ID W2YSL2_PHYPR Unreviewed; 483 AA.
AC W2YSL2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=ATP-dependent protease HslVU, ATPase subunit {ECO:0000313|EMBL:ETP37792.1};
GN ORFNames=F442_14388 {ECO:0000313|EMBL:ETP37792.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP37792.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP37792.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP37792.1,
RC ECO:0000313|Proteomes:UP000018948};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P10297.";
RL Submitted (NOV-2013) 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:ETP37792.1}.
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DR EMBL; ANIY01002995; ETP37792.1; -; Genomic_DNA.
DR AlphaFoldDB; W2YSL2; -.
DR EnsemblProtists; ETP37792; ETP37792; F442_14388.
DR Proteomes; UP000018948; Unassembled WGS sequence.
DR GO; GO:0009376; C:HslUV protease complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 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 Hydrolase {ECO:0000313|EMBL:ETP37792.1};
KW Protease {ECO:0000313|EMBL:ETP37792.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018948}.
FT DOMAIN 80..372
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 375..469
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 483 AA; 53352 MW; FCE6377CD1074E57 CRC64;
MMLRRCVGLR RFSSIATDLP LAPVGAIPRG DADRIPEDVV RALDKFIVGQ QDAKKAVAVA
LRSRWRRRQL QNDALRAEIS PMNILMSGPT GSGKTEIARR LAKISGSPFL KVEATKFTEV
GIYGANADSM IKDLVDVAVN MERAEAQKFH AAAARERAID RLVDLLDRKK LSDISRAELR
EEIATGKADN RKVRVQLKPL ASKTRPSSAN PEMMMEMPPE LAKMMSHLDT LMASRFSGGR
KKSEDNTTSM TVKEALPRLE AEEADEIIDD DEVVKRALEN VQHNGIVFLD EIDKLANAGD
QARSGGSGAN YRKGEGVQKE LLALTEGCAV NTRYGLVYTD HILFIASGAF HRSKPSDLMP
ELQGRLPIRV ALSPLGAAEF EKILKETDHN LLEQTSALME TEGVKLTFTD DAISEIATIA
EQVNAQTDNI GARRLATIIS KITEEVSFHA PKMNGMTFEV DKKYVQQRLS NVLDRTDLSK
FIL
//