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
//