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Protein

Probable T-complex protein 1 subunit theta

Gene

cct8

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-SPO-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable T-complex protein 1 subunit theta
Short name:
TCP-1-theta
Alternative name(s):
CCT-theta
Gene namesi
Name:cct8
ORF Names:SPBC337.05c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC337.05c.
PomBaseiSPBC337.05c. cct8.

Subcellular locationi

GO - Cellular componenti

  • chaperonin-containing T-complex Source: PomBase
  • cytoplasm Source: PomBase
  • cytoskeleton Source: PomBase
  • cytosol Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 546546Probable T-complex protein 1 subunit thetaPRO_0000128377Add
BLAST

Proteomic databases

MaxQBiP78921.

Interactioni

Subunit structurei

Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi276835. 5 interactions.
IntActiP78921. 1 interaction.
MINTiMINT-4691560.

Structurei

3D structure databases

ProteinModelPortaliP78921.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

HOGENOMiHOG000226734.
InParanoidiP78921.
KOiK09500.
OMAiSKSWAIK.
OrthoDBiEOG092C2629.
PhylomeDBiP78921.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012721. Chap_CCT_theta.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02346. chap_CCT_theta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P78921-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRVPKASG PQLFREGYRI MQGVEDAVIR NCNAIRELSE ITRTSLGPNG
60 70 80 90 100
KNKIVVNHLQ QTFLTNDAAT IIRELEVIHP AAKLVVDATQ QQENELGDAA
110 120 130 140 150
NFVVVFTGEL LAKAENMIRM GLTPLEIAKG YEMALSHTME VLEEICADKI
160 170 180 190 200
ETVESEKELI KAIRTCISSK QYGNEDFLSD LVAKAILTVL PKDPSKFNVD
210 220 230 240 250
NIRVVKIMGS SLYNSQVVKG MVFPREPEGT VTRSKEAKVA VFSCPLDISQ
260 270 280 290 300
TETKGTVLLH NAQEMLDFSK GEENLIESHI KEIYDAGVRV VVTSGNVNDL
310 320 330 340 350
VLHYLNRFEI LVIRVPSKFE LRRLCRVVGA TPLARMGVPM PEEMGSVDVV
360 370 380 390 400
ETIEIGGDRV TVFRQVEDIT RTATIVLRGA TKTYLDDLER AIDDGVNIVK
410 420 430 440 450
ALVKDNRLIF GAGASDMQLC IRLISVGEKT PGIYQHAIKQ YGEAFEVVPR
460 470 480 490 500
TISENAGLDP TDVISKLYAA HHKENGESIG VDVECENDGT LDAKEAGIFD
510 520 530 540
VLLAKKSAIR LATETVLTVL NVDQVVMSKP AGGPKPPGPN PHWDDD
Length:546
Mass (Da):59,956
Last modified:December 1, 2000 - v3
Checksum:i61EEBF8CE3A4ACEE
GO

Sequence cautioni

The sequence BAA13933 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041V → I in BAA13933 (PubMed:9501991).Curated
Sequence conflicti107 – 1126TGELLA → SGALLL in BAA13933 (PubMed:9501991).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89272 mRNA. Translation: BAA13933.1. Different initiation.
CU329671 Genomic DNA. Translation: CAA21275.1.
PIRiT40258.
T43202.
RefSeqiNP_595406.1. NM_001021313.2.

Genome annotation databases

EnsemblFungiiSPBC337.05c.1; SPBC337.05c.1:pep; SPBC337.05c.
GeneIDi2540305.
KEGGispo:SPBC337.05c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89272 mRNA. Translation: BAA13933.1. Different initiation.
CU329671 Genomic DNA. Translation: CAA21275.1.
PIRiT40258.
T43202.
RefSeqiNP_595406.1. NM_001021313.2.

3D structure databases

ProteinModelPortaliP78921.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276835. 5 interactions.
IntActiP78921. 1 interaction.
MINTiMINT-4691560.

Proteomic databases

MaxQBiP78921.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC337.05c.1; SPBC337.05c.1:pep; SPBC337.05c.
GeneIDi2540305.
KEGGispo:SPBC337.05c.

Organism-specific databases

EuPathDBiFungiDB:SPBC337.05c.
PomBaseiSPBC337.05c. cct8.

Phylogenomic databases

HOGENOMiHOG000226734.
InParanoidiP78921.
KOiK09500.
OMAiSKSWAIK.
OrthoDBiEOG092C2629.
PhylomeDBiP78921.

Enzyme and pathway databases

ReactomeiR-SPO-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-SPO-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Miscellaneous databases

PROiP78921.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012721. Chap_CCT_theta.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02346. chap_CCT_theta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTCPQ_SCHPO
AccessioniPrimary (citable) accession number: P78921
Secondary accession number(s): O74816
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 1, 2000
Last modified: September 7, 2016
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.