Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message

IPR012716

Description

IPR012716 is a T-complex protein 1, beta subunit.

<p>Members of this eukaryotic family are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1 or Tailless Complex Polypeptide 1) or TRiC [[cite:PUB00004127], [cite:PUB00001019]]. Chaperonins are involved in productive folding of proteins [[cite:PUB00080867]]. They share a common general morphology, a double toroid of 2 stacked rings. The archaeal equivalent group II chaperonin is often called the thermosome [[cite:PUB00080871]]. Both the thermosome and the TCP-1 family of proteins are weakly, but significantly [[cite:PUB00004124]], related to the cpn60/groEL chaperonin family (see [interpro:IPR001844]).</p> <p>The TCP-1 protein was first identified in mice where it is especially abundant in testis but present in all cell types. It has since been found and characterised in many other animal species, as well as in yeast, plants and protists. The TCP1 complex has a double-ring structure with central cavities where protein folding takes place [[cite:PUB00074264]]. TCP-1 is a highly conserved protein of about 60kDa (556 to 560 residues) which participates in a hetero-oligomeric 900kDa double-torus shaped particle [[cite:PUB00004129]] with 6 to 8 other different, but homologous, subunits [[cite:PUB00064264]]. These subunits, the chaperonin containing TCP-1 (CCT) subunit beta, gamma, delta, epsilon, zeta and eta are evolutionary related to TCP-1 itself [[cite:PUB00001034], [cite:PUB00005432]]. Non-native proteins are sequestered inside the central cavity and folding is promoted by using energy derived from ATP hydrolysis [[cite:PUB00080868], [cite:PUB00080869], [cite:PUB00080873]]. The CCT is known to act as a molecular chaperone for tubulin, actin and probably some other proteins [[cite:PUB00074265], [cite:PUB00074266]].</p> <p>This family consists exclusively of the CCT beta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .

GO term Namespace Name Definition Relationships
Cellular component Cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
Cellular component Chaperonin-containing T-complex A multisubunit ring-shaped complex that mediates protein folding in the cytosol without a cofactor.
Biological process Protein folding The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
Molecular function Unfolded protein binding Interacting selectively and non-covalently with an unfolded protein.

Associated Lotus transcripts 9

Transcript Name Description Predicted domains Domain count
PREDICTED: T-complex protein 1 subunit beta-like isoform X2 [Cicer arietinum] gi|502104047|ref|XP_004492422.1| 22
T-complex protein 1 subunit beta; TAIR: AT5G20890.1 TCP-1/cpn60 chaperonin family protein; Swiss-Prot: sp|Q940P8|TCPB_ARATH T-complex protein 1 subunit beta; TrEMBL-Plants: tr|A0A1J7HDU4|A0A1J7HDU4_LUPAN Uncharacterized protein; Found in the gene: LotjaGi1g1v0438900 22
T-complex protein 1 subunit beta; TAIR: AT5G20890.1 TCP-1/cpn60 chaperonin family protein; Swiss-Prot: sp|Q940P8|TCPB_ARATH T-complex protein 1 subunit beta; TrEMBL-Plants: tr|A0A1J7HDU4|A0A1J7HDU4_LUPAN Uncharacterized protein; Found in the gene: LotjaGi1g1v0438900 22
T-complex protein 1 subunit beta; TAIR: AT5G20890.1 TCP-1/cpn60 chaperonin family protein; Swiss-Prot: sp|Q940P8|TCPB_ARATH T-complex protein 1 subunit beta; TrEMBL-Plants: tr|I1LRE4|I1LRE4_SOYBN Uncharacterized protein; Found in the gene: LotjaGi1g1v0438900 22
T-complex protein 1 subunit beta; TAIR: AT5G20890.1 TCP-1/cpn60 chaperonin family protein; Swiss-Prot: sp|Q940P8|TCPB_ARATH T-complex protein 1 subunit beta; TrEMBL-Plants: tr|I1LRE4|I1LRE4_SOYBN Uncharacterized protein; Found in the gene: LotjaGi1g1v0438900 22
T-complex protein 1 subunit beta; TAIR: AT5G20890.1 TCP-1/cpn60 chaperonin family protein; Swiss-Prot: sp|Q940P8|TCPB_ARATH T-complex protein 1 subunit beta; TrEMBL-Plants: tr|A0A1J7HDU4|A0A1J7HDU4_LUPAN Uncharacterized protein; Found in the gene: LotjaGi1g1v0438900 22
T-complex protein 1 subunit beta; TAIR: AT5G20890.1 TCP-1/cpn60 chaperonin family protein; Swiss-Prot: sp|Q940P8|TCPB_ARATH T-complex protein 1 subunit beta; TrEMBL-Plants: tr|A0A151TNM7|A0A151TNM7_CAJCA T-complex protein 1 subunit beta; Found in the gene: LotjaGi6g1v0145000 22
T-complex protein 1 subunit beta; TAIR: AT5G20890.1 TCP-1/cpn60 chaperonin family protein; Swiss-Prot: sp|Q940P8|TCPB_ARATH T-complex protein 1 subunit beta; TrEMBL-Plants: tr|A0A151TNM7|A0A151TNM7_CAJCA T-complex protein 1 subunit beta; Found in the gene: LotjaGi6g1v0145000 22
T-complex protein 1 subunit beta; TAIR: AT5G20890.1 TCP-1/cpn60 chaperonin family protein; Swiss-Prot: sp|Q940P8|TCPB_ARATH T-complex protein 1 subunit beta; TrEMBL-Plants: tr|A0A151TNM7|A0A151TNM7_CAJCA T-complex protein 1 subunit beta; Found in the gene: LotjaGi6g1v0145000 22

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space:

Predicted domain Source Observations Saturation (%)
cd03336 CDD 1 11.11