UniProt accession
A0A8S5TCF7 [UniProt]
Protein name
Hydrolase
RBP type
TSP
Evidence RBPdetect
Probability 0,87
Protein sequence
MSINKVIYNGKTLIDISDSTVTDDNIEEGLIAYSGDGKRVVGTKMNLENRSKRKLIFIGDSYGDGYTPDGNTTGWCDKLKSKLVNCHFTANNIYINHKGGASFSNPSNNYLTLLKGVESQVNNKKMVTDVLIGGGYNELAYGDQKTTVQNCIKTLISYVQNTYPNAIIHFAPFGVAFKNRDNQFALKYKLLPMYKTVACYADLPFVVVPDAENVLSLENMMSSDGIHPNGWGLEYLSEFLKGYMLGTGSSAMEKRQLGVGLNGGTFTGTIYGQCLGDINIYRIMFDTTVKNLNSNGPNGFKLYTPTRTNAFPWRAPNMGYTDANAIIYANGGFYDVPVKFNVTNKNELYMQIKQCNSAHNNYQSYSNITQIQLDAWIVAENM
Physico‐chemical
properties
protein length:382 AA
molecular weight: 42415,55490 Da
isoelectric point:8,03851
aromaticity:0,11257
hydropathy:-0,31754

Domains

Domains [InterPro]
DC_1375
STR
2–366
IPR036514
STR
37–244
SSF52266
STR
52–244
cd00229
ENZ
55–240
IPR013830
ENZ
57–232
A0A8S5TCF7
1 382
Architecture
STR
STR 2-366 |
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
A0A8S5TCF7
1 382
Domain Start End Length (AA) Confidence
N-terminal 1 164 164 0,2725
Central domain 165 363 200 0,1853
C-terminal 364 382 18 0,9982
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
1-164
Central
165-363
C-terminal
364-382

Taxonomy

  Name Taxonomy ID Lineage
Phage Siphoviridae sp. ctVDC13
[NCBI]
2827880 Uroviricota > Caudoviricetes >
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
DAF60824.1 [NCBI]
Genbank nucleotide accession
BK032798 [NCBI]
CDS location
range 30275 -> 31423
strand +
CDS
ATGAGCATTAATAAGGTCATATACAACGGAAAGACATTGATTGATATATCAGACAGTACAGTAACTGATGATAACATTGAAGAAGGGTTGATTGCCTATTCAGGCGACGGGAAAAGGGTGGTAGGAACTAAGATGAATCTAGAAAACAGAAGCAAAAGAAAACTGATTTTTATTGGTGACAGTTATGGAGACGGTTATACCCCCGATGGTAATACGACAGGATGGTGCGATAAACTTAAAAGCAAGTTAGTTAATTGCCACTTTACTGCAAACAACATCTATATCAATCACAAGGGTGGTGCATCTTTTTCTAATCCATCCAATAACTATCTAACTCTTCTTAAAGGTGTAGAGTCGCAAGTCAACAACAAGAAAATGGTAACTGATGTATTGATTGGTGGAGGGTACAATGAACTGGCATATGGCGATCAAAAGACAACAGTGCAGAATTGTATTAAGACATTGATTAGTTATGTACAAAATACTTATCCAAATGCAATCATTCATTTTGCACCTTTTGGTGTTGCGTTTAAAAATAGGGATAATCAGTTTGCATTAAAATATAAATTGCTTCCGATGTATAAAACTGTAGCATGTTATGCCGATTTGCCATTCGTAGTAGTGCCTGATGCTGAAAATGTTCTTTCACTTGAAAATATGATGTCGAGCGATGGAATCCACCCGAATGGATGGGGATTAGAATACCTATCTGAATTTTTAAAAGGCTACATGCTAGGAACTGGAAGCAGTGCAATGGAAAAAAGACAATTAGGTGTTGGTTTAAATGGTGGAACATTTACAGGGACGATTTACGGACAGTGCTTAGGTGATATTAATATCTATAGAATTATGTTTGATACAACAGTCAAAAATCTTAATTCAAATGGGCCTAACGGCTTCAAACTATATACTCCTACTCGTACGAACGCATTTCCCTGGAGAGCTCCAAACATGGGATATACGGATGCAAATGCAATTATTTATGCAAACGGTGGCTTCTATGACGTTCCTGTTAAATTTAATGTAACAAATAAAAACGAACTATATATGCAGATCAAGCAGTGTAACTCTGCTCACAATAATTATCAGAGTTATTCGAACATCACTCAGATTCAGCTCGATGCTTGGATTGTCGCTGAAAATATGTAA

Genome Context

Genome Context

Gene Ontology

Description Category Evidence (source)
GO:0016787 hydrolase activity Molecular Function IEA:UniProtKB-KW (UniProt)

Tertiary structure

PDB ID
fc158c24857dd3161001602ba26847da8a51ba572eef92c5d7e45128fa893b96
ColabFold
Source ColabFold
Method ColabFold
Resolution 0,7879
Oligomeric State monomer
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50