Protein
View in Explore- UniProt accession
- A0A482GMD5 [UniProt]
- Protein name
- ILEI/PANDER domain-containing protein
- RBP type
-
TFTFTSP
- Protein sequence
-
MEKFMAEFGQGYVQTPFLSESNSVRYKISIAGSCPLSTAGPYVKFQDNPVGNQTFSAGLHLRVFDPSTGALVDSKSYAFSASNNTTSAAFVSFMNSLSNNRLVAILTSGKVNFPPEVVSWLRGAGTSVFPSDSVLSRFDVSYAAFYTSSKRAIALEHVKLSNRKSTDDYQTILDVVFDSLEDVGATGFPKRTYESVEQFMSAVGGTNNEIARLPTSAAISKLSDYNLIPGDVLYLKAQLYADADLLDLGTTNISIRFYDASNGYISSTQAEFTGQAGSWELKEDYVVVPENAVGFTIYAQRTAQAGQGGMRNLSFSEVSRNGGISKPAEFGVNGIRVNYVCESASPPDIMVLPTQASSKTGKVFGQEFREV
- Physico‐chemical
properties -
protein length: 371 AA molecular weight: 40087,30080 Da isoelectric point: 5,15776 aromaticity: 0,11051 hydropathy: -0,13261
Domains
Domain architecture
A0A482GMD5
1
371 aa
LEC 22–57 · STR 58–112 · LEC 113–192 ·
ATT Attachment Domain
STR Structural Domain
RBD Receptor-Binding Domain
CBM Carbohydrate-Binding Module
LEC Lectin-like Domain
ENZ Enzymatic Domain
CHP Intramolecular Chaperone
LNK Linker/Spacer Domain
TAS Tail-Associated Structural
TTP Tail Tubular Protein
UNK Uncharacterized Domain
Unmapped
Proteins with similar domain architecture
Tail Spike Domain Segmentation
Segmented into three structural domains: N-terminal, central, and C-terminal.
Domain layout
A0A482GMD5
1
371 aa
| Domain | Start | End | Length (AA) | Confidence |
|---|---|---|---|---|
| N-terminal | 1 | 152 | 152 | 0,6050 |
| Central domain | 153 | 360 | 209 | 0,4112 |
| C-terminal | 361 | 371 | 10 | 0,1378 |
Note: Constraints were applied during segmentation.
Fixed 38 C-terminal predictions appearing before Central domain|C-terminal too short, adjusted boundary
Fixed 38 C-terminal predictions appearing before Central domain|C-terminal too short, adjusted boundary
N-terminal
Central domain
C-terminal
View these domains on the 3D structure via the Color by → Tail spike option in the Tertiary structure section below.
Taxonomy
Coding sequence (CDS)
No CDS data available.
Genome Context
Gene Ontology
| Description | Category | Evidence (source) | |
|---|---|---|---|
| GO:0030246 | carbohydrate binding | Molecular Function | IEA:UniProtKB-UniRule (UniProt) |