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Database: UniProt
Entry: T0R4U0_SAPDV
LinkDB: T0R4U0_SAPDV
Original site: T0R4U0_SAPDV 
ID   T0R4U0_SAPDV            Unreviewed;       608 AA.
AC   T0R4U0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000313|EMBL:EQC27108.1};
GN   ORFNames=SDRG_15116 {ECO:0000313|EMBL:EQC27108.1};
OS   Saprolegnia diclina (strain VS20).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Saprolegnia.
OX   NCBI_TaxID=1156394 {ECO:0000313|EMBL:EQC27108.1, ECO:0000313|Proteomes:UP000030762};
RN   [1] {ECO:0000313|EMBL:EQC27108.1, ECO:0000313|Proteomes:UP000030762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VS20 {ECO:0000313|EMBL:EQC27108.1,
RC   ECO:0000313|Proteomes:UP000030762};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Nusbaum C., Tyler B., van West P., Dieguez-Uribeondo J.,
RA   de Bruijn I., Tripathy S., Jiang R., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Saprolegnia declina VS20.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; JH767215; EQC27108.1; -; Genomic_DNA.
DR   RefSeq; XP_008619502.1; XM_008621280.1.
DR   AlphaFoldDB; T0R4U0; -.
DR   STRING; 1156394.T0R4U0; -.
DR   EnsemblProtists; EQC27108; EQC27108; SDRG_15116.
DR   GeneID; 19955843; -.
DR   VEuPathDB; FungiDB:SDRG_15116; -.
DR   eggNOG; KOG0745; Eukaryota.
DR   InParanoid; T0R4U0; -.
DR   OMA; ICDCNSL; -.
DR   OrthoDB; 452393at2759; -.
DR   Proteomes; UP000030762; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   ATP-binding {ECO:0000313|EMBL:EQC27108.1};
KW   Hydrolase {ECO:0000313|EMBL:EQC27108.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:EQC27108.1};
KW   Protease {ECO:0000313|EMBL:EQC27108.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030762}.
FT   DOMAIN          281..438
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          488..575
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
SQ   SEQUENCE   608 AA;  66079 MW;  190EFA2B22286023 CRC64;
     MVLPRLGRYL RAMPRVAARH SRLTTAARYC SMYPRAPMMA TLPRLTPPTV RCFGTETRDA
     SELTCPHCGE SLKLAIAVPR STPTCGASAA PATTLPLTSR QLEPGDIVGC EGCKTYFAVK
     SLAADPPHAG SMFQTPSSQF QSTPRLRISN DSDFDRLLND SQRVNTPPAP APKVLTPREI
     YDGLNKYVIG QENVKKALAV GVHNHYKRLS MNFKPPEVPI DDGHPRSMRV SAMVDEPAIY
     QSVKHGIQLE AIAVPPSVVA AEGATPPTTP TVAVDDSVEI DKTNILVVGP TGSGKTLMAK
     TLARLAQVPL VIADATCLTQ AGYVGEDVES ILYKLYQAAN FDLEAAQKGI IYIDEIDKIS
     RKSENVSITR DVSGEGVQQA LLKMLEGCTV NVPEKGGRKN PRGEFIAIDT TNILFICGGA
     FAGLEHIVSR RTATASIGFE SQMKDTKVTD LDRVGELLTQ SEPQDLVAYG LIPEFVGRFP
     VLVSTLGLNR HELVRVVSEP KNSLIKQYRA LFALHNVDFH VTPCGLDAIA ELAVRRNTGA
     RGLRAIFERT LMDTMFHVPD MQHVRAVYVD GDVIFGAKQP VLLRGDVTIA EYEAAKDETH
     EVAYPDAA
//
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