ID A0A1J9Q9J4_9EURO Unreviewed; 1653 AA.
AC A0A1J9Q9J4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=ACJ73_03508 {ECO:0000313|EMBL:OJD25128.1};
OS Blastomyces percursus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=1658174 {ECO:0000313|EMBL:OJD25128.1, ECO:0000313|Proteomes:UP000242791};
RN [1] {ECO:0000313|EMBL:OJD25128.1, ECO:0000313|Proteomes:UP000242791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI222 {ECO:0000313|EMBL:OJD25128.1,
RC ECO:0000313|Proteomes:UP000242791};
RA Cuomo C.A., Schwartz I.S., Kenyon C., De Hoog G.S., Govender N.P.,
RA Botha A., Moreno L., De Vries M., Munoz J.F., Stielow J.B.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (AUG-2015) 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:OJD25128.1}.
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DR EMBL; LGTZ01000427; OJD25128.1; -; Genomic_DNA.
DR STRING; 1658174.A0A1J9Q9J4; -.
DR VEuPathDB; FungiDB:ACJ73_03508; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000242791; 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:UP000242791}.
FT DOMAIN 548..750
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 758..861
FT /note="DUF83"
FT /evidence="ECO:0000259|Pfam:PF01930"
FT DOMAIN 922..1013
FT /note="DNA2 rift barrel"
FT /evidence="ECO:0000259|Pfam:PF21123"
FT DOMAIN 1115..1203
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1215..1283
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1292..1518
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 27..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1653 AA; 185268 MW; B56C61A870FFDDE6 CRC64;
MPTVDQNCDD ASTMDKENVE IKLRMGEGDI PMPDTQSSET KCQEVQPEKK LPQTPAHRIP
LADLIGNTED AFSRAPGKVI SPEDHVFWKH EPCNTDPRDA SSSPITRGQK RYRSASPTSS
PLGADSKHIM SSPQPLAKPV RTPQHDIVAD LWSKYIGKST ENPGGNAPKP QFAHLVSSSP
QTPTAARENR DSSTLRRSNS CNVYWPTSNT KRRRVDNEQQ AVKRVRNIFA RSRSSLLGDG
TSKSSKISLL VGKIQETLLK SPREEISGPS SSTPLPERPD NMAELSGSPP KPRNENENNP
IDTPSRCSRR VMANDAVDND AMGTIQDLNA ILSEFDDDEL DDDFLEFAGK ADNQHKPIYS
EVGPLPDTVQ EENLRGILYT THAKPDGSGT SSINKNHKQP TLPTSHAHTN FDEVDEFNDS
DDEFPEAMQE VLARYDLEEQ TNTGKKPNDI LEELPVPAFE TAAVRKREPK TPSLDGAISS
SGDEFDEDID LESIEAAMQK AAGANGSSHN RKSRQTIERH LVLDSAENTY LNSKGQSKPE
KVLFVQEEKT NNNRAIILRE SWYDTPCSKG SYVHLIGSFD RMGRCVVDNS DNMIILHPDH
LISATVVADS FTCPRRAVLQ DRVKATSGAN KLQVYGHILH EIFQAAASAN RWDQSWFREV
ISRTLEHYVE SLYEIQVEFS EATEYLMSKM PALSSWADIF MRPHPTIESI TEDRNGTSSC
LSINKLLEVE EHIWSPMYGL KGNVDATVQV AVQEGTEKRT LTVPFELKTG RNISNEAHRA
QTALYTLLVS DRYDIDVTFG ILYYLEATKT FRVRAIRSEV RQMIQQRNRL AEFICKKSDL
PPMLTKSRIC NQCYAKDACF IYHKVMDDGD EESSGMGTSF LEIVGHLAPS HQNFFKKWDA
LLTMEERDIL KFRRELWTML SSEREGVGRC FGKVMVEPGS AYEETGIPKI NRFRYSFYKR
QPPSNFSFGD SQLSVGEPIV VSDEKGHFAL ANGYVTHISR KRISVAVDRR LQNARTRCSN
FDAERHQAFT GIMEIVETSG SNSTVFPEKA EDTTLYRLDK DEFSNGMATV RNNLVRMMDR
DTFQARRLRD LIIDGQIPLF NSTSSSTIPC LAGTELNIDQ EQAIKKVMSA NDYALILGMP
GTGKTTTIAH IIRALVSQGK SVLLTSYTHT AVDNILLKVK DDNIRTLRLG ATTRIHPDVQ
KFADLAGTPK KTIEELRDMY ENSRIVATTC LGINHPIFNS RTFDYCIVDE ASQITLPVCL
GPIRMAKTFI LVGDHYQLPP LVQDKEAREG GLDVSLFKLL CDLHPASVVN LEHQYRMCED
IMLLSNTLIY SGHLKCGTPE VAQSYLKIPN LGRLKQHHVD SLSLPPNVRN SCLGSRYGRC
WIRDLLDPVA RTRLVNTDPL EPQATESSKG SRIINPIEAT ICAQLVESFI SVGIPAGSIG
VVTLYRSQLS LLKQSLRHHP DLEMHTADRF QGRDKEIIIM SCVRSNSERN VGELLRDWRR
VNVAFTRART KLLIVGSKNT LRDGNELLGK FVQFMDSKAW TYDLPRTAVE QHVFENAENG
LTQLSPRKGT EAMLSDSISP KKRSPTKKTL KNRVTFHDQS PLKNKQRVAL SPVKNRQPSA
GLRRPQKIGG KLLDGARIVA TRPVLMDVLN DLM
//
