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 B8G736

Entry ID Method Resolution Chain Position Source
AF-B8G736-F1 Predicted AlphaFoldDB

No variants for B8G736

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B8G736

No associated diseases with B8G736

4 regional properties for B8G736

Type Name Position InterPro Accession
domain Lon protease, N-terminal domain 25 - 220 IPR003111
domain AAA+ ATPase domain 367 - 512 IPR003593
domain ATPase, AAA-type, core 371 - 508 IPR003959
domain Peptidase S16, Lon proteolytic domain 595 - 798 IPR008269

Functions

Description
EC Number 3.4.21.53 Serine endopeptidases
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.

5 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 peptidase activity Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis.
sequence-specific DNA binding Binding to DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding.
serine-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).

2 GO annotations of biological process

Name Definition
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.
protein quality control for misfolded or incompletely synthesized proteins The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNEPMSLFDD LPEEHDEPQE APERRLPMVV LGEMVIMPHM TIPLQVPQGK SYRAMERAWE
70 80 90 100 110 120
EDRDVLLIFV REHQLEGYKS NQPQNLPPIG VIAQLQEFAK LNDGTARVIL EGQSRAQIIE
130 140 150 160 170 180
AIQITPFYRV RCRPYTDPPV SGLEVEALME TVKQQVDEFV EHLGEVPQEA VQFVHRIDRP
190 200 210 220 230 240
GHLADIVTWG PAFDFKDRLE VLNTLDPVER LRKVYLVLAR QLELLKLRVK IQQDTKEVLD
250 260 270 280 290 300
QSQREYFLRE QLRIIRRELG EDEEGDDPID ELRRKIHELD APEYVKNQAL HELKRLAQQG
310 320 330 340 350 360
MNNPESGVIR TYLDWILSLP WADEELPEIS ITEAQKVLDA DHYGLEKVKE RILEYLAVRK
370 380 390 400 410 420
LAGDKMRSPI LCFVGPPGVG KTSLGRSIAR ALGRKFVRTS LGGVRDEAEI RGHRRTYIGA
430 440 450 460 470 480
MPGRIIQAMK NAKSKSPVYI LDEVDKIGLD FRGDPTSALL EVLDPEQNNA FSDHYLEIPF
490 500 510 520 530 540
DLSKVIFIAT ANQLDPIPLP LRDRMEIIEI GGYTEDEKLE IARGFLIPKQ REFHGLTEDQ
550 560 570 580 590 600
IEFTEGAILK LIREYTREAG VRGLEREIAS LCRKVARQVA EQTEANGELP PKFVIDEAAV
610 620 630 640 650 660
VKYLGPERYT YGIAEEQDEV GVATGVAWTS AGGDILSIEV LPFKGKGQLQ LTGQLGEVMK
670 680 690 700 710 720
ESAQTAVSYV RSRAADFGID PNTFEETNIH IHIPEGAVPK DDPSAGITLT TALISALTGT
730 740 750 760 770 780
PVRRDVAMTG EVTLRGKVLP IGGLKEKTLA AHRAGIRTFI LPKENAKDIS ELPEKVRREL
790 800 810 820
NLIPVSSMDE VLRIALSRMP TPANNQNGSH TNNRGQPSPA PAGT