A0A060PYA7 · A0A060PYA7_9ALPH
- ProteinRibonucleoside-diphosphate reductase large subunit
- GeneUL39
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1243 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells, as well as reactivation from latency in infected hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Catalytic activity
- [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
RHEA-COMP:10700 CHEBI:50058 Position: n/n+3+ CHEBI:73316 + CHEBI:15377 = RHEA-COMP:10698 CHEBI:29950 Position: nCHEBI:29950 Position: n+3+ CHEBI:57930
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 672 | substrate | ||||
Sequence: T | ||||||
Binding site | 687-688 | substrate | ||||
Sequence: SC | ||||||
Site | 688 | Important for hydrogen atom transfer | ||||
Sequence: C | ||||||
Binding site | 718 | substrate | ||||
Sequence: G | ||||||
Active site | 897 | Proton acceptor | ||||
Sequence: N | ||||||
Binding site | 897-901 | substrate | ||||
Sequence: NLCTE | ||||||
Active site | 899 | Cysteine radical intermediate | ||||
Sequence: C | ||||||
Active site | 901 | Proton acceptor | ||||
Sequence: E | ||||||
Site | 914 | Important for hydrogen atom transfer | ||||
Sequence: C | ||||||
Binding site | 1074-1078 | substrate | ||||
Sequence: PTVTS | ||||||
Site | 1217 | Important for electron transfer | ||||
Sequence: Y | ||||||
Site | 1218 | Important for electron transfer | ||||
Sequence: Y | ||||||
Site | 1238 | Interacts with thioredoxin/glutaredoxin | ||||
Sequence: C | ||||||
Site | 1241 | Interacts with thioredoxin/glutaredoxin | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | ribonucleoside-diphosphate reductase complex | |
Molecular Function | ATP binding | |
Molecular Function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor | |
Biological Process | deoxyribonucleotide biosynthetic process | |
Biological Process | DNA replication | |
Biological Process | viral process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibonucleoside-diphosphate reductase large subunit
- EC number
- Short namesR1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageViruses > Duplodnaviria > Heunggongvirae > Peploviricota > Herviviricetes > Herpesvirales > Orthoherpesviridae > Alphaherpesvirinae > Simplexvirus > Simplexvirus pteropodidalpha1
Accessions
- Primary accessionA0A060PYA7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 688↔914 | Redox-active | ||||
Sequence: CYLVNPQTTTNKATLDALTHNVKDILAQRGGVGLCLQSFNDAHRKQASLMPALKVLDSLVAAYNHASRRPTGVCVYIEPWHSDIMSILRMKGVLAGEEAQRCDNLFSALWMPDLFFKRLIRHLEGETGVLWTLFDKAESMALSDFHGQEFENLYEVYEQMGLGNPMPIQDVAFAIVRSAATTGSPFIMFKDAVNRHYIYDTQGAAISGSNLCTEIVHPADKDSSGVC |
Keywords
- PTM
Expression
Keywords
- Developmental stage
Interaction
Subunit
Heterotetramer composed of a homodimer of the large subunit (R1) and a homodimer of the small subunit (R2). Larger multisubunit protein complex are also active, composed of (R1)n(R2)n.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-34 | Disordered | ||||
Sequence: MASFPNASNNQRSARTFKRPRRMEPSAAGAGPSN | ||||||
Region | 134-384 | Disordered | ||||
Sequence: GAISSAAPPSPPKLTKPANPPASPTPAYPSTTSLSSTTASSWTPLYSRPRSGDSESSTESEWEDEDADTRPRGGADSEFYLDFSTKKWQPEPNQGKDAASHPNPEAPMESAIKSESESEANTDSDSDSNSESESDAGATGETALAAGPTPTANPTSGCESESETETESLCDATLLSEDEFGSDEDFLVALPHPPDAGQCCSLSTSGPTSADDRQSSGNPPPAKPPRCPESPLAQPPTCPEAAAAHSDAACQ | ||||||
Compositional bias | 143-160 | Pro residues | ||||
Sequence: SPPKLTKPANPPASPTPA | ||||||
Compositional bias | 161-186 | Polar residues | ||||
Sequence: YPSTTSLSSTTASSWTPLYSRPRSGD | ||||||
Compositional bias | 279-304 | Polar residues | ||||
Sequence: AGPTPTANPTSGCESESETETESLCD | ||||||
Compositional bias | 331-349 | Polar residues | ||||
Sequence: QCCSLSTSGPTSADDRQSS | ||||||
Compositional bias | 351-368 | Pro residues | ||||
Sequence: NPPPAKPPRCPESPLAQP | ||||||
Domain | 1052-1074 | Ribonucleotide reductase large subunit | ||||
Sequence: WDLLRQSMMRFGLRNSQFIALMP |
Sequence similarities
Belongs to the ribonucleoside diphosphate reductase large chain family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,243
- Mass (Da)137,219
- Last updated2014-09-03 v1
- ChecksumE68D68AC350BE06C
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 143-160 | Pro residues | ||||
Sequence: SPPKLTKPANPPASPTPA | ||||||
Compositional bias | 161-186 | Polar residues | ||||
Sequence: YPSTTSLSSTTASSWTPLYSRPRSGD | ||||||
Compositional bias | 279-304 | Polar residues | ||||
Sequence: AGPTPTANPTSGCESESETETESLCD | ||||||
Compositional bias | 331-349 | Polar residues | ||||
Sequence: QCCSLSTSGPTSADDRQSS | ||||||
Compositional bias | 351-368 | Pro residues | ||||
Sequence: NPPPAKPPRCPESPLAQP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB825953 EMBL· GenBank· DDBJ | BAP00718.1 EMBL· GenBank· DDBJ | Genomic DNA |