ID C5NZ41_COCP7 Unreviewed; 1630 AA.
AC C5NZ41;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
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=CPC735_013420 {ECO:0000313|EMBL:EER30024.1};
OS Coccidioides posadasii (strain C735) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=222929 {ECO:0000313|EMBL:EER30024.1, ECO:0000313|Proteomes:UP000009084};
RN [1] {ECO:0000313|EMBL:EER30024.1, ECO:0000313|Proteomes:UP000009084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C735 {ECO:0000313|Proteomes:UP000009084};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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 -!- 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:EER30024.1}.
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DR EMBL; ACFW01000001; EER30024.1; -; Genomic_DNA.
DR RefSeq; XP_003072169.1; XM_003072123.1.
DR GeneID; 9697664; -.
DR KEGG; cpw:CPC735_013420; -.
DR VEuPathDB; FungiDB:CPC735_013420; -.
DR HOGENOM; CLU_001666_2_1_1; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000009084; 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; 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; 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.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU367041};
KW ATP-binding {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|RuleBase:RU367041};
KW Iron {ECO:0000256|RuleBase:RU367041};
KW Iron-sulfur {ECO:0000256|RuleBase:RU367041};
KW Metal-binding {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|RuleBase:RU367041};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367041}.
FT DOMAIN 538..740
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 746..850
FT /note="DUF83"
FT /evidence="ECO:0000259|Pfam:PF01930"
FT DOMAIN 1104..1192
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1205..1273
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1281..1507
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 1..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1548..1589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1630 AA; 182417 MW; 6F637AF4542677A6 CRC64;
MSASNGDDES KTVGRLDERG GSRPPVESVE RAALDSNKEN LHSEGREVKP ASSCPQTPAH
RIPLADLISN TEDAFNQAPG KVLTPEDHVY WDHRSPSLKN KPRSSLCRGK KRSHSSSPTR
SPLNKDVPAE LRPTGSVMKT PQHDIAADLW SKYVGKGNEI PGGDLPKFHF SQLASSPQTP
APQSRSARDG SGLRRANSCN TDWPTSNTKR RRLDYDQQRT NNIRDGFTRS RTSLLASDRS
KSSKINLLVE KIQDTLLKYP KDDPTAPSSS SPLPDRSDNT DDGCPMSPPK ESIQNQPIDT
PSKCAPSLRY ERQPVEANFD SDSQEKFDVH GASSEFGDDD LDRDFLELAV ASPKKLFPLC
TDKPKANEPV EKVEDIPTLH PTNPPPHSMD EKVSHIIDEF NDNDDELDDG LEEIMAQYDS
KDLSAGQTTS DERIMQDLGP GKSTNGKTNG QDEMKNDPNM KAETAVTLMS DDEFDDDIDL
EAIEDAMRKG TEVAAATSKH FKHPQAIKRY LILDCAENSY TRSNGRAQLE KVLFVEEERT
KQNRAITLRE SWFDMPCKKG FYLHLIGEFD TTGQCIVDDA NNMIILHPDY LISATVVADS
FTCQRRAVLQ DRIKATSEAS KPQVYGHILH EIFQEAMQAN RWDFGCLRGL VDETLPKYLE
SLYEIQVDVP EAKAYLQAKI PALKAWAEVF LRCRPSLESI IEDRNGTKAR LCINKLLEVE
EHIWSPMYGL KGNVDATVQV VLQDKTEQKT LTVPLELKTG RNTTNETHRA QTALYTLLLS
DRYDIDVTFG ILYYLEASKT HRVRAIPAEI RQMIQQRNRL AGYVRERLDL PPMLKNPRIC
NQCYAKTPCF VYHKLMDNGD GGTSGIGKSF TELVGHLSPL HQTFFKKWDL LLTQEETEAM
KFRRELWTML SSEREGVGRC FSNVVIEPGS AFKDTDGPKI NRFRYTFVKH KPFSGFSFAE
SQITAGEPIV VSDEKGHFAL ANGYVVQISP RRLTVSVDRR LHNAQRKVVG FDADRNQSFM
GIMEVNDSKL ADSRVAEEEE VVLYRVDKDE FSNGMATVRN NLVCMMDNSH FRSKRLRDLI
IEGVPPSFKP LSSVPNLSAF AEANLNVDQK EAIEKVMSAD DYALVLGMPG TGKTTTIAQL
IRAIVAQGKS VLLASYTHTA VDNILLKIRY DGTKILRLGV PAKVHPEVQQ FADLAGFPKK
SIEEIKDSIE NSQVVATTCL GINHFIFNSR TFDYCIVDEA SQITLPVCLG PIRMAKTFIL
VGDHYQLPPL VQNKEALEGG LDVSLFKLLC DMHPGAVVNL EHQYRMCEDI MLLSNTLIYF
GHLKCGTPEV ASRSLNIPNM SGLKQHHISP LSVLSSHTPC LGPTRGRCWL RDLLDPSAKA
RLVNTDFLNP RAGESANGSR IVNVVEVALC TQLVEALISV GIPAQEIGVV TLYRSQLALL
RQNLRRHLPE LEMHTADRFQ GRDKEVIIMS CVRSNAENNV GELLRDWRRV NVAFTRARTK
FLIVGSKTTL REGNELLDRF VKLMDGKGWC YDLPPTAVES HVFEEPAFTQ VSPQRTKSKP
VSPKKKGQSP IKRSPVKRQS RTVLGPMRNE SGLFGMGCRK AEKLGGKETH AAKMVGRRPV
LRDVYHDLLG
//
