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CAZyme Information: EPrPRT00000014722-p1

You are here: Home > Sequence: EPrPRT00000014722-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Pythium arrhenomanes
Lineage Oomycota; NA; ; Pythiaceae; Pythium; Pythium arrhenomanes
CAZyme ID EPrPRT00000014722-p1
CAZy Family AA2
CAZyme Description T-complex protein 1 subunit eta.
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1403 154200.55 6.6441
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_ParrhenomanesATCC12531 13857 1223556 52 13805
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in EPrPRT00000014722-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH81 305 562 1e-36 0.35691318327974275

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
239456 TCP1_eta 0.0 864 1380 1 516
TCP-1 (CTT or eukaryotic type II) chaperonin family, eta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin.
238189 chaperonin_type_I_II 0.0 872 1380 1 462
chaperonin families, type I and type II. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I is seven-fold and they are found in eubacteria (GroEL) and in organelles of eubacterial descent (hsp60 and RBP). The symmetry of type II is eight- or nine-fold and they are found in archea (thermosome), thermophilic bacteria (TF55) and in the eukaryotic cytosol (CTT). Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.
274086 chap_CCT_eta 0.0 862 1380 1 517
T-complex protein 1, eta subunit. Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT eta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes.
395068 Cpn60_TCP1 0.0 891 1379 1 484
TCP-1/cpn60 chaperonin family. This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.
239459 cpn60 7.61e-160 865 1379 1 512
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. Archaeal cpn60 (thermosome), together with TF55 from thermophilic bacteria and the eukaryotic cytosol chaperonin (CTT), belong to the type II group of chaperonins. Cpn60 consists of two stacked octameric rings, which are composed of one or two different subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.43e-253 52 859 94 793
1.43e-253 52 859 94 793
4.01e-253 52 859 94 793
4.01e-253 52 859 94 793
1.94e-197 52 859 38 737

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.97e-230 865 1380 6 519
Chain H, T-complex protein 1 subunit eta [Homo sapiens],6QB8_h Chain h, T-complex protein 1 subunit eta [Homo sapiens],7LUM_C Chain C, T-complex protein 1 subunit eta [Homo sapiens],7LUM_K Chain K, T-complex protein 1 subunit eta [Homo sapiens],7LUP_C Chain C, T-complex protein 1 subunit eta [Homo sapiens],7LUP_K Chain K, T-complex protein 1 subunit eta [Homo sapiens],7NVL_H Chain H, T-complex protein 1 subunit eta [Homo sapiens],7NVL_h Chain h, T-complex protein 1 subunit eta [Homo sapiens],7NVM_H Chain H, T-complex protein 1 subunit eta [Homo sapiens],7NVM_h Chain h, T-complex protein 1 subunit eta [Homo sapiens],7NVN_H Chain H, T-complex protein 1 subunit eta [Homo sapiens],7NVN_h Chain h, T-complex protein 1 subunit eta [Homo sapiens],7NVO_H Chain H, T-complex protein 1 subunit eta [Homo sapiens],7NVO_h Chain h, T-complex protein 1 subunit eta [Homo sapiens]
7.01e-230 865 1380 6 519
The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning [Bos taurus],4B2T_h The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning [Bos taurus]
4.42e-228 869 1380 1 510
Ca model of bovine TRiC/CCT derived from a 4.0 Angstrom cryo-EM map [Bos taurus]
9.37e-227 871 1380 1 508
hTRiC-hPFD Class6 [Homo sapiens],6NR8_O hTRiC-hPFD Class6 [Homo sapiens],6NR9_G hTRiC-hPFD Class5 [Homo sapiens],6NR9_O hTRiC-hPFD Class5 [Homo sapiens],6NRA_G hTRiC-hPFD Class1 (No PFD) [Homo sapiens],6NRA_O hTRiC-hPFD Class1 (No PFD) [Homo sapiens],6NRB_G hTRiC-hPFD Class2 [Homo sapiens],6NRB_O hTRiC-hPFD Class2 [Homo sapiens],6NRC_G hTRiC-hPFD Class3 [Homo sapiens],6NRC_O hTRiC-hPFD Class3 [Homo sapiens],6NRD_G hTRiC-hPFD Class4 [Homo sapiens],6NRD_O hTRiC-hPFD Class4 [Homo sapiens]
3.45e-208 860 1380 4 523
The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins [Saccharomyces cerevisiae],4V81_O The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins [Saccharomyces cerevisiae],4V81_g The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins [Saccharomyces cerevisiae],4V81_o The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins [Saccharomyces cerevisiae],4V8R_AH Chain AH, T-COMPLEX PROTEIN 1 SUBUNIT ETA [Saccharomyces cerevisiae],4V8R_Ah Chain Ah, T-COMPLEX PROTEIN 1 SUBUNIT ETA [Saccharomyces cerevisiae],4V8R_BH Chain BH, T-COMPLEX PROTEIN 1 SUBUNIT ETA [Saccharomyces cerevisiae],4V8R_Bh Chain Bh, T-COMPLEX PROTEIN 1 SUBUNIT ETA [Saccharomyces cerevisiae],4V94_G Molecular architecture of the eukaryotic chaperonin TRiC/CCT derived by a combination of chemical crosslinking and mass-spectrometry, XL-MS [Saccharomyces cerevisiae S288C],4V94_O Molecular architecture of the eukaryotic chaperonin TRiC/CCT derived by a combination of chemical crosslinking and mass-spectrometry, XL-MS [Saccharomyces cerevisiae S288C],4V94_g Molecular architecture of the eukaryotic chaperonin TRiC/CCT derived by a combination of chemical crosslinking and mass-spectrometry, XL-MS [Saccharomyces cerevisiae S288C],4V94_o Molecular architecture of the eukaryotic chaperonin TRiC/CCT derived by a combination of chemical crosslinking and mass-spectrometry, XL-MS [Saccharomyces cerevisiae S288C],5GW4_H Structure of Yeast NPP-TRiC [Saccharomyces cerevisiae S288C],5GW4_h Structure of Yeast NPP-TRiC [Saccharomyces cerevisiae S288C],5GW5_H Structure of TRiC-AMP-PNP [Saccharomyces cerevisiae S288C],5GW5_h Structure of TRiC-AMP-PNP [Saccharomyces cerevisiae S288C],6KRD_H TRiC at 0.05 mM ADP-AlFx, Conformation 4, 0.05-C4 [Saccharomyces cerevisiae S288C],6KRD_h TRiC at 0.05 mM ADP-AlFx, Conformation 4, 0.05-C4 [Saccharomyces cerevisiae S288C],6KRE_H TRiC at 0.05 mM ADP-AlFx, Conformation 2, 0.05-C2 [Saccharomyces cerevisiae S288C],6KRE_h TRiC at 0.05 mM ADP-AlFx, Conformation 2, 0.05-C2 [Saccharomyces cerevisiae S288C],6KS6_H TRiC at 0.2 mM ADP-AlFx, Conformation 1, 0.2-C1 [Saccharomyces cerevisiae S288C],6KS6_h TRiC at 0.2 mM ADP-AlFx, Conformation 1, 0.2-C1 [Saccharomyces cerevisiae S288C],6KS7_H TRiC at 0.1 mM ADP-AlFx, Conformation 1, 0.1-C1 [Saccharomyces cerevisiae S288C],6KS7_h TRiC at 0.1 mM ADP-AlFx, Conformation 1, 0.1-C1 [Saccharomyces cerevisiae S288C],6KS8_H TRiC at 0.1 mM ADP-AlFx, Conformation 4, 0.1-C4 [Saccharomyces cerevisiae S288C],6KS8_h TRiC at 0.1 mM ADP-AlFx, Conformation 4, 0.1-C4 [Saccharomyces cerevisiae S288C]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.90e-244 862 1380 6 525
T-complex protein 1 subunit eta OS=Arabidopsis thaliana OX=3702 GN=CCT7 PE=1 SV=1
6.71e-230 865 1380 6 519
T-complex protein 1 subunit eta OS=Mus musculus OX=10090 GN=Cct7 PE=1 SV=1
2.56e-229 865 1380 6 519
T-complex protein 1 subunit eta OS=Homo sapiens OX=9606 GN=CCT7 PE=1 SV=2
3.60e-229 865 1380 6 519
T-complex protein 1 subunit eta OS=Bos taurus OX=9913 GN=CCT7 PE=1 SV=1
3.60e-229 865 1380 6 519
T-complex protein 1 subunit eta OS=Pongo abelii OX=9601 GN=CCT7 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000006 1.000018 CS pos: 11-12. Pr: 0.9865

TMHMM  Annotations      help

There is no transmembrane helices in EPrPRT00000014722-p1.