UniProt accession
A0A8S5U6K9 [UniProt]
Protein name
Cytosine specific methyltransferase
RBP type
TSP
Evidence DepoScope
Probability 1,00
Protein sequence
MSNLTLGSLFDGSGGFSLAGMMAGITPIWASEIEPFPIRVTTKRIPHMKHYGDISKMNGGKIEPVDIITFGSPCQNLSLAGKREGLNGEKSSMFFEAIRVIKEMRENTNGEYPRWIVWENVPGAMSSSKGQDFRTVLEEICKIKDETVHIPMPEKKWTTAGEIVGNDYSVAYRILDAQYFGVPQRRRRIFLVADFAGECAGKVLFESESVFGNFKKSICSRQGTAGTAETGIGETGTICLNDQGGERIDVTQDKTTTLRAQAHHPTCVMFENHSQDTRYIGPLEVSQTVLATFGTGGNNQPFVVHTPKTLKIRCGCDGGGKGALIQENKSATLSCNNDQTLFEPKVYGICSNDSNSMKSDNPNSGIYAADTSRTIDCGGVNPSSNQGGMAVVALQGSIIGRKEKNGSNGSGFNQDTSFTLNTVDRHAVAYGIDRAAFNQGQNALYDFAIEKEKQPTMVAKGPGAVAEPAYSASKASFFTSAEKECANTLVASDYKDPPLVNDTNGTEYIVRRLTPKECALLQGFPVWWCDGLKTENPTEEEIQKWSDIFENRRKALCKSTKPKTRNQIIKWLKNPHSDSAEYTMWGNGVALPCVFYVLNGIAHYAELTNSVM
Physico‐chemical
properties
protein length:612 AA
molecular weight: 66916,75650 Da
isoelectric point:6,41095
aromaticity:0,08333
hydropathy:-0,40980

Domains

Domains [InterPro]
IPR029063
STR
1–225
IPR029063
STR
4–602
IPR001525
ATT
4–319
IPR050750
Unmapped
4–598
IPR001525
ATT
6–140
A0A8S5U6K9
1 612
Architecture
ATT
STR
ATT 1-319 | STR 320-602 |
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
A0A8S5U6K9
1 612
Domain Start End Length (AA) Confidence
N-terminal 1 299 299 0,0398
Central domain 300 500 202 0,7216
C-terminal 501 612 111 0,8332
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
1-299
Central
300-500
C-terminal
501-612

Taxonomy

  Name Taxonomy ID Lineage
Phage Siphoviridae sp. ctEJj1
[NCBI]
2825395 Uroviricota > Caudoviricetes >
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
DAF90061.1 [NCBI]
Genbank nucleotide accession
BK016020 [NCBI]
CDS location
range 6684 -> 8522
strand -
CDS
ATGAGTAATTTAACACTTGGCTCGTTATTTGACGGCAGCGGGGGTTTTTCTCTTGCCGGAATGATGGCTGGAATTACGCCTATATGGGCGAGTGAAATCGAACCATTTCCTATTCGGGTTACTACCAAGCGTATTCCGCATATGAAACACTACGGGGATATTTCAAAAATGAACGGCGGAAAGATTGAGCCTGTTGATATAATTACATTCGGGAGCCCTTGTCAAAACTTGTCTTTGGCGGGAAAACGTGAAGGGTTAAACGGTGAAAAATCATCAATGTTTTTTGAGGCGATTCGGGTTATAAAGGAAATGAGGGAGAATACAAATGGAGAATATCCGAGATGGATTGTGTGGGAGAATGTGCCGGGAGCAATGTCAAGCTCAAAAGGACAGGATTTTAGGACAGTCCTTGAAGAAATCTGCAAAATCAAAGATGAAACCGTACATATTCCTATGCCTGAAAAGAAATGGACAACAGCCGGAGAAATTGTGGGAAATGATTATTCCGTTGCCTATCGAATACTCGATGCGCAATACTTCGGAGTCCCTCAAAGACGCAGAAGAATCTTTCTTGTCGCAGATTTTGCAGGAGAATGTGCCGGAAAAGTATTATTTGAGTCAGAGAGCGTGTTCGGGAATTTTAAGAAGAGCATCTGTTCGCGGCAAGGAACTGCCGGAACTGCTGAAACGGGCATTGGAGAAACAGGCACAATATGTTTAAACGATCAAGGCGGAGAACGTATAGATGTGACGCAAGACAAAACAACTACTTTGAGAGCTCAGGCACATCATCCGACGTGTGTAATGTTTGAAAATCACTCTCAAGATACAAGATATATAGGTCCGTTGGAAGTATCGCAGACAGTGCTTGCAACTTTCGGAACGGGCGGTAATAATCAGCCGTTTGTTGTGCATACACCGAAAACTTTAAAAATCAGATGCGGATGTGACGGCGGCGGTAAAGGTGCATTGATACAAGAAAATAAATCAGCAACATTAAGCTGTAATAATGACCAGACCTTATTTGAACCGAAAGTGTACGGGATATGTTCAAACGACAGCAATTCGATGAAGTCTGACAACCCGAACAGCGGAATATATGCGGCAGATACTTCTCGTACCATTGACTGCGGAGGTGTAAATCCGTCATCTAATCAAGGAGGAATGGCTGTTGTTGCATTACAGGGCTCAATAATTGGACGTAAGGAGAAAAACGGGTCGAATGGCAGCGGATTTAATCAGGATACATCATTTACATTAAATACAGTTGACCGGCATGCGGTTGCATACGGAATTGACCGTGCTGCATTTAATCAAGGACAAAATGCGTTATATGATTTTGCAATAGAAAAAGAGAAACAGCCGACAATGGTGGCAAAAGGTCCGGGAGCGGTAGCTGAACCTGCATATTCGGCAAGCAAGGCATCATTCTTTACAAGTGCCGAAAAAGAATGTGCAAATACACTTGTTGCAAGCGATTACAAAGACCCTCCGCTTGTAAATGATACAAACGGTACGGAATATATAGTAAGACGTCTGACACCTAAAGAATGTGCTCTGCTGCAAGGGTTCCCTGTATGGTGGTGTGACGGTTTGAAAACAGAAAATCCTACGGAAGAAGAAATTCAGAAATGGTCGGATATTTTTGAAAATCGCAGAAAAGCACTTTGTAAAAGTACAAAACCGAAAACAAGAAATCAGATTATAAAGTGGCTTAAAAATCCTCATTCCGACAGTGCGGAATATACGATGTGGGGAAATGGTGTTGCACTTCCGTGCGTGTTCTATGTATTGAACGGAATTGCTCACTATGCTGAACTCACAAATTCTGTAATGTAA

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)
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
bed1c3d5906f307cd663f05a9cb1275e61058c61b434548374f3f5a3abea9e42
ColabFold
Source ColabFold
Method ColabFold
Resolution 0,6651
Oligomeric State monomer
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50