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 B7VII6

Entry ID Method Resolution Chain Position Source
AF-B7VII6-F1 Predicted AlphaFoldDB

No variants for B7VII6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B7VII6

No associated diseases with B7VII6

3 regional properties for B7VII6

Type Name Position InterPro Accession
domain Histidine kinase/HSP90-like ATPase 26 - 183 IPR003594
conserved_site Heat shock protein Hsp90, conserved site 24 - 33 IPR019805
domain Heat shock protein Hsp90, N-terminal 4 - 207 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
MSETATQNKE TRGFQSEVKQ LLHLMIHSLY SNKEIFLREL ISNASDAADK LRFQALSNGD
70 80 90 100 110 120
LYQGDADLGV KLSFNAEANT LTISDNGIGM SRDNVIEHLG TIAKSGTADF FSKLSEDQSK
130 140 150 160 170 180
DSQLIGQFGV GFYSAFIVAD AVTVRTRAAG LANDQAVQWH SAGEGDYTIE DITKESRGTD
190 200 210 220 230 240
IILHMREDGK EFLNEWRLRE VIGKYSDHIG IPVSIFTAVK DDEGKDTEEK HWEQINKAQA
250 260 270 280 290 300
LWTRNKSDIE KEEYQEFYKH VSHDFADPLT WSHNKVEGKN DYTSLLYIPA KAPWDMMNRD
310 320 330 340 350 360
HKSGLKLYVQ RVFIMDDAEQ FMPSYMRFVR GLIDSNDLPL NVSREILQDN KVTQSLRGAC
370 380 390 400 410 420
TKRVLTMLER MAKNDNDKYL EFWKEFGLVL KEGPAEDMAN KEKIAGLLRF SSTEVDSSEQ
430 440 450 460 470 480
TIGLASYVER MKEGQDKIYY LTADSYAAAK NSPHLEQFKA KGIEVVLMYD RIDEYVMNYL
490 500 510 520 530 540
TDFDGKQFQS ITKAGLDLSK FEGEEEKEKQ KETEEEFKSV VERTQSYLGG RVKEVRTTFK
550 560 570 580 590 600
LATTPAVVVT DDFEMGTQMA KLLEAAGQAA PEVKYIFEIN PEHALVKQMA DEADEQAFGR
610 620 630
WVELLLGQAM LAEKGSMEDP SQFLGAINEL LTKR