UniProt accession
A0A6J5MQ12 [UniProt]
Protein name
Dcm Site-specific DNA methylase
RBP type
TSP
Evidence DepoScope
Probability 1,00
Protein sequence
MSKILTHASFFSGVGGVDLGFERAGIRTVSVSEIDPFARSVLASRFPEVPQLGDIVALADRELSKPVQQSADEVQRCSRPVDGIGWTPSGDDWKAADIWSAGFPCQDLSVAGKRKGFADGKRSVLAFTFLNLVERFRPRWLVLENVPGLFTSNNGRDLLALLREVDELGYGVSWRTLDARFFGVPQRRRRVFLVASLGTDRSGEVLLECEGGCGHTQAGESSWSEVTGSIERSPFVAGALLARYHKGATSTVENGQLVVTTALTRGGLGGGFGADDNDAQGNKLVVGSEAYSGGVRAFDGMAGRVDNPNISAMGAAIPSQEDIQVEHNTYSIREDAKAGNFSATPINTALALNAVWPSVQSHHAQTFIASAYRKSKRAQSTEDHETWVEDGVANTINLFDSGDVRTTHAVVGSHYDGYNQKLEPDSAHRTLRVGRDSSDFVVPPAGVVEENPLLPIGMDSNRYKVCGNGVVCNVAEWIGHRLVEVDGKWTELR
Physico‐chemical
properties
protein length:493 AA
molecular weight: 53206,73820 Da
isoelectric point:5,55916
aromaticity:0,07911
hydropathy:-0,25578

Domains

Domains [InterPro]
IPR029063
STR
1–208
IPR001525
ATT
5–489
IPR029063
STR
5–484
IPR001525
ATT
6–22
IPR001525
ATT
7–64
IPR001525
ATT
8–480
IPR001525
ATT
137–151
A0A6J5MQ12
1 493
Architecture
ATT
ATT 1-489 |
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
A0A6J5MQ12
1 493
Domain Start End Length (AA) Confidence
N-terminal 1 86 86 0,3743
Central domain 87 285 200 0,0745
C-terminal 286 493 207 0,7862
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
1-86
Central
87-285
C-terminal
286-493

Taxonomy

  Name Taxonomy ID Lineage
Phage uncultured Caudovirales phage
[NCBI]
2100421 Uroviricota > Caudoviricetes > Peduoviridae > Maltschvirus maltsch >
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:0008168 methyltransferase activity Molecular Function IEA:UniProtKB-KW (UniProt)
GO:0032259 methylation Biological Process IEA:UniProtKB-KW (UniProt)

Tertiary structure

PDB ID
6e3a4355cd32d2de36efa435832f6c3cdcde7eccccea2f621f47b59329e41838
ESMFold
Source ESMFold
Method ESMFold
Resolution 0,5543
Oligomeric State monomer
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50