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Database: UniProt
Entry: W9IEX3_FUSOX
LinkDB: W9IEX3_FUSOX
Original site: W9IEX3_FUSOX 
ID   W9IEX3_FUSOX            Unreviewed;      1083 AA.
AC   W9IEX3;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Regulator-nonsense transcripts 1 {ECO:0000313|EMBL:EWY91056.1};
GN   ORFNames=FOYG_08333 {ECO:0000313|EMBL:EWY91056.1};
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:EWY91056.1, ECO:0000313|Proteomes:UP000030753};
RN   [1] {ECO:0000313|EMBL:EWY91056.1, ECO:0000313|Proteomes:UP000030753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753}, and NRRL 32931
RC   {ECO:0000313|EMBL:EWY91056.1};
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.
RN   [2] {ECO:0000313|EMBL:EWY91056.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NRRL 32931 {ECO:0000313|EMBL:EWY91056.1};
RG   The Broad Institute Genomics Platform;
RA   Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA   Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "Annotation of the Genome Sequence of Fusarium oxysporum NRRL32931.";
RL   Submitted (JUN-2012) 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:ARBA00000600};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000256|ARBA:ARBA00000600};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007913}.
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DR   EMBL; JH717843; EWY91055.1; -; Genomic_DNA.
DR   EMBL; JH717843; EWY91056.1; -; Genomic_DNA.
DR   HOGENOM; CLU_001666_4_0_1; -.
DR   OrthoDB; 170190at2759; -.
DR   Proteomes; UP000030753; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:InterPro.
DR   CDD; cd21407; 1B_UPF1-like; 1.
DR   CDD; cd18039; DEXXQc_UPF1; 1.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   CDD; cd21400; ZBD_UPF1-like; 1.
DR   Gene3D; 2.40.30.230; -; 1.
DR   Gene3D; 6.10.140.1240; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR045055; DNA2/NAM7-like.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047187; SF1_C_Upf1.
DR   InterPro; IPR040812; UPF1_1B_dom.
DR   InterPro; IPR018999; UPF1_CH/ZBD.
DR   PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR   PANTHER; PTHR10887:SF364; REGULATOR OF NONSENSE TRANSCRIPTS 1; 1.
DR   Pfam; PF13086; AAA_11; 1.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   Pfam; PF18141; UPF1_1B_dom; 1.
DR   Pfam; PF09416; UPF1_Zn_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51997; UPF1_CH_RICH; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022806};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU01341}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030753};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01341};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU01341}.
FT   DOMAIN          87..244
FT                   /note="Upf1"
FT                   /evidence="ECO:0000259|PROSITE:PS51997"
FT   REGION          39..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          95..127
FT                   /note="C3H"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT   REGION          109..137
FT                   /note="CC/SHH/C"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT   REGION          155..185
FT                   /note="C4"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT   REGION          899..929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1049..1083
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        899..917
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1083 AA;  119464 MW;  26C1EFD54150088A CRC64;
     MEGAFTHVGN HLISDSAAAI KAGADDLSTI DPDESLLYGK YGDRNGRRRA DDDDNQTEAF
     EEDDNDSLNS VPIDGLTGLK LKGQDEEKEL PAHACAYCGI HSPGCVVKCL TCNKWFCSAR
     GNGTSTHIVN HLVRARHKEV QLHPESTLGD TVLECYNCGT KNAFLLGFIP AKSDTVVVLL
     CRQPCAANTS NKDMNWDTSR WQPLIEERAF LPWLVATPSD SEQLRARHLT PNMIAKLEEM
     WKIEPKATVV DLEKAASIDD DPQPVLLNYD DPYHYQNIFG PLVKMESDYD KKLKEAQSED
     GLLVRWDYGL NNKHLVSFNL HKIESGDVKL AVGDEMRLRY KGELRSPWEG VGYVIKIPNN
     QSDEVTLELR KTGNEKLVPT DLSHNFSADY VWKATSYDRM QLAMKTFAVD DMSVSGYIFH
     TLLGHEVQLQ VMKTNLPKKW SAPGLPDLNP SQVGAIKAVL QKPLSLIQGP PGTGKTVTSA
     TIIYHLAKMS GNQVLVCAPS NVAVDQLCER VHRTGLKVVR LTAKSREDVE SSVSFLALHE
     QVRMSEHNSE LVKLSQLKNE LGELSSQDEK KYKQLTKIAE RDILNNADVV CCTCVGAGDP
     RLSKMKFRNV LIDESTQSAE PECMIPLVLG CKQVVLVGDH KQLGPVIMNK KAAKAGLNQS
     LFERLVNLKL SPIRLNIQYR MHPCLSEFPS NMFYDGSLQN GVTHENRLRK DVDFPWPVGE
     MPMMFWSNLG HEEISASGTS YLNRTEASNV EKAVTRFFKA GVKPADIGVI TPYEGQRSYI
     VTTMQNSGTY KKEYYKEVEV ASVDAFQGRE KDFIVLSCVR SNDNQGIGFL SDPRRLNVAL
     TRAKYGLVIL GNPKVLSKHE LWHNLLVHFK DRKCFVEGPL TNLQACLLQF SRPKVSYRQK
     NQQPQFGAGS YSNGGRFNPP PSGRDFDAGS MVSYIPDDVS SVHGSAFGGA SLSSAFPPMF
     SSFTPDQWPG LPGVTAPGRG GKSRGRATES IAGESVANSE YTDASSSVIG GKGVGQGGVS
     LGAGLHDAVT GMRPVSYSQS DRLKQYVESS GRMVPGNGYG RRFDDDEKSV STAFHSQIGG
     GYD
//
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