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Database: UniProt
Entry: F9GFC6_FUSOF
LinkDB: F9GFC6_FUSOF
Original site: F9GFC6_FUSOF 
ID   F9GFC6_FUSOF            Unreviewed;      1349 AA.
AC   F9GFC6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=ATP-dependent RNA helicase ucp12 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FOXB_17360 {ECO:0000313|EMBL:EGU72116.1};
OS   Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU72116.1};
RN   [1] {ECO:0000313|EMBL:EGU72116.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU72116.1};
RX   PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA   Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT   "A highly conserved effector in Fusarium oxysporum is required for full
RT   virulence on Arabidopsis.";
RL   Mol. Plant Microbe Interact. 25:180-190(2012).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGU72116.1}.
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DR   EMBL; AFQF01006928; EGU72116.1; -; Genomic_DNA.
DR   STRING; 660025.F9GFC6; -.
DR   PaxDb; 5507-FOXG_01658P0; -.
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   CDD; cd17917; DEXHc_RHA-like; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.30.160.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006575; RWD_dom.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF145; ATP-DEPENDENT RNA HELICASE DHX29; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   Pfam; PF05773; RWD; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          591..767
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          828..993
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          191..218
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1349 AA;  149686 MW;  D8E1C477B3461324 CRC64;
     MVKKGKGKSS GGIDLSDPMP SAPPKDQGKG KKGQKGGTST PEAVPSGPPK PTVKQLIGGS
     SWTGKLPVNL LSEYCQKQKW ERPDYDTKKT PDGFTVWVTM SAKDPKTQQI TKLEPFKIPA
     THKHLIMRPT AIEAKHAAAT YALFRVCSMQ NKHTVLPPEH KSLWKDFQAL KTQDVKEGKA
     WMYEPDPFKS LQERQEAKAA AEKKRKEIEA AKAKAAAMPG ASGLVLMSNA GKGDSRSSNI
     MKGWSTAPKV EMGKKTRAQL ETLLRSGVKW NPNGVQMSKA QKDAIISELS KLSFRKSHVE
     EAVEYCKDRE ETLEWLLIHV PEDDLPRWAL PESYAAGVSV GATNLRREGI IKRLAQAGYS
     LELATRVLDE QGVDEDKAAE TLQNLLFPRE SQDSADADFL DLGSPEEQWE EEVGSLEAIY
     GEGFEREGDN VIRIKLDSVK NGQQTVDASF QVRRPATYPA NLILSIVANI PSYIKLSIIR
     KALKYIDESL RDEPMKIYLA MDWIQQNING IIEEPGKLVD ISAVSSAAAE YKPVAAIAQN
     KRSTRAPKMI KWIKDEKSRE QWLRRQESSS LKNMVSKRQG LPAWQMREAI IGTVRSNHVT
     IISGETGSGK STQSMQFILD DLYAQGLGGC ANMIVTQPRR ISALGLADRV AEERCTRVGE
     EVGYAIRGES RRSKDTKITF VTTGVLLRRL QISGGRVEDV VASLADVSHV VIDEVHERSL
     DTDFLLNLIR DVMKAKKDML KLILMSATLD AATFKRYFAS ERLSVGTVEI AGRTFPVDEY
     YLDDVIRMTA YGVESSDSEF ISGEALGKVI QKLGHRINYN LLVETVKAVD FELSYEKKPG
     GILIFLPGVG EINQACRALK AINSLHVLPL HASLETREQK RVFSGAPPGK RKVVVATNVA
     ETSITIDDIV VVVDSGKVKE TSFDVQNNMR KLEETWASRA ACKQRRGRAG RVQEGRCYKL
     FTQNLEQQMP ERPEPEIRRV PLEQLCLSVR AMGMKDVAGF LGRSPTPPDA TAIDGAMKLL
     RRMGALDGDE LTAMGQQLAM LPADLRCGKL MVFGAIFGCL DDCVTIAAIL STRSPFVSPQ
     EKRDEAKEAR MKFYRGDGDL LTDLQAFQEW DFMMQDHIPH RQIRSWCEEN FLNFQTLSDI
     SNTRAQYYTA LGEIGIVAPS EATIEAHARG ASSDGSQLLR ALVAAAFTPQ IARIQYPDKK
     FASSMSGAVE LDPEARSIKY FNQENGRVFV HPSSTLFGSQ GFSGNAAYMA YFSLISTSKI
     FIRDLTPFNA YTLLLFSGPI ELDTLGRGLL VDGWLRLRGW ARIGVLLARL RGMVDELIAK
     KVESPEMNVK DDEVIMLVRK MIELDGMDA
//
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