Protein

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UniProt accession
A0A482MVL0 [UniProt]
Protein name
ILEI/PANDER domain-containing protein
RBP type
TSP
Evidence RBPdetect
Probability 0,90
Protein sequence
MEKFMAKFGQGYVQTPFLSESNSVRFKLSIAGSCPLSTSPAYIKFQDNPLGSQVFSVGLNVRVINPTTGAVVESKTYNFSTENDATSSAFVTFMDTYASNFIFALVTNAKTNFPPEVLAWFNKAGSSAIPLAQQVLNIVDISYSAFYISGKNAIALEHIKYSNKKTSTDYSTPLDVVYDTIDDIGATGFPSRTYESTDTFLSAVGGTNNEIKRMPTTSIITPLAGYKLKPGDFLYMKFQLMADADLLAQGTTRLSIRFFKSPSTSPISFKDINFDGAAGEWKIYEDYIEIPAGADGFTIYCYRTAPVGQGGLRNVIFTEVSCNGSVSKPAEFGINGIRVNYVSESLSAPDIMTLPTQSSTDTGKVFGQEFKEASE
Physico‐chemical
properties
protein length:375 AA
molecular weight: 40819,49810 Da
isoelectric point:5,08438
aromaticity:0,12267
hydropathy:-0,09147

Domains

Domains [InterPro]
DC_0912
STR
1–375
DC_0912
PS52031
LEC
22–193
PS52031
IPR039477
STR
58–129
IPR039477
A0A482MVL0
1 375
Architecture
STR
STR 1-375
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
A0A482MVL0
1 375
Domain Start End Length (AA) Confidence
N-terminal 1 168 168 0,2572
Central domain 169 364 197 0,5526
C-terminal 365 375 10 0,5598
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
1-168
Central
169-364
C-terminal
365-375

Taxonomy

  Name Taxonomy ID Lineage
Phage Escherichia phage vB_EcoM_WFbE185
[NCBI] 		2508199 Uroviricota > Caudoviricetes > Pantevenvirales > Tevenvirinae > Mosigvirus
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)

No CDS data available.

Genome Context

Genome Context

Tertiary structure

PDB ID
e600db2d69982239d6ec4a5475a122922371f3c66aa31a279bf628cb39efca9c
ESMFold
Source ESMFold
Method ESMFold
Resolution 0,6588
Oligomeric State monomer
Download PDB
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50