Protein
View in Explore- UniProt accession
- A0A6J5MYJ0 [UniProt]
- Protein name
- WbbJ Acetyltransferase (Isoleucine patch superfamily)
- RBP type
-
TSP
- Protein sequence
-
MTYIHPTAIIGENVQIGENVYIGAYCIIGTAPEWKGKEWKDKGVIIYNGARLTGLVTVDAGAEKPTIIGRDCYLMKHSHVGHDATLEDGVTLSCGAKVGGHSVIGKGTNVGLNAVIHQKLTVPPGCMIGASAFIGKKTEMKPNSKYVGVPAKYIGENIR
- Physico‐chemical
properties -
protein length: 159 AA molecular weight: 16862,37450 Da isoelectric point: 8,84501 aromaticity: 0,06289 hydropathy: -0,02138
Domains
Domains [InterPro]
G3DSA:2.160.10.10
STR
1–154
STR
1–154
IPR050179
Unmapped
2–156
Unmapped
2–156
IPR011004
STR
2–157
STR
2–157
IPR001451
STR
2–29
STR
2–29
1
159
Architecture
STR 1-157 |
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
159
| Domain | Start | End | Length (AA) | Confidence |
|---|---|---|---|---|
| N-terminal | 1 | 22 | 22 | 0,0014 |
| Central domain | 23 | 148 | 127 | 0,4770 |
| C-terminal | 149 | 159 | 10 | 0,5478 |
Note: Constraints were applied during segmentation.
Fixed 20 C-terminal predictions appearing before Central domain|C-terminal too short, adjusted boundary
Fixed 20 C-terminal predictions appearing before Central domain|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
1-22
1-22
Central
23-148
23-148
C-terminal
149-159
149-159
Taxonomy
| Name | Taxonomy ID | Lineage | |
|---|---|---|---|
| Phage |
uncultured Caudovirales phage [NCBI] |
2100421 | Uroviricota > Caudoviricetes > Peduoviridae > Maltschvirus maltsch > |
| Host | No host information | ||
Coding sequence (CDS)
Coding sequence (CDS)
No CDS data available.
Genome Context
Genome Context
Gene Ontology
| Description | Category | Evidence (source) | |
|---|---|---|---|
| GO:0016740 | transferase activity | Molecular Function | IEA:UniProtKB-KW (UniProt) |
Tertiary structure
PDB ID
6c988077788ac9cdbf8af56c4d549c5f6ddded337dc1902033a4d78155f3947c
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