Protein

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UniProt accession
A0AAE8XJX4 [UniProt]
Protein name
Hydrolase
RBP type
TSP
Evidence DepoScope
Probability 1,00
TSP
Evidence RBPdetect2
Probability 0,95
Protein sequence
MPKHVTEAAATAAYGALVQHSATIPAALGWGASPALSPRLTNLRGGGVIGDVGATPKALFATYSAAQAAPTNRFYASPAGDDTAAGTYAAPWRTIKKCIEAANAAGAPARILVRTGTYLSGQGFEAVSPTVDTAFVAEGGPVTVSNGIASASYTFAAHATHTNTYYINPTPTGGVSRVLDLTRVDEFGNYRELVKVSSEAIANDTPGSYHEGLALYIHRHDGAAVTAANTRVLQTKSNFVLSSEVNVYVGTEDGSPWVIEGSANSVAGVDPGAVLTYVAAPTNAASKAFVMENVRADFAGEPTAGANSFTVDKWNGVAAYFNCQGNAPSKDGFNAHNGGNLATKMLVLTVNCSATDTGRSVQSCNGLTLHENVIGIDVAGRYLRGRGGTVHNIGASKHYLLGTHIDGDLGDINSGGGIHPNALRVADSAEVWAERVTINMPPGAFAYRAVSGTAKIHRRDCEPTRQPDAGPGVFDTF
Physico‐chemical
properties
protein length:477 AA
molecular weight: 49297,20760 Da
isoelectric point:6,26544
aromaticity:0,07757
hydropathy:-0,09119

Domains

Domains [InterPro]
IPR012334
STR
60–423
IPR012334
DC_1219
STR
120–474
DC_1219
A0AAE8XJX4
1 477
Architecture
STR
STR 60-474 |
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
A0AAE8XJX4
1 477
Domain Start End Length (AA) Confidence
N-terminal 1 197 197 0,1891
Central domain 198 466 270 0,8310
C-terminal 467 477 10 0,3195
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
1-197
Central
198-466
C-terminal
467-477

Taxonomy

  Name Taxonomy ID Lineage
Phage Arthrobacter phage Klevey
[NCBI] 		2867481 Viruses > Duplodnaviria > Heunggongvirae > Uroviricota > Caudoviricetes
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: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
e747d01f59ad5d2eb3a30699fc1b74862d6eb1c887050c0b6c2baeee455de0f6
ESMFold
Source ESMFold
Method ESMFold
Resolution 0,7647
Oligomeric State monomer
Download PDB
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50