ID H8X9K3_CANO9 Unreviewed; 1438 AA.
AC H8X9K3;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=CORT_0F04450 {ECO:0000313|EMBL:CCG24669.1};
OS Candida orthopsilosis (strain 90-125) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1136231 {ECO:0000313|EMBL:CCG24669.1, ECO:0000313|Proteomes:UP000005018};
RN [1] {ECO:0000313|EMBL:CCG24669.1, ECO:0000313|Proteomes:UP000005018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=90-125 {ECO:0000313|Proteomes:UP000005018};
RX PubMed=22563396; DOI=10.1371/journal.pone.0035750;
RA Riccombeni A., Vidanes G., Proux-Wera E., Wolfe K.H., Butler G.;
RT "Sequence and analysis of the genome of the pathogenic yeast Candida
RT orthopsilosis.";
RL PLoS ONE 7:e35750-e35750(2012).
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; HE681724; CCG24669.1; -; Genomic_DNA.
DR RefSeq; XP_003870797.1; XM_003870748.1.
DR GeneID; 14541595; -.
DR KEGG; cot:CORT_0F04450; -.
DR eggNOG; KOG1805; Eukaryota.
DR HOGENOM; CLU_001666_2_1_1; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000005018; Chromosome 6.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd18041; DEXXQc_DNA2; 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; 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; 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 414..613
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 975..1065
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1081..1148
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1158..1369
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1438 AA; 164001 MW; 57A0E0563B787C60 CRC64;
MTRNKNYEEQ QEPNNANMKS NSNDTESIKP LKRPKKQSYF FKPVNKLTSE AENHTQMIKP
IDTNTLRSQI QPVREADGYA HISEYSPKRK AKKHIEVQVA TDNSDDSFDG VRWRDSPDSK
SNHREESKLN ALKQGVQYSS SPLKSIKHVK TESAGGTTEV LSKYGADFYN VASISPKLSK
THSDLSNRVS KFKNESTRVS ALQRTKSTGV ESVDKSSYSG LVQGTLSSWI SKLNSGDTKD
ETPKSFNIKS SPTGKTYDET LQSNDPFSED EEILKMLSQH EIFLANQDPS GDKRSSVDSS
PSKSKQYIKS EDLKSSPKAD ISEDPFSDET DPELVNLLNG GDIKNSVFTK SFKEGMEKFE
KLLIRKGECV EKEEEFTDIA YGRSMLRRFK ILSCTEQVYG VNGTKQNILE VTNADKQKSR
LILRGEYCEL DFSVNDIIHV INTDERNPNL IDDTHNLLVL NPDILITATK IAQQVNCPRK
TVLVSRYKFP GTTSIPIIVG EMVHYIFQEC MVAETWDLQF MREIFNDLKE QYLLTLCTID
KGMEDVDQEV EKHLPYLQEW FESYYKKDSK SRPKIDDSSE RDQISFAVDD ILDIEEEIRS
PVFGLKGMID ATIIANLSNK AVNGKYLLPM EIKTGREHIS HSAQASLYAL LFKDRYDMDI
DSFILVYTRE GVTKRCQIRV SDLRSLINLR NRVSQHLRSG RTLPDILRRS SCERCEVVAG
CMTINYLSED GTKENSGIDE DDYELMTYHL ANLKYKEYFR YWDTLISKEE NIMSKSLKHL
WTLPNSLREE HGTSLNNLRI IDSNEDESSI FYIASAHGDK SQAKQFLYTF AKDQADASFN
MLSSKLTIND RVLISDEEGH FAIATGVIKS ILPSKITLST RRRIVTYDMK MKTFNQKNNQ
IMESLIHGRG KPQASGNKRF IIDKDEMFYG MGLARYNVLR IFLPDSSAEL RDLLVDLKAP
KFSNNNEPYT LESEFNHCQT MALNKVFSAE NYALILGMPG TGKSTIIVEM VRRIVEEGKT
VLLTSYTNSA VDNILLKIVE KMGDNKKFKF LRIGYPLRVH KSLHKYIPDY AEPIKSRSQY
RETYELPNIV ATTCLGITDS CFNLRQEFDY CIVDEASQIT VPINLGPISL AKKFILVGDH
YQLPPLVLHQ NAEVKYGLSQ SLFKILAEAH PPAVSELTEQ YRMCEDIMQV SNILVYENKL
KCGSPSVANQ CMDVPYPEAV TSFFLPEVPK RHQWMDLVFD KHRKVLFLDH DTVPAYETVF
GEAVRNSREA TLIQQIVKAF VTAGVDESQI GVMSFYRSQL ELLKRNLSSR TDLEILTADQ
YQGRDKQCII ISLVRSNNEK NAGDLLKEWR RLNVAVTRAK SKLVILGSRS TLSTNDTTKT
FIDFLESKGW YYSLPKDADM IYDLPQSENS SPIQKRLQKA RVSKNNPVIR NIIDDITK
//
