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 O74402

Entry ID Method Resolution Chain Position Source
AF-O74402-F1 Predicted AlphaFoldDB

No variants for O74402

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O74402

No associated diseases with O74402

8 regional properties for O74402

Type Name Position InterPro Accession
domain AAA+ ATPase domain 131 - 276 IPR003593-1
domain AAA+ ATPase domain 531 - 674 IPR003593-2
domain ATPase, AAA-type, core 137 - 249 IPR003959-1
domain ATPase, AAA-type, core 530 - 693 IPR003959-2
conserved_site ClpA/B, conserved site 1 227 - 239 IPR018368
domain Clp ATPase, C-terminal 700 - 789 IPR019489
conserved_site ClpA/B, conserved site 2 565 - 583 IPR028299
domain ClpA/ClpB, AAA lid domain 275 - 377 IPR041546

Functions

Description
EC Number
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.

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.
chaperone binding Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.
unfolded protein binding Binding to an unfolded protein.

5 GO annotations of biological process

Name Definition
cellular heat acclimation Any process that increases heat tolerance of a cell in response to high temperatures.
cellular response to heat Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism.
chaperone cofactor-dependent protein refolding The process of assisting in the correct posttranslational noncovalent assembly of proteins, which is dependent on additional protein cofactors. This process occurs over one or several cycles of nucleotide hydrolysis-dependent binding and release.
protein refolding The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones.
protein unfolding The process of assisting in the disassembly of non-covalent linkages in a protein or protein aggregate, often where the proteins are in a non-functional or denatured state.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNILPKSIPI RIQSLRRYQG SLKTSLRALS TRPIFEKRLL AETPFSIRPS NASVLIAKRS
70 80 90 100 110 120
PKFGWKQVRF YAANPNGGNF RMDLGGGRKQ GAALEEYGTD LTALAKQGKL DPVIGREEEI
130 140 150 160 170 180
QRTIQILSRR TKNNPALVGP AGVGKTAIME GLASRIIRGE VPESMKDKRV IVLDLGALIS
190 200 210 220 230 240
GAKFRGDFEE RLKSVLSDLE GAEGKVILFV DEMHLLLGFG KAEGSIDASN LLKPALARGK
250 260 270 280 290 300
LHCCGATTLE EYRKYIEKDA ALARRFQAVM VNEPSVADTI SILRGLKERY EVHHGVRITD
310 320 330 340 350 360
DALVTAATYS ARYITDRFLP DKAIDLVDEA CSSLRLQQES KPDELRRLDR QIMTIQIELE
370 380 390 400 410 420
SLRKETDTTS VERREKLESK LTDLKEEQDK LSAAWEEERK LLDSIKKAKT ELEQARIELE
430 440 450 460 470 480
RTQREGNYAR ASELQYAIIP ELERSVPKEE KTLEEKKPSM VHDSVTSDDI AVVVSRATGI
490 500 510 520 530 540
PTTNLMRGER DKLLNMEQTI GKKIIGQDEA LKAIADAVRL SRAGLQNTNR PLASFLFLGP
550 560 570 580 590 600
TGVGKTALTK ALAEFLFDTD KAMIRFDMSE FQEKHTIARL IGSPPGYIGY EESGELTEAV
610 620 630 640 650 660
RRKPYAVLLF DELEKAHHDI TNLLLQVLDE GFLTDSQGRK VDFRSTLIVM TSNLGSDILV
670 680 690 700 710 720
ADPSTTVTPK SRDAVMDVVQ KYYPPEFLNR IDDQIVFNKL SEKNLEDIVN VRLDEVQQRL
730 740 750 760 770 780
NDRRIILTVT EAARKWLAEK GYSPAYGARP LNRLIQKRIL NTMAMKIIQG EIKSDENVVI
790 800
DVLDGELEFK ANKLEPQSTS HED