Protein

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UniProt accession
A0A8S5V812 [UniProt]
Protein name
Laminarinase-like protein
RBP type
TSP
Evidence RBPdetect
Probability 0,85
Protein sequence
MDIPDGAFDWKTNGYTPVFNDEFKTPTLDRSKWQPITGGEIVTQRKSYMDFNTNGRIEDGSVVFKATREAGKVVNGTAYEFFSAAIQSVKKFSGVLYFEARMALPPKSRWMSSTFKLVPTIPTEYNSWLKRMEVTITSSPQDDGTFIACEYICGGTARNSFITGTFKKQIIDVTNFHTYAFSIEEDRIKFIYDGEVVLEKVIAGETINGQIMTGAKPFDAVEWQPHIGLEFRGPWIAGLAEMLPQEMKVDYVRVFVQGAEEEEKVGNTIRGRKMRLIQG
Physico‐chemical
properties
protein length:279 AA
molecular weight: 31545,57540 Da
isoelectric point:5,64459
aromaticity:0,12186
hydropathy:-0,31326

Domains

Domains [InterPro]
IPR000757
ENZ
8–260
IPR000757
G3DSA:2.60.120.200
STR
9–257
G3DSA:2.60.120.200
IPR013320
STR
12–256
IPR013320
IPR050546
Unmapped
15–255
IPR050546
A0A8S5V812
1 279
Architecture
STR
STR 8-260 |
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
A0A8S5V812
1 279
Domain Start End Length (AA) Confidence
N-terminal 1 10 10 0,6675
Central domain 11 255 246 0,2826
C-terminal 256 279 23 0,5018
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
1-10
Central
11-255
C-terminal
256-279

Taxonomy

  Name Taxonomy ID Lineage
Phage Siphoviridae sp. ctsUl6
[NCBI] 		2825694 Uroviricota > Caudoviricetes >
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
DAG02848.1 [NCBI]
Genbank nucleotide accession
BK016217 [NCBI]
CDS location
range 229 -> 1068
strand +
CDS
ATGGATATACCAGACGGAGCTTTTGACTGGAAAACAAACGGGTACACTCCCGTGTTTAATGATGAGTTTAAGACACCAACACTAGATAGATCAAAATGGCAGCCGATTACTGGCGGTGAGATTGTGACGCAACGCAAGTCATATATGGACTTTAACACTAACGGACGCATAGAAGATGGTTCGGTCGTGTTTAAGGCGACGAGAGAAGCCGGCAAGGTAGTCAACGGCACGGCGTATGAGTTTTTCTCTGCTGCTATTCAGAGCGTAAAAAAGTTTTCAGGAGTCCTATACTTTGAAGCACGCATGGCGCTGCCGCCCAAATCCCGGTGGATGTCCTCGACATTCAAACTTGTGCCAACTATCCCGACAGAGTACAACAGCTGGCTAAAGCGTATGGAGGTTACTATTACCTCATCACCACAAGATGATGGTACTTTTATTGCTTGTGAGTACATTTGTGGCGGCACAGCTCGCAATAGCTTTATTACTGGCACATTTAAAAAGCAAATTATTGATGTAACCAACTTTCACACGTATGCCTTCTCAATTGAAGAGGATCGCATAAAGTTTATCTACGATGGTGAAGTTGTTCTGGAAAAAGTTATAGCAGGCGAGACTATCAACGGCCAAATAATGACAGGTGCTAAACCGTTTGATGCTGTCGAATGGCAGCCGCACATTGGCCTAGAGTTTCGCGGGCCTTGGATTGCCGGCCTAGCGGAGATGCTACCGCAAGAGATGAAAGTAGACTATGTCCGTGTCTTTGTGCAGGGCGCAGAGGAAGAGGAGAAGGTGGGCAACACTATCAGAGGTAGAAAAATGCGCTTAATCCAAGGCTAA

Genome Context

Genome Context

Gene Ontology

Description Category Evidence (source)
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds Molecular Function IEA:InterPro (UniProt)
GO:0005975 carbohydrate metabolic process Biological Process IEA:InterPro (UniProt)

Tertiary structure

PDB ID
50de0935775af25036c15e78db4ebfdec4963aaaa3fd10a4c1c0adad3a17b995
ESMFold
Source ESMFold
Method ESMFold
Resolution 0,8001
Oligomeric State monomer
Download PDB
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50