ID Q0PW51_TOXGO Unreviewed; 226 AA.
AC Q0PW51; B6KV20; S8FEM2;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 22-FEB-2023, entry version 73.
DE SubName: Full=p23 co-chaperone {ECO:0000313|EMBL:ABG75605.1};
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811 {ECO:0000313|EMBL:ABG75605.1};
RN [1] {ECO:0000313|EMBL:ABG75605.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20403389; DOI=10.1016/j.molbiopara.2010.04.004;
RA Echeverria P.C., Figueras M.J., Vogler M., Kriehuber T., de Miguel N.,
RA Deng B., Dalmasso M.C., Matthews D.E., Matrajt M., Haslbeck M., Buchner J.,
RA Angel S.O.;
RT "The Hsp90 co-chaperone p23 of Toxoplasma gondii: Identification,
RT functional analysis and dynamic interactome determination.";
RL Mol. Biochem. Parasitol. 172:129-140(2010).
CC -!- SIMILARITY: Belongs to the p23/wos2 family.
CC {ECO:0000256|ARBA:ARBA00025733}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ680014; ABG75605.1; -; mRNA.
DR AlphaFoldDB; Q0PW51; -.
DR VEuPathDB; ToxoDB:TGARI_321520; -.
DR VEuPathDB; ToxoDB:TGCAST_321520; -.
DR VEuPathDB; ToxoDB:TGCOUG_321520; -.
DR VEuPathDB; ToxoDB:TGDOM2_321520; -.
DR VEuPathDB; ToxoDB:TGFOU_321520; -.
DR VEuPathDB; ToxoDB:TGGT1_321520; -.
DR VEuPathDB; ToxoDB:TGMAS_321520; -.
DR VEuPathDB; ToxoDB:TGME49_321520; -.
DR VEuPathDB; ToxoDB:TGP89_321520; -.
DR VEuPathDB; ToxoDB:TGPRC2_321520; -.
DR VEuPathDB; ToxoDB:TGRH88_020930; -.
DR VEuPathDB; ToxoDB:TGRUB_321520; -.
DR VEuPathDB; ToxoDB:TGVAND_321520; -.
DR VEuPathDB; ToxoDB:TGVEG_321520; -.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:InterPro.
DR CDD; cd06465; p23_hB-ind1_like; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR045250; p23-like.
DR PANTHER; PTHR22932:SF1; CO-CHAPERONE PROTEIN DAF-41; 1.
DR PANTHER; PTHR22932; TELOMERASE-BINDING PROTEIN P23 HSP90 CO-CHAPERONE; 1.
DR Pfam; PF04969; CS; 1.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR PROSITE; PS51203; CS; 1.
PE 2: Evidence at transcript level;
FT DOMAIN 6..91
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT REGION 159..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..180
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 226 AA; 24783 MW; 95CBD19CB97E3F89 CRC64;
MADAQVHSPQ CAWAETKEFI FLTVQVQSPE DLQVNLQESS LDFKCTSDKK AFAFHLDFPH
PIIVEDSKYS VQRNVQFKLV KKEKERWRTL SGKTKLHWLK CDWDKWIDSD DEDAKGMDMG
DFDMNSMDFG GMGGLGGMGG LGGMGGMGGL GGMGGMGDMD FGDMGDMDSD DEDDLHDLDD
SMQKEDEHEH EGGCCGGHGK ECEGEKAEEH KVNGVEGTTP AEAAQA
//
