Protein
View in Explore- UniProt accession
- A0AAE7W0E5 [UniProt]
- Protein name
- Lateral tail fiber protein with glycosidase domain
- RBP type
-
TFTFTSPTSPTSP
- Protein sequence
-
MAQDMTSFEQAVDQVIVDSERLHLVVNGNAVDEVVVEDGTTIPTVRKAMLDNLYFKTPPIPWAYGASTTVFNQLYEFKGDTGPQWWYAPAASKSNPVRMPADPSQSPNWRLYTDSAVMAKYYAKLNSPRFEGDPRVPTPPMDDKSESIANTEFVVDYVDSIFKAMEGMKVTVGSLVVKGLTELANTIVGGTLTLHGPVNGADSTARFRNLILTANTSTLTFAWSDPKHADWRSTELQPHEVSTHRVIADTITSGKPVANNNDVHFDGLGNNFFDYVYIRGNAMKAATEPTLQVDGTTRVKNLEVTGTVTGITYSVDGTMIYPSYIESTGDALINGDLEVGGSVVIRGTASIQNIALNTLRVNERATFEGEGLTANKGTITELTTTTLTATTANSENCNITRNLQVNGDVSLNAAGTGTTYLHNLEISGTVTGWLPDFSNVNFVCNGINSSGKITTSQEIEAGKTITAPTFHTGKVDFDLEEVDASSGTWTPNGQASMYVVHAKGDFTIGQWPGTSAEDKPYPFTAVIYVIQDAVGHNVTLHDKYAILSATPVINNKANSVTLLQLTYCGVGDIVDVVIAQR
- Physico‐chemical
properties -
protein length: 581 AA molecular weight: 62698,28620 Da isoelectric point: 4,80536 aromaticity: 0,08090 hydropathy: -0,18313
Domains
Domain architecture
A0AAE7W0E5
1
581 aa
ATT 6–112 · RBD 489–572 ·
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
A0AAE7W0E5
1
581 aa
| Domain | Start | End | Length (AA) | Confidence |
|---|---|---|---|---|
| N-terminal | 1 | 203 | 203 | 0,9934 |
| Central domain | 204 | 472 | 270 | 0,8257 |
| C-terminal | 473 | 581 | 108 | 0,9078 |
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)
Genbank protein accession
QXV85550.1
[NCBI]
Genbank nucleotide accession
MZ501111
[NCBI]
CDS location
range 40207 -> 41952
strand +
strand +
CDS
ATGGCGCAAGACATGACAAGCTTTGAGCAGGCGGTAGATCAAGTAATTGTTGATTCTGAACGTTTGCACTTGGTTGTCAACGGTAACGCTGTGGATGAAGTTGTCGTAGAGGATGGAACCACCATCCCTACGGTACGAAAAGCCATGCTTGACAACCTTTATTTTAAAACGCCACCGATCCCTTGGGCGTATGGTGCATCCACAACAGTTTTTAACCAGCTGTACGAGTTTAAAGGGGACACAGGCCCTCAGTGGTGGTACGCTCCCGCAGCATCAAAATCTAACCCGGTTAGAATGCCAGCAGATCCTTCACAATCTCCAAACTGGAGATTATATACCGACTCTGCAGTAATGGCAAAATACTACGCAAAACTTAACAGCCCGAGGTTCGAAGGTGACCCACGAGTACCTACACCTCCAATGGACGATAAGTCAGAGTCCATAGCAAACACAGAGTTTGTTGTTGACTATGTTGATAGCATATTTAAAGCCATGGAGGGGATGAAAGTTACTGTAGGGTCTTTGGTGGTAAAAGGTCTTACAGAACTCGCTAACACTATAGTTGGTGGCACCCTTACCTTACATGGACCTGTTAATGGGGCAGATTCTACTGCACGCTTTAGGAATCTAATCCTCACGGCAAATACTTCTACACTTACTTTTGCGTGGAGCGATCCTAAGCATGCAGACTGGAGAAGTACAGAGCTGCAACCTCATGAAGTGTCCACCCACAGGGTTATAGCTGACACTATAACTTCTGGGAAACCAGTGGCTAATAATAACGATGTGCATTTTGATGGTCTGGGTAATAACTTTTTTGACTACGTGTACATTCGTGGTAATGCCATGAAGGCAGCAACCGAACCGACATTGCAGGTCGATGGGACCACCAGGGTTAAGAACCTTGAGGTGACAGGTACCGTTACAGGGATAACATACTCTGTCGATGGCACCATGATCTACCCTAGCTATATTGAAAGCACGGGTGATGCATTGATAAATGGCGATTTGGAGGTTGGCGGGTCTGTAGTTATTCGAGGTACAGCCTCTATCCAAAATATAGCTCTGAATACTCTAAGAGTCAATGAGCGTGCAACTTTTGAAGGAGAAGGGCTTACAGCCAATAAAGGTACAATTACCGAGCTAACCACCACCACTTTAACTGCAACAACTGCAAACTCTGAAAACTGCAACATTACCAGAAACTTGCAGGTAAATGGAGATGTTAGTTTAAACGCCGCAGGGACTGGCACCACCTACCTTCACAACCTTGAAATATCTGGCACAGTGACCGGGTGGCTGCCAGACTTCTCTAATGTCAACTTTGTCTGTAATGGCATTAACTCCAGTGGTAAGATAACCACCTCTCAAGAAATTGAGGCGGGTAAAACCATTACTGCCCCTACTTTCCACACAGGAAAGGTAGATTTTGACTTAGAGGAGGTTGACGCGTCCAGTGGGACATGGACACCTAACGGGCAGGCCAGCATGTATGTTGTCCACGCGAAAGGGGATTTTACAATAGGACAGTGGCCTGGGACATCAGCGGAAGATAAACCTTATCCATTCACTGCAGTTATCTATGTCATTCAGGATGCTGTAGGTCACAACGTGACTTTGCACGATAAGTATGCTATCCTGTCGGCAACACCTGTTATTAACAACAAGGCTAACAGTGTTACCTTGCTGCAATTAACGTATTGTGGTGTTGGTGATATTGTAGACGTAGTAATTGCACAACGTTAA
Genome Context
Gene Ontology
| Description | Category | Evidence (source) | |
|---|---|---|---|
| GO:0016798 | hydrolase activity, acting on glycosyl bonds | Molecular Function | IEA:UniProtKB-KW (UniProt) |