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Database: UniProt
Entry: S0DJE3_GIBF5
LinkDB: S0DJE3_GIBF5
Original site: S0DJE3_GIBF5 
ID   S0DJE3_GIBF5            Unreviewed;      1668 AA.
AC   S0DJE3;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=FFUJ_01067 {ECO:0000313|EMBL:CCT62386.1};
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT62386.1, ECO:0000313|Proteomes:UP000016800};
RN   [1] {ECO:0000313|Proteomes:UP000016800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC   {ECO:0000313|Proteomes:UP000016800};
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
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=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00005446}.
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DR   EMBL; HF679023; CCT62386.1; -; Genomic_DNA.
DR   STRING; 1279085.S0DJE3; -.
DR   EnsemblFungi; CCT62386; CCT62386; FFUJ_01067.
DR   VEuPathDB; FungiDB:FFUJ_01067; -.
DR   HOGENOM; CLU_001103_16_1_1; -.
DR   OrthoDB; 5474026at2759; -.
DR   Proteomes; UP000016800; Chromosome 1.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   CDD; cd17920; DEXHc_RecQ; 1.
DR   CDD; cd18794; SF2_C_RecQ; 1.
DR   Gene3D; 1.10.150.80; HRDC domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR010997; HRDC-like_sf.
DR   InterPro; IPR002121; HRDC_dom.
DR   InterPro; IPR044876; HRDC_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032284; RecQ_Zn-bd.
DR   InterPro; IPR018982; RQC_domain.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   NCBIfam; TIGR00614; recQ_fam; 1.
DR   PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR   PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF16124; RecQ_Zn_bind; 1.
DR   Pfam; PF09382; RQC; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00956; RQC; 1.
DR   SUPFAM; SSF47819; HRDC-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50967; HRDC; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016800}.
FT   DOMAIN          836..1017
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1041..1189
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1452..1534
FT                   /note="HRDC"
FT                   /evidence="ECO:0000259|PROSITE:PS50967"
FT   REGION          31..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          106..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          206..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          649..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          720..743
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1341..1442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1557..1578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1590..1668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..88
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..376
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..422
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1366..1383
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1590..1609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1625..1652
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1668 AA;  184095 MW;  0C1F049C5F7FE002 CRC64;
     MTRNNLAEHL SWLLNDQACS RPVTPSFPVC SDSSQITLPQ SQHTSSQTRP NKRTTTSDHP
     EVATRGGSDA SGTSNGRAGL GPTSRQTDQV IFDDEEDVMG RLALSSKTKK PSLVSKPQQC
     PAPLTVTPDI STQRDVTLKR SNEPPPKKIQ APVSVSARQP TSSPDFPKLK AGGIDYMDLT
     DDTFASSDSL SFGSDVKLWR EDYATRPEPE PAVSSGRKRK SNEISKEEFS DFGDLPDVYE
     LLGTEPPPPS PTRSARRKNG LSSARTRQIR DIPSISEEDH VMLSPSARVR SQFVGEERTA
     PLNESNQDLE GSSNLLKAPA SSGNTKSPLR APSLPPHTIP TGDELVIPDS DDEFLTPPSH
     NDSVTILKSS AVGSDSVESP DPKPPISAVK IDLHTTSQRQ ISSGSTITGE PTSTTNSSQS
     NRLITGDAPH ESCGEVFFLS SQEPVLLKQL ASDSNALANW AEFLDRLIQE NGKKFSQAIN
     ERWSKPQRAE VKAEKERLKR QRSAIAELAG PVEEYRILGE KRESLAQQIA QAYEESLDTD
     EDEVRLDDLT DEIQEVEDGL LKSIRDARLD VGGFLATTNT LHPGPAPTPV VVLGTQPVFQ
     NNVNMSMASR DAIPASETGT QVVHQTQLPK TNAWNPPASR IEASQGLSVL SQEDTDPSAL
     FPRDPTRVSG APYQQGRILK SRPVSPIPVD AEFDISDEEP SDSEDIQSRI QARPPNIFAH
     LSSSSRRTPQ ATHHRAGDEF SDFSDDEEML AFAQDYEIRQ SLAPESQDQR KIFSETSGNA
     SAAAKSRAVS NKSLPLMATE AIPAQLMKYS WSSEVQRMLK DRFRMKGFRC NQLEAINATL
     GGQDAFVLMP TGGGKSLCYQ LPAVVKTGKT RGVTIVVSPL LSLMQDQVDH MKALGIQAVA
     FNGECSAEYK RQVMSAFNEK SPEHFLELLY VTPEMVSKNV NFNNGLETLH RKGKFARLVI
     DEAHCVSQWG HDFRPDYKIL GQVRQKYPGV PVMALTATAT KNVIVDIRHN LGMDNCQIFS
     QSFNRPNLYY EVRPKTTNEK VMDAISSLIH SRYANQSGIV YTISRKNAEK VAESLSNKGI
     TARFYHAGCD PQEKVEVQNS WQRGQVKVVV ATIAFGMGID KPDVRFVIHH GLPKSLEGYY
     QETGRAGRDG NPSDCILFYG KADIRVLKKL IADGDGSHDQ KERQMSMLNR VTAFCDNKSD
     CRRTEILRYF GEDFSATQCR KSCDNCKAGL TFEQQDFSEY AVAAIKVVQA QNRITAVQCS
     DILLGKKYPT NEAELSDEWH GMAKGLKKHE LIRVIDKLSA EKAFNEDNQV GRHGMAIQYL
     RLGPTYRSFL SGQRRLMLSI QVPEPGAAKK TPKSRSKKGS KASAEEEASN MPSTYVSSPV
     GRQKKKSRTT ETNRGNTGQT SYSWEDAGFV MDDDDDYDDA FDNLPQHRPA KPPSRTSGPP
     ILVDTDMGSL DEIHRDMVES FVREAKQTEE KIRNQKSLRR PLFTDKDFRL MAIHWTTSPE
     KMRRIPGIDP DKVNDYGPRI LRILQKHYNH YREAMDPRSG GRDQDVVDLI SSEVEMDDEA
     LEDEDGEDSH YFNGSSRPDV QAFHSRLQTL GSTQTQAKPR ASSKSSGGTK KYAGGKRYPS
     KKPTSGVTKR RSTGASSSRK ASGSSTAGRT SGAAPKTLKK SGIGLMPM
//
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