Protein

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UniProt accession
A0A0S4KWC4 [UniProt]
Protein name
GDSL-like Lipase/Acylhydrolase
RBP type
TSP
Evidence RBPdetect
Probability 0,69
Protein sequence
MMNLTPNGTLSALATIGLEGIITQGYLSSGSVKPLRRNIAIYGDSRTANCSSGALPNKITENYGYASWLGQYSDGRIFFEPAFNFGVGGNTSSQWAARVNTVIAAPADVVVCLISTNDRTADFTLAQTQQNIEATVNKLKEAGKIVIFINETPRGGANALTPARQAIHEQVRAWINSYLPRLGVRVVDVWDSMLNTAAVTVDGLHFNPVGARIVAEALAREIKDLFNTPVPLPRFDSPFDATLNPYGQINTNPLLAGTTGTLVGSSNTTGVVATGYSVSGSSWAGMSVVASKEAAEVGEAQVLKFSGIPTSSGALYTFEQIISLPNAKLAANIKAVADIEFQLEGCLGVSLDFRFLDSGTFNSKCCDRYQDGFPMANVKVDGVQETPTTAITATCTEVKIRVSVYASQNVPMTGYVKIKQLAAIAA
Physico‐chemical
properties
protein length:426 AA
molecular weight: 45198,73970 Da
isoelectric point:5,84921
aromaticity:0,07981
hydropathy:0,07629

Domains

Domains [InterPro]
IPR051532
Unmapped
4–225
IPR051532
IPR036514
STR
31–224
IPR036514
SSF52266
STR
35–226
SSF52266
SSF52266
STR
38–226
SSF52266
cd00229
ENZ
39–220
cd00229 DC_2015
IPR013830
ENZ
42–213
IPR013830
A0A0S4KWC4
1 426
Architecture
STR
RBD
STR 31-226 | RBD 227-417 |
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
A0A0S4KWC4
1 426
Domain Start End Length (AA) Confidence
N-terminal 1 32 32 0,8444
Central domain 33 233 202 0,5836
C-terminal 234 426 192 0,9959
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
1-32
Central
33-233
C-terminal
234-426

Taxonomy

  Name Taxonomy ID Lineage
Phage Pseudomonas phage VCM
[NCBI] 		1729937 Uroviricota > Caudoviricetes > Vandenendeviridae > Kremarvirus > Kremarvirus VCM
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:0016787 hydrolase activity Molecular Function IEA:UniProtKB-KW (UniProt)

Tertiary structure

PDB ID
674af9a346a861261714bbcb67e58ea40813526773c1d62cd2023d51d569bf31
ESMFold
Source ESMFold
Method ESMFold
Resolution 0,8045
Oligomeric State monomer
Download PDB
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50