ID G3JGP4_CORMM Unreviewed; 1570 AA.
AC G3JGP4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=CCM_04686 {ECO:0000313|EMBL:EGX93313.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX93313.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX93313.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX93313.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(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: Nucleus {ECO:0000256|RuleBase:RU367041}.
CC Chromosome {ECO:0000256|RuleBase:RU367041}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC {ECO:0000256|ARBA:ARBA00007913, ECO:0000256|RuleBase:RU367041}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH126401; EGX93313.1; -; Genomic_DNA.
DR RefSeq; XP_006669896.1; XM_006669833.1.
DR STRING; 983644.G3JGP4; -.
DR GeneID; 18166708; -.
DR KEGG; cmt:CCM_04686; -.
DR VEuPathDB; FungiDB:CCM_04686; -.
DR eggNOG; KOG1805; Eukaryota.
DR HOGENOM; CLU_001666_2_1_1; -.
DR InParanoid; G3JGP4; -.
DR OMA; LRESWFD; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000001610; 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; 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; 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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50890; PUA; 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 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:UP000001610}.
FT DOMAIN 485..686
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 697..797
FT /note="DUF83"
FT /evidence="ECO:0000259|Pfam:PF01930"
FT DOMAIN 1051..1138
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1151..1219
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1227..1455
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 1..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1505..1547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1570 AA; 175749 MW; 51DC4538B1CC004A CRC64;
MPLQKSYSDS RGIAKPHNRS TWQRSHSHPN GYHTPKPRPP IPASDATKTK LNKFRFEALV
DDESPQACQS AEQAQSRPGH ADQSTPVTRL NWRDLEPLAN AEDTDKDASP NDRILWDNKP
RGSYASGLSP MLGRRGKKRA RSSSPTSSPA ADKPSVPVVN IKRLTKALRS PHPDPTFELW
DRFSLASPAS RKTPVANPAL AQLMVSSSPQ PNKQPEPQPG SVNLRRAASC GLNWPKRRKL
EKSKSGSQLG KGQRDLEAAS KSSLVSALLN TVTSSMQEDS SGDARRAIES PSPKEKKHVA
VEALPVYVPC KANGKESSGG SSDYGDDEFD DDALIELELT TTTPATQETP IKPRVSKPAA
MIPPKPKSDD FDDLDDELFD NEELVRLSQK LVLQQPKREA IQKKPAVPAE DLDDEFEDDF
ADDIDFEAVE LAATQSFQQA KANAGRINKD KTIQRYLITN VLESEYIDQY NVARPEKILL
IMPDNSKLTR QVHLRGAWYD TPAHAKSYVH VIGKFSINGQ CVVDDAQNLL ILHPDQLVSA
TVVADSFGCM RRAVLQDRVK ATSEASAPLV YGTMLHEIFQ DALLANRWDL PFLARLIEKI
TEKHVEELYT IKVGLPSARE HLQSKMMELS YWAKSFVSPQ PNNDAVVEDR NGKKATMAVT
KLLDVEEHVW SPMYGLKGNI DATVEVNMMD GEQSRLLTVP FEVKTGRNAS SSHMAQTALY
TLLLSDRYDI EIAYGVLYYM ETSKTMRIPA VRHELRHMIM QRNQLACYIR ERSVQLPPML
KSKNMCGRCY AKPSCFIYHR LADDGDGESS GMDEQFDELV KHLTPRHQEF FIKWENLLTI
EEKESQKTKR ELWTMTSNER EKKSRCFADV IIEEGSASVD SDTPRINRFH YTFVKRKPGP
GFSFLESEIS VGEPIVVSDE EGHFALAIGY VTAQRKQRIS VAVDRRLHNS RIRHPGFDEV
DNQVFASIME VAPEGASVEQ SQGRIKAAPI RYRLDKDEFS NGMATVRNNI VQIMNNQFAE
PRRIRELIVD LEAPRFKHIP TQYTVSEQET LNVDQKKAIE KVMSAQDYAL VLGMPGTGKT
TTIAHIIRAL TSQGKSVLLT SHTHTAVDNI LLKLKSDKMK VLRLGAPAKV HPDVQEFAIL
AGQPKTTFEE IKEAWHDTPV VATTCLGINH PVFQERAFDY CIVDEASQIT LPICAGPIRM
ARTFVLVGDH NQLPPVVKNE TARQGGLDVS LFKLLSDSHP DSVVNLAHQY RMCEDIMTLS
NTLIYDGKLV CGTEELRKKK LHIPNMKALS QRHHNASTVL LPGTPRSFCK GPAPSQCWLY
DLLESEARVR FVNTDTIRPA AREEAHGKRI VNSAEVRIVS QLVESFLTVG IPASEVGVMT
HYRSQLSLLK DKLKGYPGVE MHTTDRFQGR DKEVIVLSLV RSNDACHIGE LLRDWRRINV
AFTRAKTKLL VIGSKSTLSG SNVNNKENML SRFVALMEQR DWIYNLPPDA LDNHYFEELG
TQATSMGGTQ VSSPQSHKKK SLGAKKALSA APGKENRRPS PRKARIGERA LLKDKLITRD
ILNEMTNGAY
//