ID   TCPD_OCHTR              Reviewed;         533 AA.
AC   Q9NB32;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=T-complex protein 1 subunit delta;
DE            Short=TCP-1-delta;
DE   AltName: Full=CCT-delta;
OS   Ochlerotatus triseriatus (Eastern treehole mosquito) (Aedes triseriatus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Ochlerotatus; Protomacleaya.
OX   NCBI_TaxID=7162;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11762197; DOI=10.3109/10425170109080776;
RA   Blitvich B.J., Rayms-Keller A., Blair C.D., Beaty B.J.;
RT   "Complete cDNA and deduced amino acid sequence of the chaperonin containing
RT   T-complex polypeptide 1 (CCT) delta subunit from Aedes triseriatus
RT   mosquitoes.";
RL   DNA Seq. 12:203-208(2001).
CC   -!- FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP
CC       hydrolysis. Known to play a role, in vitro, in the folding of actin and
CC       tubulin (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms
CC       two stacked rings, 12 to 16 nm in diameter. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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; AF271209; AAF87577.1; -; mRNA.
DR   AlphaFoldDB; Q9NB32; -.
DR   SMR; Q9NB32; -.
DR   BRENDA; 5.6.1.7; 7612.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0051082; F:unfolded protein binding; IEA:InterPro.
DR   CDD; cd03338; TCP1_delta; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012717; Chap_CCT_delta.
DR   InterPro; IPR017998; Chaperone_TCP-1.
DR   InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR   InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR   InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR   InterPro; IPR027413; GROEL-like_equatorial_sf.
DR   InterPro; IPR027410; TCP-1-like_intermed_sf.
DR   PANTHER; PTHR11353; PTHR11353; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00304; TCOMPLEXTCP1.
DR   SUPFAM; SSF48592; SSF48592; 1.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   SUPFAM; SSF54849; SSF54849; 1.
DR   TIGRFAMs; TIGR02342; chap_CCT_delta; 1.
DR   PROSITE; PS00750; TCP1_1; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
DR   PROSITE; PS00995; TCP1_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding.
FT   CHAIN           1..533
FT                   /note="T-complex protein 1 subunit delta"
FT                   /id="PRO_0000128338"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   533 AA;  57180 MW;  9A6253E987786F15 CRC64;
     MVVKPAARGM KPQGQAYKDK SKPADIRQSN INAAKAVSDA IRTSLGPRGM DKMIQAANGE
     VTITNDGATI LKQMNVIHPA AKMLVELSRA QDVEAGDGTT SVVVVAGALL KAVEKLLQMG
     IHPTAISDAF QKCSAKAVDI LTEMSTPIEL TDRESLVKSA STSLNSKVVS QHSSQLAPIA
     VEAVLKVTEA GHESGVDLKN VKIIRSLGGT IDDTELVDGL VFTQRSCGVN GPKRVEKAKI
     GLIQFCISAP KTDMDHSVIV SDYAAMDRVL KEERAYILNI VKQIKKAGCN VLLVQKSILR
     DAVSDLAMHF LDKIKVMVVK DIEHEDIEFV CKTLNCRPIA SLDHFLPEHL VNADLVEEVS
     SGSSKFVKVT GIQNMGQTVS IVVRGSNKLV LEEAERSLHD ALCVVRCLVK KRAQIAGGGA
     PEIEMAIQLA AHAQTLEGVD AYCFRAFANA LEVIPSTLAE NAGLNPIATV TELRNRHAQG
     EKNAGINVRK GAITDILAEN VVQPLLVSTS SITLASETVR SILKIDDIIN TMQ