ID F0VBZ4_NEOCL Unreviewed; 527 AA.
AC F0VBZ4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Putative ATP-dependent heat shock protein {ECO:0000313|EMBL:CBZ51128.1};
GN ORFNames=NCLIV_042030 {ECO:0000313|EMBL:CBZ51128.1};
OS Neospora caninum (strain Liverpool).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ51128.1, ECO:0000313|Proteomes:UP000007494};
RN [1] {ECO:0000313|Proteomes:UP000007494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|Proteomes:UP000007494};
RX PubMed=22457617; DOI=10.1371/journal.ppat.1002567;
RA Reid A.J., Vermont S.J., Cotton J.A., Harris D., Hill-Cawthorne G.A.,
RA Konen-Waisman S., Latham S.M., Mourier T., Norton R., Quail M.A.,
RA Sanders M., Shanmugam D., Sohal A., Wasmuth J.D., Brunk B., Grigg M.E.,
RA Howard J.C., Parkinson J., Roos D.S., Trees A.J., Berriman M., Pain A.,
RA Wastling J.M.;
RT "Comparative genomics of the apicomplexan parasites Toxoplasma gondii and
RT Neospora caninum: Coccidia differing in host range and transmission
RT strategy.";
RL PLoS Pathog. 8:e1002567-e1002567(2012).
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC {ECO:0000256|ARBA:ARBA00009771}.
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DR EMBL; FR823385; CBZ51128.1; -; Genomic_DNA.
DR RefSeq; XP_003881161.1; XM_003881112.1.
DR AlphaFoldDB; F0VBZ4; -.
DR GeneID; 13440114; -.
DR VEuPathDB; ToxoDB:NCLIV_042030; -.
DR eggNOG; KOG0745; Eukaryota.
DR InParanoid; F0VBZ4; -.
DR OrthoDB; 452393at2759; -.
DR Proteomes; UP000007494; Chromosome IX.
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:InterPro.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000007494};
KW Stress response {ECO:0000313|EMBL:CBZ51128.1}.
FT DOMAIN 125..415
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 418..513
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 44..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 527 AA; 58171 MW; C31ACDD79336F702 CRC64;
MERGRSRLLS AYPFSCSVPT PSFASSLPSF VPASASSPRF YASSAPPGSF AAPPPRPSSA
RASSAAAQTA SLDAAAKALC PQEMVEYLNK YIIGQAEAKR AVAVALRQRW RRRHIEDERL
REDITPKNIL LIGPTGVGKT EVARRLAKRI DAPFIKVEAT KFTEVGFHGR DVDQIIKDLV
EVAVKTQRTK LQEAMRPAAE HRAETKILEA LLGKMPAEEH QQWLRHLRCG ALDSRRVHVD
FPARPNVGAA SGGPAFDDGG RDSIVADLES IIRDIDRPRP AFFATRRGPR GSEARNLTVK
EAREKLMQAE LDAMITKDLV VQKALEAVEQ EGIVFIDEID KICSKGGRSG YNPDASDEGV
QRDLLPLIEG TTVSTRYGDV KTDYILFIAS GAFHCVRPSE LLAELQGRLP IRVTLTSLTE
SDLRDILTKT QNNLIEQNTA LLRTENVELH FTEEAVNEIA RVACEVNASV ENIGARRLHT
IIEKIMEDIN YAAPSMAPGT RVEIDLERVR SSVSSLLTKM DYTRFVL
//