Protein

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UniProt accession
A0A8S5NQH0 [UniProt]
Protein name
Dockerin type 1
RBP type
TSP
Evidence RBPdetect
Probability 0,89
Protein sequence
MAEYNSAYTGQQIDVAVGAVIEKQEAWDNKVSTVTITIPKGRAKGDVDGDGKWTESDESLMMSISVGNVTPTDIERWCGDVNGDGAVTSADAREVQKMAKGIYNYPSLITDYYGNWIFDAISGSWSADISLPGVDVNTNLILNVFDPDAYANIIKAEITGTGIKVYMRMPPLSDVLCMGESGAGNGKSIIVSDVSDIFYATYGVTTIAELDSAYAAGRFMVCVNDGNTAPIARVSSAGYYYFGLTLTGKRYICSKSGAWSEKLASGGLLPTVTTSDNGKFLRVVDGAWAANEALPSDIGAAAESLSHQVTLTASGWNSTTKTQTVTCADILADVTKQEIHAMPVDTSAGNAYYSAGIMPVAQAANSLTFYAETIPTADIGVYVAIHPLKFS
Physico‐chemical
properties
protein length:391 AA
molecular weight: 41387,93470 Da
isoelectric point:4,47251
aromaticity:0,08951
hydropathy:0,01330

Domains

Domains [InterPro]
DC_0611
STR
9–391
DC_0611
IPR016134
RBD
40–107
IPR016134
IPR036439
RBD
43–109
IPR036439
cd14256
RBD
44–98
cd14256
IPR002105
RBD
44–97
IPR002105
IPR036439
RBD
45–99
IPR036439
A0A8S5NQH0
1 391
Architecture
STR
STR 9-391
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
A0A8S5NQH0
1 391
Domain Start End Length (AA) Confidence
N-terminal 1 33 33 0,7361
Central domain 34 234 202 0,7819
C-terminal 235 391 156 0,8705
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
1-33
Central
34-234
C-terminal
235-391

Taxonomy

  Name Taxonomy ID Lineage
Phage Myoviridae sp. ctagO6
[NCBI] 		2826667 Uroviricota > Caudoviricetes >
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
DAD96299.1 [NCBI]
Genbank nucleotide accession
BK015215 [NCBI]
CDS location
range 24492 -> 25667
strand +
CDS
ATGGCAGAATACAACTCCGCATACACGGGGCAGCAGATCGACGTCGCGGTCGGTGCGGTCATCGAGAAGCAGGAGGCGTGGGACAACAAGGTAAGCACAGTCACGATCACGATCCCAAAGGGGAGAGCAAAAGGCGATGTGGATGGGGACGGGAAGTGGACGGAGAGCGACGAGTCTCTCATGATGAGCATATCTGTCGGGAACGTAACGCCAACGGACATCGAAAGGTGGTGCGGAGATGTAAACGGAGATGGAGCCGTCACTTCGGCCGACGCAAGAGAAGTACAGAAGATGGCTAAGGGCATTTATAACTATCCTTCTTTGATAACCGACTATTATGGGAATTGGATTTTTGACGCTATCAGTGGAAGCTGGAGCGCGGACATTTCTTTACCGGGGGTTGACGTTAATACAAACCTTATTCTCAATGTTTTTGATCCCGATGCTTACGCAAATATCATCAAGGCCGAGATCACGGGTACTGGAATCAAGGTTTACATGAGAATGCCGCCATTGAGCGACGTGCTGTGCATGGGAGAATCCGGCGCAGGTAACGGTAAAAGCATAATTGTGTCGGACGTCTCCGATATCTTTTATGCCACATATGGGGTCACGACTATAGCGGAACTGGATAGCGCTTATGCCGCCGGAAGATTTATGGTTTGCGTTAATGATGGCAATACAGCGCCGATTGCCAGAGTTTCTTCTGCTGGATACTATTATTTCGGACTGACGCTTACGGGGAAGAGATACATATGCAGCAAATCTGGCGCATGGTCTGAGAAACTGGCAAGCGGCGGTCTTCTCCCCACCGTCACCACCTCAGACAATGGAAAGTTTCTGCGAGTCGTGGATGGGGCGTGGGCAGCAAACGAGGCGCTGCCTTCTGACATCGGGGCGGCCGCCGAGTCCCTCTCCCACCAAGTTACTCTGACGGCTTCCGGGTGGAACTCTACGACGAAGACGCAGACGGTCACATGCGCGGACATCCTTGCGGACGTGACGAAGCAGGAGATCCACGCGATGCCGGTCGACACGAGCGCGGGGAACGCGTACTACTCCGCCGGTATCATGCCGGTCGCGCAGGCGGCGAACAGTCTGACCTTCTACGCGGAGACGATCCCGACGGCGGACATTGGCGTGTACGTCGCGATCCACCCACTGAAGTTCTCGTGA

Genome Context

Genome Context

Gene Ontology

Description Category Evidence (source)
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds Molecular Function IEA:InterPro (UniProt)
GO:0000272 polysaccharide catabolic process Biological Process IEA:InterPro (UniProt)

Tertiary structure

PDB ID
09cb17f13d5e375b290647c0bfc302101d0084206722f00fdbfa62b0c046044a
ColabFold
Source ColabFold
Method ColabFold
Resolution 0,7531
Oligomeric State monomer
Download PDB
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50