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 A1ANS1

Entry ID Method Resolution Chain Position Source
AF-A1ANS1-F1 Predicted AlphaFoldDB

No variants for A1ANS1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1ANS1

No associated diseases with A1ANS1

3 regional properties for A1ANS1

Type Name Position InterPro Accession
domain Histidine kinase/HSP90-like ATPase 28 - 181 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
MSKTTKQFQT EVKQLLDLVI HSLYSNRDIF LRELISNSSD AIDKIRFEAH SNEELLEGNS
70 80 90 100 110 120
DWKIKLIPDK DAGTLTILDN GIGMTMAEVE ENIGTIARSG TKAFMQALKD KSATDNPELI
130 140 150 160 170 180
GQFGVGFYAS FMVADRVILE TRKGGTASDG CRWESIGDGS YTIEECSLDR RGTEIVLHLK
190 200 210 220 230 240
DEFKEYLEEW KIRSIVKKYS DYIQYPVVMD ITRTETPKGV DGEEIEGAGT IEKTVEETLN
250 260 270 280 290 300
SMKAIWARPK SEVTEEEYQE FYKHISHDFE NPFNTIHFSA EGISEFKALI YLPAKKPFDL
310 320 330 340 350 360
FMADRKKGLQ LYVKRVFITD RCEELLPDYL RFVKGVVDSS DLPLNVSREI LQEDVQIKRI
370 380 390 400 410 420
QKSLVGKILS TLAEVKEKNF DEYVNFWKEF GPVLKEGLHF DYANKEKLQE LALFESTATE
430 440 450 460 470 480
AGSFTSLKEY VERMPEAQQE IYFITGDSRA TLKISPHLEA FKAKGYEVLF LTDPVDEWVV
490 500 510 520 530 540
QALTEYKEKK LKAVDRGDVD LDSEEEKKEK ETKQEEARKE YGDLISFIKS HLEDRVKDAR
550 560 570 580 590 600
LSKRLTDSAC CLVADEYGIN ANMERILKAM NQPVPDSKRV LELNPDHPIM KIMTEIFREN
610 620 630 640
KEDARLTDYA DLLYDQALLT EGSPIKDPLR FTRLVSELMV KAATK