A0A7S5SRR8 · A0A7S5SRR8_9VIRU
- ProteinPolyprotein P1234
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids2489 (go to sequence)
- Protein existencePredicted
- Annotation score5/5
Function
function
Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2.
Catalytic activity
- 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = L-aspartyl-[protein] + ADP-D-ribose + H+This reaction proceeds in the forward direction.
- 5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + H2O = L-glutamyl-[protein] + ADP-D-ribose + H+This reaction proceeds in the forward direction.
- GTP + S-adenosyl-L-methionine = N7-methyl-GTP + S-adenosyl-L-homocysteine
- N7-methyl-GTP + L-histidyl-[protein] = N(tele)-(N7-methylguanosine 5'-phospho)-L-histidyl-[protein] + diphosphateThis reaction proceeds in the forward direction.
- N(tele)-(N7-methylguanosine 5'-phospho)-L-histidyl-[protein] + a 5'-end diphospho-(purine-ribonucleoside) in mRNA + H+ = a 5'-end (N7-methyl 5'-triphosphoguanosine)-(purine-ribonucleoside) in mRNA + L-histidyl-[protein]
Cofactor
Protein has several cofactor binding sites:
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 1016 | For cysteine protease nsP2 activity | ||||
Sequence: C | ||||||
Active site | 1086 | For cysteine protease nsP2 activity | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasmic vesicle membrane | |
Cellular Component | host cell cytoplasmic vesicle membrane | |
Cellular Component | host cell filopodium | |
Cellular Component | host cell nucleus | |
Cellular Component | host cell plasma membrane | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | cysteine-type peptidase activity | |
Molecular Function | GTP binding | |
Molecular Function | helicase activity | |
Molecular Function | metal ion binding | |
Molecular Function | mRNA methyltransferase activity | |
Molecular Function | RNA binding | |
Molecular Function | RNA-dependent RNA polymerase activity | |
Biological Process | 7-methylguanosine mRNA capping | |
Biological Process | DNA-templated transcription | |
Biological Process | methylation | |
Biological Process | mRNA modification | |
Biological Process | proteolysis | |
Biological Process | symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity | |
Biological Process | viral RNA genome replication |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended namePolyprotein P1234
- Alternative names
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Kitrinoviricota > Alsuviricetes > Martellivirales > Togaviridae > Alphavirus
Accessions
- Primary accessionA0A7S5SRR8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Host cell membrane ; Lipid-anchor
Host cytoplasmic vesicle membrane ; Lipid-anchor
Host cytoplasmic vesicle membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Interaction
Subunit
Interacts with RNA-directed RNA polymerase nsP4. Interacts with mRNA-capping enzyme nsP1. Interacts with KPNA1/karyopherin-alpha1; this interaction probably allows the active transport of protease nsP2 into the host nucleus.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 32-263 | Alphavirus-like MT | ||||
Sequence: EARQVSANDHANARAFSHLAIKLIESEVPKDRVILDIGSAPARRMFAEHRYHCVCPMMTAEDPERMSRYVDRLKAESMLITNRNLANKMQDLRDVLATPALETESICLKTDSSCEMRGDVAVYQDVYAVHAPSSIYCQAIKGVRTVYWIGFDTTPFAFDALAGSYPLYSTNWADEKVLESRNIGLCASTLSEGKRRGWSICKSKKLKPSDNILFSVGSTLYHESRKMLKSWH | ||||||
Domain | 679-994 | +RNA virus helicase C-terminal | ||||
Sequence: CKPRSMAKGLVLVGELTNPPYHEMAYESLNYRPSNVHDVEIVGVYGVPGSGKSGIIKQLVGPDDLVSSGKKENCLEIQRDVKQQRGLSIIARTVDSVLLNGVKRPVNVLFIDEAFACHAGTLLALIAIVKPKSKVILCGDPKQCGFFNMMQMKVNYNMEICDRVFNKSISRRCTQAVTAIVSTLHYDGKMRTVNPIIGNPVVDTTGSTKPKKGDLILTCFRGWVKQLQLDYRGYEVMTAAASQGLTRHGVYAVRQKVNENPLYALQSEHVNVLLTRTDNTLVWKTLSGDPWIKVLTSIPKGNFSATMQEWQREHDE | ||||||
Domain | 1007-1329 | Peptidase C9 | ||||
Sequence: DVFVGKTKVCWAKTLAPVLRTAGYTLTATEWGSLIPAFEDDEAFSPEVALNMICTRLFGHDLDSGLFSLEAVAMTYKDNHWDNSPGGKMWGFNEQVFNTLARRFPIMRQAIQHRQCALLQEHRIAPIEECPPIVPVNRELPHPLCTVILDRVRNNNSIYWKQLPGDTVMYIGMQAPNFGSKRVEWLGPLECGAASVKTDLSLGVPPTMGRYDGVFVDVPSRAMEHYKRCEEHAMKLRMIAGDSLRHLKPGAWMLVRTYGYADRISEVVLTTLLKKFRTYTVIQADLITCNAEVLILMKGFDNGNRNVSLARFSQATCGAFRGV | ||||||
Domain | 1325-1494 | Macro | ||||
Sequence: AFRGVQPAGSAPMYTVVRADIRTAETEAVVNAANPRGVPGDGVCGAVARRWPGSFVTGRIPVGECRAVRAEGTLILHAVGPDFRKVDEMSGGELLYKAYQACAKEVMKNGVKTVAVPLLSTGVYAGSKDRLEQSMMCLMDAFDATEANVHIYCRDKKWEERLKNIIKDKD | ||||||
Domain | 2243-2358 | RdRp catalytic | ||||
Sequence: DPVLETDIASFDKSQDDAMALTALMILEDLGVDTSLMDLIEVSFGEITSVHLPTGTRFRFGAMMKSGMFLTLFVNTILNVVIASRILEDRLTNSRCAAFIGDDNIIHGVVSDRLMA |
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,489
- Mass (Da)278,474
- Last updated2021-06-02 v1
- Checksum6AE344D80B95E822
Keywords
- Coding sequence diversity