UniProt accession
A0A8S5TR77 [UniProt]
Protein name
DNA (cytosine-5-)-methyltransferase
RBP type
TSP
Evidence DepoScope
Probability 0,86
Protein sequence
MKHLGDITKINGAEIEAVDVITGGSPCQDLSIAGKRAGLAGARSGLFMEQIRIVKEMREHDRANGRTGDMVRPRFMVWENVPGAFSSNGGQDFAAVLEEIIRIAEPEAPNIEVPEKGWNTWGGYHDEVGGRWSVAWRVHDAQHWGVAQRRRRISIVADFGGDTAGEILFERKSVSGYLTESGTARERLAADAESSSSYAVRIRGGCDGGGKGALVQEDKSGTLGTGNDQTIFCLQGNGIDRADTAGCNGKGWREDTSYTLNTIDRPAVCAYSFDSLSSNSMKSKNPHSGCREVEIAKTLDTTYPDPSKNQGGIAVVALDMTHACDVIRECGEVVPSLQARMGTGGNQVPLTYQQTTGTLSPGAHAGSYNGQDAYNDMLVVSSEISPTLRARASDPCREDMAAYIASVDCRNFCEGGETNGTLQAKSSGGASYNLQNTVRTGMIVRRLTPMECERLQGFPDHWTDIGEWRDSKGKLRKPSDSPRYKALGNSIALPFWDFLAKRISAQYLRPVTMGSLFDGIGGFPLVFERHNGKGTARWASEIEEFPIAVTKLRFGEE
Physico‐chemical
properties
protein length:557 AA
molecular weight: 60425,86730 Da
isoelectric point:5,81988
aromaticity:0,07361
hydropathy:-0,46068

Domains

Domains [InterPro]
IPR001525
ATT
1–510
IPR050390
Unmapped
2–60
IPR029063
STR
3–503
IPR001525
ATT
3–100
IPR018117
Unmapped
19–31
A0A8S5TR77
1 557
Architecture
ATT
STR
ATT 1-510 | STR 511-557
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
A0A8S5TR77
1 557
Domain Start End Length (AA) Confidence
N-terminal 1 73 73 0,0885
Central domain 74 432 360 0,6003
C-terminal 433 557 124 0,6270
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
1-73
Central
74-432
C-terminal
433-557

Taxonomy

  Name Taxonomy ID Lineage
Phage Siphoviridae sp. ctss15
[NCBI]
2825699 Uroviricota > Caudoviricetes >
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
DAF84713.1 [NCBI]
Genbank nucleotide accession
BK015908 [NCBI]
CDS location
range 17967 -> 19640
strand -
CDS
ATGAAGCACCTCGGCGATATCACGAAGATCAACGGTGCGGAGATCGAAGCCGTGGACGTTATCACGGGAGGCTCACCGTGCCAGGATTTGAGCATTGCAGGAAAACGCGCTGGGTTAGCCGGAGCAAGAAGCGGGTTATTCATGGAACAGATTCGCATCGTAAAGGAGATGAGGGAACATGACAGAGCGAACGGACGGACAGGTGACATGGTCCGACCTCGGTTTATGGTCTGGGAAAACGTGCCAGGAGCGTTCTCAAGCAACGGAGGGCAAGACTTCGCGGCAGTCCTCGAAGAGATTATCCGCATCGCAGAGCCGGAAGCCCCCAATATTGAAGTGCCTGAAAAAGGGTGGAACACCTGGGGGGGATACCACGATGAAGTGGGAGGACGATGGAGCGTGGCTTGGCGAGTGCATGACGCGCAACACTGGGGAGTCGCCCAACGTCGCCGTCGTATCTCGATTGTCGCAGATTTTGGAGGAGACACCGCAGGAGAAATATTGTTTGAGCGCAAAAGCGTGTCAGGGTATCTTACGGAGAGCGGAACGGCGCGGGAAAGACTTGCCGCCGACGCTGAAAGCAGTTCTTCTTATGCAGTCCGAATCAGGGGGGGCTGTGACGGAGGAGGAAAAGGAGCCTTAGTTCAAGAAGACAAGAGCGGGACGCTCGGCACCGGCAACGATCAGACGATTTTCTGCTTGCAGGGAAACGGGATCGACCGCGCAGACACCGCTGGATGCAATGGGAAAGGCTGGAGGGAGGATACAAGCTACACGCTAAACACCATCGATCGGCCGGCAGTCTGCGCGTACAGTTTTGACAGCCTTTCCAGCAATAGCATGAAAAGCAAAAATCCGCATAGCGGTTGCCGAGAAGTCGAAATTGCAAAAACTTTAGACACAACATACCCCGACCCAAGCAAGAACCAAGGCGGCATTGCAGTGGTTGCACTGGATATGACACACGCTTGTGACGTCATACGCGAGTGCGGCGAGGTCGTTCCCAGTTTGCAAGCAAGGATGGGCACAGGCGGCAACCAAGTGCCGCTGACGTATCAGCAAACGACCGGGACGCTTTCACCCGGCGCTCACGCTGGGAGCTACAACGGGCAGGACGCTTACAACGATATGTTGGTCGTATCGAGTGAAATCTCGCCTACGTTGAGAGCAAGGGCGAGTGACCCATGCCGCGAAGATATGGCGGCATATATTGCAAGCGTTGACTGCCGGAACTTTTGCGAGGGGGGAGAAACCAACGGAACATTACAGGCAAAATCGAGCGGCGGTGCCAGTTACAATTTGCAGAACACCGTGAGAACGGGCATGATCGTGCGCCGGCTTACGCCGATGGAGTGCGAACGGCTGCAAGGATTTCCAGACCACTGGACTGACATCGGCGAGTGGCGCGACAGTAAGGGCAAGCTGCGCAAGCCGAGCGATAGCCCGCGCTATAAGGCGCTGGGCAACTCCATTGCCCTGCCATTTTGGGACTTCCTGGCAAAACGTATCAGCGCGCAATATTTGCGCCCTGTTACGATGGGAAGCTTGTTTGACGGCATCGGCGGCTTTCCGCTGGTGTTTGAACGGCACAACGGAAAGGGCACGGCGCGCTGGGCGAGCGAGATCGAAGAGTTCCCCATTGCCGTGACAAAACTGAGATTCGGGGAGGAATGA

Genome Context

Genome Context

Gene Ontology

Description Category Evidence (source)
GO:0003886 DNA (cytosine-5-)-methyltransferase activity Molecular Function IEA:UniProtKB-EC (UniProt)
GO:0032259 methylation Biological Process IEA:UniProtKB-KW (UniProt)
GO:0099018 symbiont-mediated evasion of host restriction-modification system Biological Process IEA:UniProtKB-KW (UniProt)
GO:0052170 symbiont-mediated suppression of host innate immune response Biological Process IEA:UniProtKB-KW (UniProt)

Tertiary structure

PDB ID
fc3a34ae01f1462da2bc217b52aacd9ec7f2ee7fe2d85c928166b7794b5f9bc7
ColabFold
Source ColabFold
Method ColabFold
Resolution 0,6326
Oligomeric State monomer
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50