ID C5DTV1_ZYGRC Unreviewed; 1510 AA.
AC C5DTV1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN OrderedLocusNames=ZYRO0C11528g {ECO:0000313|EMBL:CAR27212.1};
OS Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS / NRRL Y-229) (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=559307 {ECO:0000313|EMBL:CAR27212.1, ECO:0000313|Proteomes:UP000008536};
RN [1] {ECO:0000313|Proteomes:UP000008536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC Y-229 {ECO:0000313|Proteomes:UP000008536};
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC {ECO:0000256|ARBA:ARBA00007913}.
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DR EMBL; CU928175; CAR27212.1; -; Genomic_DNA.
DR RefSeq; XP_002496145.1; XM_002496100.1.
DR STRING; 559307.C5DTV1; -.
DR GeneID; 8203363; -.
DR KEGG; zro:ZYRO0C11528g; -.
DR HOGENOM; CLU_001666_2_1_1; -.
DR InParanoid; C5DTV1; -.
DR Proteomes; UP000008536; Chromosome C.
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; 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; PTHR43788:SF19; DNA-BINDING PROTEIN SMUBP-2; 1.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 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};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022806};
KW Iron {ECO:0000256|ARBA:ARBA00022485};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008536}.
FT DOMAIN 423..638
FT /note="DNA replication factor Dna2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08696"
FT DOMAIN 1021..1112
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1122..1188
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1198..1414
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 1..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1457..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..304
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1457..1477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1510 AA; 170488 MW; 48C39249D7F3346F CRC64;
MPRTPQKKRS GSLVVSPEAT TSKNRPPITS AATERDNLDE RRRRKNYQFA PINNLDNNNK
PENSVLKSIS VSQVRNTSYS NSKKVQRSKQ QQKATLQPSF KNDPILKPVR RQESLEEGPT
EEVIWKYSPT ARDLSDKVNS SNDNSEDNVQ AEKDQEPSST PLVPKRLKSV LSFTNINDRE
QSEPPLTTLS MQQRDSLRSR GTTDSMKESL RDIDDILGDI EGDLSMKPKL NRVNDLPSSP
SGIQQRQENV EEDYEDSDSN NGDESLINIL TQKPTLDDPT PELPTPGTTA PAPAPGPTAP
APAPVLPEHK SSSDNELLDD SLLDYFEEDE KNNDEITDNL ANKDLEDLNQ VGKQFSQNLN
IEKNDGNEDP ESSDSEIISE NQEFIELAKS AVIREGVERL VILNVSELQL PKVGRQKILH
CIDHKGETSS VMVRHPWVYL EFSRGDAIHI IQGQNVDNKR LLSDDINPKT NVRNDNLLVL
NPDILLSATT VGNSIGCLRR STIETIFDDP RGEPKISMTI GNIVHELLQD ALRCKLENQK
LTVDYLEEVL DSLLKTYSFA IFVCNYTIEQ VKDEIMNSHA TNILQFVNQF VQKSNLGSYV
SISGRRTTRP ISIPVILDIE ENILSHIYGL KGFLDATVLA HEEKKHEIVP LEVKTGKLGS
VSHEAQGLIY TLLLKDKYEV PVDFFLLLQT RTNNFIKHPK ILHSIKHVIM ARNQLATKLK
YRLKEITWDK SHDVILPPIL QSSVCDNCFT KESCMVLNNL LEDGTAEESG LRPGEYETIT
SHLSTNHDKY GAFFKKYNDL ITQEESSIMH IKKQLFLLDS NTKESTSGLC LSNLCLVDIS
EENSTSEEFL HVFKRNFQEG QKPQSMLLSQ LNVNDYVFIS DERGHFGLCQ GRVTSITRGS
ITICSKKRLR NPEVVAKEIL SAAKKQPIEG SQPLITYRLD KNVIEQGLSL TRFNLLNLFL
PPVTEDHFVV DQQTGQERSI KKSEGGDQRM RTFLVDKAPP EFIPDELPPL IPYDPNELES
FNYDQRKAVG KVMRAKDYAL ILGMPGSGKT TVIAQIIKIL ASRGQKVLLT SYTHSAVDNI
LLKLKGSPIN IIRLGSARKI HPEIHEYQPS YQDAESYEDI MKQISDTQVV ATTCLGLNDI
FFTLQQKDFD YAILDEASQI SMPVALGPLR YASKFIMVGD HYQLPPLVRN EEARLGGLQE
SLFKILCEAQ PKAVIELTYQ YRMCDDVAAL SNFLIYSNKL KCGNEQVAKK KINLPRLKEL
ENFHCPQELH EKDWLCEILE PHKKVIFLNY DLCEEEQLIE INEQKTITNP GEVDIAEQCV
NGLIHAGMDC RDIGVMTLYR AQLQLLNKRF ASDHYSNLEI LTADQFQGRD KESIIISLVR
SNVEHNAGSL LRELRRVNVA MTRAKSKLII IGSRATISSV PQMARLVNFL HSKGWIYDLP
HHFRDFHKFP ISSPSSSFLH SSQGKNKSYQ GSTVDHKSTN GTERKGAKNI TASSQLVKDH
PIIKQSLLEF
//
