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 O44001

Entry ID Method Resolution Chain Position Source
AF-O44001-F1 Predicted AlphaFoldDB

No variants for O44001

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O44001

No associated diseases with O44001

3 regional properties for O44001

Type Name Position InterPro Accession
domain Histidine kinase/HSP90-like ATPase 27 - 182 IPR003594
conserved_site Heat shock protein Hsp90, conserved site 25 - 34 IPR019805
domain Heat shock protein Hsp90, N-terminal 5 - 206 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
MENKETFAFN ADIQQLMSLI INTFYSNKEI FLRELISNAS DALDKIRYEA ITEPEKLKTK
70 80 90 100 110 120
PELFIRLIPD KANNTLTIEN SGIGMTKADL VNNLGTIARS GTKAFMEALQ AGGDISMIGQ
130 140 150 160 170 180
FGVGFYSAYL VADSVTVVSK HNDDEQYVWE SAAGGSFTVQ KDDKYEPLGR GTRIILHLKE
190 200 210 220 230 240
DQGEYLEERR LKDLVKKHSE FISFPIELAV EKTHEREVTE SEDEEEKKAD EKAEEKEGEE
250 260 270 280 290 300
KKEGEEKKEG EEEKKEKTGK TKKVQEVTRE WEQLNKQKPL WMRKPEEVTE EEYASFYKSL
310 320 330 340 350 360
SNDWEEHLAV KHFSVEGQLE FKALLFVPKR APFDLFETRK KRNNIKLYVR RVFIMDDCED
370 380 390 400 410 420
IIPEWLNFVK GVVDSEDLPL NISRESLQQN KILKVIRKNL VKKCLEMFAE IEEKKENYAK
430 440 450 460 470 480
FYEQFSKNLK LGIHEDSANR AKIAELLRFH SSKSGEDMVS FKEYVDRMKE GQKDIYYITG
490 500 510 520 530 540
ESRQTVANSP FLEKLTKKGY EVLYMTDPID EYAVQQLKEF DNHKLRCCTK EGLEIDESEE
550 560 570 580 590 600
EKKKFEELKA EFEPLLKLIK EVLHDKVDKV VLSNRITDSP CVLVTTEFGW SANMERIMKA
610 620 630 640 650 660
QALRDNSMTS YMVSKKTMEV NGHHSIMIEI KNKAAVDKSD KTVKDLIWLL YDTALLTSGF
670 680 690 700 710
SLEEPTQFAA RIHRMIKLGL SIDDDEEAKD DDLPPLEEVE GAADEASKME EVD