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Protein

T-complex protein 1 subunit delta

Gene

cct4

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.

Names & Taxonomyi

Protein namesi
Recommended name:
T-complex protein 1 subunit delta
Short name:
TCP-1-delta
Alternative name(s):
CCT-delta
Gene namesi
Name:cct4
ORF Names:SPBC106.06
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC106.06.
PomBaseiSPBC106.06. cct4.

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 – 527527T-complex protein 1 subunit deltaPRO_0000128343Add
BLAST

Proteomic databases

MaxQBiP50999.
PRIDEiP50999.

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

BioGridi276591. 8 interactions.
IntActiP50999. 2 interactions.
MINTiMINT-4690820.

Structurei

3D structure databases

ProteinModelPortaliP50999.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

HOGENOMiHOG000226735.
InParanoidiP50999.
KOiK09496.
OMAiAYCVRAY.
OrthoDBiEOG773XR5.
PhylomeDBiP50999.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012717. Chap_CCT_delta.
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.
TIGRFAMsiTIGR02342. chap_CCT_delta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P50999-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKAATVPVA FQDREKPQEV RLSNIMAARS VADAIRTSLG PKGMDKMIQT
60 70 80 90 100
GKGEVILTND GATILKHLSV LHPAAKMLVD LSAAQDVEAG DGTTSVVILA
110 120 130 140 150
GSMLACAEKL LKKGIHPTVI AESFQRAAGF TVDCMKENAL AIELSDRESL
160 170 180 190 200
LRAATTSLNS KIVSQYSNLL APIAVDAVLK VIDPRVATNV DLKDIRIVKK
210 220 230 240 250
LGGIIDDTEL IPGLALTQTA VKSAGGPTRI EKANIALIQF QLSPPKPDME
260 270 280 290 300
NQVVVNDYRQ MDKILKEERQ YLLNMCKKIK KAGANVILIQ KSILRDAVND
310 320 330 340 350
LALHFLAKLK IMVIKDIERD EVEFICKSTG CKPIADIESF AEDKLGHADL
360 370 380 390 400
VEETSSSGEK IVKFSGVKNA GKTVSILCRG ANLLTLEEAE RSLHDALCVI
410 420 430 440 450
RCLVKQRALI AGGGSPEIEA AQRLLEHARQ LEGREAICIR AFSEALEIIP
460 470 480 490 500
VTLAENAGLN AIQVVTELRS RHANGEKTAG INVRKGIVTN ILEENVLQPL
510 520
LVNISAIQLA AETTKMIMKI DDITLAR
Length:527
Mass (Da):56,968
Last modified:December 1, 2000 - v2
Checksum:iACB5D86F9A83C02E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 781L → R in AAC05213 (Ref. 1) Curated
Sequence conflicti226 – 2261Missing in AAC05213 (Ref. 1) Curated
Sequence conflicti316 – 3161D → EV in AAC05213 (Ref. 1) Curated
Sequence conflicti440 – 4401R → G in AAC05213 (Ref. 1) Curated
Sequence conflicti463 – 4642QV → RI in AAC05213 (Ref. 1) Curated
Sequence conflicti470 – 48112SRHAN…KTAGI → KSYLREDCGY in AAC05213 (Ref. 1) CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF050465 mRNA. Translation: AAC05213.1.
CU329671 Genomic DNA. Translation: CAB53722.1.
X91498 Genomic DNA. Translation: CAA62798.1.
PIRiT39263.
T43649.
RefSeqiNP_595155.1. NM_001021064.2.

Genome annotation databases

EnsemblFungiiSPBC106.06.1; SPBC106.06.1:pep; SPBC106.06.
GeneIDi2540053.
KEGGispo:SPBC106.06.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF050465 mRNA. Translation: AAC05213.1.
CU329671 Genomic DNA. Translation: CAB53722.1.
X91498 Genomic DNA. Translation: CAA62798.1.
PIRiT39263.
T43649.
RefSeqiNP_595155.1. NM_001021064.2.

3D structure databases

ProteinModelPortaliP50999.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276591. 8 interactions.
IntActiP50999. 2 interactions.
MINTiMINT-4690820.

Proteomic databases

MaxQBiP50999.
PRIDEiP50999.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC106.06.1; SPBC106.06.1:pep; SPBC106.06.
GeneIDi2540053.
KEGGispo:SPBC106.06.

Organism-specific databases

EuPathDBiFungiDB:SPBC106.06.
PomBaseiSPBC106.06. cct4.

Phylogenomic databases

HOGENOMiHOG000226735.
InParanoidiP50999.
KOiK09496.
OMAiAYCVRAY.
OrthoDBiEOG773XR5.
PhylomeDBiP50999.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi20801190.
PROiP50999.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012717. Chap_CCT_delta.
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.
TIGRFAMsiTIGR02342. chap_CCT_delta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Mueller U.W., Sazer S.
    Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 972 / ATCC 24843.
  2. "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.
  3. Rochet M., Levesque H., Gaillardin C.
    Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102.
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiTCPD_SCHPO
AccessioniPrimary (citable) accession number: P50999
Secondary accession number(s): O59929, Q9URV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 1, 2000
Last modified: April 13, 2016
This is version 119 of the entry and version 2 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.