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 Q39SQ3

Entry ID Method Resolution Chain Position Source
AF-Q39SQ3-F1 Predicted AlphaFoldDB

No variants for Q39SQ3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q39SQ3

No associated diseases with Q39SQ3

3 regional properties for Q39SQ3

Type Name Position InterPro Accession
domain Histidine kinase/HSP90-like ATPase 26 - 184 IPR003594
conserved_site Heat shock protein Hsp90, conserved site 24 - 33 IPR019805
domain Heat shock protein Hsp90, N-terminal 4 - 208 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
MTKTTKKFET EVQQLLDLVI HSLYSNKDIF LRELISNSSD AIDKVLFEAH QNAAVIEGEP
70 80 90 100 110 120
EGKIKLIPDK EAGTITIRDN GVGMTMEEVE KNIGTIAHSG TKAFLANLKE QNVSEHPELI
130 140 150 160 170 180
GQFGVGFYAS FMVADRVTLV TRRAGQDKAA GVRWESTGDG TYTVEEAVKE TRGTEITLHL
190 200 210 220 230 240
KEEMKEYLDE WKIRSIVRKY SDYVQYPVVM DVTRTEVPKG VNGEEIEGAG TIEKTVEETL
250 260 270 280 290 300
NSMKAIWARA KSEVTEEEYE EFYKHVSHDF EKPLKTIHYS AEGVSEFKAL LYLPAHKPFD
310 320 330 340 350 360
LFMPERKKGV QLYVRRVFIT DSCEQLIPDY LRFVKGVVDS SDLPLNVSRE ILQEDVQIKR
370 380 390 400 410 420
IQKSLVSKII STLSEMREKE ADDYLAFYKE FGQVLKEGVH FDYANREKLQ DLLLFESTRT
430 440 450 460 470 480
EAGKFTSLKE YVERMPAGQE EIYFITGTSR TALEQSPHLE IFRKKEYEVL FLTDPVDEWV
490 500 510 520 530 540
VQGVTEYDGK KLKAVDRGDV IPATEEEKKE QEAKREEAFK QYGDLLSFVK EKLDARVKEV
550 560 570 580 590 600
RLSSRLTDSA CCLVADEHGL NANMERILRA MNQDVPESKR ILELNPDHPL MQVMANLFAR
610 620 630 640
DKANPRLGDY CDLLYDQALL TEGSPISDPL RFTRLVAELM VADGKAAAGE