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

1 structures for P50016

Entry ID Method Resolution Chain Position Source
AF-P50016-F1 Predicted AlphaFoldDB

No variants for P50016

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P50016

No associated diseases with P50016

3 regional properties for P50016

Type Name Position InterPro Accession
conserved_site Chaperonin TCP-1, conserved site 42 - 54 IPR002194-1
conserved_site Chaperonin TCP-1, conserved site 63 - 79 IPR002194-2
conserved_site Chaperonin TCP-1, conserved site 91 - 99 IPR002194-3

Functions

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

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

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.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAMLAGDGRQ VLILPEGYQR FVGRDAQRMN IMAARVVAET VRTTLGPMGM DKMLVDEMGD
70 80 90 100 110 120
VVVTNDGVTI LEEMDIEHPA AKMVVEVAKT QEDEVGDGTT TAVVLAGELL HKAEDLLQQD
130 140 150 160 170 180
IHPTVIARGY RMAVEKAEEI LEEIAEEIDP DDEETLKKIA KTAMTGKGVE KARDYLAELV
190 200 210 220 230 240
VKAVKQVAEE EDGEIVIDTD HIKLEKKEGG GLEDTELVKG MVIDKERVHP GMPRRVENAK
250 260 270 280 290 300
IALLNCPIEV KETETDAEIR ITDPEQLQAF IEEEERMLSE MVDKIAETGA NVVFCQKGID
310 320 330 340 350 360
DLAQHYLAKK GILAVRRVKK SDMQKLARAT GARIVTNIDD LSEEDLGEAE VVEEKKVAGD
370 380 390 400 410 420
KMIFVEGCKD PKAVTILIRG GTEHVVDEAE RAIEDAIGVV AAALEDGKVV AGGGAPEVEV
430 440 450 460 470 480
ARQLRDFADG VEGREQLAVE AFADALEIIP RTLAENSGLD PIDVLVQLRA KHEDGQVTAG
490 500 510 520 530 540
IDVYDGDVKD MLEEGVVEPL RVKTQALASA TEAAEMILRI DDVIAARELS KEEEEEEEEG
GSSEF