Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

T-complex protein 1 subunit alpha

Gene

cct1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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.

Names & Taxonomyi

Protein namesi
Recommended name:
T-complex protein 1 subunit alpha
Short name:
TCP-1-alpha
Alternative name(s):
CCT-alpha
Gene namesi
Name:cct1
ORF Names:SPBC12D12.03
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC12D12.03.
PomBaseiSPBC12D12.03. cct1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 556556T-complex protein 1 subunit alphaPRO_0000128314Add
BLAST

Proteomic databases

MaxQBiO94501.
PRIDEiO94501.

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

BioGridi276245. 3 interactions.
IntActiO94501. 1 interaction.
MINTiMINT-4684710.

Structurei

3D structure databases

ProteinModelPortaliO94501.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

HOGENOMiHOG000226729.
InParanoidiO94501.
KOiK09493.
OMAiHYLAQEG.
OrthoDBiEOG773XR5.
PhylomeDBiO94501.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012715. Chap_CCT_alpha.
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.
TIGRFAMsiTIGR02340. chap_CCT_alpha. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O94501-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFQAPRESTL FLSGEKISGE DVRNQNVLAT TAIANVVKSS LGPVGLDKML
60 70 80 90 100
VDDIGDVTVT NDGATILSLL DVEHPAGKVL VELAQQQDKE VGDGTTSVVI
110 120 130 140 150
IAAELLRRAN ELVKNKIHPT TIITGYRLAI REAVKFMTDV LSCSVDSLGK
160 170 180 190 200
ESLINVAKTS MSSKIIGNDS DFFSTMAVDA MLSVKTSNSK GETRYPVKAV
210 220 230 240 250
NILKAHGKSS RESVLVKGYA LNCTIASQAM KTRVQNAKIA VLDMDLQKTK
260 270 280 290 300
MALGVHVTID DPDQLEKIRE REVMITLERV KKILNAGANV ILTTKGIDDL
310 320 330 340 350
CLKSIIEAGA MAVRRCKKED LRRIAKASGA TLLSSLSNLE GEETFESSYL
360 370 380 390 400
GSAEEVVQEK FSDDECILVK GTKAYSSASI VLRGPNEYSL DEMERSMHDS
410 420 430 440 450
LSVVKRTLES GKVVPGGGAV ETALSIYLEN FATSLGSREQ LAIAEFAQAL
460 470 480 490 500
LIIPRTLAVN AAKDSTELTA KLRAYHAASQ NAEVTDVKKR GYKNYGLDLL
510 520 530 540 550
NGVIRDNVKA GVLEPSMSKL KSLKSAVEAC IAILRIDTSI KLDPERQPED

PHAGLH
Length:556
Mass (Da):60,047
Last modified:May 1, 1999 - v1
Checksum:i34DE8D22AA56D812
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA22677.1.
PIRiT39383.
RefSeqiNP_595949.1. NM_001021858.2.

Genome annotation databases

EnsemblFungiiSPBC12D12.03.1; SPBC12D12.03.1:pep; SPBC12D12.03.
GeneIDi2539691.
KEGGispo:SPBC12D12.03.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA22677.1.
PIRiT39383.
RefSeqiNP_595949.1. NM_001021858.2.

3D structure databases

ProteinModelPortaliO94501.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276245. 3 interactions.
IntActiO94501. 1 interaction.
MINTiMINT-4684710.

Proteomic databases

MaxQBiO94501.
PRIDEiO94501.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC12D12.03.1; SPBC12D12.03.1:pep; SPBC12D12.03.
GeneIDi2539691.
KEGGispo:SPBC12D12.03.

Organism-specific databases

EuPathDBiFungiDB:SPBC12D12.03.
PomBaseiSPBC12D12.03. cct1.

Phylogenomic databases

HOGENOMiHOG000226729.
InParanoidiO94501.
KOiK09493.
OMAiHYLAQEG.
OrthoDBiEOG773XR5.
PhylomeDBiO94501.

Enzyme and pathway databases

ReactomeiR-SPO-390471. Association of TriC/CCT with target proteins during biosynthesis.

Miscellaneous databases

NextBioi20800844.
PROiO94501.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012715. Chap_CCT_alpha.
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.
TIGRFAMsiTIGR02340. chap_CCT_alpha. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiTCPA_SCHPO
AccessioniPrimary (citable) accession number: O94501
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: December 9, 2015
This is version 117 of the entry and version 1 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.