A0A455LI28 · A0A455LI28_EAV
- ProteinReplicase polyprotein 1ab
- GeneORF1ab
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids3175 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
Catalytic activity
- ATP + H2O = ADP + phosphate + H+
- ATP + H2O = ADP + phosphate + H+
- uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-RNA
Features
Showing features for active site, site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 164 | For Nsp1 papain-like cysteine proteinase activity | ||||
Sequence: C | ||||||
Active site | 230 | For Nsp1 papain-like cysteine proteinase activity | ||||
Sequence: H | ||||||
Site | 260-261 | Cleavage; by PCP | ||||
Sequence: GG | ||||||
Active site | 270 | For Nsp2 cysteine proteinase activity | ||||
Sequence: C | ||||||
Binding site | 319 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 332 | For Nsp2 cysteine proteinase activity | ||||
Sequence: H | ||||||
Binding site | 349 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 354 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 356 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Site | 831-832 | Cleavage; by Nsp2 cysteine proteinase | ||||
Sequence: GG | ||||||
Site | 1064-1065 | Cleavage; by 3CLSP | ||||
Sequence: EG | ||||||
Active site | 1103 | Charge relay system; for 3C-like serine proteinase activity | ||||
Sequence: H | ||||||
Active site | 1129 | Charge relay system; for 3C-like serine proteinase activity | ||||
Sequence: D | ||||||
Active site | 1184 | Charge relay system; for 3C-like serine proteinase activity | ||||
Sequence: S | ||||||
Site | 1268-1269 | Cleavage; by 3CLSP; in major pathway | ||||
Sequence: ES | ||||||
Site | 1430-1431 | Cleavage; by 3CLSP; in minor pathway | ||||
Sequence: EG | ||||||
Site | 1452-1453 | Cleavage; by 3CLSP; in minor pathway | ||||
Sequence: ES | ||||||
Site | 1575-1576 | Cleavage; by 3CLSP | ||||
Sequence: EA | ||||||
Site | 1677-1678 | Cleavage; by 3CLSP | ||||
Sequence: EG | ||||||
Site | 2370-2371 | Cleavage; by 3CLSP | ||||
Sequence: ES | ||||||
Binding site | 2374 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2377 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2387 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2392 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2395 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2399 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2402 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2403 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2412 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2414 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2423 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2426 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Site | 2429 | Involved in mRNA transcription process | ||||
Sequence: S | ||||||
Site | 2837-2838 | Cleavage; by 3CLSP | ||||
Sequence: QS | ||||||
Active site | 2963 | |||||
Sequence: H | ||||||
Active site | 2978 | |||||
Sequence: H | ||||||
Active site | 3007 | |||||
Sequence: K | ||||||
Site | 3056-3057 | Cleavage; by 3CLSP | ||||
Sequence: EG |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | host cell membrane | |
Cellular Component | host cell perinuclear region of cytoplasm | |
Cellular Component | membrane | |
Molecular Function | ATP binding | |
Molecular Function | cysteine-type endopeptidase activity | |
Molecular Function | endonuclease activity | |
Molecular Function | hydrolase activity, acting on acid anhydrides | |
Molecular Function | lyase activity | |
Molecular Function | RNA binding | |
Molecular Function | RNA helicase activity | |
Molecular Function | RNA nuclease activity | |
Molecular Function | RNA-dependent RNA polymerase activity | |
Molecular Function | serine-type endopeptidase activity | |
Molecular Function | serine-type exopeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | DNA-templated transcription | |
Biological Process | proteolysis | |
Biological Process | viral protein processing | |
Biological Process | viral RNA genome replication | |
Biological Process | viral translational frameshifting |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameReplicase polyprotein 1ab
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Nidovirales > Arnidovirineae > Arteriviridae > Equarterivirinae > Alphaarterivirus > Alphaarterivirus equid
- Virus hosts
Accessions
- Primary accessionA0A455LI28
Subcellular Location
UniProt Annotation
GO Annotation
Host membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 603-621 | Helical | ||||
Sequence: ITGALSLVLNLLGQVGYIS | ||||||
Transmembrane | 627-646 | Helical | ||||
Sequence: AAYVPCTVFDLCSFAILYLC | ||||||
Transmembrane | 832-853 | Helical | ||||
Sequence: GWIYGLCYFVLVVVSTFTCLPI | ||||||
Transmembrane | 903-923 | Helical | ||||
Sequence: YWIAAVTSGLVVLLVCHRLAI | ||||||
Transmembrane | 935-958 | Helical | ||||
Sequence: LVLLVFPWASVGLLLACSLAGAAV | ||||||
Transmembrane | 970-995 | Helical | ||||
Sequence: LFFPQAALVTMGYWACVAALAVYSLM | ||||||
Transmembrane | 1318-1343 | Helical | ||||
Sequence: LLWLCCLFTPLSMRLCLFHLVCATVT | ||||||
Transmembrane | 1386-1409 | Helical | ||||
Sequence: WAIGAVLAVCSVTMLAAALGYTLL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Glycosylation | 1501 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N |
PTM databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 66-156 | Peptidase C31 | ||||
Sequence: SPVPVGHKFLIGWYRAAKVTGRYNFLELLQHPAFAQLRVVDARLAIEEASVFISTDHASAKRFPGARFALTPVYANAWVVSPAANSLIVTI | ||||||
Domain | 157-260 | Peptidase C32 | ||||
Sequence: DQEQDGFCWLKLLPPDRREAGLRLYYNHYREQRTGWLSKTGLRLWLGDLGLGINASSGGLKFHIMRGSPQRAWHITTRSCKLKSYYVCDISEADWSCLPAGNYG | ||||||
Domain | 261-360 | Peptidase C33 | ||||
Sequence: GYNPPGDGACGYRCLAFMNGATAVSAGCSSDLWCDDELAYRVFQLSPTFTVTIPGGRVCPNAKHVMICDKQHWRVKRAKGVGLCLDESCFRGTCNCQRMS | ||||||
Region | 388-454 | Disordered | ||||
Sequence: TTEEQSRPVPAPRARPSVNSSGDGKDPAPVPPVPKPRTKLVKPNPTQAPIPAPRTRPPGTSAQEPPV | ||||||
Compositional bias | 433-447 | Pro residues | ||||
Sequence: TQAPIPAPRTRPPGT | ||||||
Domain | 1065-1268 | Peptidase S32 | ||||
Sequence: GLFRSPKARGNVGFVAGSSYGTGSVWARDNEVVVLTASHVVGRANMATLKIGDTMLTLTFKKNGDFAEAVTTQSELPGHWPQLHFAQPTTGPASWCTATGDEEGLLSGEVCLAWTTSGDSGSAVVQGDAVVGIHTGSNTSGVAYVTTPSGKLLGADTVTLSSLSKHFTGPLTSIPKDIPDNIIADVDTVPRSLAMLIDGLSNRE | ||||||
Region | 1577-1614 | Disordered | ||||
Sequence: NDTPVKPVPSRRRRKALPKGAQLEWDRHQEEKRNAGDD | ||||||
Compositional bias | 1593-1614 | Basic and acidic residues | ||||
Sequence: LPKGAQLEWDRHQEEKRNAGDD | ||||||
Domain | 1716-1883 | NiRAN | ||||
Sequence: LADPVEAVNQLNLRAPHIFPGDVGRRTFADSKDKGFVALHSRTMFLAARDFLFNIKFVCDEEFTKTPKDTLLGYVRACPGYWFIFRRTHRSLIDAYWDSMECVYALPTISDFDVSPGDVAVTGERWDFESPGGGRSKRLTADLVHAFQGYHGASYSYDDKVAVAVSGD | ||||||
Domain | 2116-2251 | RdRp catalytic | ||||
Sequence: KYCLETDLESCDRSTPALVRWFATNLIFELAGQPELVHSYVLNCCHDLVVAGSVAFTKRGGLSSGDPITSISNTIYSLVLYTQHMLLCGLEGYFPEIAEKYLDGSLELRDMFKYVRVYIYSDDVVLTTPNQHYAAS | ||||||
Domain | 2371-2438 | AV ZBD | ||||
Sequence: SAVCTVCGAAPVAKSACGGWFCGNCVPYHVGHCHTTSLFANCGHDIMYRSTYCTMCEGSPKQMVPKVP | ||||||
Domain | 2496-2793 | +RNA virus helicase C-terminal | ||||
Sequence: PGSHLAVPLQDTLKGVVVNKALKNAAASEYVEGPPGSGKTFHLVKDVLAVVGSATLVVPTHASMLDCINKLKQEGADPYFVVPKYTVLDFPRPGCGNITVRLPQVGTSEGETFVDEVAYFSPVDLARILTQGRVKGYGDLNQLGCVGPASVPRDLWLRHFVSLEPLRACHRFGAAVCDLIKGIYPYYEPAPHTTKVVFVPNPDFEKGVVITAYHKDRGLGHRTIDSIQGCTFPVVTLRLPTPQSLTRPRAVVAVTRASQELYIYDPFDQLSGLLKFTKEAEAQDLIHGPPIACHLGQE | ||||||
Domain | 2840-2930 | AV-Nsp11N/CoV-Nsp15M | ||||
Sequence: KISCLPRVAQNLGYHYSPDLPGFCPIPKELAEHWPVVSNDRYPNCLQITLQQVCELSKPCSAGYMVGQSVFVQTPGVTSYWLTEWVDGKAR | ||||||
Domain | 2932-3054 | NendoU | ||||
Sequence: LPDSLFSSGRFETNSRAFLDDAEEKFAAAHPHACLGEITKSTVGGSHFIFSQYLPPLLPADAVALVGASLAGKAAKAACSVVDVYAPSFEPYLHPETLSRVYKIMIDFKPCRLMVWRNATFYV |
Sequence similarities
Belongs to the arteriviridae polyprotein family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length3,175
- Mass (Da)345,503
- Last updated2019-06-05 v1
- Checksum3FC89DDAF7C3E653
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 433-447 | Pro residues | ||||
Sequence: TQAPIPAPRTRPPGT | ||||||
Compositional bias | 1593-1614 | Basic and acidic residues | ||||
Sequence: LPKGAQLEWDRHQEEKRNAGDD |
Keywords
- Coding sequence diversity