYRSQLALL KHNMKNTLGG SAGAIRAGVK VAAEEIEMHT
ADRFQGRDKS VVVLSLVRSN EGCSIGELLK DWRRINVAFT RAKTKLLVVG SRETLRGASS
SVAGSPTAIA SPELGETGDD QGEGQGEPEG GEMLARFVRM MEDRNWVYEL RPGALEGHRF
ADANAASTAA DALSPRKPNP IFKPVSPRKG SALSPSKRAN AKLAGKGYKV QSKLQFGTPS
QGKENVGSQS LKSPKKGIVG RGKHNPKRIG ISERAIMKGR PIMRDIMNEI TDGRF
//
