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 Q8D228

Entry ID Method Resolution Chain Position Source
AF-Q8D228-F1 Predicted AlphaFoldDB

No variants for Q8D228

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8D228

No associated diseases with Q8D228

2 regional properties for Q8D228

Type Name Position InterPro Accession
domain Histidine kinase/HSP90-like ATPase 30 - 187 IPR003594
domain Heat shock protein Hsp90, N-terminal 8 - 211 IPR020575

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
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.

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
MQKKETLEFQ SEVKQLLNLM IHSLYSNKEI FLRELISNAS DALDKLRFLS ISDEKIKIKQ
70 80 90 100 110 120
NKLCIFIDYD KNKKSITIQD NGIGMSKKEV IENLGTIAKS GTKSFIKSIE KSNSEKNNQL
130 140 150 160 170 180
IGKFGVGFYS VFIVSEKVLV LTRSFKENEK NGVLWESSGK GEYTISNIIK KDVGTEITIF
190 200 210 220 230 240
LKESEKEFCD ELNIKNIVLK YSNHINFPIK LKTKITKDNK ILTPEEKKSY TWKQINTGKS
250 260 270 280 290 300
LWSKKKSEIK DIEYKEFYKN FFNDNYDPLI WSHNHVEGKQ EYVSLLYIPR KASWDIWNRE
310 320 330 340 350 360
HKHGLKLYVK KVFIMDQSSE FIPNYLRFIK GIIDSNDLPL NVSREILQNN ENIYKIKINL
370 380 390 400 410 420
TKKALLMLEN LSKNHPDEYK LFWKEFGLIL KEGPSEDIKN YENVIKLFRF SSTYINSENQ
430 440 450 460 470 480
EVSLEDYVKR MQSGQNKIFY ITSDNYLSAK NNPHLEKLKE KKIEVLLLFD RIDEWMMNYM
490 500 510 520 530 540
TEFKKIKFQS ISKYSSYLEN IFKDENNDQK NTEQKLSTII LRIKSYLKDR VKDVRFTSKL
550 560 570 580 590 600
TNSPSTVTTD ENDITTQMSK LLISTGQESP EIKYIFELNA NHPIIKHVFN IEDKNIFNNW
610 620 630
IELLFEESIL SERGNLDDPN KFIHRINNLL LSNIIRLN