UniProtKB - P0C6X4 (R1AB_CVHN5)
Replicase polyprotein 1ab
rep
Functioni
The replicase polyprotein of coronaviruses is a multifunctional protein: it 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.
By similarityInhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response.
By similarityMay play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses.
By similarityResponsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling.
By similarityParticipates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.
By similarityCleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP).
PROSITE-ProRule annotationBy similarityPlays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes.
By similarityForms 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 similarityMay participate in viral replication by acting as a ssRNA-binding protein.
By similarityPlays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation.
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 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. 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 similarityMiscellaneous
Catalytic activityi
- EC:2.7.7.48
- EC:3.6.4.12 EC:3.6.4.13
- 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). EC:3.4.19.12
Cofactori
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 1111 | For PL1-PRO activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1262 | For PL1-PRO activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1707 | For PL2-PRO activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1864 | For PL2-PRO activityPROSITE-ProRule annotation | 1 | |
Active sitei | 3325 | For 3CL-PRO activityPROSITE-ProRule annotation | 1 | |
Active sitei | 3429 | For 3CL-PRO activityPROSITE-ProRule annotation | 1 | |
Metal bindingi | 4344 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4347 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4353 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4360 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4386 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4389 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4397 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4399 | Zinc 2PROSITE-ProRule annotation | 1 | |
Active sitei | 5162 | PROSITE-ProRule annotation | 1 | |
Active sitei | 5163 | PROSITE-ProRule annotation | 1 | |
Active sitei | 5164 | PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5340 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5343 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5351 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5354 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5361 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5364 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5368 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5374 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5385 | Zinc 5PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5390 | Zinc 5PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5407 | Zinc 5PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5410 | Zinc 5PROSITE-ProRule annotation | 1 | |
Active sitei | 6027 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6029 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6128 | PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6144 | Zinc 6PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6147 | Zinc 6PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6163 | Zinc 6PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6166 | Zinc 6PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6194 | Zinc 7PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6198 | Zinc 7PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6201 | Zinc 7PROSITE-ProRule annotation | 1 | |
Active sitei | 6205 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6210 | PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6216 | Zinc 7PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6384 | Zinc 8PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6405 | Zinc 8PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6416 | Zinc 8PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6419 | Zinc 8PROSITE-ProRule annotation | 1 | |
Active sitei | 6721 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6736 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6776 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6879 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6963 | PROSITE-ProRule annotation | 1 | |
Active sitei | 7003 | PROSITE-ProRule annotation | 1 | |
Active sitei | 7036 | PROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 1188 – 1216 | C4-type 1PROSITE-ProRule annotationAdd BLAST | 29 | |
Zinc fingeri | 1785 – 1821 | C4-type 2PROSITE-ProRule annotationAdd BLAST | 37 | |
Zinc fingeri | 4344 – 4360 | By similarityAdd BLAST | 17 | |
Zinc fingeri | 4386 – 4399 | By similarityAdd BLAST | 14 | |
Nucleotide bindingi | 5616 – 5623 | 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
- RNA-directed 5'-3' RNA polymerase activity Source: UniProtKB-KW
- RNA helicase activity Source: UniProtKB-EC
- single-stranded RNA binding Source: InterPro
- thiol-dependent deubiquitinase Source: UniProtKB-EC
- zinc ion binding Source: InterPro
GO - Biological processi
- induction by virus of catabolism of host mRNA Source: UniProtKB-KW
- induction by virus of host autophagy Source: UniProtKB-KW
- methylation Source: UniProtKB-KW
- modulation by virus of host protein ubiquitination Source: UniProtKB-KW
- suppression by virus of host gene expression Source: UniProtKB-KW
- suppression by virus of host ISG15-protein conjugation Source: UniProtKB-KW
- suppression by virus of host NF-kappaB cascade Source: UniProtKB-KW
- suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
- transcription, DNA-templated Source: InterPro
- viral genome replication Source: InterPro
- viral protein processing Source: InterPro
Keywordsi
Names & Taxonomyi
Protein namesi | Recommended name: Replicase polyprotein 1abShort name: pp1ab Alternative name(s): ORF1ab polyprotein Cleaved into the following 15 chains: Alternative name(s): p28 Alternative name(s): p65 Alternative name(s): Non-structural protein 3 Short name: nsp3 p210 Alternative name(s): Peptide HD2 p44 Alternative name(s): M-PRO nsp5 p27 Alternative name(s): p10 Alternative name(s): p22 Alternative name(s): p12 Alternative name(s): Growth factor-like peptide Short name: GFL p15 Alternative name(s): nsp12 p100 Alternative name(s): nsp13 p67 Alternative name(s): nsp14 Alternative name(s): NendoU nsp15 p35 Alternative name(s): nsp16 |
Gene namesi | Name:rep ORF Names:1a-1b |
Organismi | Human coronavirus HKU1 (isolate N5) (HCoV-HKU1) |
Taxonomic identifieri | 443241 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Pisuviricota › Pisoniviricetes › Nidovirales › Cornidovirineae › Coronaviridae › Orthocoronavirinae › Betacoronavirus › Embecovirus › |
Virus hosti | Homo sapiens (Human) [TaxID: 9606] |
Proteomesi |
|
Subcellular locationi
- Host membrane ; Multi-pass membrane protein
- Host cytoplasm Note: Localizes in virally-induced cytoplasmic double-membrane vesicles.By similarity
- Host membrane Curated; Multi-pass membrane protein Curated
- host perinuclear region 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 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 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 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.
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transmembranei | 2176 – 2196 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 2237 – 2257 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 2268 – 2288 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 2351 – 2371 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 2393 – 2413 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 2794 – 2814 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3069 – 3089 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3101 – 3121 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3128 – 3148 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3153 – 3173 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3601 – 3621 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3626 – 3646 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3651 – 3671 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3694 – 3714 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3722 – 3742 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3750 – 3770 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3793 – 3813 | HelicalSequence analysisAdd BLAST | 21 |
Keywords - Cellular componenti
Host cytoplasm, Host membrane, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000297788 | 1 – 222 | Host translation inhibitor nsp1By similarityAdd BLAST | 222 | |
ChainiPRO_0000297789 | 223 – 809 | Non-structural protein 2By similarityAdd BLAST | 587 | |
ChainiPRO_0000297790 | 810 – 2788 | Papain-like proteinaseBy similarityAdd BLAST | 1979 | |
ChainiPRO_0000297791 | 2789 – 3284 | Non-structural protein 4By similarityAdd BLAST | 496 | |
ChainiPRO_0000297792 | 3285 – 3587 | 3C-like proteinaseBy similarityAdd BLAST | 303 | |
ChainiPRO_0000297793 | 3588 – 3874 | Non-structural protein 6By similarityAdd BLAST | 287 | |
ChainiPRO_0000297794 | 3875 – 3966 | Non-structural protein 7By similarityAdd BLAST | 92 | |
ChainiPRO_0000297795 | 3967 – 4160 | Non-structural protein 8By similarityAdd BLAST | 194 | |
ChainiPRO_0000297796 | 4161 – 4270 | Non-structural protein 9By similarityAdd BLAST | 110 | |
ChainiPRO_0000297797 | 4271 – 4407 | Non-structural protein 10By similarityAdd BLAST | 137 | |
ChainiPRO_0000297798 | 4408 – 5335 | RNA-directed RNA polymeraseBy similarityAdd BLAST | 928 | |
ChainiPRO_0000297799 | 5336 – 5938 | HelicaseBy similarityAdd BLAST | 603 | |
ChainiPRO_0000297800 | 5939 – 6459 | Guanine-N7 methyltransferaseBy similarityAdd BLAST | 521 | |
ChainiPRO_0000297801 | 6460 – 6833 | Uridylate-specific endoribonucleaseBy similarityAdd BLAST | 374 | |
ChainiPRO_0000297802 | 6834 – 7132 | 2'-O-methyltransferaseBy similarityAdd BLAST | 299 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 222 – 223 | Cleavage; by PL1-PROBy similarity | 2 | |
Sitei | 809 – 810 | Cleavage; by PL1-PROBy similarity | 2 | |
Sitei | 2788 – 2789 | Cleavage; by PL2-PROBy similarity | 2 | |
Sitei | 3284 – 3285 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 3587 – 3588 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 3874 – 3875 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 3966 – 3967 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 4160 – 4161 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 4270 – 4271 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 4407 – 4408 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 5335 – 5336 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 6459 – 6460 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 6833 – 6834 | Cleavage; by 3CL-PROBy similarity | 2 |
Proteomic databases
PRIDEi | P0C6X4 |
Interactioni
Subunit structurei
Nsp2 interacts with host PHB and PHB2. 3CL-PRO exists as monomer and homodimer. Nsp4 interacts with PL-PRO and nsp6. Only the homodimer shows catalytic activity. Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure. Nsp9 is a dimer. Nsp10 forms a dodecamer and interacts with nsp14 and nsp16; these interactions enhance nsp14 and nsp16 enzymatic activities. Nsp14 interacts (via N-terminus) with DDX1.
By similarityChemistry databases
BindingDBi | P0C6X4 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 54 – 179 | CoV Nsp1 globularPROSITE-ProRule annotationAdd BLAST | 126 | |
Domaini | 192 – 222 | BetaCoV Nsp1 C-terminalPROSITE-ProRule annotationAdd BLAST | 31 | |
Domaini | 810 – 923 | Ubiquitin-like 1PROSITE-ProRule annotationAdd BLAST | 114 | |
Repeati | 945 – 954 | 1 | 10 | |
Repeati | 955 – 964 | 2 | 10 | |
Repeati | 965 – 974 | 3 | 10 | |
Repeati | 975 – 984 | 4 | 10 | |
Repeati | 985 – 994 | 5 | 10 | |
Repeati | 995 – 1004 | 6 | 10 | |
Repeati | 1005 – 1014 | 7 | 10 | |
Repeati | 1015 – 1024 | 8 | 10 | |
Repeati | 1025 – 1034 | 9 | 10 | |
Domaini | 1073 – 1323 | Peptidase C16 1PROSITE-ProRule annotationAdd BLAST | 251 | |
Domaini | 1301 – 1472 | MacroPROSITE-ProRule annotationAdd BLAST | 172 | |
Domaini | 1528 – 1599 | DPUPPROSITE-ProRule annotationAdd BLAST | 72 | |
Domaini | 1599 – 1654 | Ubiquitin-like 2PROSITE-ProRule annotationAdd BLAST | 56 | |
Domaini | 1668 – 1928 | Peptidase C16 2PROSITE-ProRule annotationAdd BLAST | 261 | |
Domaini | 1942 – 2043 | Nucleic acid-bindingPROSITE-ProRule annotationAdd BLAST | 102 | |
Domaini | 3187 – 3284 | Nsp4CPROSITE-ProRule annotationAdd BLAST | 98 | |
Domaini | 3285 – 3587 | Peptidase C30PROSITE-ProRule annotationAdd BLAST | 303 | |
Domaini | 3875 – 3963 | RdRp Nsp7 cofactorPROSITE-ProRule annotationAdd BLAST | 89 | |
Domaini | 3964 – 4160 | RdRp Nsp8 cofactorPROSITE-ProRule annotationAdd BLAST | 197 | |
Domaini | 4161 – 4270 | Nsp9 ssRNA-bindingPROSITE-ProRule annotationAdd BLAST | 110 | |
Domaini | 4271 – 4408 | ExoN/MTase coactivatorPROSITE-ProRule annotationAdd BLAST | 138 | |
Domaini | 4413 – 4668 | NiRANPROSITE-ProRule annotationAdd BLAST | 256 | |
Domaini | 4768 – 5335 | Nsp12 RNA-dependent RNA polymerasePROSITE-ProRule annotationAdd BLAST | 568 | |
Domaini | 5015 – 5177 | RdRp catalyticAdd BLAST | 163 | |
Domaini | 5336 – 5419 | CV ZBDPROSITE-ProRule annotationAdd BLAST | 84 | |
Domaini | 5591 – 5772 | (+)RNA virus helicase ATP-bindingAdd BLAST | 182 | |
Domaini | 5773 – 5942 | (+)RNA virus helicase C-terminalAdd BLAST | 170 | |
Domaini | 6009 – 6224 | ExoNPROSITE-ProRule annotationAdd BLAST | 216 | |
Domaini | 6233 – 6459 | N7-MTasePROSITE-ProRule annotationAdd BLAST | 227 | |
Domaini | 6460 – 6520 | Nsp15 N-terminal oligomerizationPROSITE-ProRule annotationAdd BLAST | 61 | |
Domaini | 6521 – 6641 | AV-Nsp11N/CoV-Nsp15MPROSITE-ProRule annotationAdd BLAST | 121 | |
Domaini | 6691 – 6830 | NendoUPROSITE-ProRule annotationAdd BLAST | 140 | |
Domaini | 6835 – 7129 | Nidovirus-type SAM-dependent 2'-O-MTasePROSITE-ProRule annotationAdd BLAST | 295 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 945 – 1034 | 9 X 10 AA tandem repeat of N-[DN]-D-E-D-V-V-T-G-DAdd BLAST | 90 | |
Regioni | 947 – 1042 | DisorderedSequence analysisAdd BLAST | 96 | |
Regioni | 2176 – 2413 | HD1By similarityAdd BLAST | 238 | |
Regioni | 2794 – 3173 | HD2By similarityAdd BLAST | 380 | |
Regioni | 3601 – 3813 | HD3By similarityAdd BLAST | 213 | |
Regioni | 6268 – 6274 | SAM-bindingPROSITE-ProRule annotation | 7 | |
Regioni | 6346 – 6360 | GpppA-bindingPROSITE-ProRule annotationAdd BLAST | 15 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 1188 – 1216 | C4-type 1PROSITE-ProRule annotationAdd BLAST | 29 | |
Zinc fingeri | 1785 – 1821 | C4-type 2PROSITE-ProRule annotationAdd BLAST | 37 | |
Zinc fingeri | 4344 – 4360 | By similarityAdd BLAST | 17 | |
Zinc fingeri | 4386 – 4399 | By similarityAdd BLAST | 14 |
Keywords - Domaini
Repeat, Transmembrane, Transmembrane helix, Zinc-fingerFamily and domain databases
CDDi | cd21409, 1B_cv_Nsp13-like, 1 hit cd21560, betaCoV-Nsp6, 1 hit cd21659, betaCoV_Nsp14, 1 hit cd21666, betaCoV_Nsp5_Mpro, 1 hit cd20762, capping_2-OMTase_Nidovirales, 1 hit cd21519, cv_beta_Nsp2_MHV-like, 1 hit cd21473, cv_Nsp4_TM, 1 hit cd21593, HCoV_HKU1-like_RdRp, 1 hit cd21167, M_alpha_beta_cv_Nsp15-like, 1 hit cd21557, Macro_X_Nsp3-like, 1 hit cd21161, NendoU_cv_Nsp15-like, 1 hit cd21467, Ubl1_cv_Nsp3_N-like, 1 hit cd21466, Ubl2_cv_PLpro_N_Nsp3-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, 2 hits 1.10.8.370, 1 hit 2.40.10.10, 2 hits 2.40.10.250, 1 hit 2.60.120.1680, 1 hit 3.10.20.350, 1 hit 3.10.20.540, 1 hit 3.30.160.820, 1 hit 3.30.70.3540, 1 hit 3.40.220.10, 1 hit 3.40.50.11020, 1 hit 3.40.50.11580, 1 hit 3.40.50.300, 2 hits |
InterProi | View protein in InterPro IPR027351, (+)RNA_virus_helicase_core_dom IPR022570, B-CoV_A_NSP1 IPR043608, CoV_NSP15_M IPR043606, CoV_NSP15_N IPR043613, CoV_NSP2_C IPR043611, CoV_NSP3_C IPR043612, CoV_NSP4_N IPR043502, DNA/RNA_pol_sf IPR041679, DNA2/NAM7-like_C IPR022733, DPUP_SUD_C_bCoV IPR037227, EndoU-like IPR002589, Macro_dom IPR043472, Macro_dom-like IPR044371, Macro_X_NSP3-like IPR042570, NAR_sf IPR043609, NendoU_nidovirus IPR044863, NIRAN IPR036333, NSP10_sf_CoV IPR044343, NSP13_1B_dom_CoV IPR027352, NSP13_ZBD_CoV-like IPR044315, NSP14_betaCoV IPR009466, NSP14_CoV IPR044322, NSP15_M_alpha_beta_CoV IPR043174, NSP15_middle_sf IPR042515, NSP15_N_CoV IPR044401, NSP15_NendoU_CoV IPR009461, NSP16_CoV-like IPR044384, NSP2_MHV-like IPR032592, NSP3_NAB_bCoV IPR044357, NSP3_Ubl1_dom_CoV IPR044353, Nsp3_Ubl2_dom_CoV IPR038083, NSP3A-like IPR032505, NSP4_C_CoV IPR038123, NSP4_C_sf_CoV IPR044367, NSP6_betaCoV IPR043610, NSP6_CoV 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 IPR002705, Pept_C30/C16_B_coronavir IPR013016, Peptidase_C16_CoV IPR008740, Peptidase_C30_CoV IPR043477, Peptidase_C30_dom3_CoV IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR043177, PLpro_N_sf_CoV IPR043503, PLpro_palm_finger_dom_CoV IPR043178, PLpro_thumb_sf_CoV IPR044347, RdRp_HCoV_HKU1-like IPR001205, RNA-dir_pol_C IPR009469, RNA_pol_N_coronovir IPR018995, RNA_synth_NSP10_CoV IPR029063, SAM-dependent_MTases |
Pfami | View protein in Pfam PF13087, AAA_12, 1 hit PF16251, bCoV_NAR, 1 hit 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 PF19212, CoV_NSP2_C, 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 PF11963, DUF3477, 1 hit PF01661, Macro, 1 hit PF01831, Peptidase_C16, 1 hit PF05409, Peptidase_C30, 1 hit PF00680, RdRP_1, 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 SSF159936, SSF159936, 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 PS51963, BCOV_NSP1_C, 1 hit PS51942, BCOV_NSP3C_C, 1 hit PS51945, BCOV_NSP3E_NAB, 1 hit PS51952, COV_EXON_MTASE_COACT, 1 hit PS51954, COV_N7_MTASE, 1 hit PS51962, COV_NSP1, 1 hit PS51948, COV_NSP12_RDRP, 1 hit PS51960, COV_NSP15_NTD, 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, 2 hits PS51657, PSRV_HELICASE, 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
MIKTSKYGLG FKWAPEFRWL LPDAAEELAS PMKSDEGGLC PSTGQAMESV
60 70 80 90 100
GFVYDNHVKI DCRCILGQEW HVQSNLIRDI FVHEDLHVVE VLTKTAVKSG
110 120 130 140 150
TAILIKSPLH SLGGFPKGYV MGLFRSYKTK RYVVHHLSMT TSTTNFGEDF
160 170 180 190 200
FGWIVPFGFM PSYVHKWFQF CRLYIEESDL IISNFKFDDY DFSVEAAYAE
210 220 230 240 250
VHAEPKGKYS QKAYALLRQY RGIKPVLFVD QYGCDYSGKL ADCLQAYGHY
260 270 280 290 300
SLQDMRQKQS VWLANCDFDI VVAWHVVRDS RFVMRLQTIA TICGIKYVAQ
310 320 330 340 350
PTEDVVDGDV VIREPVHLLS ADAIVLKLPS LMKVMTHMDD FSIKSIYNVD
360 370 380 390 400
LCDCGFVMQY GYVDCFNDNC DFYGWVSGNM MDGFSCPLCC TVYDSSEVKA
410 420 430 440 450
QSSGVIPENP VLFTNSTDTV NPDSFNLYGY SVTPFGSCIY WSPRPGLWIP
460 470 480 490 500
IIKSSVKSYD DLVYSGVVGC KSIVKETALI THALYLDYVQ CKCGNLEQNH
510 520 530 540 550
ILGVNNSWCR QLLLNRGDYN MLLKNIDLFV KRRADFACKF AVCGDGFVPF
560 570 580 590 600
LLDGLIPRSY YLIQSGIFFT SLMSQFSQEV SDMCLKMCIL FMDRVSVATF
610 620 630 640 650
YIEHYVNRLV TQFKLLGTTL VNKMVNWFNT MLDASAPATG WLLYQLLNGF
660 670 680 690 700
FVVSQANLNF VALIPDYAKI LVNKFYTFFK LLLECVTVDV LKDMPVLKTI
710 720 730 740 750
NGLVCIVGNK FYNVSTGLIP GFVLPCNAQE QQIYFFEGVA ESVIVEDDVI
760 770 780 790 800
ENVKSSLSSY EYCQPPKSVE KICIIDNMYM GKCGDKFFPI VMNDKNICLL
810 820 830 840 850
DHAWRFPCAG RKVNFNEKPV VMEIPSLMTV KVMFDLDSTF DDILGKVCSE
860 870 880 890 900
FEVEKGVTVD DFVAVVCDAI ENALNSCKEH PVVGYQVRAF LNKLNENVVY
910 920 930 940 950
LFDEAGDEAM ASRMYCTFAI EDVEDVISSE AVEDTIDGVV EDTINDDEDV
960 970 980 990 1000
VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV
1010 1020 1030 1040 1050
VTGDNDDEDV VTGDNDDEDV VTGDNNDEDV VTGDNNDEES VTGDNDDQIV
1060 1070 1080 1090 1100
VTGDDVDDIE SIYDFDTYKA LLVFNDVYND ALFVSYGSSV ETETYFKVNG
1110 1120 1130 1140 1150
LWSPTITHTN CWLRSVLLVM QKLPFKFKDL AIENMWLSYK VGYNQSFVDY
1160 1170 1180 1190 1200
LLTTIPKAIV LPQGGYVADF AYWFLNQFDI NAYANWCCLK CGFSFDLNGL
1210 1220 1230 1240 1250
DAVFFYGDIV SHVCKCGHNM TLIAADLPCT LHFSLFDDNF CAFCTPKKIF
1260 1270 1280 1290 1300
IAACAVDVNV CHSVAVIGDE QIDGKFVTKF SGDKFDFIVG YGMSFSMSSF
1310 1320 1330 1340 1350
ELAQLYGLCI TPNVCFVKGD IINVARLVKA DVIVNPANGH MLHGGGVAKA
1360 1370 1380 1390 1400
IAVAAGKKFS KETAAMVKSK GVCQVGDCYV STGGKLCKTI LNIVGPDARQ
1410 1420 1430 1440 1450
DGRQSYVLLA RAYKHLNNYD CCLSTLISAG IFSVPADVSL TYLLGVVDKQ
1460 1470 1480 1490 1500
VILVSNNKED FDIIQKCQIT SVVGTKALAV RLTANVGRVI KFETDAYKLF
1510 1520 1530 1540 1550
LSGDDCFVSN SSVIQEVLLL RHDIQLNNDV RDYLLSKMTS LPKDWRLINK
1560 1570 1580 1590 1600
FDVINGVKTV KYFECPNSIY ICSQGKDFGY VCDGSFYKAT VNQVCVLLAK
1610 1620 1630 1640 1650
KIDVLLTVDG VNFKSISLTV GEVFGKILGN VFCDGIDVTK LKCSDFYADK
1660 1670 1680 1690 1700
ILYQYENLSL ADISAVQSSF GFDQQQLLAY YNFLTVCKWS VVVNGPFFSF
1710 1720 1730 1740 1750
EQSHNNCYVN VACLMLQHIN LKFNKWQWQE AWYEFRAGRP HRLVALVLAK
1760 1770 1780 1790 1800
GHFKFDEPSD ATDFIRVVLK QADLSGAICE LELICDCGIK QESRVGVDAV
1810 1820 1830 1840 1850
MHFGTLAKTD LFNGYKIGCN CAGRIVHCTK LNVPFLICSN TPLSKDLPDD
1860 1870 1880 1890 1900
VVAANMFMGV GVGHYTHLKC GSPYQHYDAC SVKKYTGVSG CLTDCLYLKN
1910 1920 1930 1940 1950
LTQTFTSMLT NYFLDDVEMV AYNPDLSQYY CDNGKYYTKP IIKAQFKPFA
1960 1970 1980 1990 2000
KVDGVYTNFK LVGHDICAQL NDKLGFNVDL PFVEYKVTVW PVATGDVVLA
2010 2020 2030 2040 2050
SDDLYVKRYF KGCETFGKPV IWFCHDEASL NSLTYFNKPS FKSENRYSVL
2060 2070 2080 2090 2100
SVDSVSEESQ GNVVTSVMES QISTKEVKLK GVRKTVKIED AIIVNDENSS
2110 2120 2130 2140 2150
IKVVKSLSLV DVWDMYLTGC DYVVWVANEL SRLVKSPTVR EYIRYGIKPI
2160 2170 2180 2190 2200
TIPIDLLCLR DDNQTLLVPK IFKARAIEFY GFLKWLFIYV FSLLHFTNDK
2210 2220 2230 2240 2250
TIFYTTEIAS KFTFNLFCLA LKNAFQTFRW SIFIKGFLVV ATVFLFWFNF
2260 2270 2280 2290 2300
LYINVIFSDF YLPNISVFPI FVGRIVMWIK ATFGLVTICD FYSKLGVGFT
2310 2320 2330 2340 2350
SHFCNGSFIC ELCHSGFDML DTYAAIDFVQ YEVDRRVLFD YVSLVKLIVE
2360 2370 2380 2390 2400
LVIGYSLYTV WFYPLFCLIG LQLFTTWLPD LFMLETMHWL IRFIVFVANM
2410 2420 2430 2440 2450
LPAFVLLRFY IVVTAMYKVV GFIRHIVYGC NKAGCLFCYK RNCSVRVKCS
2460 2470 2480 2490 2500
TIVGGVIRYY DITANGGTGF CVKHQWNCFN CHSFKPGNTF ITVEAAIELS
2510 2520 2530 2540 2550
KELKRPVNPT DASHYVVTDI KQVGCMMRLF YDRDGQRVYD DVDASLFVDI
2560 2570 2580 2590 2600
NNLLHSKVKV VPNLYVVVVE SDADRANFLN AVVFYAQSLY RPILLVDKKL
2610 2620 2630 2640 2650
ITTACNGISV TQIMFDVYVD TFMSHFDVDR KSFNNFVNIA HASLREGVQL
2660 2670 2680 2690 2700
EKVLDTFVGC VRKCCSIDSD VETRFITKSM ISAVAAGLEF TDENYNNLVP
2710 2720 2730 2740 2750
TYLKSDNIVA ADLGVLIQNG AKHVQGNVAK VANISCIWFI DAFNQLTADL
2760 2770 2780 2790 2800
QHKLKKACVK TGLKLKLTFN KQEASVPILT TPFSLKGGVV LSNLLYILFF
2810 2820 2830 2840 2850
ISLICFILLW ALLPTYSVYK SDIHLPAYAS FKVIDNGVVR DISVNDLCFA
2860 2870 2880 2890 2900
NKFFQFDQWY ESTFGSVYYH NSMDCPIVVA VMDEDIGSTM FNVPTKVLRY
2910 2920 2930 2940 2950
GFHVLHFLTY AFASDSVQCY TPHIQISYND FYASGCVLSS LCTMFKRGDG
2960 2970 2980 2990 3000
TPHPYCYTDG VMKNASLYTS LVPHTRYSLA NSNGFIRFPD VISEGIVRIV
3010 3020 3030 3040 3050
RTRSMTYCRV GACEYAEEGI CFNFNSSWVL NNDYYRSMPG TFCGRDFFDL
3060 3070 3080 3090 3100
FYQFFSSLIR PIDFFSLTAS SIFGAILAIV VVLVFYYLIK LKRAFGDYTS
3110 3120 3130 3140 3150
VVVINVIVWC INFLMLFVFQ VYPICACVYA CFYFYVTLYF PSEISVIMHL
3160 3170 3180 3190 3200
QWIVMYGAIM PFWFCVTYVA MVIANHVLWL FSYCRKIGVN VCSDSTFEET
3210 3220 3230 3240 3250
SLTTFMITKD SYCRLKNSVS DVAYNRYLSL YNKYRYYSGK MDTAAYREAA
3260 3270 3280 3290 3300
CSQLAKAMET FNHNNGNDVL YQPPTASVST SFLQSGIVKM VSPTSKIEPC
3310 3320 3330 3340 3350
LVSVTYGSMT LNGLWLDDKV YCPRHVICLS SNMNEPDYSA LLCRVTLGDF
3360 3370 3380 3390 3400
TIMSGRMSLT VVSYQMQGCQ LVLTVSLQNP YTPKYTFGVV KPGETFTVLA
3410 3420 3430 3440 3450
AYNGRPQGAF HVTMRSSYTI KGSFLCGSCG SVGYVLTGDS VKFVYMHQLE
3460 3470 3480 3490 3500
LSTGCHTGTD FNGNFYGPYR DAQVVQLPVK DYVQTVNVIA WLYAAILNNC
3510 3520 3530 3540 3550
AWFVQNDVCS IEDFNVWAMT NGFSQVKADL VLDALASMTG VSIETLLAAI
3560 3570 3580 3590 3600
KRLYMGFQGR QILGSCTFED ELAPSDVYQQ LAGVKLQSKT KRFIKETIYW
3610 3620 3630 3640 3650
ILISTFLFSC IISAFVKWTI FMYINTHMIG VTLCVLCFVS FMMLLVKHKH
3660 3670 3680 3690 3700
FYLTMYIIPV LCTLFYVNYL VVYKEGFRGF TYVWLSHFVP AVNFTYVYEV
3710 3720 3730 3740 3750
FYGCILCVFA IFITMHSINH DIFSLMFLVG RIVTLISMWY FGSNLEEDVL
3760 3770 3780 3790 3800
LFITAFLGTY TWTTILSLAI AKIVANWLSV NIFYFTDVPY IKLILLSYLF
3810 3820 3830 3840 3850
IGYILSCYWG FFSLLNSVFR MPMGVYNYKI SVQELRYMNA NGLRPPRNSF
3860 3870 3880 3890 3900
EAILLNLKLL GIGGVPVIEV SQIQSKLTDV KCANVVLLNC LQHLHVASNS
3910 3920 3930 3940 3950
KLWQYCSVLH NEILSTSDLS VAFDKLAQLL IVLFSNPAAV DTKCLASIDE
3960 3970 3980 3990 4000
VSDDYVQDST VLQALQSEFV NMASFVEYEV AKKNLADAKN SGSVNQQQIK
4010 4020 4030 4040 4050
QLEKACNIAK SVYERDKAVA RKLERMADLA LTNMYKEARI NDKKSKVVSA
4060 4070 4080 4090 4100
LQTMLFSMVR KLDNQALNSI LDNAVKGCVP LSAIPALAAN TLTIIIPDKQ
4110 4120 4130 4140 4150
VFDKVVDNVY VTYAGSVWHI QTVQDADGIN KQLTDISVDS NWPLVIIANR
4160 4170 4180 4190 4200
YNEVANAVMQ NNELMPHKLK IQVVNSGSDI NCNIPTQCYY NNVSSGRIVY
4210 4220 4230 4240 4250
AVLSDVDGLK YTKIMKDDGN CVVLELDPPC KFSIQDVKGL KIKYLYFIKG
4260 4270 4280 4290 4300
CNTLARGWVV GTLSSTIRLQ AGVATEYAAN SSILSLCAFS VDPKKTYLDY
4310 4320 4330 4340 4350
IQQGGVPIIN CVKMLCDHAG TGMAITIKPE ATINQDSYGG ASVCIYCRAR
4360 4370 4380 4390 4400
VEHPDVDGIC KLRGKFVQVP LGIKDPILYV LTHDVCQVCG FWRDGSCSCV
4410 4420 4430 4440 4450
GSSVAVQSKD LNFLNRVRGT SVNARLVPCA SGLSTDVQLR AFDICNTNRA
4460 4470 4480 4490 4500
GIGLYYKVNC CRFQRIDDDG NKLDKFFVVK RTNLEVYNKE KTYYELTKSC
4510 4520 4530 4540 4550
GVVAEHDFFT FDIDGSRVPH IVRRNLSKYT MLDLCYALRH FDRNDCSILC
4560 4570 4580 4590 4600
EILCEYADCK ESYFSKKDWY DFVENPDIIN IYKKLGPIFN RALLNTVIFA
4610 4620 4630 4640 4650
DTLVEVGLVG VLTLDNQDLY GQWYDFGDFI QTAPGFGVAV ADSYYSYMMP
4660 4670 4680 4690 4700
MLTMCHVLDC ELFVNDSYRQ FDLVQYDFTD YKLELFNKYF KYWGMKYHPN
4710 4720 4730 4740 4750
TVDCDNDRCI IHCANFNILF SMVLPNTCFG PLVRQIFVDG VPFVVSIGYH
4760 4770 4780 4790 4800
YKELGVVMNL DVDTHRYRLS LKDLLLYAAD PAMHVASASA LLDLRTCCFS
4810 4820 4830 4840 4850
VAAITSGIKF QTVKPGNFNQ DFYEFVKSKG LFKEGSTVDL KHFFFTQDGN
4860 4870 4880 4890 4900
AAITDYNYYK YNLPTMVDIK QLLFVLEVVY KYFEIYDGGC IPASQVIVNN
4910 4920 4930 4940 4950
YDKSAGYPFN KFGKARLYYE ALSFEEQNEI YAYTKRNVLP TLTQMNLKYA
4960 4970 4980 4990 5000
ISAKNRARTV AGVSILSTMT GRMFHQKCLK SIAATRGVPV VIGTTKFYGG
5010 5020 5030 5040 5050
WDDMLRHLIK DVDNPVLMGW DYPKCDRAMP NILRIVSSLV LARKHEFCCS
5060 5070 5080 5090 5100
HGDRFYRLAN ECAQVLSEIV MCGGCYYVKP GGTSSGDATT AFANSVFNIC
5110 5120 5130 5140 5150
QAVTANVCSL MACNGHKIED LSIRNLQKRL YSNVYRTDYV DYTFVNEYYE
5160 5170 5180 5190 5200
FLCKHFSMMI LSDDGVVCYN SDYANKGYIA NISAFQQVLY YQNNVFMSES
5210 5220 5230 5240 5250
KCWVENDITN GPHEFCSQHT MLVKIDGDYV YLPYPDPSRI LGAGCFVDDL
5260 5270 5280 5290 5300
LKTDSVLLIE RFVSLAIDAY PLVYHENEEY QKVFRVYLEY IKKLYNDLGT
5310 5320 5330 5340 5350
QILDSYSVIL STCDGLKFTE ESFYKNMYLK SAVMQSVGAC VVCSSQTSLR
5360 5370 5380 5390 5400
CGSCIRKPLL CCKCCYDHVM ATNHKYVLSV SPYVCNAPNC DVSDVTKLYL
5410 5420 5430 5440 5450
GGMSYYCENH KPHYSFKLVM NGMVFGLYKQ SCTGSPYIDD FNKIASCKWT
5460 5470 5480 5490 5500
EVDDYVLANE CIERLKLFAA ETQKATEEAF KQSYASATIQ EIVSDREVIL
5510 5520 5530 5540 5550
CWETGKVKPP LNKNYVFTGY HFTSTGKTVL GEYVFDKSEL TNGVYYRATT
5560 5570 5580 5590 5600
TYKLSIGDVF VLTSHSVASL SAPTLVPQEN YASIRFSSVY SVPLVFQNNV
5610 5620 5630 5640 5650
ANYQHIGMKR YCTVQGPPGT GKSHLAIGLA VYYYTARVVY TAASHAAVDA
5660 5670 5680 5690 5700
LCEKAYKFLN INDCTRIIPA KVRVDCYDKF KINDTTCKYV FTTINALPEL
5710 5720 5730 5740 5750
VTDIVVVDEV SMLTNYELSV INARIKAKHY VYIGDPAQLP APRVLLSKGS
5760 5770 5780 5790 5800
LEPRHFNSIT KIMCCLGPDI FLGNCYRCPK EIVETVSALV YDNKLKAKND
5810 5820 5830 5840 5850
NSSLCFKVYF KGQTTHESSS AVNIQQIYLI SKFLKANPVW NSAVFISPYN
5860 5870 5880 5890 5900
SQNYVAKRVL GVQTQTVDSA QGSEYDYVIY SQTAETAHSV NVNRFNVAIT
5910 5920 5930 5940 5950
RAKKGIFCVM SNMQLFESLN FITLPLDKIQ NQTLPRLHCT TNLFKDCSKS
5960 5970 5980 5990 6000
CLGYHPAHAP SFLAVDDKYK VNENLAVNLN ICEPVLTYSR LISLMGFKLD
6010 6020 6030 6040 6050
LTLDGYSKLF ITKDEAIKRV RGWVGFDVEG AHATRENIGT NFPLQIGFST
6060 6070 6080 6090 6100
GVDFVVEATG LFAERDCYTF KKTVAKAPPG EKFKHLIPLM SKGQKWDIVR
6110 6120 6130 6140 6150
IRIVQMLSDY LLDLSDSVVF ITWSASFELT CLRYFAKLGR ELNCNVCSNR
6160 6170 6180 6190 6200
ATCYNSRTGY YGCWRHSYTC DYVYNPLIVD IQQWGYTGSL TSNHDIICNV
6210 6220 6230 6240 6250
HKGAHVASAD AIMTRCLAIY DCFCKSVNWN LEYPIISNEV SINTSCRLLQ
6260 6270 6280 6290 6300
RVMLKAAMLC NRYNLCYDIG NPKGLACVKD YEFKFYDAFP VAKSVKQLFY
6310 6320 6330 6340 6350
VYDVHKDNFK DGLCMFWNCN VDKYPSNSIV CRFDTRVLNK LNLPGCNGGS
6360 6370 6380 6390 6400
LYVNKHAFHT NPFTRTVFEN LKPMPFFYYS DTPCVYVDGL ESKQVDYVPL
6410 6420 6430 6440 6450
RSATCITRCN LGGAVCSKHA EEYCNYLESY NIVTTAGFTF WVYKTFDFYN
6460 6470 6480 6490 6500
LWNTFTTLQS LENVIYNLVN VGHYDGRTGE LPCAIMNDKV VVKINNVDTV
6510 6520 6530 6540 6550
IFKNNTSFPT NIAVELFTKR SIRHHPELKI LRNLNIDICW KHVLWDYVKD
6560 6570 6580 6590 6600
SLFCSSTYGV CKYTDLKFIE NLNILFDGRD TGALEAFRKA RNGVFISTEK
6610 6620 6630 6640 6650
LSRLSMIKGP QRADLNGVIV DKVGELKVEF WFAMRKDGDD VIFSRTDSLC
6660 6670 6680 6690 6700
SSHYWSPQGN LGGNCAGNVI GNDALTRFTI FTQSRVLSSF EPRSDLERDF
6710 6720 6730 6740 6750
IDMDDNLFIA KYGLEDYAFD HIVYGSFNHK VIGGLHLLIG LFRRLKKSNL
6760 6770 6780 6790 6800
LIQEFLQYDS SIHSYFITDQ ECGSSKSVCT VIDLLLDDFV SIVKSLNLSC
6810 6820 6830 6840 6850
VSKVVNINVD FKDFQFMLWC NDNKIMTFYP KMQATNDWKP GYSMPVLYKY
6860 6870 6880 6890 6900
LNVPLERVSL WNYGKPINLP TGCMMNVAKY TQLCQYLNTT TLAVPVNMRV
6910 6920 6930 6940 6950
LHLGAGSDKE VAPGSAVLRQ WLPSGSILVD NDLNPFVSDS LVTYFGDCMT
6960 6970 6980 6990 7000
LPFDCHWDLI ISDMYDPLTK NIGDYNVSKD GFFTYICHLI RDKLSLGGSV
7010 7020 7030 7040 7050
AIKITEFSWN ADLYKLMSCF AFWTVFCTNV NASSSEGFLI GINYLGKSSF
7060 7070 7080 7090 7100
EIDGNVMHAN YLFWRNSTTW NGGAYSLFDM TKFSLKLAGT AVVNLRPDQL
7110 7120 7130
NDLVYSLIER GKLLVRDTRK EIFVGDSLVN TC
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DQ339101 Genomic RNA Translation: ABC70717.1 |
Keywords - Coding sequence diversityi
Ribosomal frameshiftingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DQ339101 Genomic RNA Translation: ABC70717.1 |
3D structure databases
SMRi | P0C6X4 |
ModBasei | Search... |
Chemistry databases
BindingDBi | P0C6X4 |
Proteomic databases
PRIDEi | P0C6X4 |
Family and domain databases
CDDi | cd21409, 1B_cv_Nsp13-like, 1 hit cd21560, betaCoV-Nsp6, 1 hit cd21659, betaCoV_Nsp14, 1 hit cd21666, betaCoV_Nsp5_Mpro, 1 hit cd20762, capping_2-OMTase_Nidovirales, 1 hit cd21519, cv_beta_Nsp2_MHV-like, 1 hit cd21473, cv_Nsp4_TM, 1 hit cd21593, HCoV_HKU1-like_RdRp, 1 hit cd21167, M_alpha_beta_cv_Nsp15-like, 1 hit cd21557, Macro_X_Nsp3-like, 1 hit cd21161, NendoU_cv_Nsp15-like, 1 hit cd21467, Ubl1_cv_Nsp3_N-like, 1 hit cd21466, Ubl2_cv_PLpro_N_Nsp3-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, 2 hits 1.10.8.370, 1 hit 2.40.10.10, 2 hits 2.40.10.250, 1 hit 2.60.120.1680, 1 hit 3.10.20.350, 1 hit 3.10.20.540, 1 hit 3.30.160.820, 1 hit 3.30.70.3540, 1 hit 3.40.220.10, 1 hit 3.40.50.11020, 1 hit 3.40.50.11580, 1 hit 3.40.50.300, 2 hits |
InterProi | View protein in InterPro IPR027351, (+)RNA_virus_helicase_core_dom IPR022570, B-CoV_A_NSP1 IPR043608, CoV_NSP15_M IPR043606, CoV_NSP15_N IPR043613, CoV_NSP2_C IPR043611, CoV_NSP3_C IPR043612, CoV_NSP4_N IPR043502, DNA/RNA_pol_sf IPR041679, DNA2/NAM7-like_C IPR022733, DPUP_SUD_C_bCoV IPR037227, EndoU-like IPR002589, Macro_dom IPR043472, Macro_dom-like IPR044371, Macro_X_NSP3-like IPR042570, NAR_sf IPR043609, NendoU_nidovirus IPR044863, NIRAN IPR036333, NSP10_sf_CoV IPR044343, NSP13_1B_dom_CoV IPR027352, NSP13_ZBD_CoV-like IPR044315, NSP14_betaCoV IPR009466, NSP14_CoV IPR044322, NSP15_M_alpha_beta_CoV IPR043174, NSP15_middle_sf IPR042515, NSP15_N_CoV IPR044401, NSP15_NendoU_CoV IPR009461, NSP16_CoV-like IPR044384, NSP2_MHV-like IPR032592, NSP3_NAB_bCoV IPR044357, NSP3_Ubl1_dom_CoV IPR044353, Nsp3_Ubl2_dom_CoV IPR038083, NSP3A-like IPR032505, NSP4_C_CoV IPR038123, NSP4_C_sf_CoV IPR044367, NSP6_betaCoV IPR043610, NSP6_CoV 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 IPR002705, Pept_C30/C16_B_coronavir IPR013016, Peptidase_C16_CoV IPR008740, Peptidase_C30_CoV IPR043477, Peptidase_C30_dom3_CoV IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR043177, PLpro_N_sf_CoV IPR043503, PLpro_palm_finger_dom_CoV IPR043178, PLpro_thumb_sf_CoV IPR044347, RdRp_HCoV_HKU1-like IPR001205, RNA-dir_pol_C IPR009469, RNA_pol_N_coronovir IPR018995, RNA_synth_NSP10_CoV IPR029063, SAM-dependent_MTases |
Pfami | View protein in Pfam PF13087, AAA_12, 1 hit PF16251, bCoV_NAR, 1 hit 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 PF19212, CoV_NSP2_C, 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 PF11963, DUF3477, 1 hit PF01661, Macro, 1 hit PF01831, Peptidase_C16, 1 hit PF05409, Peptidase_C30, 1 hit PF00680, RdRP_1, 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 SSF159936, SSF159936, 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 PS51963, BCOV_NSP1_C, 1 hit PS51942, BCOV_NSP3C_C, 1 hit PS51945, BCOV_NSP3E_NAB, 1 hit PS51952, COV_EXON_MTASE_COACT, 1 hit PS51954, COV_N7_MTASE, 1 hit PS51962, COV_NSP1, 1 hit PS51948, COV_NSP12_RDRP, 1 hit PS51960, COV_NSP15_NTD, 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, 2 hits PS51657, PSRV_HELICASE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | R1AB_CVHN5 | |
Accessioni | P0C6X4Primary (citable) accession number: P0C6X4 Secondary accession number(s): Q0ZME9 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 10, 2008 |
Last sequence update: | June 10, 2008 | |
Last modified: | February 23, 2022 | |
This is version 104 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |