UniProt accession
A0A1C3S620 [UniProt]
Protein name
DNA condensation protein
RBP type
TSP
Evidence DepoScope
Probability 1,00
Protein sequence
MLPFVRMFDYGNIAPGVPTPKDFFLSVLSGKPTMLMLLDNGEVWGCSNNRQLLGLNSTASAYGKPYFVMENVKLMFAASWGTLLITKDNKVKYAGSQVMFKGSSNFWGTFQDFTTNYTSVGIDISTIEKVVFNSGTLFLRTTNGDLWGHGDNAKGYFGKGNTVANFTPTKIMTNTLDFWLTNRNAIVQTGPKQFYATGDNYYYQMGVTTTGYITTWTQIFKDATDDPEFEYNAMRTSHATLILYGKGTTFYASGRNYMSSWGVSGAPVDVNTTLYKGTLPFVPGDLTYFYAGREQAYWTNLIIDTNGVLYIAGTKNGGNTSNAPTFEVLPTPSSAVGFKCGTATRSYAIMDCTGNQFMYACGSTWSDPAGFTPMSTPLNHTWTHITDFKFNR
Physico‐chemical
properties
protein length:392 AA
molecular weight: 43338,39380 Da
isoelectric point:8,16126
aromaticity:0,15051
hydropathy:-0,20102

Domains

Domains [InterPro]
DC_0433
ATT
1–132
IPR009091
STR
15–231
IPR009091
STR
18–320
DC_0065
STR
109–315
A0A1C3S620
1 392
Architecture
ATT
STR
RBD
ATT 1-132 | STR 133-320 | RBD 321-392
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
A0A1C3S620
1 392
Domain Start End Length (AA) Confidence
N-terminal 1 116 116 0,1172
Central domain 117 381 266 0,6190
C-terminal 382 392 10 0,4106
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
1-116
Central
117-381
C-terminal
382-392

Taxonomy

  Name Taxonomy ID Lineage
Phage Escherichia phage vB_Eco_slurp01
[NCBI]
1874688 Uroviricota > Caudoviricetes > Asteriusvirus >
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)

No CDS data available.

Genome Context

Genome Context

Tertiary structure

PDB ID
24003f2194950d576a45cf411ba28f5f55558c347c0287cdc1277f24056d7512
ESMFold
Source ESMFold
Method ESMFold
Resolution 0,8004
Oligomeric State monomer
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50