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Database: UniProt
Entry: A0A0W8CWU3_PHYNI
LinkDB: A0A0W8CWU3_PHYNI
Original site: A0A0W8CWU3_PHYNI 
ID   A0A0W8CWU3_PHYNI        Unreviewed;       513 AA.
AC   A0A0W8CWU3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   13-SEP-2023, entry version 33.
DE   SubName: Full=ATP-dependent hsl protease ATP-binding subunit hslU {ECO:0000313|EMBL:KUF88586.1};
DE   SubName: Full=Bzip transcription factor {ECO:0000313|EMBL:KUF99517.1};
GN   ORFNames=AM587_10013578 {ECO:0000313|EMBL:KUF66786.1}, AM587_10016022
GN   {ECO:0000313|EMBL:KUF88586.1}, AM588_10009965
GN   {ECO:0000313|EMBL:KUF99517.1};
OS   Phytophthora nicotianae (Buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF88586.1, ECO:0000313|Proteomes:UP000052943};
RN   [1] {ECO:0000313|Proteomes:UP000052943, ECO:0000313|Proteomes:UP000054636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943}, Race 0
RC   {ECO:0000313|EMBL:KUF88586.1}, race 1
RC   {ECO:0000313|Proteomes:UP000054636}, and Race 1
RC   {ECO:0000313|EMBL:KUF99517.1};
RA   Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT   "Genomes and virulence difference between two physiological races of
RT   Phytophthora nicotianae.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC       {ECO:0000256|ARBA:ARBA00009771}.
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:KUF88586.1}.
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DR   EMBL; LNFO01006083; KUF66786.1; -; Genomic_DNA.
DR   EMBL; LNFO01001815; KUF88586.1; -; Genomic_DNA.
DR   EMBL; LNFP01000024; KUF99517.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W8CWU3; -.
DR   STRING; 4790.A0A0W8CWU3; -.
DR   EnsemblProtists; KUF66786; KUF66786; AM587_10013578.
DR   EnsemblProtists; KUF88586; KUF88586; AM587_10016022.
DR   EnsemblProtists; KUF99517; KUF99517; AM588_10009965.
DR   OrthoDB; 452393at2759; -.
DR   Proteomes; UP000052943; Unassembled WGS sequence.
DR   Proteomes; UP000054636; Unassembled WGS sequence.
DR   GO; GO:0009376; C:HslUV protease complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004491; HslU.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00390; hslU; 1.
DR   PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR48102:SF3; ATP-DEPENDENT PROTEASE ATPASE SUBUNIT HSLU; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF13401; AAA_22; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000313|EMBL:KUF88586.1};
KW   Hydrolase {ECO:0000313|EMBL:KUF88586.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:KUF88586.1};
KW   Protease {ECO:0000313|EMBL:KUF88586.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052943}.
FT   DOMAIN          127..405
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          404..496
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   513 AA;  57472 MW;  6D2842B52AA36688 CRC64;
     MRRAVHSQAF KSLTRRAQQV TAPRAASYSQ IQSRALFQSP QTLRTFSTAA PKASEEDASV
     PVQVVEEAAA EEEDEDDIGR HLKPREVVEQ LNKYIVGQAD AKRAVAIALR NRWRRQKISD
     ELRQEVSPKN ILMIGPTGCG KTEIARRLAK LSEAPFVKVE ATKFTEVGFH GRDVDQIIRD
     LVENAINMVK KHRKERLRKQ VQHLVESRIL DVLTGANVAE RSRATFERLL RTGELEDRII
     EFDVPVSKNP GGQPISFVGG EGKGISMEVF GRAFGEKKTE RKRMTIAESR EVFEEMEMEN
     AIDMTDVVRE AIQETEENGI VFIDEIDKIC SSGDYRRSSD PSSEGVQRDL LPLIEGSVIS
     TKHGNVNTDH ILFVGSGAFH SSKPSDLLAE LQGRLPIRVE LKGLTEEDLH RILTEPVTNL
     IKQQTELIQT EGVTLNFTDD AVREIARVAA EVNKTVENIG ARRLHTVVEK VVEEISFDSS
     EMAPGSTVTI TKEFVLERVG KLMKKTDLSK FIL
//
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