UniProtKB - P0C6Y3 (R1AB_IBVM)
Replicase polyprotein 1ab
rep
Functioni
Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein.
CuratedMay play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2 (By similarity).
Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (By similarity).
By similarityResponsible for the cleavages located at the N-terminus of the replicase polyprotein (By similarity).
In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (By similarity).
By similarityPlays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:30200673).
Alone is able to induce paired membranes (PubMed:30200673).
Coexpression of nsp3 and nsp4 does not result in the formation of DMVs (PubMed:30200673).
1 PublicationResponsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK.
PROSITE-ProRule annotationForms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.
By similarityForms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.
By similarityPlays an essential role in viral replication by forming a homodimer that binds single-stranded RNA.
1 PublicationPlays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities (By similarity).
Therefore plays an essential role in viral mRNAs cap methylation (By similarity).
By similarityResponsible for replication and transcription of the viral RNA genome.
By similarityMulti-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium.
By similarityEnzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity (By similarity).
Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens (By similarity).
By similarityPlays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity).
Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs (By similarity).
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).
By similarityMethyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system.
By similarityCatalytic activityi
- EC:2.7.7.48PROSITE-ProRule annotation
- EC:3.6.4.12By similarity EC:3.6.4.13By similarity
- a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H+ + S-adenosyl-L-homocysteineBy similarityEC:2.1.1.57By similarity
- Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).By similarity EC:3.4.19.12
Cofactori
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 1276 | For PL-PRO activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1439 | For PL-PRO activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1450 | For PL-PRO activityBy similarity | 1 | |
Active sitei | 2822 | For 3CL-PRO activityPROSITE-ProRule annotation | 1 | |
Active sitei | 2924 | For 3CL-PRO activityPROSITE-ProRule annotation | 1 | |
Metal bindingi | 3860 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 3863 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 3869 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 3880 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 3906 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 3909 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 3917 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 3919 | Zinc 2PROSITE-ProRule annotation | 1 | |
Active sitei | 4697 | PROSITE-ProRule annotation | 1 | |
Active sitei | 4698 | PROSITE-ProRule annotation | 1 | |
Active sitei | 4699 | PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4875 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4878 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4886 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4889 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4896 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4899 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4903 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4909 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4920 | Zinc 5PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4925 | Zinc 5PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4942 | Zinc 5PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4945 | Zinc 5PROSITE-ProRule annotation | 1 | |
Active sitei | 5559 | PROSITE-ProRule annotation | 1 | |
Active sitei | 5561 | PROSITE-ProRule annotation | 1 | |
Active sitei | 5660 | PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5676 | Zinc 6PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5678 | Zinc 6PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5694 | Zinc 6PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5697 | Zinc 6PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5725 | Zinc 7PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5729 | Zinc 7PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5732 | Zinc 7PROSITE-ProRule annotation | 1 | |
Active sitei | 5736 | PROSITE-ProRule annotation | 1 | |
Active sitei | 5741 | PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5747 | Zinc 7PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5917 | Zinc 8PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5937 | Zinc 8PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5948 | Zinc 8PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5951 | Zinc 8PROSITE-ProRule annotation | 1 | |
Active sitei | 6214 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6229 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6269 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6373 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6457 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6501 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6534 | PROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 1355 – 1392 | C4-typePROSITE-ProRule annotationAdd BLAST | 38 | |
Zinc fingeri | 3860 – 3880 | By similarityAdd BLAST | 21 | |
Zinc fingeri | 3906 – 3919 | By similarityAdd BLAST | 14 | |
Nucleotide bindingi | 5152 – 5159 | ATPBy similarity | 8 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- ATP hydrolysis activity Source: RHEA
- cysteine-type endopeptidase activity Source: InterPro
- DNA helicase activity Source: UniProtKB-EC
- endonuclease activity Source: UniProtKB-KW
- exoribonuclease activity Source: InterPro
- lyase activity Source: UniProtKB-KW
- methyltransferase activity Source: UniProtKB-KW
- omega peptidase activity Source: InterPro
- RNA binding Source: UniProtKB-KW
- RNA-directed 5'-3' RNA polymerase activity Source: UniProtKB-KW
- RNA helicase activity Source: UniProtKB-EC
- zinc ion binding Source: InterPro
GO - Biological processi
- induction by virus of host autophagy Source: UniProtKB-KW
- methylation Source: UniProtKB-KW
- transcription, DNA-templated Source: InterPro
- viral protein processing Source: InterPro
- viral RNA genome replication Source: InterPro
Keywordsi
Molecular function | Endonuclease, Exonuclease, Helicase, Hydrolase, Lyase, Methyltransferase, Nuclease, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase |
Biological process | Activation of host autophagy by virus, Host-virus interaction, Viral RNA replication |
Ligand | ATP-binding, Metal-binding, Nucleotide-binding, Zinc |
Enzyme and pathway databases
SABIO-RKi | P0C6Y3 |
Protein family/group databases
MEROPSi | C30.002 |
Names & Taxonomyi
Protein namesi | Recommended name: Replicase polyprotein 1abShort name: pp1ab Alternative name(s): ORF1ab polyprotein Cleaved into the following 14 chains: Alternative name(s): p87 Alternative name(s): Non-structural protein 3 Short name: nsp3 p195 Alternative name(s): Peptide HD2 p41 Alternative name(s): Main protease Short name: Mpro Non-structural protein 5 Short name: nsp5 p33 Alternative name(s): p34 Alternative name(s): p9 Alternative name(s): p24 Alternative name(s): p10 Alternative name(s): Growth factor-like peptide Short name: GFL p16 Alternative name(s): nsp12 p100 Alternative name(s): nsp13 p68 Alternative name(s): Guanine-N7 methyltransferaseBy similarity Non-structural protein 14 Short name: nsp14 p58 Uridylate-specific endoribonuclease (EC:4.6.1.-By similarity) Alternative name(s): NendoU Non-structural protein 15 Short name: nsp15 p39 Alternative name(s): Non-structural protein 16 Short name: nsp16 p35 |
Gene namesi | Name:rep ORF Names:1a-1b |
Organismi | Avian infectious bronchitis virus (strain M41) (IBV) |
Taxonomic identifieri | 11127 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Pisuviricota › Pisoniviricetes › Nidovirales › Cornidovirineae › Coronaviridae › Orthocoronavirinae › Gammacoronavirus › Igacovirus › |
Virus hosti | Gallus gallus (Chicken) [TaxID: 9031] |
Proteomesi |
|
Subcellular locationi
- Host endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein Curated
- Host cytoplasm By similarity Note: Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER).1 Publication
- Host endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein Curated
- Host cytoplasm By similarity Note: Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER).1 Publication
- Host endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein Curated Note: Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER).1 Publication
- host perinuclear region By similarity
- Host cytoplasm By similarity
- Host endoplasmic reticulum By similarity Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.
- host perinuclear region By similarity
- Host cytoplasm By similarity
- Host endoplasmic reticulum By similarity Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.
- host perinuclear region By similarity
- Host cytoplasm By similarity
- Host endoplasmic reticulum By similarity Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.
- host perinuclear region By similarity
- Host cytoplasm By similarity
- Host endoplasmic reticulum By similarity Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.
- Host endoplasmic reticulum-Golgi intermediate compartment Curated Note: The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA.
- Host cytoplasm By similarity
- Host endoplasmic reticulum By similarity
- Host cytoplasm By similarity
- Host endoplasmic reticulum By similarity
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 1752 | CytoplasmicBy similarityAdd BLAST | 1752 | |
Transmembranei | 1753 – 1773 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1774 – 1845 | LumenalBy similarityAdd BLAST | 72 | |
Transmembranei | 1846 – 1866 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1867 – 2282 | CytoplasmicBy similarityAdd BLAST | 416 | |
Transmembranei | 2283 – 2303 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 2304 – 2561 | LumenalBy similarityAdd BLAST | 258 | |
Transmembranei | 2562 – 2582 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 2583 – 2613 | CytoplasmicBy similarityAdd BLAST | 31 | |
Transmembranei | 2614 – 2634 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 2635 – 2645 | LumenalBy similarityAdd BLAST | 11 | |
Transmembranei | 2646 – 2666 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 2667 – 3098 | CytoplasmicBy similarityAdd BLAST | 432 | |
Transmembranei | 3099 – 3119 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 3120 – 3123 | LumenalBy similarity | 4 | |
Transmembranei | 3124 – 3144 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 3145 – 3153 | CytoplasmicBy similarity | 9 | |
Transmembranei | 3154 – 3174 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 3175 – 3190 | LumenalBy similarityAdd BLAST | 16 | |
Transmembranei | 3191 – 3211 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 3212 – 3259 | CytoplasmicBy similarityAdd BLAST | 48 | |
Transmembranei | 3260 – 3280 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 3281 – 3298 | LumenalBy similarityAdd BLAST | 18 | |
Transmembranei | 3299 – 3319 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 3320 – 6631 | CytoplasmicBy similarityAdd BLAST | 3312 |
Keywords - Cellular componenti
Host cytoplasm, Host endoplasmic reticulum, Host membrane, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 3747 | F → G: Loss of dimerization for Non-structural protein 9. 1 Publication | 1 | |
Mutagenesisi | 3769 | I → D: Loss of dimerization and nucleic acid binding for Non-structural protein 9. 1 Publication | 1 | |
Mutagenesisi | 3772 | G → D: Loss of dimerization and nucleic acid binding for Non-structural protein 9. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000283889 | 1 – 673 | Non-structural protein 2Add BLAST | 673 | |
ChainiPRO_0000283890 | 674 – 2267 | Papain-like proteaseAdd BLAST | 1594 | |
ChainiPRO_0000283891 | 2268 – 2781 | Non-structural protein 4Add BLAST | 514 | |
ChainiPRO_0000283892 | 2782 – 3088 | 3C-like proteinaseAdd BLAST | 307 | |
ChainiPRO_0000283893 | 3089 – 3381 | Non-structural protein 6Add BLAST | 293 | |
ChainiPRO_0000283894 | 3382 – 3464 | Non-structural protein 7Add BLAST | 83 | |
ChainiPRO_0000283895 | 3465 – 3674 | Non-structural protein 8Add BLAST | 210 | |
ChainiPRO_0000283896 | 3675 – 3785 | Non-structural protein 9Add BLAST | 111 | |
ChainiPRO_0000283897 | 3786 – 3930 | Non-structural protein 10Add BLAST | 145 | |
ChainiPRO_0000283898 | 3931 – 4870 | RNA-directed RNA polymeraseAdd BLAST | 940 | |
ChainiPRO_0000283899 | 4871 – 5470 | HelicaseAdd BLAST | 600 | |
ChainiPRO_0000283900 | 5471 – 5991 | Proofreading exoribonucleaseAdd BLAST | 521 | |
ChainiPRO_0000283901 | 5992 – 6329 | Uridylate-specific endoribonucleaseAdd BLAST | 338 | |
ChainiPRO_0000283902 | 6330 – 6631 | 2'-O-methyl transferaseAdd BLAST | 302 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 673 – 674 | Cleavage; by PL-PROBy similarity | 2 | |
Sitei | 2267 – 2268 | Cleavage; by PL-PROBy similarity | 2 | |
Sitei | 2781 – 2782 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 3088 – 3089 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 3381 – 3382 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 3464 – 3465 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 3674 – 3675 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 3785 – 3786 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 3930 – 3931 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 4870 – 4871 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 5470 – 5471 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 5991 – 5992 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 6329 – 6330 | Cleavage; by 3CL-PROBy similarity | 2 |
Interactioni
Subunit structurei
Interacts with papain-like protease and non-structural protein 6.
By similarityEight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure.
By similarityEight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure (By similarity).
Interacts with ORF6 protein (By similarity).
By similarityHomododecamer (By similarity).
Interacts with proofreading exoribonuclease nsp14 and 2'-O-methyltransferase nsp16; these interactions enhance nsp14 and nsp16 enzymatic activities (By similarity).
By similarityInteracts with host DDX1 (via C-terminus) (By similarity).
Interacts with non-structural protein 10 (By similarity).
By similarityStructurei
Secondary structure
3D structure databases
SMRi | P0C6Y3 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0C6Y3 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 675 – 780 | Ubiquitin-like 1PROSITE-ProRule annotationAdd BLAST | 106 | |
Domaini | 1005 – 1181 | MacroPROSITE-ProRule annotationAdd BLAST | 177 | |
Domaini | 1177 – 1229 | Ubiquitin-like 2PROSITE-ProRule annotationAdd BLAST | 53 | |
Domaini | 1238 – 1499 | Peptidase C16PROSITE-ProRule annotationAdd BLAST | 262 | |
Domaini | 2163 – 2265 | CoV Nsp3 Y3PROSITE-ProRule annotationAdd BLAST | 103 | |
Domaini | 2686 – 2781 | Nsp4CPROSITE-ProRule annotationAdd BLAST | 96 | |
Domaini | 2782 – 3088 | Peptidase C30PROSITE-ProRule annotationAdd BLAST | 307 | |
Domaini | 3382 – 3464 | RdRp Nsp7 cofactorPROSITE-ProRule annotationAdd BLAST | 83 | |
Domaini | 3465 – 3674 | RdRp Nsp8 cofactorPROSITE-ProRule annotationAdd BLAST | 210 | |
Domaini | 3675 – 3785 | Nsp9 ssRNA-bindingPROSITE-ProRule annotationAdd BLAST | 111 | |
Domaini | 3787 – 3928 | ExoN/MTase coactivatorPROSITE-ProRule annotationAdd BLAST | 142 | |
Domaini | 3942 – 4200 | NiRANPROSITE-ProRule annotationAdd BLAST | 259 | |
Domaini | 4304 – 4870 | Nsp12 RNA-dependent RNA polymerasePROSITE-ProRule annotationAdd BLAST | 567 | |
Domaini | 4550 – 4712 | RdRp catalyticPROSITE-ProRule annotationAdd BLAST | 163 | |
Domaini | 4871 – 4954 | CV ZBDPROSITE-ProRule annotationAdd BLAST | 84 | |
Domaini | 5127 – 5307 | (+)RNA virus helicase ATP-bindingAdd BLAST | 181 | |
Domaini | 5308 – 5479 | (+)RNA virus helicase C-terminalAdd BLAST | 172 | |
Domaini | 5541 – 5755 | ExoNPROSITE-ProRule annotationAdd BLAST | 215 | |
Domaini | 5764 – 5991 | N7-MTasePROSITE-ProRule annotationAdd BLAST | 228 | |
Domaini | 5992 – 6052 | Nsp15 N-terminal oligomerizationPROSITE-ProRule annotationAdd BLAST | 61 | |
Domaini | 6053 – 6168 | AV-Nsp11N/CoV-Nsp15MPROSITE-ProRule annotationAdd BLAST | 116 | |
Domaini | 6185 – 6326 | NendoUPROSITE-ProRule annotationAdd BLAST | 142 | |
Domaini | 6329 – 6628 | Nidovirus-type SAM-dependent 2'-O-MTasePROSITE-ProRule annotationAdd BLAST | 300 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1753 – 1866 | HD1By similarityAdd BLAST | 114 | |
Regioni | 2283 – 2666 | HD2By similarityAdd BLAST | 384 | |
Regioni | 3099 – 3319 | HD3By similarityAdd BLAST | 221 | |
Regioni | 5799 – 5805 | SAM-bindingPROSITE-ProRule annotation | 7 | |
Regioni | 5879 – 5893 | GpppA-bindingPROSITE-ProRule annotationAdd BLAST | 15 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 1355 – 1392 | C4-typePROSITE-ProRule annotationAdd BLAST | 38 | |
Zinc fingeri | 3860 – 3880 | By similarityAdd BLAST | 21 | |
Zinc fingeri | 3906 – 3919 | By similarityAdd BLAST | 14 |
Keywords - Domaini
Repeat, Transmembrane, Transmembrane helix, Zinc-fingerFamily and domain databases
CDDi | cd21409, 1B_cv_Nsp13-like, 1 hit cd20762, capping_2-OMTase_Nidovirales, 1 hit cd21512, cv_gamma-delta_Nsp2_IBV-like, 1 hit cd21473, cv_Nsp4_TM, 1 hit cd21559, gammaCoV-Nsp6, 1 hit cd21658, gammaCoV_Nsp14, 1 hit cd21667, gammaCoV_Nsp5_Mpro, 1 hit cd21587, gammaCoV_RdRp, 1 hit cd21168, M_gcv_Nsp15-like, 1 hit cd21557, Macro_X_Nsp3-like, 1 hit cd21161, NendoU_cv_Nsp15-like, 1 hit cd21170, NTD_cv_Nsp15-like, 1 hit cd18808, SF1_C_Upf1, 1 hit cd21467, Ubl1_cv_Nsp3_N-like, 1 hit cd21401, ZBD_cv_Nsp13-like, 1 hit |
Gene3Di | 1.10.150.420, 1 hit 1.10.1840.10, 1 hit 1.10.8.1190, 1 hit 1.10.8.370, 1 hit 2.40.10.10, 2 hits 2.40.10.250, 1 hit 2.60.120.1680, 1 hit 3.30.160.820, 1 hit 3.30.70.3540, 1 hit 3.40.220.10, 1 hit 3.40.50.11580, 1 hit 3.40.50.150, 1 hit 3.40.50.300, 2 hits |
InterProi | View protein in InterPro IPR027351, (+)RNA_virus_helicase_core_dom IPR043608, CoV_NSP15_M IPR043606, CoV_NSP15_N IPR043611, CoV_NSP3_C IPR043612, CoV_NSP4_N IPR043502, DNA/RNA_pol_sf IPR041679, DNA2/NAM7-like_C IPR037227, EndoU-like IPR002589, Macro_dom IPR043472, Macro_dom-like IPR044371, Macro_X_NSP3-like IPR043609, NendoU_nidovirus IPR044863, NIRAN IPR036333, NSP10_sf_CoV IPR044343, NSP13_1B_dom_CoV IPR027352, NSP13_ZBD_CoV-like IPR009466, NSP14_CoV IPR044316, NSP14_gammaCoV IPR044328, NSP15_gammaCoV_N IPR044325, NSP15_M_gammaCoV IPR043174, NSP15_middle_sf IPR042515, NSP15_N_CoV IPR044401, NSP15_NendoU_CoV IPR009461, NSP16_CoV-like IPR040795, NSP2_gammaCoV IPR044383, NSP2_IBV-like IPR044357, NSP3_Ubl1_dom_CoV IPR044353, Nsp3_Ubl2_dom_CoV IPR032505, NSP4_C_CoV IPR038123, NSP4_C_sf_CoV IPR044308, NSP5_Mpro_GammaCoV IPR043610, NSP6_CoV IPR044368, NSP6_gammaCoV IPR014828, NSP7_CoV IPR037204, NSP7_sf_CoV IPR014829, NSP8_CoV-like IPR037230, NSP8_sf_CoV IPR014822, NSP9_CoV IPR036499, NSP9_sf_CoV IPR027417, P-loop_NTPase IPR013016, Peptidase_C16_CoV IPR008740, Peptidase_C30_CoV IPR043477, Peptidase_C30_dom3_CoV IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR043503, PLpro_palm_finger_dom_CoV IPR043178, PLpro_thumb_sf_CoV IPR044358, RdRp_gammaCoV IPR001205, RNA-dir_pol_C IPR007094, RNA-dir_pol_PSvirus IPR009469, RNA_pol_N_CoV IPR018995, RNA_synth_NSP10_CoV IPR029063, SAM-dependent_MTases |
Pfami | View protein in Pfam PF06471, CoV_ExoN, 1 hit PF06460, CoV_Methyltr_2, 1 hit PF09401, CoV_NSP10, 1 hit PF19215, CoV_NSP15_C, 1 hit PF19216, CoV_NSP15_M, 1 hit PF19219, CoV_NSP15_N, 1 hit PF19218, CoV_NSP3_C, 1 hit PF16348, CoV_NSP4_C, 1 hit PF19217, CoV_NSP4_N, 1 hit PF19213, CoV_NSP6, 1 hit PF08716, CoV_NSP7, 1 hit PF08717, CoV_NSP8, 1 hit PF08710, CoV_NSP9, 1 hit PF08715, CoV_peptidase, 1 hit PF06478, CoV_RPol_N, 1 hit PF01661, Macro, 1 hit PF17896, NSP2_gammaCoV, 1 hit PF05409, Peptidase_C30, 1 hit PF00680, RdRP_1, 1 hit PF01443, Viral_helicase1, 1 hit |
SMARTi | View protein in SMART SM00506, A1pp, 1 hit |
SUPFAMi | SSF101816, SSF101816, 1 hit SSF140367, SSF140367, 1 hit SSF142877, SSF142877, 1 hit SSF143076, SSF143076, 1 hit SSF144246, SSF144246, 1 hit SSF50494, SSF50494, 1 hit SSF52540, SSF52540, 1 hit SSF52949, SSF52949, 1 hit SSF53335, SSF53335, 1 hit SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS51961, AV_NSP11N_COV_NSP15M, 1 hit PS51952, COV_EXON_MTASE_COACT, 1 hit PS51954, COV_N7_MTASE, 1 hit PS51948, COV_NSP12_RDRP, 1 hit PS51960, COV_NSP15_NTD, 1 hit PS51992, COV_NSP3_Y3, 1 hit PS51943, COV_NSP3A_UBL, 1 hit PS51944, COV_NSP3D_UBL, 1 hit PS51946, COV_NSP4C, 1 hit PS51949, COV_NSP7, 1 hit PS51950, COV_NSP8, 1 hit PS51951, COV_NSP9_SSRNA_BD, 1 hit PS51653, CV_ZBD, 1 hit PS51442, M_PRO, 1 hit PS51154, MACRO, 1 hit PS51958, NENDOU, 1 hit PS51947, NIRAN, 1 hit PS51955, NIV_2_O_MTASE, 1 hit PS51953, NIV_EXON, 1 hit PS51124, PEPTIDASE_C16, 1 hit PS51657, PSRV_HELICASE, 1 hit PS50507, RDRP_SSRNA_POS, 1 hit |
s (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsiribosomal frameshifting. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MASSLKQGVS PKLRDVILVS KDIPEQLCDA LFFYTSHNPK DYADAFAVRQ
60 70 80 90 100
KFDRNLQTGK QFKFETVCGL FLLKGVDKIT PGVPAKVLKA TSKLADLEDI
110 120 130 140 150
FGVSPFARKY RELLKTACQW SLTVETLDAR AQTLDEIFDP TEILWLQVAA
160 170 180 190 200
KIQVSAMAMR RLVGEVTAKV MDALGSNMSA LFQIFKQQIV RIFQKALAIF
210 220 230 240 250
ENVSELPQRI AALKMAFAKC AKSITVVVME RTLVVREFAG TCLASINGAV
260 270 280 290 300
AKFFEELPNG FMGAKIFTTL AFFREAAVKI VDNIPNAPRG TKGFEVVGNA
310 320 330 340 350
KGTQVVVRGM RNDLTLLDQK AEIPVESEGW SAILGGHLCY VFKSGDRFYA
360 370 380 390 400
APLSGNFALH DVHCCERVVC LSDGVTPEIN DGLILAAIYS SFSVAELVAA
410 420 430 440 450
IKRGEPFKFL GHKFVYAKDA AVSFTLAKAA TIADVLKLFQ SARVKVEDVW
460 470 480 490 500
SSLTEKSFEF WRLAYGKVRN LEEFVKTCFC KAQMAIVILA TVLGEGIWHL
510 520 530 540 550
VSQVIYKVGG LFTKVVDFCE KYWKGFCAQL KRAKLIVTET LCVLKGVAQH
560 570 580 590 600
CFQLLLDAIQ FMYKSFKKCA LGRIHGDLLF WKGGVHKIIQ EGDEIWFDAI
610 620 630 640 650
DSIDVEDLGV VQEKLIDFDV CDNVTLPENQ PGHMVQIEDD GKNYMFFRFK
660 670 680 690 700
KDENIYYTPM SQLGAINVVC KAGGKTVTFG ETTVQEIPPP DVVFIKVSIE
710 720 730 740 750
CCGEPWNTIF KKAYKEPIEV ETDLTVEQLL SVVYEKMCDD LKLFPEAPEP
760 770 780 790 800
PPFENVTLVD KNGKDLDCIK SCHLIYRDYE SDDDIEEEDA EECDTDSGDA
810 820 830 840 850
EECDTNLECE EEDEDTKVLA LIQDPASNKY PLPLDDDYSV YNGCIVHKDA
860 870 880 890 900
LDVVNLPSGE ETFVVNNCFE GAVKALPQKV IDVLGDWGEA VDAQEQLCQQ
910 920 930 940 950
ESTRVISEKS VEGFTGSCDA MAEQAIVEEQ EIVPVVEQSQ DVVVFTPADL
960 970 980 990 1000
EVVKETAEEV DEFILISAVP KEEVVSQEKE EPQVEQEPTL VVKAQREKKA
1010 1020 1030 1040 1050
KKFKVKPATC EKPKFLEYKT CVGDLAVVIA KALDEFKEFC IVNAANEHMS
1060 1070 1080 1090 1100
HGGGVAKAIA DFCGPDFVEY CADYVKKHGP QQKLVTPSFV KGIQCVNNVV
1110 1120 1130 1140 1150
GPRHGDSNLR EKLVAAYKSV LVGGVVNYVV PVLSSGIFGV DFKISIDAMR
1160 1170 1180 1190 1200
EAFKGCAIRV LLFSLSQEHI DYFDATCKQK TIYLTEDGVK YRSVVLKPGD
1210 1220 1230 1240 1250
SLGQFGQVFA RNKVVFSADD VEDKEILFIP TTDKTILEYY GLDAQKYVTY
1260 1270 1280 1290 1300
LQTLAQKWDV QYRDNFVILE WRDGNCWISS AIVLLQAAKI RFKGFLAEAW
1310 1320 1330 1340 1350
AKLLGGDPTD FVAWCYASCN AKVGDFSDAN WLLANLAEHF DADYTNALLK
1360 1370 1380 1390 1400
KCVSCNCGVK SYELRGLEAC IQPVRAPNLL HFKTQYSNCP TCGASSTDEV
1410 1420 1430 1440 1450
IEASLPYLLL FATDGPATVD CDENAVGTVV FIGSTNSGHC YTQADGKAFD
1460 1470 1480 1490 1500
NLAKDRKFGR KSPYITAMYT RFSLRSENPL LVVEHSKGKA KVVKEDVSNL
1510 1520 1530 1540 1550
ATSSKASFDD LTDFEQWYDS NIYESLKVQE TPDNLDEYVS FTTKEDSKLP
1560 1570 1580 1590 1600
LTLKVRGIKS VVDFRSKDGF TYKLTPDTDE NSKTPVYYPV LDSISLRAIW
1610 1620 1630 1640 1650
VEGSANFVVG HPNYYSKSLR IPTFWENAES FVKMGYKIDG VTMGLWRAEH
1660 1670 1680 1690 1700
LNKPNLERIF NIAKKAIVGS SVVTTQCGKI LVKAATYVAD KVGDGVVRNI
1710 1720 1730 1740 1750
TDRIKGLCGF TRGHFEKKMS LQFLKTLVFF FFYFLKASSK SLVSSYKIVL
1760 1770 1780 1790 1800
CKVVFATLLI VWFIYTSNPV VFTGIRVLDF LFEGSLCGPY NDYGKDSFDV
1810 1820 1830 1840 1850
LRYCAGDFTC RVCLHDRDSL HLYKHAYSVE QIYKDAASGI NFNWNWLYLV
1860 1870 1880 1890 1900
FLILFVKPVA GFVIICYCVK YLVLSSTVLQ TGVGFLDWFV KTVFTHFNFM
1910 1920 1930 1940 1950
GAGFYFWLFY KIYVQVHHIL YCKDVTCEVC KRVARSNRQE VSVVVGGRKQ
1960 1970 1980 1990 2000
IVHVYTNSGY NFCKRHNWYC RNCDDYGHQN TFMSPEVAGE LSEKLKRHVK
2010 2020 2030 2040 2050
PTAYAYHVVY EACVVDDFVN LKYKAAIPGK DNASSAVKCF SVTDFLKKAV
2060 2070 2080 2090 2100
FLKEALKCEQ ISNDGFIVCN TQSAHALEEA KNAAVYYAQY LCKPILILDQ
2110 2120 2130 2140 2150
ALYEQLIVEP VSKSVIDKVC SILSNIISVD TAALNYKAGT LRDALLSITK
2160 2170 2180 2190 2200
DEEAVDMAIF CHNHEVEYTG DGFTNVIPSY GMDTDKLTPR DRGFLINADA
2210 2220 2230 2240 2250
SIANLRVKNA PPVVWKFSDL IKLSDSCLKY LISATVKSGG RFFITKSGAK
2260 2270 2280 2290 2300
QVISCHTQKL LVEKKAGGVI NNTFKWFMSC FKWLFVFYIL FTACCLGYYY
2310 2320 2330 2340 2350
MEMNKSFVHP MYDVNSTLHV EGFKVIDKGV IREIVSEDNC FSNKFVNFDA
2360 2370 2380 2390 2400
FWGKSYENNK NCPIVTVVID GDGTVAVGVP GFVSWVMDGV MFVHMTQTDR
2410 2420 2430 2440 2450
RPWYIPTWFN REIVGYTQDS IITEGSFYTS IALFSARCLY LTASNTPQLY
2460 2470 2480 2490 2500
CFNGDNDAPG ALPFGSIIPH RVYFQPNGVR LIVPQQILHT PYIVKFVSDS
2510 2520 2530 2540 2550
YCRGSVCEYT KPGYCVSLDS QWVLFNDEYI SKPGVFCGST VRELMFNMVS
2560 2570 2580 2590 2600
TFFTGVNPNI YIQLATMFLI LVVIVLIFAM VIKFQGVFKA YATIVFTIML
2610 2620 2630 2640 2650
VWVINAFVLC VHSYNSVLAV ILLVLYCYAS MVTSRNTAII MHCWLVFTFG
2660 2670 2680 2690 2700
LIVPTWLACC YLGFILYMYT PLVFWCYGTT KNTRKLYDGN EFVGNYDLAA
2710 2720 2730 2740 2750
KSTFVIRGTE FVKLTNEIGD KFEAYLSAYA RLKYYSGTGS EQDYLQACRA
2760 2770 2780 2790 2800
WLAYALDQYR NSGVEVVYTP PRYSIGVSRL QAGFKKLVSP SSAVEKCIVS
2810 2820 2830 2840 2850
VSYRGNNLNG LWLGDSIYCP RHVLGKFSGD QWGDVLNLAN NHEFEVVTQN
2860 2870 2880 2890 2900
GVTLNVVSRR LKGAVLILQT AVANAETPKY KFVKANCGDS FTIACSYGGT
2910 2920 2930 2940 2950
VIGLYPVTMR SNGTIRASFL AGACGSVGFN IEKGVVNFFY MHHLELPNAL
2960 2970 2980 2990 3000
HTGTDLMGEF YGGYVDEEVA QRVPPDNLVT NNIVAWLYAA IISVKESSFS
3010 3020 3030 3040 3050
QPKWLESTTV SIEDYNRWAS DNGFTPFSTS TAITKLSAIT GVDVCKLLRT
3060 3070 3080 3090 3100
IMVKSAQWGS DPILGQYNFE DELTPESVFN QVGGVRLQSS FVRKATSWFW
3110 3120 3130 3140 3150
SRCVLACFLF VLCAIVLFTA VPLKFYVHAA VILLMAVLFI SFTVKHVMAY
3160 3170 3180 3190 3200
MDTFLLPTLI TVIIGVCAEV PFIYNTLISQ VVIFLSQWYD PVVFDTMVPW
3210 3220 3230 3240 3250
MLLPLVLYTA FKCVQGCYMN SFNTSLLMLY QFMKLGFVIY TSSNTLTAYT
3260 3270 3280 3290 3300
EGNWELFFEL VHTIVLANVS SNSLIGLIVF KCAKWMLYYC NATYFNNYVL
3310 3320 3330 3340 3350
MAVMVNGIGW LCTCYFGLYW WVNKVFGLTL GKYNFKVSVD QYRYMCLHKV
3360 3370 3380 3390 3400
NPPKTVWEVF TTNILIQGIG GDRVLPIATV QSKLSDVKCT TVVLMQLLTK
3410 3420 3430 3440 3450
LNVEANSKMH AYLVELHNKI LASDDVGECM DNLLGMLITL FCIDSTIDLG
3460 3470 3480 3490 3500
EYCDDILKRS TVLQSVTQEF SHIPSYAEYE RAKSIYEKVL ADSKNGGVTQ
3510 3520 3530 3540 3550
QELAAYRKAA NIAKSVFDRD LAVQKKLDSM AERAMTTMYK EARVTDRRAK
3560 3570 3580 3590 3600
LVSSLHALLF SMLKKIDSEK LNVLFDQANS GVVPLATVPI VCSNKLTLVI
3610 3620 3630 3640 3650
PDPETWVKCV EGVHVTYSTV VWNIDCVTDA DGTELHPTST GSGLTYCISG
3660 3670 3680 3690 3700
DNIAWPLKVN LTRNGHNKVD VALQNNELMP HGVKTKACVA GVDQAHCSVE
3710 3720 3730 3740 3750
SKCYYTSISG SSVVAAITSS NPNLKVASFL NEAGNQIYVD LDPPCKFGMK
3760 3770 3780 3790 3800
VGDKVEVVYL YFIKNTRSIV RGMVLGAISN VVVLQSKGHE TEEVDAVGIL
3810 3820 3830 3840 3850
SLCSFAVDPA DTYCKYVAAG NQPLGNCVKM LTVHNGSGFA ITSKPSPTPD
3860 3870 3880 3890 3900
QDSYGGASVC LYCRAHIAHP GGAGNLDGRC QFKGSFVQIP TTEKDPVGFC
3910 3920 3930 3940 3950
LRNKVCTVCQ CWIGYGCQCD SLRQPKPSVQ SVAVASGFDK NYLNRVRGSS
3960 3970 3980 3990 4000
EARLIPLANG CDPDVVKRAF DVCNKESAGM FQNLKRNCAR FQEVRDTEDG
4010 4020 4030 4040 4050
NLEYCDSYFV VKQTTPSNYE HEKACYEDLK SEVTADHDFF VFNKNIYNIS
4060 4070 4080 4090 4100
RQRLTKYTMM DFCYALRHFD PKDCEVLKEI LVTYGCIEDY HPKWFEENKD
4110 4120 4130 4140 4150
WYDPIENPKY YAMLAKMGPI VRRALLNAIE FGNLMVEKGY VGVITLDNQD
4160 4170 4180 4190 4200
LNGKFYDFGD FQKTAPGAGV PVFDTYYSYM MPIIAMTDAL APERYFEYDV
4210 4220 4230 4240 4250
HKGYKSYDLL KYDYTEEKQD LFQKYFKYWD QEYHPNCRDC SDDRCLIHCA
4260 4270 4280 4290 4300
NFNILFSTLV PQTSFGNLCR KVFVDGVPFI ATCGYHSKEL GVIMNQDNTM
4310 4320 4330 4340 4350
SFSKMGLSQL MQFVGDPALL VGTSNKLVDL RTSCFSVCAL ASGITHQTVK
4360 4370 4380 4390 4400
PGHFNKDFYD FAEKAGMFKE GSSIPLKHFF YPQTGNAAIN DYDYYRYNRP
4410 4420 4430 4440 4450
TMFDIRQLLF CLEVTSKYFE CYEGGCIPAS QVVVNNLDKS AGYPFNKFGK
4460 4470 4480 4490 4500
ARLYYEMSLE EQDQLFESTK KNVLPTITQM NLKYAISAKN RARTVAGVSI
4510 4520 4530 4540 4550
LSTMTNRQFH QKILKSIVNT RNAPVVIGTT KFYGGWDNML RNLIQGVEDP
4560 4570 4580 4590 4600
ILMGWDYPKC DRAMPNLLRI AASLVLARKH TNCCTWSERV YRLYNECAQV
4610 4620 4630 4640 4650
LSETVLATGG IYVKPGGTSS GDATTAYANS VFNIIQATSA NVARLLSVIT
4660 4670 4680 4690 4700
RDIVYDDIKS LQYELYQQVY RRVNFDPAFV EKFYSYLCKN FSLMILSDDG
4710 4720 4730 4740 4750
VVCYNNTLAK QGLVADISGF REVLYYQNNV FMADSKCWVE PDLEKGPHEF
4760 4770 4780 4790 4800
CSQHTMLVEV DGEPRYLPYP DPSRILCACV FVDDLDKTES VAVMERYIAL
4810 4820 4830 4840 4850
AIDAYPLVHH ENEEYKKVFF VLLSYIRKLY QELSQNMLMD YSFVMDIDKG
4860 4870 4880 4890 4900
SKFWEQEFYE NMYRAPTTLQ SCGVCVVCNS QTILRCGNCI RKPFLCCKCC
4910 4920 4930 4940 4950
YDHVMHTDHK NVLSINPYIC SQPGCGEADV TKLYLGGMSY FCGNHKPKLS
4960 4970 4980 4990 5000
IPLVSNGTVF GIYRANCAGS ENVDDFNQLA TTNWSTVEPY ILANRCVDSL
5010 5020 5030 5040 5050
RRFAAETVKA TEELHKQQFA SAEVREVLSD RELILSWEPG KTRPPLNRNY
5060 5070 5080 5090 5100
VFTGFHFTRT SKVQLGDFTF EKGEGKDVVY YRATSTAKLS VGDIFVLTSH
5110 5120 5130 5140 5150
NVVSLIAPTL CPQQTFSRFV NLRPNVMVPA CFVNNIPLYH LVGKQKRTTV
5160 5170 5180 5190 5200
QGPPGSGKSH FAIGLAAYFS NARVVFTACS HAAVDALCEK AFKFLKVDDC
5210 5220 5230 5240 5250
TRIVPQRTTI DCFSKFKAND TGKKYIFSTI NALPEVSCDI LLVDEVSMLT
5260 5270 5280 5290 5300
NYELSFINGK INYQYVVYVG DPAQLPAPRT LLNGSLSPKD YNVVTNLMVC
5310 5320 5330 5340 5350
VKPDIFLAKC YRCPKEIVDT VSTLVYDGKF IANNPESRQC FKVIVNNGNS
5360 5370 5380 5390 5400
DVGHESGSAY NITQLEFVKD FVCRNKEWRE ATFISPYNAM NQRAYRMLGL
5410 5420 5430 5440 5450
NVQTVDSSQG SEYDYVIFCV TADSQHALNI NRFNVALTRA KRGILVVMRQ
5460 5470 5480 5490 5500
RDELYSALKF IELDSVASLQ GTGLFKICNK EFSGVHPAYA VTTKALAATY
5510 5520 5530 5540 5550
KVNDELAALV NVEAGSEITY KHLISLLGFK MSVNVEGCHN MFITRDEAIR
5560 5570 5580 5590 5600
NVRGWVGFDV EATHACGTNI GTNLPFQVGF STGADFVVTP EGLVDTSIGN
5610 5620 5630 5640 5650
NFEPVNSKAP PGEQFNHLRA LFKSAKPWHV VRPRIVQMLA DNLCNVSDCV
5660 5670 5680 5690 5700
VFVTWCHGLE LTTLRYFVKI GKDQVCSCGS RATTFNSHTQ AYACWKHCLG
5710 5720 5730 5740 5750
FDFVYNPLLV DIQQWGYSGN LQFNHDLHCN VHGHAHVASA DAIMTRCLAI
5760 5770 5780 5790 5800
NNAFCQDVNW DLTYPHIANE DEVNSSCRYL QRMYLNACVD ALKVNVVYDI
5810 5820 5830 5840 5850
GNPKGIKCVR RGDLNFRFYD KNPIVPNVKQ FEYDYNQHKD KFADGLCMFW
5860 5870 5880 5890 5900
NCNVDCYPDN SLVCRYDTRN LSVFNLPGCN GGSLYVNKHA FHTPKFDRTS
5910 5920 5930 5940 5950
FRNLKAMPFF FYDSSPCETI QLDGVAQDLV SLATKDCITK CNIGGAVCKK
5960 5970 5980 5990 6000
HAQMYADFVT SYNAAVTAGF TFWVTNNFNP YNLWKSFSAL QSIDNIAYNM
6010 6020 6030 6040 6050
YKGGHYDAIA GEMPTIVTGD KVFVIDQGVE KAVFFNQTIL PTSVAFELYA
6060 6070 6080 6090 6100
KRNIRTLPNN RILKGLGVDV TNGFVIWDYT NQTPLYRNTV KVCAYTDIEP
6110 6120 6130 6140 6150
NGLIVLYDDR YGDYQSFLAA DNAVLVSTQC YKRYSYVEIP SNLLVQNGIP
6160 6170 6180 6190 6200
LKDGANLYVY KRVNGAFVTL PNTLNTQGRS YETFEPRSDV ERDFLDMSEE
6210 6220 6230 6240 6250
SFVEKYGKEL GLQHILYGEV DKPQLGGLHT VIGMCRLLRA NKLNAKSVTN
6260 6270 6280 6290 6300
SDSDVMQNYF VLADNGSYKQ VCTVVDLLLD DFLELLRNIL KEYGTNKSKV
6310 6320 6330 6340 6350
VTVSIDYHSI NFMAWFEDGI IKTCYPQLQS AWTCGYNMPE LYKVQNCVME
6360 6370 6380 6390 6400
PCNIPNYGVG IALPSGIMMN VAKYTQLCQY LSKTTMCVPH NMRVMHFGAG
6410 6420 6430 6440 6450
SDKGVAPGST VLKQWLPEGT LLVDNDIVDY VSDAHVSVLS DCNKYKTEHK
6460 6470 6480 6490 6500
FDLVISDMYT DNDSKRKHEG VIANNGNDDV FIYLSSFLRN NLALGGSFAV
6510 6520 6530 6540 6550
KVTETSWHEV LYDIAQDCAW WTMFCTAVNA SSSEAFLVGV NYLGASEKVK
6560 6570 6580 6590 6600
VSGKTLHANY IFWRNCNYLQ TSAYSIFDVA KFDLRLKATP VVNLKTEQKT
6610 6620 6630
DLVFNLIKCG KLLVRDVGNT SFTSDSFVCT M
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Sequence cautioni
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 807 | L → S. | 1 | |
Natural varianti | 1618 | S → F. | 1 | |
Natural varianti | 1739 | S → A. | 1 | |
Natural varianti | 2631 | M → L. | 1 | |
Natural varianti | 2774 | S → P. | 1 | |
Natural varianti | 4230 | D → G. | 1 | |
Natural varianti | 4692 | S → P. | 1 | |
Natural varianti | 4859 | Y → C. | 1 | |
Natural varianti | 5104 | S → P. | 1 | |
Natural varianti | 6033 | V → A. | 1 | |
Natural varianti | 6080 | T → M. | 1 | |
Natural varianti | 6314 | A → T. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DQ834384 Genomic RNA Translation: ABI26421.1 Sequence problems. DQ834384 Genomic RNA Translation: ABI26422.1 Sequence problems. AY851295 Genomic RNA Translation: AAW33784.1 Sequence problems. AY851295 Genomic RNA Translation: AAW33785.1 Sequence problems. |
Keywords - Coding sequence diversityi
Ribosomal frameshiftingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DQ834384 Genomic RNA Translation: ABI26421.1 Sequence problems. DQ834384 Genomic RNA Translation: ABI26422.1 Sequence problems. AY851295 Genomic RNA Translation: AAW33784.1 Sequence problems. AY851295 Genomic RNA Translation: AAW33785.1 Sequence problems. |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2Q6D | X-ray | 2.35 | A/B/C | 2783-3088 | [»] | |
2Q6F | X-ray | 2.00 | A/B | 2783-3088 | [»] | |
5C94 | X-ray | 2.44 | A | 3675-3785 | [»] | |
7F52 | X-ray | 2.56 | A/B | 1-673 | [»] | |
SMRi | P0C6Y3 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein family/group databases
MEROPSi | C30.002 |
Enzyme and pathway databases
SABIO-RKi | P0C6Y3 |
Miscellaneous databases
EvolutionaryTracei | P0C6Y3 |
Family and domain databases
CDDi | cd21409, 1B_cv_Nsp13-like, 1 hit cd20762, capping_2-OMTase_Nidovirales, 1 hit cd21512, cv_gamma-delta_Nsp2_IBV-like, 1 hit cd21473, cv_Nsp4_TM, 1 hit cd21559, gammaCoV-Nsp6, 1 hit cd21658, gammaCoV_Nsp14, 1 hit cd21667, gammaCoV_Nsp5_Mpro, 1 hit cd21587, gammaCoV_RdRp, 1 hit cd21168, M_gcv_Nsp15-like, 1 hit cd21557, Macro_X_Nsp3-like, 1 hit cd21161, NendoU_cv_Nsp15-like, 1 hit cd21170, NTD_cv_Nsp15-like, 1 hit cd18808, SF1_C_Upf1, 1 hit cd21467, Ubl1_cv_Nsp3_N-like, 1 hit cd21401, ZBD_cv_Nsp13-like, 1 hit |
Gene3Di | 1.10.150.420, 1 hit 1.10.1840.10, 1 hit 1.10.8.1190, 1 hit 1.10.8.370, 1 hit 2.40.10.10, 2 hits 2.40.10.250, 1 hit 2.60.120.1680, 1 hit 3.30.160.820, 1 hit 3.30.70.3540, 1 hit 3.40.220.10, 1 hit 3.40.50.11580, 1 hit 3.40.50.150, 1 hit 3.40.50.300, 2 hits |
InterProi | View protein in InterPro IPR027351, (+)RNA_virus_helicase_core_dom IPR043608, CoV_NSP15_M IPR043606, CoV_NSP15_N IPR043611, CoV_NSP3_C IPR043612, CoV_NSP4_N IPR043502, DNA/RNA_pol_sf IPR041679, DNA2/NAM7-like_C IPR037227, EndoU-like IPR002589, Macro_dom IPR043472, Macro_dom-like IPR044371, Macro_X_NSP3-like IPR043609, NendoU_nidovirus IPR044863, NIRAN IPR036333, NSP10_sf_CoV IPR044343, NSP13_1B_dom_CoV IPR027352, NSP13_ZBD_CoV-like IPR009466, NSP14_CoV IPR044316, NSP14_gammaCoV IPR044328, NSP15_gammaCoV_N IPR044325, NSP15_M_gammaCoV IPR043174, NSP15_middle_sf IPR042515, NSP15_N_CoV IPR044401, NSP15_NendoU_CoV IPR009461, NSP16_CoV-like IPR040795, NSP2_gammaCoV IPR044383, NSP2_IBV-like IPR044357, NSP3_Ubl1_dom_CoV IPR044353, Nsp3_Ubl2_dom_CoV IPR032505, NSP4_C_CoV IPR038123, NSP4_C_sf_CoV IPR044308, NSP5_Mpro_GammaCoV IPR043610, NSP6_CoV IPR044368, NSP6_gammaCoV IPR014828, NSP7_CoV IPR037204, NSP7_sf_CoV IPR014829, NSP8_CoV-like IPR037230, NSP8_sf_CoV IPR014822, NSP9_CoV IPR036499, NSP9_sf_CoV IPR027417, P-loop_NTPase IPR013016, Peptidase_C16_CoV IPR008740, Peptidase_C30_CoV IPR043477, Peptidase_C30_dom3_CoV IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR043503, PLpro_palm_finger_dom_CoV IPR043178, PLpro_thumb_sf_CoV IPR044358, RdRp_gammaCoV IPR001205, RNA-dir_pol_C IPR007094, RNA-dir_pol_PSvirus IPR009469, RNA_pol_N_CoV IPR018995, RNA_synth_NSP10_CoV IPR029063, SAM-dependent_MTases |
Pfami | View protein in Pfam PF06471, CoV_ExoN, 1 hit PF06460, CoV_Methyltr_2, 1 hit PF09401, CoV_NSP10, 1 hit PF19215, CoV_NSP15_C, 1 hit PF19216, CoV_NSP15_M, 1 hit PF19219, CoV_NSP15_N, 1 hit PF19218, CoV_NSP3_C, 1 hit PF16348, CoV_NSP4_C, 1 hit PF19217, CoV_NSP4_N, 1 hit PF19213, CoV_NSP6, 1 hit PF08716, CoV_NSP7, 1 hit PF08717, CoV_NSP8, 1 hit PF08710, CoV_NSP9, 1 hit PF08715, CoV_peptidase, 1 hit PF06478, CoV_RPol_N, 1 hit PF01661, Macro, 1 hit PF17896, NSP2_gammaCoV, 1 hit PF05409, Peptidase_C30, 1 hit PF00680, RdRP_1, 1 hit PF01443, Viral_helicase1, 1 hit |
SMARTi | View protein in SMART SM00506, A1pp, 1 hit |
SUPFAMi | SSF101816, SSF101816, 1 hit SSF140367, SSF140367, 1 hit SSF142877, SSF142877, 1 hit SSF143076, SSF143076, 1 hit SSF144246, SSF144246, 1 hit SSF50494, SSF50494, 1 hit SSF52540, SSF52540, 1 hit SSF52949, SSF52949, 1 hit SSF53335, SSF53335, 1 hit SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS51961, AV_NSP11N_COV_NSP15M, 1 hit PS51952, COV_EXON_MTASE_COACT, 1 hit PS51954, COV_N7_MTASE, 1 hit PS51948, COV_NSP12_RDRP, 1 hit PS51960, COV_NSP15_NTD, 1 hit PS51992, COV_NSP3_Y3, 1 hit PS51943, COV_NSP3A_UBL, 1 hit PS51944, COV_NSP3D_UBL, 1 hit PS51946, COV_NSP4C, 1 hit PS51949, COV_NSP7, 1 hit PS51950, COV_NSP8, 1 hit PS51951, COV_NSP9_SSRNA_BD, 1 hit PS51653, CV_ZBD, 1 hit PS51442, M_PRO, 1 hit PS51154, MACRO, 1 hit PS51958, NENDOU, 1 hit PS51947, NIRAN, 1 hit PS51955, NIV_2_O_MTASE, 1 hit PS51953, NIV_EXON, 1 hit PS51124, PEPTIDASE_C16, 1 hit PS51657, PSRV_HELICASE, 1 hit PS50507, RDRP_SSRNA_POS, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | R1AB_IBVM | |
Accessioni | P0C6Y3Primary (citable) accession number: P0C6Y3 Secondary accession number(s): Q0GNB9 Q5I5Y1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 10, 2008 |
Last sequence update: | June 10, 2008 | |
Last modified: | May 25, 2022 | |
This is version 96 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families