ID G4YS66_PHYSP Unreviewed; 703 AA.
AC G4YS66;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 13-SEP-2023, entry version 47.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0008006|Google:ProtNLM};
GN ORFNames=PHYSODRAFT_554819 {ECO:0000313|EMBL:EGZ24767.1};
OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS (Phytophthora megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ24767.1, ECO:0000313|Proteomes:UP000002640};
RN [1] {ECO:0000313|EMBL:EGZ24767.1, ECO:0000313|Proteomes:UP000002640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ24767.1,
RC ECO:0000313|Proteomes:UP000002640};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
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DR EMBL; JH159152; EGZ24767.1; -; Genomic_DNA.
DR RefSeq; XP_009520055.1; XM_009521760.1.
DR AlphaFoldDB; G4YS66; -.
DR STRING; 1094619.G4YS66; -.
DR EnsemblProtists; EGZ24767; EGZ24767; PHYSODRAFT_554819.
DR GeneID; 20663033; -.
DR KEGG; psoj:PHYSODRAFT_554819; -.
DR InParanoid; G4YS66; -.
DR OMA; LIRGDMT; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR CDD; cd19497; RecA-like_ClpX; 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; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00382; clpX; 1.
DR PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002640}.
FT DOMAIN 377..528
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 584..678
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 91..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..202
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 COMPBIAS 97..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 75195 MW; 6F6CFA569887773C CRC64;
MLRRLRPDAR ALACASHLLQ SVRVSAAPSA RALSLLPSAR TQRPLDLKLQ RALRVATLIT
GPPGHSKKPA GDALCCPQCG DALVLAEALG GGKTPAASDS KSPSSSSSPA SAAAAASSPV
EFKKGDVVKC ETCNLHFALK AQPTTPAQPS PAFRNAAAAA ALSSLSSSLS PGMQTTRGSS
LGGPTYSGNF PSPTRGGGGR MTADGEYEKL ANEALFGGAA ATDATVTKDR VLTPREIYEG
LNEYVIGQDK VKKTLAVGVH NHYKRLHALE LLQARKDAEA ACAKQQHARA GGVTRQHVDL
DDSRLSSIGR RLLLEEIYPG LEKKEAGLEQ EAKQRAAEGT SETSEAAAAA PSHAHATRLQ
HHSLGDKLQY LEGVELDKTN VMLVGPTGSG KTLLAKTLAR LAKVPIVIAD ATCLTQAGYV
GEDVESVLFK LYQAANYNLE ATQRGIVYID EIDKITRKSE NVSITRDVSG EGVQQALLKI
LEGSMVNVPE KGGRKNPRGE YITIDTTNIL FICGGAFAGL EKQVTRRTSR SSIGFGAQMP
NMRLKDSDQI GQLLSQAEPE DLVSYGLIPE FIGRFPMLVS TTGLSKDELV QVLTEPKNSL
VRQYKALFAL SDVEFHATEG ALEAVAESAL SKNTGARGLR SIFERALMET MFDLPDMNDV
RAVYVDEEAI LGRKRPVLIR GDMTLDEYLK NLEEDSDKRE EAV
//