Protein
View in Explore- UniProt accession
- A0A6J7XH04 [UniProt]
- Protein name
- WbbJ Acetyltransferase (Isoleucine patch superfamily)
- RBP type
-
TSP
- Protein sequence
-
MHELASVHTSCIIYPGVYIGPNVTIGEGCIIGPNTCIGQPGFGYNTLDDGTREYRDHQQGVLLERDVHVGANTCIDQGRHRRTEIGAGTRIDNLVHIAHNVIIGKRCLIIAHTMLGGSVTIGDDAHIAPGSLIRDWRNVATQATSGLGAVVIRDIPEGETHAGNPARNLEEHHDRQRTGPS
- Physico‐chemical
properties -
protein length: 181 AA molecular weight: 19487,63400 Da isoelectric point: 6,14659 aromaticity: 0,03315 hydropathy: -0,28619
Domains
Domains [InterPro]
G3DSA:2.160.10.10
STR
2–169
STR
2–169
IPR001451
STR
7–38
STR
7–38
IPR011004
STR
7–171
STR
7–171
IPR007691
STR
8–170
STR
8–170
1
181
Architecture
STR 2-171 |
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
181
| Domain | Start | End | Length (AA) | Confidence |
|---|---|---|---|---|
| N-terminal | 1 | 63 | 63 | 0,0005 |
| Central domain | 64 | 170 | 108 | 0,1561 |
| C-terminal | 171 | 181 | 10 | 0,9837 |
Note: Constraints were applied during segmentation.
Fixed 93 C-terminal predictions appearing before Central domain|C-terminal too short, adjusted boundary
Fixed 93 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
1-63
1-63
Central
64-170
64-170
C-terminal
171-181
171-181
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:0016020 | membrane | Cellular Component | IEA:GOC (UniProt) |
| GO:0016410 | N-acyltransferase activity | Molecular Function | IEA:InterPro (UniProt) |
| GO:0009245 | lipid A biosynthetic process | Biological Process | IEA:UniProtKB-KW (UniProt) |
Tertiary structure
PDB ID
9f859a315dfac861646367f562af0f0adac2922cd870caa420e26c1276023cbe
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