Q9Z6P3
Gene name |
CPn_1016 (CP_0837, CPj1016, CpB1054) |
Protein name |
Protein CPn_1016/CP_0837/CPj1016/CpB1054 |
Names |
|
Species |
Chlamydia pneumoniae (Chlamydophila pneumoniae) |
KEGG Pathway |
cpt:CpB1054 |
EC number |
|
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 Q9Z6P3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9Z6P3-F1 | Predicted | AlphaFoldDB |
1 variants for Q9Z6P3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| 619 | L>S | strain: CWL029 and TW-183 [UniProt] | No |
No associated diseases with Q9Z6P3
1 regional properties for Q9Z6P3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | OTU domain | 255 - 349 | IPR003323 |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| serine-type peptidase activity | Catalysis of the hydrolysis of 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). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKKGKLGAIV | FGLLFTSSVA | GFSKDLTKDN | AYQDLNVIEH | LISLKYAPLP | WKELLFGWDL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SQQTQQARLQ | LVLEEKPTTN | YCQKVLSNYV | RSLNDYHAGI | TFYRTESAYI | PYVLKLSEDG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| HVFVVDVQTS | QGDIYLGDEI | LEVDGMGIRE | AIESLRFGRG | SATDYSAAVR | SLTSRSAAFG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DAVPSGIAML | KLRRPSGLIR | STPVRWRYTP | EHIGDFSLVA | PLIPEHKPQL | PTQSCVLFRS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GVNSQSSSSS | LFSSYMVPYF | WEELRVQNKQ | RFDSNHHIGS | RNGFLPTFGP | ILWEQDKGPY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RSYIFKAKDS | QGNPHRIGFL | RISSYVWTDL | EGLEEDHKDS | PWELFGEIID | HLEKETDALI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IDQTHNPGGS | VFYLYSLLSM | LTDHPLDTPK | HRMIFTQDEV | SSALHWQDLL | EDVFTDEQAV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AVLGETMEGY | CMDMHAVASL | QNFSQSVLSS | WVSGDINLSK | PMPLLGFAQV | RPHPKHQYTK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| PLFMLIDEDD | FSCGDLAPAI | LKDNGRATLI | GKPTAGAGGF | VFQVTFPNRS | GIKGLSLTGS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LAVRKDGEFI | ENLGVAPHID | LGFTSRDLQT | SRFTDYVEAV | KTIVLTSLSE | NAKKSEEQTS |
| 610 | |||||
| PQETPEVIRV | SYPTTTSAL |