Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

16 structures for P42943

Entry ID Method Resolution Chain Position Source
4V81 X-ray 380 A G/O/g/o 1-550 PDB
4V8R X-ray 380 A AH/Ah/BH/Bh 1-550 PDB
4V94 X-ray 380 A G/O/g/o 1-550 PDB
5GW4 EM 470 A H/h 1-550 PDB
5GW5 EM 460 A H/h 1-550 PDB
6KRD EM 438 A H/h 1-550 PDB
6KRE EM 445 A H/h 1-550 PDB
6KS6 EM 299 A H/h 1-550 PDB
6KS7 EM 462 A H/h 1-550 PDB
6KS8 EM 469 A H/h 1-550 PDB
7YLU EM 455 A H/h 1-550 PDB
7YLV EM 391 A H/h 1-550 PDB
7YLW EM 339 A H/h 1-550 PDB
7YLX EM 320 A H/h 1-550 PDB
7YLY EM 305 A H/h 1-550 PDB
AF-P42943-F1 Predicted AlphaFoldDB

1 variants for P42943

Variant ID(s) Position Change Description Diseaes Association Provenance
s10-209317 482 V>D No SGRP

No associated diseases with P42943

2 regional properties for P42943

Type Name Position InterPro Accession
conserved_site Chaperonin TCP-1, conserved site 62 - 78 IPR002194-1
conserved_site Chaperonin TCP-1, conserved site 90 - 98 IPR002194-2

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
chaperonin-containing T-complex A multisubunit ring-shaped complex that mediates protein folding in the cytosol without a cofactor.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
ATP-dependent protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis.
unfolded protein binding Binding to an unfolded protein.

2 GO annotations of biological process

Name Definition
chaperone mediated protein folding independent of cofactor The process of assisting in the correct noncovalent assembly of posttranslational proteins and does not depend on additional protein cofactors. This function occurs over one or more cycles of nucleotide-dependent binding and release.
protein folding The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P80313 Cct7 T-complex protein 1 subunit eta Mus musculus (Mouse) PR
10 20 30 40 50 60
MNFGSQTPTI VVLKEGTDAS QGKGQIISNI NACVAVQEAL KPTLGPLGSD ILIVTSNQKT
70 80 90 100 110 120
TISNDGATIL KLLDVVHPAA KTLVDISRAQ DAEVGDGTTS VTILAGELMK EAKPFLEEGI
130 140 150 160 170 180
SSHLIMKGYR KAVSLAVEKI NELAVDITSE KSSGRELLER CARTAMSSKL IHNNADFFVK
190 200 210 220 230 240
MCVDAVLSLD RNDLDDKLIG IKKIPGGAME ESLFINGVAF KKTFSYAGFE QQPKKFNNPK
250 260 270 280 290 300
ILSLNVELEL KAEKDNAEVR VEHVEDYQAI VDAEWQLIFE KLRQVEETGA NIVLSKLPIG
310 320 330 340 350 360
DLATQFFADR NIFCAGRVSA DDMNRVIQAV GGSIQSTTSD IKPEHLGTCA LFEEMQIGSE
370 380 390 400 410 420
RYNLFQGCPQ AKTCTLLLRG GAEQVIAEVE RSLHDAIMIV KRALQNKLIV AGGGATEMEV
430 440 450 460 470 480
SKCLRDYSKT IAGKQQMIIN AFAKALEVIP RQLCENAGFD AIEILNKLRL AHSKGEKWYG
490 500 510 520 530 540
VVFETENIGD NFAKFVWEPA LVKINALNSA TEATNLILSV DETITNKGSE SANAGMMPPQ
GAGRGRGMPM