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Database: UniProt
Entry: G3JGP4_CORMM
LinkDB: G3JGP4_CORMM
Original site: G3JGP4_CORMM 
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}.
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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
//
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