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 C1DD88

Entry ID Method Resolution Chain Position Source
AF-C1DD88-F1 Predicted AlphaFoldDB

No variants for C1DD88

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C1DD88

No associated diseases with C1DD88

3 regional properties for C1DD88

Type Name Position InterPro Accession
conserved_site Heat shock protein 70, conserved site 7 - 14 IPR018181-1
conserved_site Heat shock protein 70, conserved site 193 - 206 IPR018181-2
conserved_site Heat shock protein 70, conserved site 338 - 352 IPR018181-3

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

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
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
MGKIIGIDLG TTNSCVAVLE NGQPKVIENS EGARTTPSVV AYMEDGEILV GAPAKRQAVT
70 80 90 100 110 120
NAKNTIFASK RLIGRRFEEK EVQKDIDLMP FSIVKADNGD AWIDVRGKKL APPQISAEVL
130 140 150 160 170 180
RKMKKTAEDY LGEEVTEAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAFG
190 200 210 220 230 240
MDKSEKGDKK IAVYDLGGGT FDISIIEIAD VDGEKQFEVL ATNGDTFLGG EDFDQRLIDY
250 260 270 280 290 300
IVTEFKKEQG VDLKNDVMAL QRLKEAAEKA KIELSSGQQT EINLPYITMD ATGPKHLTMK
310 320 330 340 350 360
ITRAKFESLV DELIERSIEP CRVAIKDAGL KVSDIDDVIL VGGQSRMPKV QEAVKTFFGK
370 380 390 400 410 420
EPRRDVNPDE AVAVGAAIQG SVLSGERKDL LLLDVTPLSL GIETMGGIMT KLIQKNTTIP
430 440 450 460 470 480
TKATQVFSTA DDNQTAVTIH VLQGEREKAA ANKSLGQFNL SDIPPAPRGL PQIEVTFDID
490 500 510 520 530 540
ANGILHVSAK DKATGKQANI TIQASSGLSE AEIEKMVRDA ELNAEEDKKL AELVQARNQA
550 560 570 580 590 600
EGLIHSVKKS LADYGDKIGS DEKARIEAAI KDAEEAVKGE DKAAIEAKSE ELAKASQKLG
610 620 630 640
EIMYAQAQAE SQAAGEGQPD AGKKDDGNVV DAEFEEVKKD KQ