A0A386JTF7 · A0A386JTF7_9NIDO
- ProteinReplicase polyprotein 1ab
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids3860 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Cleaves the majority of cleavage sites present in the C-terminus of the polyprotein. Triggers host apoptosis through caspase-3, -8, and -9 activations. Subverts host innate immune responses through its protease activity. Targets the NF-kappa-B essential modulator NEMO and mediates its cleavage. Blocks host interferon beta induction and downstream signaling by cleaving mitochondrial MAVS, dislodging it from the mitochondria. Impairs host defense by cleaving host mRNA-decapping enzyme DCP1A to attenuate its antiviral activity.
Contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.
Displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity.
Plays a role in the inhibition of host STAT3 signaling pathway by inducing the degradation of STAT3.
Plays a role in the inhibition of the immune response by interacting with host IFITM1. This interaction leads to the proteasomal degradation of the IFN-induced antiviral protein IFITM1.
Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic.
Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, PKR (By similarity) and NLRP3 inflammasome (By similarity).
Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity).
If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity).
Also plays a role in the inhibition of host type I interferon production by recruiting host OTULIN to promote removal of linear ubiquitination targeting host NEMO
Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity).
If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity).
Also plays a role in the inhibition of host type I interferon production by recruiting host OTULIN to promote removal of linear ubiquitination targeting host NEMO
Responsible for replication and transcription of the viral RNA genome.
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
- ATP + H2O = ADP + H+ + phosphate
- 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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 3613 | |||||
Sequence: H | ||||||
Active site | 3628 | |||||
Sequence: H | ||||||
Active site | 3657 | |||||
Sequence: K |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameReplicase polyprotein 1ab
- Alternative names
Organism names
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Nidovirales > Arnidovirineae > Arteriviridae > Variarterivirinae > Betaarterivirus > Ampobartevirus > Betaarterivirus suid 2
Accessions
- Primary accessionA0A386JTF7
Subcellular Location
UniProt Annotation
GO Annotation
Host membrane ; Multi-pass membrane protein
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 1551-1573 | Helical | ||||
Sequence: LVAGFGIQEIALVVLIFVSIGGL | ||||||
Transmembrane | 1585-1609 | Helical | ||||
Sequence: FVILAIASYVWEPLTWLLCVFPCWL | ||||||
Transmembrane | 1621-1647 | Helical | ||||
Sequence: WLVFFLISVNMPSGILALVLLVSLWLL | ||||||
Transmembrane | 1921-1947 | Helical | ||||
Sequence: LLCVFFLLWRMMGHAWTPLVAVSFFIL | ||||||
Transmembrane | 1959-1980 | Helical | ||||
Sequence: VFSFGMFVLSWLTPWSAQVLMI | ||||||
Transmembrane | 1992-2012 | Helical | ||||
Sequence: LSLAFFSLGAVTGFVADLATT | ||||||
Transmembrane | 2032-2057 | Helical | ||||
Sequence: MVVVTSPVPVIACGVVHLLAIILYLF | ||||||
Transmembrane | 2064-2082 | Helical | ||||
Sequence: HILVGDGVFSAAFFLRYFA |
Keywords
- Cellular component
Interaction
Subunit
Interacts with host DDX18; this interaction redistributes host DDX18 to the cytoplasm.
Interacts with host DDX5.
Interacts with host IFITM1.
Interacts with host LGALS3.
Interacts with host OTULIN.
Nsp1-alpha papain-like: Interacts with host RNF31.
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 69-180 | Peptidase C31 | ||||
Sequence: ECSPAGACWLSAIFPIARMTSGNLNFQQRLVRVAAEIYRAGQLTPAVLKNLQVYERGCRWYPIVGPVPGVGVYANSLHVSDRPFPGATHVLTNLPLPQKPKPEDFCPFECAM | ||||||
Domain | 263-383 | Peptidase C32 | ||||
Sequence: DTVPEGNCWWSLFSSLPWKVQYEEIRRASQFGYQTKHGVAGKYLQRRMQVNGLRAVTDTSGPIVVQYFCVKESWIRHLRLAEEPSLPGFEDLIRIRVEPNTSPLVGEGEKIFRFGTHKWYG | ||||||
Region | 387-417 | Disordered | ||||
Sequence: RTRKARSGAATTGTRRVSPVRETQQAKEHED | ||||||
Domain | 428-535 | Peptidase C33 | ||||
Sequence: HYSPPADGNCGWHCISAIINHLVNSKLETTLPERVRPSDDWATDENLVNAIQTLRLPVSLDRNGACVGARYVLKLEGEHWTVSVAPGVTPLLLPLECVQGCCEHKSGL | ||||||
Region | 702-782 | Disordered | ||||
Sequence: QGLLEDGPAPSPPLTPRVQPRKTRSVRSLPDCKPIPAPRRRIRSDCGGPILMGDNVPDGREDLTVSGPSDLPTPSELMTPP | ||||||
Compositional bias | 725-741 | Basic and acidic residues | ||||
Sequence: RSVRSLPDCKPIPAPRR | ||||||
Compositional bias | 853-867 | Polar residues | ||||
Sequence: PLDSSSSSLTEYEAS | ||||||
Region | 853-875 | Disordered | ||||
Sequence: PLDSSSSSLTEYEASPLGPLQNV | ||||||
Region | 1049-1112 | Disordered | ||||
Sequence: GKATDQGPLAPFAGELTDGQPAREPRTQAPSACTSGVGLVLDSGSSLEPADLPPPNGTDAGGGG | ||||||
Compositional bias | 1075-1089 | Polar residues | ||||
Sequence: TQAPSACTSGVGLVL | ||||||
Domain | 1285-1316 | 4Fe-4S ferredoxin-type | ||||
Sequence: GAYVLSQGRCKKCWGSCVRTAPSEVAFNVFPF | ||||||
Domain | 1710-1913 | Peptidase S32 | ||||
Sequence: GAFRTQKPSLNTVNVVGSSMGSGGVFTIDGKIKCVTAAHVLTGNSARVSGVGFNQMLDFDVRGDFAIADCPNWHGAAPKTQFCADEWTGRAYWLTSSGVEPGVIGKGFAFCFTACGDSGSPVITEAGELVGIHTGSNKQGGGIVTRPSGQLCSVAPVKLSELSEFFAGPKVPLGDVKVGSHIIKDISEVPSDLCALLAAKPELE | ||||||
Domain | 2388-2550 | NiRAN | ||||
Sequence: IIDKLQGLTREQCLNYLAASGLTRCGRGGLVVTETAVKIVKFHNRTFTLGPVNLKVASEVELKDAVEHNQHPVAKPVDGGVVLLRSAVPSLVDVLISGADASPKLIARHGPGNTGIDGTLWDFEAEATKEEIALSAQIIQACDIRRGDAPEIGLPYKLHPVRG | ||||||
Domain | 2789-2923 | RdRp catalytic | ||||
Sequence: GRCLEADLASCDRSTPAIVRWFAAHLLYELACAEEHLPSYVLNCCHDLLITQSGAVTKRGGLSSGDPITSVSNTIYSLVIYAQHMVLSYFKSGHPHGLLFLQDQLKFEDMLKVQPLIVYSDDLVLYAESPTMPNY | ||||||
Domain | 3044-3107 | AV ZBD | ||||
Sequence: GKKSRVCGYCGASAPYATACGLDVCVYHTHFHQHCPVIIWCGHPAGSGSCDECKSPIGKGTSPL | ||||||
Domain | 3164-3445 | +RNA virus helicase C-terminal | ||||
Sequence: ASTALLPTCKEINMVAVASNVLRSRFIIGPPGAGKTHWLLQQVQDGDVIYTPTHQTMLDMIKALGTCRFNVPVGTTLQFPAPSRTGPWVRILAGGWCPGKNSFLDEAAYCNHLDVLRLLSKTTLTCLGDFKQLHPVGFDSHCYVFDIMPQTQLKTIWRFGQNICDAIQPDYRDKLMSMVNTTRVTYVEKPVNYGQVLTPYHRDREDSAITIDSSQGATFDVVTLHLPTKDSLNKQRALVAITRARHAIFVYDPHGQLQSLFDLPAKSTPVNLAVLRDGQLIV | ||||||
Domain | 3484-3580 | AV-Nsp11N/CoV-Nsp15M | ||||
Sequence: EGSSSPLPKVAHNLGFYFSPDLTQFAKLPIELAPHWPVVTTQNNENWPDRLVASLRPIHKYSRACIGAGYMVGPSVFLGAPGVVSYYLTKFVKGEAQ | ||||||
Domain | 3582-3704 | NendoU | ||||
Sequence: LPETIFSTGRIEVDCREYLDDREREVAASLPHAFIGDVKGTTVGGCHHVTSKYLPRFLPKESVAVVGVSSPGKAAKAVCTLTDVYLPDLEAYLHPVTQSKCWKMMLDFKEVRLMVWKDRTAYF |
Sequence similarities
Belongs to the arteriviridae polyprotein family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length3,860
- Mass (Da)421,613
- Last updated2018-12-05 v1
- ChecksumBC063D50739AC741
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 725-741 | Basic and acidic residues | ||||
Sequence: RSVRSLPDCKPIPAPRR | ||||||
Compositional bias | 853-867 | Polar residues | ||||
Sequence: PLDSSSSSLTEYEAS | ||||||
Compositional bias | 1075-1089 | Polar residues | ||||
Sequence: TQAPSACTSGVGLVL |
Keywords
- Coding sequence diversity