ID C1G4F6_PARBD Unreviewed; 1690 AA.
AC C1G4F6;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 62.
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=PADG_01822 {ECO:0000313|EMBL:EEH45672.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH45672.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH45672.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH45672.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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; KN275958; EEH45672.2; -; Genomic_DNA.
DR RefSeq; XP_010757088.1; XM_010758786.1.
DR STRING; 502780.C1G4F6; -.
DR GeneID; 22581416; -.
DR KEGG; pbn:PADG_01822; -.
DR VEuPathDB; FungiDB:PADG_01822; -.
DR eggNOG; KOG1805; Eukaryota.
DR HOGENOM; CLU_001666_2_1_1; -.
DR InParanoid; C1G4F6; -.
DR OMA; LRESWFD; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000001628; 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; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001628}.
FT DOMAIN 582..784
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 791..894
FT /note="DUF83"
FT /evidence="ECO:0000259|Pfam:PF01930"
FT DOMAIN 955..1047
FT /note="DNA2 rift barrel"
FT /evidence="ECO:0000259|Pfam:PF21123"
FT DOMAIN 1149..1237
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1248..1317
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1326..1553
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 51..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1594..1643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1594..1612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1690 AA; 189088 MW; E899F4D342A30B88 CRC64;
MPGDAFVISS NSRSKLNAFR YVPTARQQPE NMPTSLERSR DDSIVLPVDK ENQEVKTQAG
DRGLPVPITQ PNGMKHQDSQ PEKALPQTPV HRIPLADLIS NTEEAFSRAP GKVITPEDHV
FWKHEPCSMD YRDSSRSPST RGQKRHRSAS PTSSPLGRDL KNSKTSPLPP QKLLKTPQHD
IAADLWSKYI GKSTGKPDGD DPQSQFSHLI SSSPQTPAPG QLGKDSPALR RSISCNVYWP
TSNTKRRGVD NEQQAVNRVR NIFAGSRSSL LGPGTSKTSK INLLVGKIQE TLLNLPREDI
TGPSSSTPLP ERSGNMAELP RPPSKPASIN ENNPMNTPCR SSRRVIPKDA VDNKDVDTNQ
DLSVMSEFDD DDLDDDFLEF AGTADNQNTT AHPEVEVLHN TQQSQKPTQV MPTMVAAHDC
PDTNFRQKHH TQLISHISPS NNNPNEVNEF YDSDDEFPDG MEEVLAQYDI KEFPDSEKQQ
NRSLEGRLAP DTEEAAAACK GESNTTSVDG GVSLSGDEFD EDIDLESIES AMKKTASTGF
ASQNGKCSQP IKRYLILDLA ENTYLNCKGQ SRPQKVLFVE EEKTKINRAI TLRESWFDTP
CTKGSYIHLI GSFDPTGQCV VNNSDNIIIL HPDHLLSATV VADSFTCQRR AVLQDRVKAT
SEANKPQVYG HILHEIFQAA MTANRWDLPW LREIISRTLE RYVESLYEIR VDFPEAIEYL
MSKMPSLRSW ADMFVRSRPT TESIMEDRNG TSSRISINKL LEVEEHIWSP MYGLKGNIDA
TVQVVVQEGT EQKTLTVPLE VKTGRNNTNE AHRAQTALYT LLLSDRYDID VTFGILYYLE
VTKTSRVRAI RTEIRQMIQQ RNRLSEFVCQ TSKLPPMLKK PRICNQCYAK NACFTYHKIM
DNGDGETSEL GNSFLEVVGH LTPSHQVFFK KWDALLTMEE RDIMKFRREL WTMLSSEREA
VGRCFGNIMV EPGSAYEETD APKINRFRYT FFKHQPPANF SFGDSQLSVG DPIVVSDEKG
HFALAGGYVT HISRKRISVT LDRRLHNART RRSNFDADRH QAFIGIMEIV ETGGRESTIS
PEKAEDKNMY RLDKDEFSSG MATVRNNLVC MMDNTMLQAK RLRDVIIDGR APSFKPTSSS
TISSLANAEL NVDQKQAINK VMSANDYALV LGMPGTGKTT TIAHIIRALV SQGKSVLLTS
YTHTAVDNIL LKIKDDNIRT LRLGATTKIH PDVQKFADLA ATPKKTIEEL RDIYENSLVV
ATTCLGINHP IFNNRTFDYC IVDEASQITL PVCLGPIRMA KAFILVGDHY QLPPLVQDKE
AQEGGLDVSL FKLLCDLQPA SVVNLEHQYR MCEDIMLLSN TLIYSGHLKC GTPAVASSYL
KILNLSGLKQ HHVNSSSLPS NIRSPCLGSR YGHCWIRDLL DPVAKARLVN TDFLVPQAKE
SSKGSRIVNS IEATLCAQLV NSFISVGISA RDIGVITLYR SQLALLKQNL RHYLPDLEMH
TADRFQGRDK EIIIMSCVRS NSERNVGELF RDWRRVNVAF TRAKTKLLII GSKDTLRDGN
ELLGKFVELM DGKGWTYDLP PAAVESHVFE SFDNGPTQLS PMKGTNKAPL PPSISNKLKR
SPIKKSPRKR ISTNEQSPLK GKQRVALSPI KHEQAPIGFK RPQKMGWKAL DGAKIVATRP
VLRDVLNDLN
//
