UniProt accession
A0AAE9C1W0 [UniProt]
Protein name
Glycoside hydrolase
RBP type
TSP
Evidence DepoScope
Probability 1,00
TSP
Evidence RBPdetect
Probability 0,91
TSP
Evidence RBPdetect2
Probability 0,95
Protein sequence
MAYMKDSKGRRLDAYTPLSTSALAVTMPSGLGWDTTNFPFIALLRDYPGTPRSMAELNTTPEAIFDAYSTARSAPGATFYVSNSGLDTNNGTTAGTPFKSIWKAVAAANTAAVPSKIIVAAGTYFRTNNPWYNGGTGVIPTVDIAFIADGGRVITGTMDPPGTPTKDATQTNCYSYAVSSVNRVQDMVNFNAFGNQVEYQNVATAALCNATPNSWNLTSGTLYINRRDGAAVTNTTTRVFRPSTSCFTFSNPVNIYIGGTAGNDGWDCEGGSNIGVLAAFTNPPGTTRHVLIVKNSTFKYGGGVSDTVTRGVSVEGWQGLAWFSNCRADANQTDGFNFHNVYGATNRNGLTTNCTGYDNGRYPNQSNQGLTTHEDWVHVDIAGHYAGNHGGTVRCINTSKTWLAGTWVENDLGDQAYGGSVPPTAFRVDDTAVFWCDRTKVTMPAGGYSYVVSTGTAAIHKRDAWPSPHPDTPGTGTIDSY
Physico‐chemical
properties
protein length:481 AA
molecular weight: 51246,92140 Da
isoelectric point:6,23293
aromaticity:0,10811
hydropathy:-0,32121

Domains

Domains [InterPro]
IPR012334
STR
65–433
IPR011050
STR
69–430
DC_1219
STR
105–481
A0AAE9C1W0
1 481
Architecture
STR
STR 65-481
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
A0AAE9C1W0
1 481
Domain Start End Length (AA) Confidence
N-terminal 1 89 89 0,7201
Central domain 90 470 382 0,9013
C-terminal 471 481 10 0,2793
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
1-89
Central
90-470
C-terminal
471-481

Taxonomy

  Name Taxonomy ID Lineage
Phage Arthrobacter phage Sarge
[NCBI]
2885974 Uroviricota > Caudoviricetes > Sargevirus >
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)

No CDS data available.

Genome Context

Genome Context

Gene Ontology

Description Category Evidence (source)
GO:0044423 virion component Cellular Component IEA:UniProtKB-KW (UniProt)
GO:0016787 hydrolase activity Molecular Function IEA:UniProtKB-KW (UniProt)
GO:0051701 biological process involved in interaction with host Biological Process IEA:UniProtKB-ARBA (UniProt)
GO:0019058 viral life cycle Biological Process IEA:UniProtKB-ARBA (UniProt)

Tertiary structure

PDB ID
715074c5526a2a882d9f02ccc9a2f5f257048fb11b71345893499bd3a1d31512
ESMFold
Source ESMFold
Method ESMFold
Resolution 0,7874
Oligomeric State monomer
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50