UniProt accession
A0A222Z082 [UniProt]
Protein name
Tail fibers protein
RBP type
TF
Evidence GenBank
Probability 1,00
TSP
Evidence DepoScope
Probability 0,53
TF
Evidence RBPdetect
Probability 0,90
TF
Evidence RBPdetect2
Probability 0,93
Protein sequence
MLAYSSGTGTEVGDSDGIAWNAKTGLYNVTGYSGGSTQLVFQMYQGASSTPSAQLKFNYRNGGFWYRSSRDGFGFEEDFTQIYTEKYKPTPSDIGAYTKSETDQKIAQAISDSTDLNKIYPVGIVTWFNSNVNPNTALPGLTWTYLNNGVGRTIRVAAANGSDVATTGGSDSVTLAVGNLPSHTHSFSATTSSFDYGTKTTNTTGAHTHSVSGSTNNTGAHTHTVGGHYGGDSIGGKPRVQVFGTEQVSSSAGAHAHTVSGTAASNGNHAHTVGIGAHSHTVSGNTGGTGSGSAFSVTNQFYKLMAWVRTA
Physico‐chemical
properties
protein length:311 AA
molecular weight: 32345,58910 Da
isoelectric point:6,89221
aromaticity:0,09968
hydropathy:-0,41447

Domains

Domains [InterPro]
DC_0905
STR
4–311
IPR051934
Unmapped
17–283
A0A222Z082
1 311
Architecture
STR
STR 4-311
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
A0A222Z082
1 311
Domain Start End Length (AA) Confidence
N-terminal 1 16 16 0,4139
Central domain 17 215 200 0,0434
C-terminal 216 311 95 0,9937
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
1-16
Central
17-215
C-terminal
216-311

Taxonomy

  Name Taxonomy ID Lineage
Phage Salmonella phage ST11
[NCBI]
2023990 Uroviricota > Caudoviricetes > Andersonviridae > Felixounavirus > Felixounavirus ST11
Host Salmonella enterica subsp. enterica
[NCBI]
59201 Bacteria > Proteobacteria > Gammaproteobacteria > Enterobacteriales > Enterobacteriaceae > Salmonella

Coding sequence (CDS)

Coding sequence (CDS)

No CDS data available.

Genome Context

Genome Context

Gene Ontology

Description Category Evidence (source)
GO:0098024 virus tail, fiber Cellular Component IEA:UniProtKB-KW (UniProt)
GO:0005198 structural molecule activity Molecular Function IEA:InterPro (UniProt)
GO:0019062 virion attachment to host cell Biological Process IEA:UniProtKB-KW (UniProt)

Tertiary structure

PDB ID
ce57304a95f64e103582f58e838cb623b8ab9807c8a4aa49d78133d7775cbbdd
ESMFold
Source ESMFold
Method ESMFold
Resolution 0,7890
Oligomeric State monomer
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50