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Database: UniProt
Entry: W9HX59_FUSOX
LinkDB: W9HX59_FUSOX
Original site: W9HX59_FUSOX 
ID   W9HX59_FUSOX            Unreviewed;      1197 AA.
AC   W9HX59;
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=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=FOYG_11434 {ECO:0000313|EMBL:EWY87208.1};
OS   Fusarium oxysporum NRRL 32931.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY87208.1, ECO:0000313|Proteomes:UP000030753};
RN   [1] {ECO:0000313|EMBL:EWY87208.1, ECO:0000313|Proteomes:UP000030753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
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., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL   Submitted (JUN-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=3.6.4.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001556};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; JH717845; EWY87208.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9HX59; -.
DR   HOGENOM; CLU_001832_2_3_1; -.
DR   OrthoDB; 3682876at2759; -.
DR   Proteomes; UP000030753; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
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:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR   CDD; cd17971; DEXHc_DHX8; 1.
DR   CDD; cd05684; S1_DHX8_helicase; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR044762; DHX8/Prp22_DEXHc.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF85; ATP-DEPENDENT RNA HELICASE DHX8; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50126; S1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030753}.
FT   DOMAIN          224..300
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          542..705
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          730..903
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          79..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          328..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          435..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..157
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..174
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..471
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1197 AA;  134833 MW;  1BD9734947C6A588 CRC64;
     MDDLSNLELL SLVSKVSSEL KNHMNLEDKT VAEFLIDKRT KCSNFEDFRD DLAKALPSIP
     LSLIESIDRL VIALHPQFKG KKANHEEHHS RTLEEKEKVF SGLALPDKEP ARDDGSGAFD
     DTLALLEGLE GKAKKEKSTR KRSRSPREAD YKESRRRKRS RSRERRKRDK YRSRSRSHER
     GDEDWRDGYR DSRKDRRGRR RHDDDDDRFR NAPAPEVDDS PQLHKVYEGH VTGLKEFGAF
     INLHNVRGRV DGLVHVSRMS AGQRVNHPSD LVSHGQKVWV KVTSLDKDQN GRDRVGLSMK
     DVDQSTGEDL EPQARMTTGA NMEALGGGGG GLRDGFAEPT GMPRDSLGPP RRQKKRMTSP
     ERWEIRQLIA SGVAKASDYP DLEEDYNATL RGDGELELEE DVDIEVREEE PPFLAGQTKQ
     SLELSPIRVV KAPEGSMNRA AMSGTALAKE RKELKQQEAD AAAKDEPKEN LSSQWQDPMA
     DPDKRKFASD LRNARKNQPS EDVPEWKKAV IPKGQSLGKR TNLSIKEQRE SLPVYAFREQ
     LIKAVHENQI LIVVGETGSG KTTQLTQYLA EAGFANDGII GCTQPRRVAA MSVAKRVAEE
     VGCKLGEEVG YTIRFEDCTS PSTKIKYMTD GMLQREILVD PDMSRYSCIM LDEAHERTIA
     TDVLFALLKK ALKRRPDMKV IVTSATLDAD KFSAYFNECP IFTIPGRTYP VEILYSKEPE
     SDYLDTALVT VMQIHITEPK GDILLFLTGQ EEIDTACEVL YERMKALGPN VPDLIILPVY
     ASLPTEMQSR IFDPAPPGSR KVVIATNIAE TSITIDEIYY VVDPGFVKQN AYDPKLGMDS
     LVVTPISQAQ ANQRAGRAGR TGPGKCFRLY TEAAYQSEML PTSIPEIQRQ NLSTTILMLK
     AMGINDLLHF DFMDPPPINT MLTALEELYA LSALDDEGLL TRLGRKMADF PMEPSLAKVL
     IAAVDLECAD EVLSIVSMLN IPTVFYRPKE KQSQADQKKA KFHDPHGDHL TFLNVYNSWK
     QSGYSAPWCF ENFIQARSMR RAKDVRDQIV KIMDRYKHSI KSCGRDTEKV RRALCAGFFR
     NAARKDPQEG YKTLIEGTPV YLHPSSALFG KQAEWVIYHE LILTSKEYMH CTTSIEPKWL
     VEAAPTFFKV APTDKLSKRK KAERIQPLYN KFATEDDWRL SAQRKGGRGG GGGGTWG
//
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