ID M4BZM6_HYAAE Unreviewed; 694 AA.
AC M4BZM6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 13-SEP-2023, entry version 46.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS (Peronospora arabidopsidis).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Hyaloperonospora.
OX NCBI_TaxID=559515 {ECO:0000313|EnsemblProtists:HpaP812049, ECO:0000313|Proteomes:UP000011713};
RN [1] {ECO:0000313|Proteomes:UP000011713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Emoy2 {ECO:0000313|Proteomes:UP000011713};
RX PubMed=21148394; DOI=10.1126/science.1195203;
RA Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K., Dong S.,
RA Downton P., Dumas B., Fabro G., Fronick C., Fuerstenberg S.I., Fulton L.,
RA Gaulin E., Govers F., Hughes L., Humphray S., Jiang R.H., Judelson H.,
RA Kamoun S., Kyung K., Meijer H., Minx P., Morris P., Nelson J.,
RA Phuntumart V., Qutob D., Rehmany A., Rougon-Cardoso A., Ryden P.,
RA Torto-Alalibo T., Studholme D., Wang Y., Win J., Wood J., Clifton S.W.,
RA Rogers J., Van den Ackerveken G., Jones J.D., McDowell J.M., Beynon J.,
RA Tyler B.M.;
RT "Signatures of adaptation to obligate biotrophy in the Hyaloperonospora
RT arabidopsidis genome.";
RL Science 330:1549-1551(2010).
RN [2] {ECO:0000313|EnsemblProtists:HpaP812049}
RP IDENTIFICATION.
RC STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP812049};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
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DR EMBL; JH598063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M4BZM6; -.
DR STRING; 559515.M4BZM6; -.
DR EnsemblProtists; HpaT812049; HpaP812049; HpaG812049.
DR VEuPathDB; FungiDB:HpaG812049; -.
DR eggNOG; KOG0745; Eukaryota.
DR HOGENOM; CLU_014218_6_0_1; -.
DR InParanoid; M4BZM6; -.
DR OMA; LIRGDMT; -.
DR Proteomes; UP000011713; 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:UP000011713}.
FT DOMAIN 368..519
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 575..669
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 172..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 694 AA; 75064 MW; 3B4945181C52BC38 CRC64;
MLCRLRPNNP LLTSVYHLQL TTRMLTTTSC RAFPLLYGNP NHSQRLPKHC RMPSGVWYIT
TVTPTSDDHP KKAATGGDRL CCPQCSVPLV LAEPLSADKL TSSNLKRNMT LNTSTSTSTL
PEFKKGDVVK CVSCKLYFAL KVQPLTHPNP TFRNAAAAAA LSSLSSSLSA GMSTTRGSTA
GGPSCSSNFL SPTRPSPMNA DGEYAKLATD GAVARAARDA SARKDRVLTP REIYDGLNEY
VVGQSKVKKT LAVGVYNHYK RLQALDLLQA RREADVSCAK SNEQHVGVGA TGATGQQGNA
NDARRSILGR RLLLEEIYPT PAAEYCKEFE GTTQQTLNDS SGSNLAAAHA PDAAVQDKLQ
SLEGVELEKT NIMLVGPTGS GKTLLAKTLA RLAKVPIVIA DATCLTQAGY VGEDVESVLF
KLYQAANYNL EATQRGIVYI DEIDKITRKS ENVSIARDVS GEGVQQALLK LLEGSMMNVP
EKGGRKNPRG EYITIDTTNI LFICGGAFAG LEKQVTSRTA QSSIGFGATM PNMRLKDSDQ
IGQLLSHAEP EDLVSYGLIP EFIGRFPLLV STTGLSKDEL VRVLTEPKNS LVRQYKALFA
LNDVGFHATE GALEAVAQLA LHKNTGARGL RSIFERALME TMFDLPDKND VHAVYVDEEA
ILGHKQPVLI RGAMTLDGYL KNLEDDNDKR EEAV
//
