Protein
View in Explore- UniProt accession
- A0A4Y1NUW9 [UniProt]
- Protein name
- Chitin-binding type-3 domain-containing protein
- RBP type
-
TFTSPTFTF
- Protein sequence
-
MATVNLGSIKFKWKGTYAGGTAYTVDDVVSYNGSSYICILASTGNLPTNATYFEQMSQAGTNGTDLTTTLTTQGDILYRDGSGLQRLGIGTAGQALKVNSGATGYEFGTAGGIVQVKSARQTSAESWTGDNIMIGATATITPTSASNKILVMAQGVISTSGTTATGTMGMRYATGTSVTNSGTLVGGGDAAGSRSRGIAWAGNIGAAWNGTNFGYHILHAPATTSQISYRLCHLSHDGETMYLNRTGRDTDDADHGRFDTNITLMEISSGVL
- Physico‐chemical
properties -
protein length: 272 AA molecular weight: 28121,81810 Da isoelectric point: 6,17615 aromaticity: 0,07353 hydropathy: -0,14522
Domains
Domains [InterPro]
DC_0393
STR
1–272
STR
1–272
G3DSA:2.10.10.20
ATT
16–62
ATT
16–62
IPR003610
CBM
17–43
CBM
17–43
1
272
Architecture
STR 1-15 | ATT 16-62 | STR 63-272
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
272
| Domain | Start | End | Length (AA) | Confidence |
|---|---|---|---|---|
| N-terminal | 1 | 26 | 26 | 0,3791 |
| Central domain | 27 | 225 | 200 | 0,0041 |
| C-terminal | 226 | 272 | 46 | 0,9995 |
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
1-26
1-26
Central
27-225
27-225
C-terminal
226-272
226-272
Taxonomy
| Name | Taxonomy ID | Lineage | |
|---|---|---|---|
| Phage |
Pelagibacter phage HTVC025P [NCBI] |
2259657 | Uroviricota > Caudoviricetes > Autographivirales > Thoosavirus > Thoosavirus HTVC025P |
| Host |
Candidatus Pelagibacter ubique HTCC1062 [NCBI] |
335992 | Bacteria > Proteobacteria > Alphaproteobacteria > Pelagibacterales > Pelagibacteraceae > Candidatus Pelagibacter |
Coding sequence (CDS)
Coding sequence (CDS)
No CDS data available.
Genome Context
Genome Context
Gene Ontology
| Description | Category | Evidence (source) | |
|---|---|---|---|
| GO:0005576 | extracellular region | Cellular Component | IEA:InterPro (UniProt) |
| GO:0030246 | carbohydrate binding | Molecular Function | IEA:InterPro (UniProt) |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds | Molecular Function | IEA:InterPro (UniProt) |
| GO:0005975 | carbohydrate metabolic process | Biological Process | IEA:InterPro (UniProt) |
Tertiary structure
PDB ID
1c4db3b076aef3cc5d717be2dbd09debfca7c8c9d8ae02e715ab1942925efaea
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