Protein
View in Explore- UniProt accession
- A0A6B9XDK5 [UniProt]
- Protein name
- Tail protein/depolymerase
- RBP type
-
TSP
- Protein sequence
-
MHLPNGSQIFIGVNMGDPIQATAITNAKEPVFTASDTKNIKKGAYVLIETSSWGKLVSRVLRVKAVTDNESVTLEGVDTTDTNVFPVGENTATFREVKSWVEIPCVQDLAQDGGEQQYYTYQCLADDQEQQLPTYKSAVSLTYTFAHEYDNPIYPILREAEESGDVTALRMYVPKAKEMRCWAGVLSFNDIPQTTMNEMETVSLSVSLKGRFTFLSSDIN
- Physico‐chemical
properties -
protein length: 220 AA molecular weight: 24486,25510 Da isoelectric point: 4,63422 aromaticity: 0,09091 hydropathy: -0,28727
Domains
Domains [InterPro]
DC_0037
ATT
1–50
ATT
1–50
1
220
Architecture
ATT 1-50 | TAS 51-216 |
Legend:
ATT
STR
RBD
CBM
LEC
ENZ
CHP
LNK
TAS
TTP
UNK
Unmapped
Tail Spike Domain Segmentation
Tail Spike Domain Segmentation
This protein has been segmented into three structural domains: N-terminal, central domain, and C-terminal.
Domain Layout
1
220
| Domain | Start | End | Length (AA) | Confidence |
|---|---|---|---|---|
| N-terminal | 1 | 58 | 58 | 0,4563 |
| Central domain | 59 | 209 | 152 | 0,0943 |
| C-terminal | 210 | 220 | 10 | 0,5877 |
Note: Constraints were applied during segmentation.
C-terminal too short, adjusted boundary
C-terminal too short, adjusted boundary
Legend:
N-terminal
Central domain
C-terminal
3D Structure with Domain Coloring
The structure is colored according to the domain segmentation: N-terminal (blue), Central (green), C-terminal (pink).
Domain Coloring
N-terminal
1-58
1-58
Central
59-209
59-209
C-terminal
210-220
210-220
Taxonomy
| Name | Taxonomy ID | Lineage | |
|---|---|---|---|
| Phage |
Escherichia phage tonijn [NCBI] |
2696450 | Viruses > Duplodnaviria > Heunggongvirae > Uroviricota > Caudoviricetes |
| Host |
Escherichia coli K-12 [NCBI] |
83333 | Bacteria > Proteobacteria > Gammaproteobacteria > Enterobacteriales > Enterobacteriaceae > Escherichia |
Coding sequence (CDS)
Coding sequence (CDS)
No CDS data available.
Genome Context
Genome Context
Tertiary structure
PDB ID
e157e1e5e2d7d850f266bd511391cdf337e49d2b856a5a8bdf4e7143eab38262
Model Confidence
Very high
pLDDT > 90
pLDDT > 90
High
90 > pLDDT > 70
90 > pLDDT > 70
Low
70 > pLDDT > 50
70 > pLDDT > 50
Very low
pLDDT < 50
pLDDT < 50