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
//