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Protein

T-complex protein 1 subunit gamma

Gene

cct3

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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.

Names & Taxonomyi

Protein namesi
Recommended name:
T-complex protein 1 subunit gamma
Short name:
TCP-1-gamma
Alternative name(s):
CCT-gamma
Gene namesi
Name:cct3
ORF Names:SPBC1A4.08c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC1A4.08c.
PomBaseiSPBC1A4.08c. cct3.

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 – 528528T-complex protein 1 subunit gammaPRO_0000128330Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei250 – 2501Phosphoserine1 Publication
Disulfide bondi364 ↔ 370By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiO74341.
PRIDEiO74341.

PTM databases

iPTMnetiO74341.

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi277094. 4 interactions.
IntActiO74341. 1 interaction.
MINTiMINT-4678339.

Structurei

3D structure databases

ProteinModelPortaliO74341.
SMRiO74341. Positions 210-376.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

HOGENOMiHOG000226732.
InParanoidiO74341.
KOiK09495.
OMAiTQCGLFE.
OrthoDBiEOG773XR5.
PhylomeDBiO74341.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012719. Chap_CCT_gamma.
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]
PANTHERiPTHR11353:SF63. PTHR11353:SF63. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02344. chap_CCT_gamma. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O74341-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSPVFVMNT NGNRQVGHKA QMSNIQAAKA VADVIRTCLG PRAMLKMLLD
60 70 80 90 100
PVGSVLLTND GHAILREIEV AHPAAKSMIE LARTQDEEVG DGTTSVIILA
110 120 130 140 150
GEILAAASPL LDRKIHPVVM IRSFKQALED ALSIIDEITL PVNVDDNAEM
160 170 180 190 200
FRLIRTCIGT KLVARWSDLM CHLALRAVRT VASTSNGRME IDIKRYARVE
210 220 230 240 250
KVPGGEIESS CVLDGVMLNK DVTHPKMRRR IENPRIVLLD CPLEYRKGES
260 270 280 290 300
QTNIEISKDT DWNRILEIEE EQVKRMCDYI IAVKPDLVIT EKGVSDLAQH
310 320 330 340 350
YLLKANITAL RRTRKSDNNR IARACGANIV NRLEDLREKD VGTGCGLFYI
360 370 380 390 400
DKLGDEYYTF LTGCKNPKAC TILLRGPSKD IINEVERNLQ DAMAVARNVF
410 420 430 440 450
FHPKLSPGGG ATEMAVSVRL AEKARSIEGV AQWPYRAVAD AIEIIPRTLV
460 470 480 490 500
QNCGANPIKA LTELRAKHAE GQHSFGIDGE TGRVVDMHEY GVWEPEAVKL
510 520
QSIKTAIESA CLLLRVDDIV SGVRKHSE
Length:528
Mass (Da):58,481
Last modified:November 1, 1998 - v1
Checksum:i260BC1A6DA295E8E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA20112.1.
PIRiT39856.
RefSeqiNP_595810.1. NM_001021713.2.

Genome annotation databases

EnsemblFungiiSPBC1A4.08c.1; SPBC1A4.08c.1:pep; SPBC1A4.08c.
GeneIDi2540567.
KEGGispo:SPBC1A4.08c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA20112.1.
PIRiT39856.
RefSeqiNP_595810.1. NM_001021713.2.

3D structure databases

ProteinModelPortaliO74341.
SMRiO74341. Positions 210-376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277094. 4 interactions.
IntActiO74341. 1 interaction.
MINTiMINT-4678339.

PTM databases

iPTMnetiO74341.

Proteomic databases

MaxQBiO74341.
PRIDEiO74341.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC1A4.08c.1; SPBC1A4.08c.1:pep; SPBC1A4.08c.
GeneIDi2540567.
KEGGispo:SPBC1A4.08c.

Organism-specific databases

EuPathDBiFungiDB:SPBC1A4.08c.
PomBaseiSPBC1A4.08c. cct3.

Phylogenomic databases

HOGENOMiHOG000226732.
InParanoidiO74341.
KOiK09495.
OMAiTQCGLFE.
OrthoDBiEOG773XR5.
PhylomeDBiO74341.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi20801693.
PROiO74341.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012719. Chap_CCT_gamma.
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]
PANTHERiPTHR11353:SF63. PTHR11353:SF63. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02344. chap_CCT_gamma. 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.
  2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiTCPG_SCHPO
AccessioniPrimary (citable) accession number: O74341
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1998
Last modified: April 13, 2016
This is version 122 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.