Protein

View in Explore
UniProt accession
A0A0K2FL61 [UniProt]
Protein name
Glycosyl hydrolase
RBP type
TSP
Evidence DepoScope
Probability 1,00
TF
Evidence GenBank
Probability 1,00
TF
Evidence Phold
Probability 1,00
TSP
Evidence RBPdetect
Probability 0,90
TSP
Evidence RBPdetect2
Probability 0,95
TF
Evidence UniProt/TrEMBL
Probability 1,00
Protein sequence
MIYVKDFTGITEAVKIQNAINAAAVATSSSKTVMLEEKDYYLESSLTLLNDVELLFGYRSRLVIGGNFPVLLIGRNASVTNPFIAIDAPTFDSPVFYLDGKNKYYNTWNKTAIKDGVVLNWTGSHKGVGIRFYSGGTDHEISFVDTSNIKLVGLRKGIELEAKAPATGMAWVNANRFDKISIEDCVEMITIDSSETIPNECSGNTFSNLQLQPSTATTKVLKVSGQHNRFDGMLWDISLIPTAKFVDITANSSFTKIDFNRSLPSTKVQDNGASTIVL
Physico‐chemical
properties
protein length:278 AA
molecular weight: 30473,25690 Da
isoelectric point:5,68369
aromaticity:0,09353
hydropathy:-0,05180

Domains

Domains [InterPro]
IPR011050
STR
15–219
IPR011050
IPR011050
STR
15–230
IPR011050
DC_0399
RBD
213–278
DC_0399
A0A0K2FL61
1 278
Architecture
STR
RBD
STR 15-230 | RBD 231-278
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
A0A0K2FL61
1 278
Domain Start End Length (AA) Confidence
N-terminal 1 11 11 0,8574
Central domain 12 267 257 0,9941
C-terminal 268 278 10 0,2276
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
1-11
Central
12-267
C-terminal
268-278

Taxonomy

  Name Taxonomy ID Lineage
Phage Bacillus phage Eyuki
[NCBI] 		1690431 Uroviricota > Caudoviricetes > Herelleviridae > Wphvirus > Wphvirus megatron
Host Bacillus thuringiensis serovar kurstaki
[NCBI] 		29339 Bacteria > Firmicutes > Bacilli > Bacillales > Bacillaceae > Bacillus

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
ALA46742.1 [NCBI]
Genbank nucleotide accession
KT207918 [NCBI]
CDS location
range 33649 -> 34485
strand +
CDS
ATGATATATGTGAAGGATTTTACTGGGATTACTGAGGCTGTCAAGATACAGAATGCTATCAATGCGGCAGCCGTAGCAACATCTTCATCAAAGACTGTCATGCTAGAAGAGAAAGATTATTACCTAGAGTCATCTCTTACTTTGTTAAATGATGTAGAGTTATTGTTTGGCTATCGTTCAAGATTAGTTATTGGCGGTAATTTCCCTGTACTACTAATAGGGCGCAATGCTTCTGTTACAAATCCATTCATAGCTATCGATGCACCAACTTTCGATTCACCTGTCTTTTATCTTGATGGTAAAAATAAATATTACAACACATGGAATAAGACAGCTATAAAAGACGGTGTCGTTCTCAACTGGACAGGTTCGCATAAAGGTGTGGGTATCCGTTTCTACTCTGGAGGAACCGACCACGAGATTTCATTCGTAGATACATCGAATATCAAACTAGTAGGTTTAAGAAAAGGTATTGAGCTAGAAGCTAAAGCTCCAGCTACTGGAATGGCTTGGGTGAATGCAAATCGTTTCGATAAGATATCAATTGAAGATTGCGTAGAGATGATTACGATTGATAGCAGCGAGACAATCCCGAATGAATGTAGTGGTAATACTTTCTCCAATCTTCAACTACAGCCATCTACCGCAACTACAAAAGTCTTAAAAGTAAGTGGACAGCATAACCGATTCGATGGTATGCTCTGGGATATCTCTTTAATACCTACAGCTAAGTTTGTAGATATTACAGCGAATAGTTCCTTTACGAAGATAGATTTTAACCGTTCCTTACCTAGTACGAAAGTACAAGATAATGGAGCAAGTACAATTGTACTTTAG

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
1fd4296036af64a834d2d8ec40f6f48a8cc0547c162970f958fb3b99816cba16
ESMFold
Source ESMFold
Method ESMFold
Resolution 0,9162
Oligomeric State monomer
Download PDB
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50