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Database: UniProt
Entry: K3VGR2_FUSPC
LinkDB: K3VGR2_FUSPC
Original site: K3VGR2_FUSPC 
ID   K3VGR2_FUSPC            Unreviewed;       795 AA.
AC   K3VGR2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN   ORFNames=FPSE_07635 {ECO:0000313|EMBL:EKJ72178.1};
OS   Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ72178.1, ECO:0000313|Proteomes:UP000007978};
RN   [1] {ECO:0000313|EMBL:EKJ72178.1, ECO:0000313|Proteomes:UP000007978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS3096 {ECO:0000313|EMBL:EKJ72178.1,
RC   ECO:0000313|Proteomes:UP000007978};
RX   PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA   Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA   Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT   "Comparative pathogenomics reveals horizontally acquired novel virulence
RT   genes in fungi infecting cereal hosts.";
RL   PLoS Pathog. 8:E1002952-E1002952(2012).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914}.
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:EKJ72178.1}.
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DR   EMBL; AFNW01000214; EKJ72178.1; -; Genomic_DNA.
DR   RefSeq; XP_009259028.1; XM_009260753.1.
DR   AlphaFoldDB; K3VGR2; -.
DR   EnsemblFungi; EKJ72178; EKJ72178; FPSE_07635.
DR   GeneID; 20366253; -.
DR   KEGG; fpu:FPSE_07635; -.
DR   eggNOG; KOG0740; Eukaryota.
DR   HOGENOM; CLU_000688_15_1_1; -.
DR   OrthoDB; 276256at2759; -.
DR   Proteomes; UP000007978; Chromosome 4.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd19509; RecA-like_VPS4-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015415; Spast_Vps4_C.
DR   PANTHER; PTHR23074; AAA DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR23074:SF17; FIDGETIN-LIKE PROTEIN 1; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF09336; Vps4_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007978}.
FT   DOMAIN          539..690
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          91..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          155..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..186
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..295
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..469
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   795 AA;  87669 MW;  A96504C534A31BF0 CRC64;
     MLRNRALAVL QKTYDDSYLS CSTAIYYEGQ GSEAEAMRHW RAALDQIYDY NANRAPPSYS
     PRTDTEKALQ EALKQLELQC KERIDLLEAL RVSRQEDSTP PPGKLTKRPS IPEGRGSLGQ
     GTITAMQYSE LSRPSLPHRP SQPRRTSSEL AIVDGPSAHL DPNLPALPRS ASPGGPALPP
     RPNKTLRTPS PEKYTMRTTL RSGKPGEKST KPRKASKPLA EGSSKAATLA WSALGSRDRF
     TRGTQSEFTP PAASPNSRTS LEQTRRPAPT QWDSHSRRLV VPRDREFDGD VSGNSRHSDE
     YCYARPSMLS VSAASSALNS SSYQDLPSSD VYTTRDERPS ISYNAIASPS PRKVSKQELA
     NDIETADDSG EGSERRNFSN NLPARSTVVR PPARPQKPSK ANTEVGDRSR RRSRKTQQTS
     VSSTSDDDTN RSGPKPRRVK AKETPVEADS GEETSDISES EKSPDDLTEW KNKKKQILKT
     LPPGVDSAAA KQILNDIVVQ GDEVHWNDVA GLDIAKNALR ETVVYPFLRP DLFMGLREPA
     RGMLLFGPPG TGKTMLARAV ATESKSTFFS ISASSLTSKY LGESEKLVRA LFGLARTLAP
     SIIFVDEIDS LLSQRSGSGE HEATMRIKTE FLIQWSDLQR AAAGRETTEK DKERGDANRV
     LVLAATNLPW AIDEAARRRF VRRQYIPLPE PTTRETQLRT LLGQQKHDLS NEDILKLVGM
     TDGFSGSDIT ALAKDAAMGP LRSLGEALLH MTMDEIRPIQ LLDFEASLTN IRPSVSKTGL
     KEYEDWAQEF GERGG
//
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