UniProt accession
A0A4Y1NUW9 [UniProt]
Protein name
Chitin-binding type-3 domain-containing protein
RBP type
TF
Evidence Phold
Probability 1,00
TSP
Evidence DepoScope
Probability 1,00
TF
Evidence RBPdetect
Probability 0,78
TF
Evidence RBPdetect2
Probability 0,58
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
G3DSA:2.10.10.20
ATT
16–62
IPR003610
CBM
17–43
A0A4Y1NUW9
1 272
Architecture
STR
ATT
STR
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
N-terminal
Central
C-terminal
A0A4Y1NUW9
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
Central
27-225
C-terminal
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
ESMFold
Source ESMFold
Method ESMFold
Resolution 0,8363
Oligomeric State monomer
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50