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 P50143

Entry ID Method Resolution Chain Position Source
AF-P50143-F1 Predicted AlphaFoldDB

No variants for P50143

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P50143

No associated diseases with P50143

2 regional properties for P50143

Type Name Position InterPro Accession
domain ResB-like domain 30 - 295 IPR007816-1
domain ResB-like domain 318 - 447 IPR007816-2

Functions

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

1 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.

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
MMGRPVLVLS QNMKRESGRK VQSGNINAAK TIADIIRTCL GPRAMMKMLL DPMGGIVMTN
70 80 90 100 110 120
DGNAILREIQ VQHPAAKSMI EISRTQDEEV GDGTTSVIIL AGEMLSVAEQ FLEQQMHPTV
130 140 150 160 170 180
IISAYRKALD DMVNTLKEIS TPVDTNDREL MLKIINSAIN TKAIKLWADM ACGIALDAVK
190 200 210 220 230 240
TVELEENGRK EIDIKKYAKV EKIPGGIIED SCVLRGVMVN KDVTHPKMRR LIKNPRIILL
250 260 270 280 290 300
DCSLEYKKGE SQTEIEITRE EDFARILQME EEYIQQVCED IIRLKPDVVI TEKGISDLAQ
310 320 330 340 350 360
HYLVKANITA VRRVRKTDNN RIARACGARI ASRTDELREE DVGTGAGLFE IKKIGDEYFT
370 380 390 400 410 420
FITDCKDPKA CTIVLRGASK EILAEVERNL QDAMQVCRNV VIDPYLVPGG GASEMSVAHI
430 440 450 460 470 480
LTEKSKTMTG VEQWPYRAVA QALEVIPRTL IQNCGASTIR ILTSLRAKHT QEGCQTWGVD
490 500 510 520 530 540
GEAGVLADMK ELGIWEPLAV KLQTYKTAVE TAILLLRIDD IVSGHKKKGE DHGRQPAAAP
EAPQQAE