UniProtKB - P0C6W2 (R1AB_BCHK3)
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:2.7.7.48PROSITE-ProRule annotation
- 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 |
---|---|---|---|---|
Metal bindingi | 200 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 231 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 234 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 236 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 323 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 326 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 341 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 344 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 370 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 373 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 382 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 416 | Zinc 3PROSITE-ProRule annotation | 1 | |
Active sitei | 1645 | For PL-PRO activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1806 | For PL-PRO activityPROSITE-ProRule annotation | 1 | |
Active sitei | 3275 | For 3CL-PRO activityPROSITE-ProRule annotation | 1 | |
Active sitei | 3379 | For 3CL-PRO activityPROSITE-ProRule annotation | 1 | |
Metal bindingi | 4298 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4301 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4307 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4314 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4341 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4344 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4352 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4354 | Zinc 2PROSITE-ProRule annotation | 1 | |
Active sitei | 5122 | PROSITE-ProRule annotation | 1 | |
Active sitei | 5123 | PROSITE-ProRule annotation | 1 | |
Active sitei | 5124 | PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5300 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5303 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5311 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5314 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5321 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5324 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5328 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5334 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5345 | Zinc 5PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5350 | Zinc 5PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5367 | Zinc 5PROSITE-ProRule annotation | 1 | |
Metal bindingi | 5370 | Zinc 5PROSITE-ProRule annotation | 1 | |
Active sitei | 5986 | PROSITE-ProRule annotation | 1 | |
Active sitei | 5988 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6087 | PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6103 | Zinc 6PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6106 | Zinc 6PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6122 | Zinc 6PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6125 | Zinc 6PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6153 | Zinc 7PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6157 | Zinc 7PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6160 | Zinc 7PROSITE-ProRule annotation | 1 | |
Active sitei | 6164 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6169 | PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6175 | Zinc 7PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6348 | Zinc 8PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6369 | Zinc 8PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6380 | Zinc 8PROSITE-ProRule annotation | 1 | |
Metal bindingi | 6383 | Zinc 8PROSITE-ProRule annotation | 1 | |
Active sitei | 6657 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6672 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6712 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6815 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6899 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6939 | PROSITE-ProRule annotation | 1 | |
Active sitei | 6972 | PROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 1723 – 1760 | C4-typePROSITE-ProRule annotationAdd BLAST | 38 | |
Zinc fingeri | 4298 – 4314 | By similarityAdd BLAST | 17 | |
Zinc fingeri | 4341 – 4354 | By similarityAdd BLAST | 14 | |
Nucleotide bindingi | 5577 – 5584 | 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
- G-quadruplex RNA binding 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 protein processing Source: InterPro
- viral RNA genome replication Source: InterPro
Keywordsi
Protein family/group databases
MEROPSi | C30.005 |
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): Leader protein Alternative name(s): p65 homolog Alternative name(s): Non-structural protein 3 Short name: nsp3 Alternative name(s): nsp5 Alternative name(s): Growth factor-like peptide Short name: GFL Alternative name(s): nsp12 Alternative name(s): nsp13 Alternative name(s): nsp14 Alternative name(s): NendoU nsp15 Alternative name(s): nsp16 |
Gene namesi | Name:rep ORF Names:1a-1b |
Organismi | Bat coronavirus HKU3 (BtCoV) (SARS-like coronavirus HKU3) |
Taxonomic identifieri | 442736 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Pisuviricota › Pisoniviricetes › Nidovirales › Cornidovirineae › Coronaviridae › Orthocoronavirinae › Betacoronavirus › Sarbecovirus › |
Virus hosti | Rhinolophus sinicus (Chinese rufous horseshoe bat) [TaxID: 89399] |
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 (By similarity).By similarity
- 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 (By similarity).By similarity
- 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 (By similarity).By similarity
- 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 (By similarity).By similarity
- 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.By similarity
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transmembranei | 2197 – 2217 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 2298 – 2318 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 2345 – 2365 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 2744 – 2764 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 2986 – 3006 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3016 – 3036 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3048 – 3068 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3071 – 3091 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3099 – 3119 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3136 – 3156 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3558 – 3578 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3580 – 3600 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3606 – 3626 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3652 – 3672 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3679 – 3698 | HelicalSequence analysisAdd BLAST | 20 | |
Transmembranei | 3722 – 3742 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3750 – 3770 | HelicalSequence analysisAdd BLAST | 21 |
Keywords - Cellular componenti
Host cytoplasm, Host membrane, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000291335 | 1 – 179 | Host translation inhibitor nsp1By similarityAdd BLAST | 179 | |
ChainiPRO_0000291336 | 180 – 818 | Non-structural protein 2By similarityAdd BLAST | 639 | |
ChainiPRO_0000291337 | 819 – 2734 | Papain-like proteinaseBy similarityAdd BLAST | 1916 | |
ChainiPRO_0000291338 | 2735 – 3234 | Non-structural protein 4By similarityAdd BLAST | 500 | |
ChainiPRO_0000291339 | 3235 – 3540 | 3C-like proteinaseBy similarityAdd BLAST | 306 | |
ChainiPRO_0000291340 | 3541 – 3830 | Non-structural protein 6By similarityAdd BLAST | 290 | |
ChainiPRO_0000291341 | 3831 – 3913 | Non-structural protein 7By similarityAdd BLAST | 83 | |
ChainiPRO_0000291342 | 3914 – 4111 | Non-structural protein 8By similarityAdd BLAST | 198 | |
ChainiPRO_0000291343 | 4112 – 4224 | Non-structural protein 9By similarityAdd BLAST | 113 | |
ChainiPRO_0000291344 | 4225 – 4363 | Non-structural protein 10By similarityAdd BLAST | 139 | |
ChainiPRO_0000291345 | 4364 – 5295 | RNA-directed RNA polymeraseBy similarityAdd BLAST | 932 | |
ChainiPRO_0000291346 | 5296 – 5896 | HelicaseBy similarityAdd BLAST | 601 | |
ChainiPRO_0000291347 | 5897 – 6423 | Guanine-N7 methyltransferaseBy similarityAdd BLAST | 527 | |
ChainiPRO_0000291348 | 6424 – 6769 | Uridylate-specific endoribonucleaseBy similarityAdd BLAST | 346 | |
ChainiPRO_0000291349 | 6770 – 7067 | 2'-O-methyltransferaseBy similarityAdd BLAST | 298 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 179 – 180 | Cleavage; by PL-PROBy similarity | 2 | |
Sitei | 818 – 819 | Cleavage; by PL-PROBy similarity | 2 | |
Sitei | 3234 – 3235 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 3540 – 3541 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 3830 – 3831 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 3913 – 3914 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 4111 – 4112 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 4224 – 4225 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 4363 – 4364 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 5295 – 5296 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 5896 – 5897 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 6423 – 6424 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 6769 – 6770 | Cleavage; by 3CL-PROBy similarity | 2 |
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 similarityFamily & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 12 – 127 | CoV Nsp1 globularPROSITE-ProRule annotationAdd BLAST | 116 | |
Domaini | 148 – 179 | BetaCoV Nsp1 C-terminalPROSITE-ProRule annotationAdd BLAST | 32 | |
Domaini | 183 – 456 | CoV Nsp2 N-terminalPROSITE-ProRule annotationAdd BLAST | 274 | |
Domaini | 458 – 688 | CoV Nsp2 middlePROSITE-ProRule annotationAdd BLAST | 231 | |
Domaini | 690 – 818 | CoV Nsp2 C-terminalPROSITE-ProRule annotationAdd BLAST | 129 | |
Domaini | 822 – 930 | Ubiquitin-like 1PROSITE-ProRule annotationAdd BLAST | 109 | |
Domaini | 998 – 1164 | Macro 1PROSITE-ProRule annotationAdd BLAST | 167 | |
Domaini | 1201 – 1329 | Macro 2PROSITE-ProRule annotationAdd BLAST | 129 | |
Domaini | 1337 – 1464 | Macro 3PROSITE-ProRule annotationAdd BLAST | 128 | |
Domaini | 1466 – 1532 | DPUPPROSITE-ProRule annotationAdd BLAST | 67 | |
Domaini | 1536 – 1591 | Ubiquitin-like 2PROSITE-ProRule annotationAdd BLAST | 56 | |
Domaini | 1605 – 1869 | Peptidase C16PROSITE-ProRule annotationAdd BLAST | 265 | |
Domaini | 1882 – 1992 | Nucleic acid-bindingPROSITE-ProRule annotationAdd BLAST | 111 | |
Domaini | 2017 – 2126 | G2MPROSITE-ProRule annotationAdd BLAST | 110 | |
Domaini | 2631 – 2734 | CoV Nsp3 Y3PROSITE-ProRule annotationAdd BLAST | 104 | |
Domaini | 3136 – 3234 | Nsp4CPROSITE-ProRule annotationAdd BLAST | 99 | |
Domaini | 3235 – 3540 | Peptidase C30PROSITE-ProRule annotationAdd BLAST | 306 | |
Domaini | 3831 – 3913 | RdRp Nsp7 cofactorPROSITE-ProRule annotationAdd BLAST | 83 | |
Domaini | 3914 – 4111 | RdRp Nsp8 cofactorPROSITE-ProRule annotationAdd BLAST | 198 | |
Domaini | 4112 – 4224 | Nsp9 ssRNA-bindingPROSITE-ProRule annotationAdd BLAST | 113 | |
Domaini | 4225 – 4363 | ExoN/MTase coactivatorPROSITE-ProRule annotationAdd BLAST | 139 | |
Domaini | 4370 – 4624 | NiRANPROSITE-ProRule annotationAdd BLAST | 255 | |
Domaini | 4728 – 5295 | Nsp12 RNA-dependent RNA polymerasePROSITE-ProRule annotationAdd BLAST | 568 | |
Domaini | 4975 – 5137 | RdRp catalyticPROSITE-ProRule annotationAdd BLAST | 163 | |
Domaini | 5296 – 5379 | CV ZBDPROSITE-ProRule annotationAdd BLAST | 84 | |
Domaini | 5552 – 5733 | (+)RNA virus helicase ATP-bindingAdd BLAST | 182 | |
Domaini | 5734 – 5903 | (+)RNA virus helicase C-terminalAdd BLAST | 170 | |
Domaini | 5968 – 6183 | ExoNPROSITE-ProRule annotationAdd BLAST | 216 | |
Domaini | 6192 – 6423 | N7-MTasePROSITE-ProRule annotationAdd BLAST | 232 | |
Domaini | 6424 – 6484 | Nsp15 N-terminal oligomerizationPROSITE-ProRule annotationAdd BLAST | 61 | |
Domaini | 6485 – 6610 | AV-Nsp11N/CoV-Nsp15MPROSITE-ProRule annotationAdd BLAST | 126 | |
Domaini | 6627 – 6766 | NendoUPROSITE-ProRule annotationAdd BLAST | 140 | |
Domaini | 6771 – 7065 | Nidovirus-type SAM-dependent 2'-O-MTasePROSITE-ProRule annotationAdd BLAST | 295 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 200 – 236 | C2H2PROSITE-ProRule annotationAdd BLAST | 37 | |
Regioni | 323 – 344 | C4PROSITE-ProRule annotationAdd BLAST | 22 | |
Regioni | 370 – 416 | C2HCPROSITE-ProRule annotationAdd BLAST | 47 | |
Regioni | 2086 – 2365 | HD1By similarityAdd BLAST | 280 | |
Regioni | 2749 – 3156 | HD2By similarityAdd BLAST | 408 | |
Regioni | 3558 – 3770 | HD3By similarityAdd BLAST | 213 | |
Regioni | 6227 – 6233 | SAM-bindingPROSITE-ProRule annotation | 7 | |
Regioni | 6310 – 6324 | GpppA-bindingPROSITE-ProRule annotationAdd BLAST | 15 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 1723 – 1760 | C4-typePROSITE-ProRule annotationAdd BLAST | 38 | |
Zinc fingeri | 4298 – 4314 | By similarityAdd BLAST | 17 | |
Zinc fingeri | 4341 – 4354 | 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 cd21516, cv_beta_Nsp2_SARS-like, 1 hit cd21473, cv_Nsp4_TM, 1 hit cd21167, M_alpha_beta_cv_Nsp15-like, 1 hit cd21562, Macro_cv_SUD-N_Nsp3-like, 1 hit cd21557, Macro_X_Nsp3-like, 1 hit cd21161, NendoU_cv_Nsp15-like, 1 hit cd21171, NTD_alpha_beta_cv_Nsp15-like, 1 hit cd21591, SARS-CoV-like_RdRp, 1 hit cd21525, SUD_C_SARS-CoV_Nsp3, 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, 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 3.10.20.350, 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 3.40.220.20, 1 hit 3.40.220.30, 1 hit 3.40.30.150, 1 hit 3.40.50.11020, 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 IPR043613, CoV_NSP2_C IPR043611, CoV_NSP3_C IPR043612, CoV_NSP4_N IPR043502, DNA/RNA_pol_sf 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 IPR044330, NSP15_alpha_betaCoV_N IPR044322, NSP15_M_alpha_beta_CoV IPR043174, NSP15_middle_sf IPR042515, NSP15_N_CoV IPR044401, NSP15_NendoU_CoV IPR009461, NSP16_CoV-like IPR021590, NSP1_bCoV IPR038030, NSP1_sf_bCoV IPR043615, NSP2_N_CoV IPR044389, NSP2_SARS-CoV-like IPR024375, NSP3_bCoV IPR024358, NSP3_N_bCoV IPR032592, NSP3_NAB_bCoV IPR038166, NSP3_PL2pro_sf_CoV IPR038400, NSP3_SUD-M_sf_bCoV IPR044864, NSP3_SUD-N_bCoV IPR044374, NSP3_SUD-N_SARS-CoV IPR043478, NSP3_SUD-N_sf_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 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 IPR044351, RdRp_SARS-CoV-like 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 PF16251, bCoV_NAR, 1 hit PF11501, bCoV_NSP1, 1 hit PF12379, bCoV_NSP3_N, 1 hit PF12124, bCoV_SUD_C, 1 hit PF11633, bCoV_SUD_M, 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 PF19211, CoV_NSP2_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 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 SSF159936, SSF159936, 1 hit SSF160099, SSF160099, 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 PS51941, BCOV_NSP3C_M, 1 hit PS51994, BCOV_NSP3E_G2M, 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 PS51991, COV_NSP2_C, 1 hit PS51990, COV_NSP2_M, 1 hit PS51989, COV_NSP2_N, 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 PS51940, SARS_NSP3C_N, 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
MESLVLGVNE KTHVQLSLPV LQVRDVLVRG FGDSVEEALS EAREHLKNGT
60 70 80 90 100
CGLVELEKGV LPQLEQPYVF IKRSDALSTN HGHKVVELVA ELDGIQFGRS
110 120 130 140 150
GITLGVLVPH VGETPIAYRN VLLRKNGNKG AGGHSFGIDL KSYDLGDELG
160 170 180 190 200
TDPIEDYEQN WNTKHGSGAL RELTRELNGG VVTRYVDNNF CGPDGYPLEC
210 220 230 240 250
IKDFLARAGK SMCTLSEQLD YIESKRGVYC CREHEHEIVW FTERSEKSYE
260 270 280 290 300
HQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI
310 320 330 340 350
RSVYPVATPQ ECNDMHLSTL MKCNHCDEVS WQTCDFLKAT CEQCGTENLV
360 370 380 390 400
CEGPTTCGYL PTNAVVKMPC PACQDPEVGP EHSVADYHNH SNIETRLRKG
410 420 430 440 450
GRTKCFGGCV FSYVGCYNKR AYWVPRASAN IGANHTGITG ENVETLNEDL
460 470 480 490 500
LEILNRERVN INIVGDFRFN EEVAIILASF SASPSAFIET VKGLDYKSFK
510 520 530 540 550
VIVESCGNYK VTNGKPVTGA WNIGQQRSIL TPLCGFPSQA AGVIRSIFSR
560 570 580 590 600
TLDAANHSIL DLQRAAVTTL DGISEQSLRL VDAMVYTSDL LTNSVVVMAY
610 620 630 640 650
VTGGLVQQTM QWLSNMLGTA VDKLKPVFTW VEAKLSAGVE FLRDAWEILK
660 670 680 690 700
FLITGVFDVI KGQIQVATDN IKECVKIFLG VVNKALEMCL DQVTIAGTKL
710 720 730 740 750
RALNLGEVFI AQSRGLYRQC IRGKEQLQLL MPLKAPKEVT FLEGDAHDTV
760 770 780 790 800
LTSEEVVLKS GELEALETPI DSFTSGAVVG TPVCINGLML LELENKEQYC
810 820 830 840 850
ALSPGLLATN NVFRLKGGAP VKGVTFGEDT VLEVQGYKNV KITFELDVRV
860 870 880 890 900
DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTPMGIDLDE
910 920 930 940 950
WSVATFYLFD DAGEEKLSSR MYCSFYPPDE EEDCEECEDE EETCEHEYGT
960 970 980 990 1000
EDDYKGLPLE FGASTETPHV EEEEEEEDWL DDAIEAEPEP EPLPEEPVNQ
1010 1020 1030 1040 1050
FVGYLKLTDN VAIKCIDIVK EAQSAKPTVI VNAANTHLKH GGGVAGALNK
1060 1070 1080 1090 1100
ATNGAMQNES DEYIRQNGPL TVGGSCLLSG HNLAEKCLHV VGPNLNAGED
1110 1120 1130 1140 1150
VQLLKRAYEN FNSQDVLLAP LLSAGIFGAK PLQSLKMCVE IVRTQVYLAV
1160 1170 1180 1190 1200
NDKSLYDQIV LDYLDSLKPK VESPNKEEEP KLEEPKAVQP VAEKPVDVKP
1210 1220 1230 1240 1250
KIKACIDEVT TTLEETKFLT NKLLLFADIN GKLYQDSQNM LRGEDMSFLE
1260 1270 1280 1290 1300
KDAPYIVGDV ITSGDITCVI IPAKKSGGTT EMLARALKEV PVAEYITTYP
1310 1320 1330 1340 1350
GQGCAGYTLE EAKTALKKCK SAFYVLPSET PNEKEEVLGT VSWNLREMLA
1360 1370 1380 1390 1400
HAEETRKLMP ICLDVRAIMA TIQRKYKGIK VQEGIVDYGV RFFFYTSKEP
1410 1420 1430 1440 1450
VASIITKLNS LNEPLVTMPI GYVTHGLNLE EAARCMRSLK APAVVSVSSP
1460 1470 1480 1490 1500
DAVTAYNGYL TSSSKTPEEY FVETTSLAGS YRDWSYSGQR TELGVEFLKR
1510 1520 1530 1540 1550
GDKIVYHTTG SPIEFHLDGE VLPLDKLKSL LSLREVKTIK VFTTVDNTNL
1560 1570 1580 1590 1600
HTHIVDMSMT YGQQFGPTYL DGADVTKIKP HVNHEGKTFF VLPSDDTLRS
1610 1620 1630 1640 1650
EAFEYYHTID ESFLGRYMSA LNHTKKWKFP QVGGLTSIKW ADNNCYLSSV
1660 1670 1680 1690 1700
LLALQQVEVK FNAPALQEAY YRARAGDAAN FCALILAYSN KTVGELGDVR
1710 1720 1730 1740 1750
ETMTHLLQHA NLESAKRVLN VVCKHCGQKT TTLKGVEAVM YMGTLSYDEL
1760 1770 1780 1790 1800
KTGVSIPCVC GRNATQYLVQ QESSFVMMSA PPAEYKLQQG AFLCANEYTG
1810 1820 1830 1840 1850
NYQCGHYTHI TAKETLYRVD GAHLTKMSEY KGPVTDVFYK ETSYTTAIKP
1860 1870 1880 1890 1900
VSYKLDGVTY TEIEPKLDGY YKKGNAYYTE QPIDLVPTQP MPNASFDNFK
1910 1920 1930 1940 1950
LTCSNTKFAD DLNQMTGFKK PASRELTVTF FPDLNGDVVA IDYRHYSTSF
1960 1970 1980 1990 2000
KKGAKLVHKP ILWHINQTTN KTTYKPNIWC LRCLWSTKPV DTSNSFEVLV
2010 2020 2030 2040 2050
VEDTQGMDNL ACESQTTTSE EVVENPTVQK EIIECDVKTT EVVGNVILKP
2060 2070 2080 2090 2100
SEEGVKVTQE LGHEDLMAAY VEETSITIKK PNELSLALGL KTLATHGAAA
2110 2120 2130 2140 2150
INSVPWSKIL AYVKPFLGQT AVITSNCIKK CVQRVFSNYM PYVITLLFQL
2160 2170 2180 2190 2200
CTFTKSTNSR IKASLPTTIA KNSVKSVAKL CLDVCINYVK SPKFSKLFTI
2210 2220 2230 2240 2250
VMWLLLLSIC LGSLTYVTAV LGVCLSSLGV PSYCDGVREL YINSSNVTTM
2260 2270 2280 2290 2300
DFCQGYFPCS VCLSGLDSLD SYPALETIQV TISSYKLDLT FLGLAAEWLL
2310 2320 2330 2340 2350
AYMLFTKFFY LLGLSAIMQA FFGYFASHFI SNSWLMWFII SIVQMAPVSA
2360 2370 2380 2390 2400
MVRMYIFFAS FYYVWKSYVH IMDGCTSSTC MMCYKRNRAT RVECTTIVNG
2410 2420 2430 2440 2450
VKRSFYVYAN GGRGFCKAHN WNCLNCDTFC AGSTFISDEV ARDLSLQFKR
2460 2470 2480 2490 2500
PINPTDQSAY VVDSVTVKNG ALHLYFDKAG QKTYERHPLS HFVNLDNLRA
2510 2520 2530 2540 2550
NNTKGSLPIN VIVFDGKSKC EESAAKSASV YYSQLMCQPI LLLDQALVSD
2560 2570 2580 2590 2600
VGDSTEVSVK MFDAYVDTFS ATFSVPMEKL KALVATAHSE LAKGVALDGV
2610 2620 2630 2640 2650
LSTFVSAARQ GVVDTDVDTK DVIECLKLSH HSDIEVTGDS CNNFMLTYNK
2660 2670 2680 2690 2700
VENMTPRDLG ACIDCNARHI NAQVAKSHNV SLVWNVKDYM SLSEQLRKQI
2710 2720 2730 2740 2750
RSAAKKNNIP FRLTCATTRQ VVNVITTKIS LKGGKVVSTW FKLLLKVTLL
2760 2770 2780 2790 2800
CVLAALFCYV IMPVHSLSVH DGYTNEIIGY KAIQDGVTRD IVSTDDCFAN
2810 2820 2830 2840 2850
KHAGFDSWFS QRGGSYRNDK NCPVVAAIIT REIGFIVPGL PGTVLRALNG
2860 2870 2880 2890 2900
DFLHFLPRVF SAVGNICYTP SKLIEYSDFA TSACVLAAEC TIFKDAMGKP
2910 2920 2930 2940 2950
VPYCYDTNLL EGSISYSELR PDTRYVLMDG SIIQFPNTYL EGSVRVVTTF
2960 2970 2980 2990 3000
DAEYCRHGTC ERSEVGVCLS TSGRWVLNNE HYRALPGVFC GVDAMNLIAN
3010 3020 3030 3040 3050
IFTPLVQPVG ALDVSASVVA GGIIAILVTC AAYYFMKFRR AFGEYNHVVA
3060 3070 3080 3090 3100
ANALLFLMSF TILCLAPAYS FLPGVYSIFY LYLTFYFTND VSFLAHLQWF
3110 3120 3130 3140 3150
AMFSPIVPFW ITAIYVFCIS LKHFHWFFSN YLKKRVMFNG VTFSTFEEAA
3160 3170 3180 3190 3200
LCTFLLNKEM YLRLRSETLL PLTQYNRYLA LYNKYKYFSG ALDTTSYREA
3210 3220 3230 3240 3250
ACCHLAKALN DFSNSGADVL YQPPQTSITS AVLQSGFRKM AFPSGKVEGC
3260 3270 3280 3290 3300
MVQVTCGTTT LNGLWLDDTV YCPRHVVCTA EDMLNPNYDD LLIRKSNHSF
3310 3320 3330 3340 3350
LVQAGNVQLR VIGHSMQNCL LRLKVDTSNP KTPKYKFVRI QPGQTFSVLA
3360 3370 3380 3390 3400
CYNGSPSGVY QCAMRPNHTI KGSFLNGSCG SVGFNIDYDC VSFCYMHHME
3410 3420 3430 3440 3450
LPTGVHAGTD LEGKFYGPFV DRQTAQAAGT DTTITLNVLA WLYAAVINGD
3460 3470 3480 3490 3500
RWFLNRFTTT LNDFNLVAMK YNYEPLTQDH VDILGPLSAQ TGIAVLDMCA
3510 3520 3530 3540 3550
ALKELLQNGM NGRTILGSTI LEDEFTPFDV VRQCSGVTFQ GKFKKIVKGT
3560 3570 3580 3590 3600
HHWMLLTFLT SLLILVQSTQ WSLFFFVYEN AFLPFALGIM AVAACAMLLV
3610 3620 3630 3640 3650
KHKHAFLCLF LLPSLATVAY FNMVYMPASW VMRIMTWLEL ADTSLSGYRL
3660 3670 3680 3690 3700
KDCVMYASAL VLLILMTART VYDDAARRVW TLMNVITLVY KVYYGNSLDQ
3710 3720 3730 3740 3750
AISMWALVIS VTSNYSGVVT TIMFLARAIV FVCVEYYPLL FITGNTLQCI
3760 3770 3780 3790 3800
MLVYCFLGYC CCCYFGLFCL LNRYFRLTLG VYDYLVSTQE FRYMNSQGLL
3810 3820 3830 3840 3850
PPKSSIDAFK LNIKLLGIGG KPCIKVATVQ SKMSDVKCTS VVLLSVLQQL
3860 3870 3880 3890 3900
RVESSSKLWA QCVQLHNDIL LAKDTTEAFE KMVSLLSVLL SMQGAVDINK
3910 3920 3930 3940 3950
LCEEMLDNRA TLQAIASEFS SLPSYAAYAT AQEAYEQAVS NGDSEVVLKK
3960 3970 3980 3990 4000
LKKSLNVAKS EFDHDAAMQR KLEKMADQAM TQMYKQARSE DKRAKVTSAM
4010 4020 4030 4040 4050
QTMLFTMLRK LDNDALNNII NNARDGCVPL NIIPLTTAAK LMVVVPDYGT
4060 4070 4080 4090 4100
YKNTCDGNTF TYASALWEIQ QVVDADSKIV QLSEINMDNS PNLAWPLIVT
4110 4120 4130 4140 4150
ALRANSAVKL QNNELSPVAL RQMSCAAGTT QTACTDDNAL AYYNNAKGGR
4160 4170 4180 4190 4200
FVLALLSDHQ DLKWARFPKS DGTGTIYTEL EPPCRFVTDT PKGPKVKYLY
4210 4220 4230 4240 4250
FIKGLNNLNR GMVLGSLAAT VRLQAGNATE VPANSTVLSF CAFAVDPAKA
4260 4270 4280 4290 4300
YKDYLASGGQ PITNCVKMLC THTGTGQAIT VTPEANMDQE SFGGASCCLY
4310 4320 4330 4340 4350
CRCHIDHPNP KGFCDLKGKY VQIPTTCAND PVGFTLRNTV CTVCGMWKGY
4360 4370 4380 4390 4400
GCSCDQLREP MMQSADASTF LNRVCGVSAA RLTPCGTGTS TDVVYRAFDI
4410 4420 4430 4440 4450
YNEKVAGFAK FLKTNCCRFQ EKDEEGNLLD SYFVVKRHTM SNYQHEETIY
4460 4470 4480 4490 4500
NLIKECPAVA VHDFFKFRVD GDMVPHISRQ RLTKYTMADL VYALRHFDEG
4510 4520 4530 4540 4550
NCDTLKEILV TYNCCDDNYF NKKDWYDFVE NPDVLRVYAN LGERVRRALL
4560 4570 4580 4590 4600
KTVQFCDAMR DAGIVGVLTL DNQDLNGNWY DFGDFVQVAP GCGVPIVDSY
4610 4620 4630 4640 4650
YSLLMPILTL TKALAAESHM DADLAKPLVK WDLLKYDFTE ERLCLFDRYF
4660 4670 4680 4690 4700
KYWDQTYHPN CINCLDDRCI LHCANFNVLF STVFPPTSFG PLVRKIFVDG
4710 4720 4730 4740 4750
VPFVVSTGYH FRELGVVHNQ DVNLHSSRLS FKELLVYAAD PAMHAASGNL
4760 4770 4780 4790 4800
LLDKRTTCFS VAALTNNVAF QTVKPGNFNK DFYDFAVSKG FFKEGSSVEL
4810 4820 4830 4840 4850
KHFFFAQDGN AAISDYDYYR YNLPTMCDIR QLLFVVEVVD KYFDCYDGGC
4860 4870 4880 4890 4900
INANQVIVNN LDKSAGFPFN KWGKARLYYD SMSYEDQDAL FAYTKRNVIP
4910 4920 4930 4940 4950
TITQMNLKYA ISAKNRARTV AGVSICSTMT NRQFHQKLLK SIAATRGATV
4960 4970 4980 4990 5000
VIGTSKFYGG WHNMLKTVYS DVESPHLMGW DYPKCDRAMP NMLRIMASLI
5010 5020 5030 5040 5050
LARKHSTCCN LSHRFYRLAN ECAQVLSEMV MCGGSLYVKP GGTSSGDATT
5060 5070 5080 5090 5100
AYANSVFNIC QAVTANVNAL LSTDGNKIAD KYVRNLQHRL YECLYRNRDV
5110 5120 5130 5140 5150
DHEFVDEFYA YLRKHFSMMI LSDDAVVCYN SNYAAQGLVA SIKNFKAVLY
5160 5170 5180 5190 5200
YQNNVFMSEA KCWTETDLTR GPHEFCSQHT MLVKQGDDYV YLPYPDPSRI
5210 5220 5230 5240 5250
LGAGCFVDDI VKTDGTLMIE RFVSLAIDAY PLTKHPNQEY ADVFHLYLQY
5260 5270 5280 5290 5300
IRKLHDELTG HMLDMYSVML TNDNTSRYWE PEFYEAMYTP HTVLQAVGAC
5310 5320 5330 5340 5350
VLCNSQTSLR CGACIRRPFL CCKCCYDHVI STSHKLVLSV NPYVCNAPGC
5360 5370 5380 5390 5400
DVTDVTQLYL GGMSYYCKSH KPPISFPLCA NGQVFGLYKN TCVGSDNVTD
5410 5420 5430 5440 5450
FNAIATCDWT NAGDYILANT CTERLKLFAA ETLKATEETF KLSYGIATVR
5460 5470 5480 5490 5500
EVLSDRELYL SWEVGKPRPP LNRNYVFTGY RVTKNSKVQI GEYTFEKGDY
5510 5520 5530 5540 5550
GDAVVYRGTT TYKLNVGDYF VLTSHTVMPL SAPTLVPQEH YVRITGLYPT
5560 5570 5580 5590 5600
LNISNEFSSN VANYQKIGMQ KYSTLQGPPG TGKSHFAIGL ALYYPSARIV
5610 5620 5630 5640 5650
YTACSHAAVD ALCEKALKYL PIDKCSRIIP ARARVECFDK FKVNSTLEQY
5660 5670 5680 5690 5700
VFCTVNALPE TTADIVVFDE ISMATNYDLS VVNARLRAKH YVYIGDPAQL
5710 5720 5730 5740 5750
PAPRTLLTKG TLEPEYFNSV CRLMKTIGPD MFLGTCRRCP AEIVDTVSAL
5760 5770 5780 5790 5800
VYDNKLKAHK EKSAQCFKMY YKGVITHDVS SAINRPQIGV VREFLTRNPA
5810 5820 5830 5840 5850
WRKAVFISPY NSQNAVASKI LGLPTQTVDS SQGSEYDYVI FTQTTETAHS
5860 5870 5880 5890 5900
CNVNRFNVAI TRAKIGILCI MSDRDLYDKL QFTSLEVPRR NVATLQAENV
5910 5920 5930 5940 5950
TGLFKDCSKI ITGLHPTQAP THLSVDTKFK TEGLCVDIPG IPKDMTYRRL
5960 5970 5980 5990 6000
ISMMGFKMNY QVNGYPNMFI TREEAIRHVR AWIGFDVEGC HATRDAVGTN
6010 6020 6030 6040 6050
LPLQLGFSTG VNLVAVPTGY VDTENSTEFT RVNAKPPPGD QFKHLIPLMY
6060 6070 6080 6090 6100
KGLPWNVVRI KIVQMLSDTL KGLSDRVVFV LWAHGFELTS MKYFVKIGPE
6110 6120 6130 6140 6150
RTCCLCDKRA TCFSTSSDTY ACWNHSVGFD YVYNPFMIDV QQWGFTGNLQ
6160 6170 6180 6190 6200
SNHDQHCQVH GNAHVASCDA IMTRCLAVHE CFVKRVDWSV EYPIIGDELK
6210 6220 6230 6240 6250
INAACRKVQH MVVKSALLAD KFTVLHDIGN PKAIRCVPQA EVDWKFYDAQ
6260 6270 6280 6290 6300
PCSDKAYKIE ELFYSYATHH DKFTDGVCLF WNCNVDRYPA NAIVCRFDTR
6310 6320 6330 6340 6350
VLSNLNLPGC DGGSLYVNKH AFHTPAFDKS AFTHLKQLPF FYYSDSPCES
6360 6370 6380 6390 6400
HGKQVVSDID YVPLKSATCI TRCNLGGAVC RHHANEYRQY LDAYNMMISA
6410 6420 6430 6440 6450
GFSLWIYKQF DTYNLWNTFT KLQSLENVAY NVVNKGHFDG QSGEAPVSII
6460 6470 6480 6490 6500
NNAVYTKVDG IDVEIFENKT TLPVNVAFEL WAKRNIKPVP EIKILNNLGV
6510 6520 6530 6540 6550
DIAANNVIWD YKREAPAHVS TIGVCTMTDI AKKPTESACS SLIVLFDGRV
6560 6570 6580 6590 6600
EGQVDFFRNA RNGVLITEGS VKGLTPSKGP AQASVNGVTL IGESVKTQFN
6610 6620 6630 6640 6650
YFKKVDGIIQ QLPETYFTQS RDLEDFKPRS QMETDFLELA MDEFIQRYKL
6660 6670 6680 6690 6700
EGYAFEHIVY GDFSHGQLGG LHLMIGLAKR SQDSLLKLED FIPMDSTVKN
6710 6720 6730 6740 6750
YFITDAQTGS SKCVCSVIDL LLDDFVEIIK SQDLSVVSKV VKVTIDYAEI
6760 6770 6780 6790 6800
SFMLWCKDGH VETFYPKLQA SQAWQPGVAM PNLYKMQRML LEKCDLQNYG
6810 6820 6830 6840 6850
ENAVIPKGIM MNVAKYTQLC QYLNTLTLAV PYNMRVIHFG AGSDKGVAPG
6860 6870 6880 6890 6900
TAVLRQWLPT GTLLVDSDLN DFVSDADSTL IGDCATVHTA NKWDLIISDM
6910 6920 6930 6940 6950
YDPKTKHVLK DNDSKEGFFT YLCGFIKQKL ALGGSVAVKI TEHSWNADLY
6960 6970 6980 6990 7000
KLMGHFSWWT AFVTNVNASS SEAFLIGVNY LGKPKEQIDG YTMHANYIFW
7010 7020 7030 7040 7050
RNTNPIQLSS YSLFDMSKFP LKLRGTAVMS LKENQINDMI YSLLEKGRLI
7060
IRENNRVVVS SDILVNN
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 | DQ022305 Genomic RNA Translation: AAY88865.2 |
Keywords - Coding sequence diversityi
Ribosomal frameshiftingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DQ022305 Genomic RNA Translation: AAY88865.2 |
3D structure databases
BMRBi | P0C6W2 |
SMRi | P0C6W2 |
ModBasei | Search... |
Protein family/group databases
MEROPSi | C30.005 |
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 cd21516, cv_beta_Nsp2_SARS-like, 1 hit cd21473, cv_Nsp4_TM, 1 hit cd21167, M_alpha_beta_cv_Nsp15-like, 1 hit cd21562, Macro_cv_SUD-N_Nsp3-like, 1 hit cd21557, Macro_X_Nsp3-like, 1 hit cd21161, NendoU_cv_Nsp15-like, 1 hit cd21171, NTD_alpha_beta_cv_Nsp15-like, 1 hit cd21591, SARS-CoV-like_RdRp, 1 hit cd21525, SUD_C_SARS-CoV_Nsp3, 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, 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 3.10.20.350, 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 3.40.220.20, 1 hit 3.40.220.30, 1 hit 3.40.30.150, 1 hit 3.40.50.11020, 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 IPR043613, CoV_NSP2_C IPR043611, CoV_NSP3_C IPR043612, CoV_NSP4_N IPR043502, DNA/RNA_pol_sf 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 IPR044330, NSP15_alpha_betaCoV_N IPR044322, NSP15_M_alpha_beta_CoV IPR043174, NSP15_middle_sf IPR042515, NSP15_N_CoV IPR044401, NSP15_NendoU_CoV IPR009461, NSP16_CoV-like IPR021590, NSP1_bCoV IPR038030, NSP1_sf_bCoV IPR043615, NSP2_N_CoV IPR044389, NSP2_SARS-CoV-like IPR024375, NSP3_bCoV IPR024358, NSP3_N_bCoV IPR032592, NSP3_NAB_bCoV IPR038166, NSP3_PL2pro_sf_CoV IPR038400, NSP3_SUD-M_sf_bCoV IPR044864, NSP3_SUD-N_bCoV IPR044374, NSP3_SUD-N_SARS-CoV IPR043478, NSP3_SUD-N_sf_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 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 IPR044351, RdRp_SARS-CoV-like 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 PF16251, bCoV_NAR, 1 hit PF11501, bCoV_NSP1, 1 hit PF12379, bCoV_NSP3_N, 1 hit PF12124, bCoV_SUD_C, 1 hit PF11633, bCoV_SUD_M, 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 PF19211, CoV_NSP2_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 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 SSF159936, SSF159936, 1 hit SSF160099, SSF160099, 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 PS51941, BCOV_NSP3C_M, 1 hit PS51994, BCOV_NSP3E_G2M, 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 PS51991, COV_NSP2_C, 1 hit PS51990, COV_NSP2_M, 1 hit PS51989, COV_NSP2_N, 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 PS51940, SARS_NSP3C_N, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | R1AB_BCHK3 | |
Accessioni | P0C6W2Primary (citable) accession number: P0C6W2 Secondary accession number(s): Q3LZX2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 10, 2008 |
Last sequence update: | June 10, 2008 | |
Last modified: | May 25, 2022 | |
This is version 95 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |