A0A126HHJ6 · A0A126HHJ6_9CAUD
- ProteinSingle-stranded DNA-binding protein
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids308 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Single-stranded DNA-binding protein that participates in viral DNA replication, recombination, and repair. Coats the lagging-strand ssDNA as the replication fork advances. Stimulates the activities of viral DNA polymerase and the replicative helicase, probably via its interaction with the helicase assembly factor. Together with the replicative helicase and the helicase assembly factor, promotes pairing of two homologous DNA molecules containing complementary single-stranded regions and mediates homologous DNA strand exchange. Promotes also the formation of joint molecules. mRNA specific autogenous translational repressor.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | metal ion binding | |
Molecular Function | single-stranded DNA binding | |
Biological Process | bidirectional double-stranded viral DNA replication | |
Biological Process | DNA recombination | |
Biological Process | DNA repair |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameSingle-stranded DNA-binding protein
- Short namesSSB protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageViruses > Duplodnaviria > Heunggongvirae > Uroviricota > Caudoviricetes > Straboviridae > Schizotequatrovirus
Accessions
- Primary accessionA0A126HHJ6
Proteomes
Interaction
Subunit
Homodimer in the absence of DNA, monomer when binding DNA. Interacts with the DNA helicase assembly protein; a ternary complex between the helicase assembly protein, the single-stranded DNA-binding protein and ssDNA is an obligatory intermediate in the helicase loading mechanism. Part of the replicase complex that includes the DNA polymerase, the polymerase clamp, the clamp loader complex, the single-stranded DNA binding protein, the primase, the replicative helicase and the helicase assembly factor. Interacts (via C-terminus) with the viral SF1 dDA helicase. Interacts with the viral SF2 UvsW repair helicase.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-26 | Disordered | ||||
Sequence: MSMFKRKSPAKLQEKLEQMSSKKSFD | ||||||
Region | 5-9 | LAST | ||||
Sequence: KRKSP | ||||||
Compositional bias | 8-26 | Basic and acidic residues | ||||
Sequence: SPAKLQEKLEQMSSKKSFD | ||||||
Domain | 39-238 | Bacteriophage T4 Gp32 single-stranded DNA-binding | ||||
Sequence: GNGSAVIRFLPAKGEDDLPFVKIFTHGFKENGNWYIENCPSTIDLPCPCCQANGELWKTENEDNQNIARKRKRTLSYWANIVVIKDEAAPENEGKVFKYRFGKKILDKITQAAQADEDLGVPGMDVTCVFDGANFSLKAKKVSGFPNYDDSKFGPSTELYGGDEAKLKEVWDQMHDLNAIIAPSAFKSEADLQKRFLQVT | ||||||
Compositional bias | 258-289 | Polar residues | ||||
Sequence: TGAPAQANAPRTVAKPSATIDTDDTPASQEPV | ||||||
Region | 258-293 | Disordered | ||||
Sequence: TGAPAQANAPRTVAKPSATIDTDDTPASQEPVTDSV |
Domain
The acidic C-terminus is involved in modulating the ssDNA binding properties. The N-terminus LAST motif is involved in the cooperative binding of the protein to single-stranded nucleic acids.
The acidic C-terminus is involved in modulating the ssDNA binding properties. The N-terminus LAST motif is involved in the cooperative binding of the protein to ssDNA.
Sequence similarities
Belongs to the Tequatrovirus single-stranded DNA-binding protein family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length308
- Mass (Da)33,924
- Last updated2016-05-11 v1
- ChecksumBB79750C1E899690
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 8-26 | Basic and acidic residues | ||||
Sequence: SPAKLQEKLEQMSSKKSFD | ||||||
Compositional bias | 258-289 | Polar residues | ||||
Sequence: TGAPAQANAPRTVAKPSATIDTDDTPASQEPV |