Q3A334
Gene name |
lon2 |
Protein name |
Lon protease 2 |
Names |
ATP-dependent protease La 2 |
Species |
Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1) (Pelobacter carbinolicus) |
KEGG Pathway |
pca:Pcar_1982 |
EC number |
3.4.21.53: Serine endopeptidases |
Protein Class |
|
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 Q3A334
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q3A334-F1 | Predicted | AlphaFoldDB |
No variants for Q3A334
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q3A334 | |||||
No associated diseases with Q3A334
5 regional properties for Q3A334
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Lon protease, N-terminal domain | 12 - 202 | IPR003111 |
| domain | AAA+ ATPase domain | 348 - 493 | IPR003593 |
| domain | ATPase, AAA-type, core | 352 - 488 | IPR003959 |
| active_site | Peptidase S16, active site | 676 - 684 | IPR008268 |
| domain | Peptidase S16, Lon proteolytic domain | 570 - 773 | IPR008269 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.21.53 | Serine endopeptidases |
| Subcellular Localization |
|
|
| 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 |
| MTGHPLDAIP | PELPVYPLHD | QVIFPHMSFP | LFIGKEHMGL | VEEALRNNRL | LVVLTVLAID |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PITGREQFAR | VGTICRINQV | LRFPEGGCKI | ILEGVNRVRL | ITTLQVTPFA | MASVSLIPER |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ENRNSVAQAL | MQSIIALLRV | AQSLGQMLPE | DAHHAIDRID | ESGKLADSLA | VYLNMEVKDQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QRLLETLDPL | ERLKDVYLFL | TTEIQKMQAR | GGGSADRSRQ | AVRSQKEHLL | REQLKHIQNQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LGEEDPHQAD | IRQFRSIVQS | DEMPEVVRSV | AEKELARLER | INPSSPEYTV | ARSYVEYLCN |
| 310 | 320 | 330 | 340 | 350 | 360 |
| MPWQRGTSDI | LDIDRAQQTL | DDDHYDLVEV | KERILEFLAV | HSLKSSLKGP | ILCFVGPPGV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GKTSLGRSIA | RSLGRKFIRI | SLGGMKDEAE | IRGHRRTYIG | AMPGRIIQEI | CRAGANNPVF |
| 430 | 440 | 450 | 460 | 470 | 480 |
| MLDEVDKIGQ | DFRGDPAAAL | LEVLDPEQNY | SFTDHYLDVP | FDLSHVMFIT | TANVMDTVPP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| PLRDRMEVLR | LPGYSDEEKL | QIAFKYLIPK | QVSENGLDKH | PLQFEEQAVL | KIIKNYTREA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GVRSIDRQIA | SVCRKVAKAV | AQGKDAPEVI | RSDQVEKMLG | PRKYFSDVAA | EEDRVGVVTG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LAWTESGGDI | IFVEVSTMAG | RKDLTLTGSL | GNVMQESAKT | ALSYVRAHHA | DFGIDAQVFE |
| 670 | 680 | 690 | 700 | 710 | 720 |
| NLDIHLHVPS | GAIPKDGPSA | GVTIATALIS | QLTRRPARRN | VAMTGELTLT | GRILPIGGVK |
| 730 | 740 | 750 | 760 | 770 | 780 |
| EKVLAARRAG | VTTVLLPERN | RENLKELDDH | ILAEMTVLLV | DNLSEVVAHT | LIPDTEHGPR |
| 790 | |||||
| LFDCPQHLAV | DPPSGS |