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Database: UniProt
Entry: X0B3U8_FUSOX
LinkDB: X0B3U8_FUSOX
Original site: X0B3U8_FUSOX 
ID   X0B3U8_FUSOX            Unreviewed;      1336 AA.
AC   X0B3U8;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=FOQG_18828 {ECO:0000313|EMBL:EXK76431.1};
OS   Fusarium oxysporum f. sp. raphani 54005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK76431.1, ECO:0000313|Proteomes:UP000030663};
RN   [1] {ECO:0000313|EMBL:EXK76431.1, ECO:0000313|Proteomes:UP000030663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54005 {ECO:0000313|EMBL:EXK76431.1,
RC   ECO:0000313|Proteomes:UP000030663};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum PHW815.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00005446}.
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DR   EMBL; KI979511; EXK76431.1; -; Genomic_DNA.
DR   eggNOG; KOG0351; Eukaryota.
DR   HOGENOM; CLU_001103_16_1_1; -.
DR   Proteomes; UP000030663; Unassembled WGS sequence.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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:0046872; F:metal ion binding; 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; 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; 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; 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.
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:UP000030663}.
FT   DOMAIN          762..943
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          967..1118
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          95..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          647..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1271..1323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1336 AA;  148950 MW;  DEBD935DFDA0F0E4 CRC64;
     MARLKSSSRS RKPGLISRPQ QLLSSSCITP NRLARQDASA RRTNLSTWSP EPCKTQSPPK
     TAPASAVVRT IRMSSPNFPD LKADSVEYLD LTNDASETSD SLPFNGNAKP CREDYASRPN
     LVTSSGRKRK SSEISEEEFS DLGDFPDIYE LPGTYSPTSS PGNRSGTRRR DGSRGSRTRR
     TRDSFKNHLS TEILPISEEG EDEILSPSRY VHSPFAHGQS PRKALPVIDT QHPSKGPTSP
     LKESAVNSEA SNPVHQTNSL PPRMEDGRDE PFIPDSDGES LMPPSHNNPI AVLKVSTNKP
     AQICTHAWPT AMPAVQPDFA SPSQRLITPG IAAPRERAIA SNSSQTTKAT PEESFNELPS
     KTHPESSQTL FLLNQLSSQP STLTKWSEFM DKLIQQNDKN FLRAINERLP KEKRSEVKSE
     KERLLRQQKA FKQLAVPTDE YRALCRKREE LTQVITQAYA QGLDTDEDEV RLDDLIDEIQ
     AVEHVLLKTI DGTGLDVADF LGTVQKPTHG RPPASVIVKG TQLMFQKSAN MSMMSNVATL
     ASEMGTRVVH ETQLPNASQN PQYPATSRIE FSQRTSAISQ ENNAVGAPLF PKDTAKPSNA
     PYQSRPATRP SMVNPMPVDT EFGVGDDGFS DLDGLQLQPM LKAARNLVPG SRSPPQATHR
     HPDDEFSDFS DDEEMLAFAQ DYETRQSHVP ISQDFREVFS ETTGNAEAAA KPRTSSTELL
     TSVAPESIPA ELMRHSWSSE VQRMLKDRFR MKGFRHNQLE AINATLGGKD AFVLMPTGGG
     KSLCYQLPAV IRTGKTQGIT IVVSPLLSLM QDQVDHMKAL GIQAVAFNGE YSAEYKRQVM
     TAFEKRSPED YIELLYVTPE MVSKNTTFNN GLRTLYDKGK LARIVIDEAH CVSQWGHDFR
     PDYKTLGEVR QKYPGVPVMA LTATATQNVI VDIRHSLGMD NCQTFSQSFN RPNLYYEVRG
     KTTNAKCMDE IASLIKSKYA NQSGIVYTVS RKNAEKVAEN LSIQGITARH YHAGLDPQEK
     VEVQTSWQQG QVKIVVATIA FGMGIDKPDV RFVIHHGLPK TLEGYYQEMG RAGRDGDPSD
     CILFYGKQDI RILKKLIADG EGNNEQKERQ MTMLNRVTAF CDNKSDCRRV EILRYFGEDF
     SAAQCRKTCD NCKAGLIFEQ REFSEYAIAA IRVVQAQRRI TAVQCADILM GRKYPPYEAR
     RSDDWYGMAK SLKKHELVRV LDKMLAEKAF HENNQVGHHG MAIQYLKLGS TYRLFLSGQR
     KLMLSVQVPE EGANNKPFKP RSKQASKKPK DQDVTAVPSP DVSLPVGRRS KRSRTVESDD
     ENGALAWTAM RMMGSW
//
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