K9N7C7 · R1AB_MERS1
- ProteinReplicase polyprotein 1ab
- Generep
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids7078 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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.
Host translation inhibitor nsp1
Promotes the degradation of host mRNAs by inducing an endonucleolytic RNA cleavage in template mRNAs, and inhibits of host mRNA translation, a function that is separable from its RNA cleavage activity. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response.
Non-structural protein 2
May 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.
Papain-like proteinase nsp3
Responsible 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.
Non-structural protein 4
Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.
3C-like proteinase nsp5
Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN] (By similarity).
May cleave human NLRP1 in lung epithelial cells, thereby activating the NLRP1 inflammasome pathway (PubMed:35594856).
Also able to bind an ADP-ribose-1''-phosphate (ADRP) (By similarity).
May cleave human NLRP1 in lung epithelial cells, thereby activating the NLRP1 inflammasome pathway (PubMed:35594856).
Also able to bind an ADP-ribose-1''-phosphate (ADRP) (By similarity).
Non-structural protein 6
Plays 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.
Non-structural protein 7
Forms 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.
Non-structural protein 8
Forms 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.
Viral protein genome-linked nsp9
Forms a primer, NSP9-pU, which is utilized by the polymerase for the initiation of RNA chains. Interacts with ribosome signal recognition particle RNA (SRP). Together with NSP8, suppress protein integration into the cell membrane, thereby disrupting host immune defenses.
Non-structural protein 10
Plays 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.
RNA-directed RNA polymerase nsp12
RNA-directed RNA polymerase that catalyzes the transcription of viral genomic and subgenomic RNAs. Acts in complex with nsp7 and nsp8 to transcribe both the minus and positive strands of genomic RNA. The kinase-like NiRAN domain of NSP12 attaches one or more nucleotides to the amino terminus of NSP9, forming a covalent RNA-protein intermediate that serves as transcription/replication primer. Subgenomic RNAs (sgRNAs) are formed by discontinuous transcription: The polymerase has the ability to pause at transcription-regulating sequences (TRS) and jump to the leader TRS, resulting in a major deletion. This creates a series of subgenomic RNAs that are replicated, transcribed and translated. In addition, Nsp12 is a subunit of the viral RNA capping enzyme that catalyzes the RNA guanylyltransferase reaction for genomic and sub-genomic RNAs. Subsequently, the NiRAN domain transfers RNA to GDP, and forms the core cap structure GpppA-RNA.
Helicase nsp13
Multi-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.
Guanine-N7 methyltransferase nsp14
Plays a role in viral RNA synthesis through two distinct activities: an N7-guanine methyltransferase activity involved in the formation of the cap structure GpppA-RNA; a proofreading exoribonuclease for RNA replication that reduces the sensitivity of the virus to RNA mutagens. This activity acts on both ssRNA and dsRNA in a 3'-5' direction.
Uridylate-specific endoribonuclease nsp15
Plays 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).
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).
2'-O-methyltransferase nsp16
Methyltransferase 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.
Catalytic activity
RNA-directed RNA polymerase nsp12
a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)Helicase nsp13
ATP + H2O = ADP + H+ + phosphateHelicase nsp13
ATP + H2O = ADP + H+ + phosphatePapain-like proteinase nsp3
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).2'-O-methyltransferase nsp16
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-homocysteineUridylate-specific endoribonuclease nsp15
uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-RNARNA-directed RNA polymerase nsp12
a 5'-end diphospho-ribonucleoside in mRNA + GTP + H+ = a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphateThis reaction proceeds in the forward direction.Guanine-N7 methyltransferase nsp14
a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
Cofactor
Protein has several cofactor binding sites:
Uridylate-specific endoribonuclease nsp15
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )Note: Likely affects Nsp15 binding to RNA.
RNA-directed RNA polymerase nsp12
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )Features
Showing features for site, binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 193-194 | Cleavage | ||||
Sequence: GD | ||||||
Binding site | 338 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 341 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 357 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 359 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 383 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 386 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 400 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 436 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Site | 853-854 | Cleavage; by PL-PRO | ||||
Sequence: GA | ||||||
Active site | 1592 | For PL-PRO activity | ||||
Sequence: C | ||||||
Binding site | 1672 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1675 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1707 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1709 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 1759 | For PL-PRO activity | ||||
Sequence: H | ||||||
Active site | 1774 | For PL-PRO activity | ||||
Sequence: D | ||||||
Binding site | 2368 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2373 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2378 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2381 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2414 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2417 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2421 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 2424 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Site | 2740-2741 | Cleavage; by PL-PRO | ||||
Sequence: GA | ||||||
Site | 3247-3248 | Cleavage; by 3CL-PRO | ||||
Sequence: QS | ||||||
Active site | 3288 | For 3CL-PRO activity | ||||
Sequence: H | ||||||
Active site | 3395 | For 3CL-PRO activity | ||||
Sequence: C | ||||||
Site | 3553-3554 | Cleavage; by 3CL-PRO | ||||
Sequence: QS | ||||||
Site | 3845-3846 | Cleavage; by 3CL-PRO | ||||
Sequence: QS | ||||||
Site | 3928-3929 | Cleavage; by 3CL-PRO | ||||
Sequence: QA | ||||||
Site | 4127-4128 | Cleavage; by 3CL-PRO | ||||
Sequence: QN | ||||||
Site | 4237-4238 | Cleavage; by 3CL-PRO | ||||
Sequence: QA | ||||||
Binding site | 4311 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 4314 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 4320 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 4327 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 4354 | Zn2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 4357 | Zn2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 4365 | Zn2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 4367 | Zn2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Site | 4377-4378 | Cleavage; by 3CL-PRO | ||||
Sequence: QS | ||||||
Binding site | 4587 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 4596 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 4673 | Zn2+ 8 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 4679 | Zn2+ 8 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 4684 | Zn2+ 8 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 4688 | Zn2+ 8 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 4865 | Zn2+ 9 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 5020 | Zn2+ 9 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 5023 | Zn2+ 9 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 5024 | Zn2+ 9 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 5137 | |||||
Sequence: S | ||||||
Active site | 5138 | |||||
Sequence: D | ||||||
Active site | 5139 | |||||
Sequence: D | ||||||
Site | 5310-5311 | Cleavage; by 3CL-PRO | ||||
Sequence: QA | ||||||
Binding site | 5315 | Zn2+ 10 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 5318 | Zn2+ 10 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 5326 | Zn2+ 11 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 5329 | Zn2+ 11 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 5336 | Zn2+ 10 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 5339 | Zn2+ 10 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 5343 | Zn2+ 11 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 5349 | Zn2+ 11 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 5360 | Zn2+ 12 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 5365 | Zn2+ 12 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 5382 | Zn2+ 12 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 5385 | Zn2+ 12 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 5592-5599 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GPPGTGKS | ||||||
Site | 5908-5909 | Cleavage; by 3CL-PRO | ||||
Sequence: QS | ||||||
Active site | 5998 | |||||
Sequence: D | ||||||
Active site | 6000 | |||||
Sequence: E | ||||||
Active site | 6099 | |||||
Sequence: E | ||||||
Binding site | 6115 | Zn2+ 13 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 6118 | Zn2+ 13 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 6134 | Zn2+ 13 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 6137 | Zn2+ 13 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 6165 | Zn2+ 14 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 6169 | Zn2+ 14 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 6172 | Zn2+ 14 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 6176 | |||||
Sequence: H | ||||||
Active site | 6181 | |||||
Sequence: D | ||||||
Binding site | 6187 | Zn2+ 14 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 6239-6245 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: DIGNPKG | ||||||
Binding site | 6356 | Zn2+ 15 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 6378 | Zn2+ 15 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 6389 | Zn2+ 15 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 6392 | Zn2+ 15 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 6432-6433 | Cleavage; by 3CL-PRO | ||||
Sequence: QG | ||||||
Active site | 6663 | |||||
Sequence: H | ||||||
Active site | 6678 | |||||
Sequence: H | ||||||
Active site | 6718 | |||||
Sequence: K | ||||||
Site | 6775-6776 | Cleavage; by 3CL-PRO | ||||
Sequence: QA | ||||||
Active site | 6821 | |||||
Sequence: K | ||||||
Active site | 6905 | |||||
Sequence: D | ||||||
Active site | 6945 | |||||
Sequence: K | ||||||
Active site | 6978 | |||||
Sequence: E |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameReplicase polyprotein 1ab
- Short namespp1ab
- Alternative names
- Cleaved into 15 chains
Gene names
Organism names
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Nidovirales > Cornidovirineae > Coronaviridae > Orthocoronavirinae > Betacoronavirus > Merbecovirus > Middle East respiratory syndrome-related coronavirus
- Virus hosts
Accessions
- Primary accessionK9N7C7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Papain-like proteinase nsp3
Host membrane ; Multi-pass membrane protein
Non-structural protein 4
Host membrane ; Multi-pass membrane protein
Note: Localizes in virally-induced cytoplasmic double-membrane vesicles.
Non-structural protein 6
Host membrane ; Multi-pass membrane protein
Non-structural protein 7
Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity).
Non-structural protein 8
Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity).
Viral protein genome-linked nsp9
Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity).
Non-structural protein 10
Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity).
Helicase nsp13
Note: The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA.
Uridylate-specific endoribonuclease nsp15
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 2105-2125 | Helical | ||||
Sequence: GILTGCFSFVKMLFMLPLAYF | ||||||
Transmembrane | 2177-2197 | Helical | ||||
Sequence: LLLMLCTTMVLLSSVYHLYVF | ||||||
Transmembrane | 2281-2301 | Helical | ||||
Sequence: YVLNIDWLWFAFETGLAYMLY | ||||||
Transmembrane | 2305-2325 | Helical | ||||
Sequence: FNWLLLAGTLHYFFAQTSIFV | ||||||
Transmembrane | 2330-2350 | Helical | ||||
Sequence: YNYAVSSAFWLFTHIPMAGLV | ||||||
Transmembrane | 2757-2777 | Helical | ||||
Sequence: VLATIIVFLCAVLMYLCLPTF | ||||||
Transmembrane | 3028-3048 | Helical | ||||
Sequence: TTSLVLGIGLCAFLTLLFYYI | ||||||
Transmembrane | 3062-3082 | Helical | ||||
Sequence: AVIAVVAAVLNSLCICFVASI | ||||||
Transmembrane | 3104-3124 | Helical | ||||
Sequence: PAFIMHVSWYIMFGPIVPIWM | ||||||
Transmembrane | 3125-3145 | Helical | ||||
Sequence: TCVYTVAMCFRHFFWVLAYFS | ||||||
Transmembrane | 3559-3579 | Helical | ||||
Sequence: VTYGTAHWLFATLVSTYVIIL | ||||||
Transmembrane | 3593-3613 | Helical | ||||
Sequence: TIPTQLFPLLFVTMAFVMLLV | ||||||
Transmembrane | 3618-3638 | Helical | ||||
Sequence: TFLTLFLLPVAICLTYANIVY | ||||||
Transmembrane | 3664-3684 | Helical | ||||
Sequence: TTHTDIGVYISMSLVLVIVVK | ||||||
Transmembrane | 3691-3711 | Helical | ||||
Sequence: LSNFALALCSGVMWLYTYSIG | ||||||
Transmembrane | 3740-3760 | Helical | ||||
Sequence: LAKVCTYAIFAYSPQLTLVFP | ||||||
Transmembrane | 3765-3785 | Helical | ||||
Sequence: ILLLYTCLGFMCTCYFGVFSL |
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000422439 | 1-193 | Host translation inhibitor nsp1 | |||
Sequence: MSFVAGVTAQGARGTYRAALNSEKHQDHVSLTVPLCGSGNLVEKLSPWFMDGENAYEVVKAMLLKKEPLLYVPIRLAGHTRHLPGPRVYLVERLIACENPFMVNQLAYSSSANGSLVGTTLQGKPIGMFFPYDIELVTGKQNILLRKYGRGGYHYTPFHYERDNTSCPEWMDDFEADPKGKYAQNLLKKLIGG | ||||||
Chain | PRO_0000422440 | 194-853 | Non-structural protein 2 | |||
Sequence: DVTPVDQYMCGVDGKPISAYAFLMAKDGITKLADVEADVAARADDEGFITLKNNLYRLVWHVERKDVPYPKQSIFTINSVVQKDGVENTPPHYFTLGCKILTLTPRNKWSGVSDLSLKQKLLYTFYGKESLENPTYIYHSAFIECGSCGNDSWLTGNAIQGFACGCGASYTANDVEVQSSGMIKPNALLCATCPFAKGDSCSSNCKHSVAQLVSYLSERCNVIADSKSFTLIFGGVAYAYFGCEEGTMYFVPRAKSVVSRIGDSIFTGCTGSWNKVTQIANMFLEQTQHSLNFVGEFVVNDVVLAILSGTTTNVDKIRQLLKGVTLDKLRDYLADYDVAVTAGPFMDNAINVGGTGLQYAAITAPYVVLTGLGESFKKVATIPYKVCNSVKDTLTYYAHSVLYRVFPYDMDSGVSSFSELLFDCVDLSVASTYFLVRLLQDKTGDFMSTIITSCQTAVSKLLDTCFEATEATFNFLLDLAGLFRIFLRNAYVYTSQGFVVVNGKVSTLVKQVLDLLNKGMQLLHTKVSWAGSNISAVIYSGRESLIFPSGTYYCVTTKAKSVQQDLDVILPGEFSKKQLGLLQPTDNSTTVSVTVSSNMVETVVGQLEQTNMHSPDVIVGDYVIISEKLFVRSKEEDGFAFYPACTNGHAVPTLFRLKGG | ||||||
Chain | PRO_0000422441 | 854-2740 | Papain-like proteinase nsp3 | |||
Sequence: APVKKVAFGGDQVHEVAAVRSVTVEYNIHAVLDTLLASSSLRTFVVDKSLSIEEFADVVKEQVSDLLVKLLRGMPIPDFDLDDFIDAPCYCFNAEGDASWSSTMIFSLHPVECDEECSEVEASDLEEGESECISETSTEQVDVSHEISDDEWAAAVDEAFPLDEAEDVTESVQEEAQPVEVPVEDIAQVVIADTLQETPVVSDTVEVPPQVVKLPSEPQTIQPEVKEVAPVYEADTEQTQSVTVKPKRLRKKRNVDPLSNFEHKVITECVTIVLGDAIQVAKCYGESVLVNAANTHLKHGGGIAGAINAASKGAVQKESDEYILAKGPLQVGDSVLLQGHSLAKNILHVVGPDARAKQDVSLLSKCYKAMNAYPLVVTPLVSAGIFGVKPAVSFDYLIREAKTRVLVVVNSQDVYKSLTIVDIPQSLTFSYDGLRGAIRKAKDYGFTVFVCTDNSANTKVLRNKGVDYTKKFLTVDGVQYYCYTSKDTLDDILQQANKSVGIISMPLGYVSHGLDLIQAGSVVRRVNVPYVCLLANKEQEAILMSEDVKLNPSEDFIKHVRTNGGYNSWHLVEGELLVQDLRLNKLLHWSDQTICYKDSVFYVVKNSTAFPFETLSACRAYLDSRTTQQLTIEVLVTVDGVNFRTVVLNNKNTYRSQLGCVFFNGADISDTIPDEKQNGHSLYLADNLTADETKALKELYGPVDPTFLHRFYSLKAAVHKWKMVVCDKVRSLKLSDNNCYLNAVIMTLDLLKDIKFVIPALQHAFMKHKGGDSTDFIALIMAYGNCTFGAPDDASRLLHTVLAKAELCCSARMVWREWCNVCGIKDVVLQGLKACCYVGVQTVEDLRARMTYVCQCGGERHRQIVEHTTPWLLLSGTPNEKLVTTSTAPDFVAFNVFQGIETAVGHYVHARLKGGLILKFDSGTVSKTSDWKCKVTDVLFPGQKYSSDCNVVRYSLDGNFRTEVDPDLSAFYVKDGKYFTSEPPVTYSPATILAGSVYTNSCLVSSDGQPGGDAISLSFNNLLGFDSSKPVTKKYTYSFLPKEDGDVLLAEFDTYDPIYKNGAMYKGKPILWVNKASYDTNLNKFNRASLRQIFDVAPIELENKFTPLSVESTPVEPPTVDVVALQQEMTIVKCKGLNKPFVKDNVSFVADDSGTPVVEYLSKEDLHTLYVDPKYQVIVLKDNVLSSMLRLHTVESGDINVVAASGSLTRKVKLLFRASFYFKEFATRTFTATTAVGSCIKSVVRHLGVTKGILTGCFSFVKMLFMLPLAYFSDSKLGTTEVKVSALKTAGVVTGNVVKQCCTAAVDLSMDKLRRVDWKSTLRLLLMLCTTMVLLSSVYHLYVFNQVLSSDVMFEDAQGLKKFYKEVRAYLGISSACDGLASAYRANSFDVPTFCANRSAMCNWCLISQDSITHYPALKMVQTHLSHYVLNIDWLWFAFETGLAYMLYTSAFNWLLLAGTLHYFFAQTSIFVDWRSYNYAVSSAFWLFTHIPMAGLVRMYNLLACLWLLRKFYQHVINGCKDTACLLCYKRNRLTRVEASTVVCGGKRTFYITANGGISFCRRHNWNCVDCDTAGVGNTFICEEVANDLTTALRRPINATDRSHYYVDSVTVKETVVQFNYRRDGQPFYERFPLCAFTNLDKLKFKEVCKTTTGIPEYNFIIYDSSDRGQESLARSACVYYSQVLCKSILLVDSSLVTSVGDSSEIATKMFDSFVNSFVSLYNVTRDKLEKLISTARDGVRRGDNFHSVLTTFIDAARGPAGVESDVETNEIVDSVQYAHKHDIQITNESYNNYVPSYVKPDSVSTSDLGSLIDCNAASVNQIVLRNSNGACIWNAAAYMKLSDALKRQIRIACRKCNLAFRLTTSKLRANDNILSVRFTANKIVGG | ||||||
Disulfide bond | 2230↔2258 | |||||
Sequence: CDGLASAYRANSFDVPTFCANRSAMCNWC | ||||||
Disulfide bond | 2248↔2255 | |||||
Sequence: CANRSAMC | ||||||
Chain | PRO_0000422442 | 2741-3247 | Non-structural protein 4 | |||
Sequence: APTWFNALRDFTLKGYVLATIIVFLCAVLMYLCLPTFSMVPVEFYEDRILDFKVLDNGIIRDVNPDDKCFANKHRSFTQWYHEHVGGVYDNSITCPLTVAVIAGVAGARIPDVPTTLAWVNNQIIFFVSRVFANTGSVCYTPIDEIPYKSFSDSGCILPSECTMFRDAEGRMTPYCHDPTVLPGAFAYSQMRPHVRYDLYDGNMFIKFPEVVFESTLRITRTLSTQYCRFGSCEYAQEGVCITTNGSWAIFNDHHLNRPGVYCGSDFIDIVRRLAVSLFQPITYFQLTTSLVLGIGLCAFLTLLFYYINKVKRAFADYTQCAVIAVVAAVLNSLCICFVASIPLCIVPYTALYYYATFYFTNEPAFIMHVSWYIMFGPIVPIWMTCVYTVAMCFRHFFWVLAYFSKKHVEVFTDGKLNCSFQDAASNIFVINKDTYAALRNSLTNDAYSRFLGLFNKYKYFSGAMETAAYREAAACHLAKALQTYSETGSDLLYQPPNCSITSGVLQ | ||||||
Chain | PRO_0000422443 | 3248-3553 | 3C-like proteinase nsp5 | |||
Sequence: SGLVKMSHPSGDVEACMVQVTCGSMTLNGLWLDNTVWCPRHVMCPADQLSDPNYDALLISMTNHSFSVQKHIGAPANLRVVGHAMQGTLLKLTVDVANPSTPAYTFTTVKPGAAFSVLACYNGRPTGTFTVVMRPNYTIKGSFLCGSCGSVGYTKEGSVINFCYMHQMELANGTHTGSAFDGTMYGAFMDKQVHQVQLTDKYCSVNVVAWLYAAILNGCAWFVKPNRTSVVSFNEWALANQFTEFVGTQSVDMLAVKTGVAIEQLLYAIQQLYTGFQGKQILGSTMLEDEFTPEDVNMQIMGVVMQ | ||||||
Chain | PRO_0000422444 | 3554-3845 | Non-structural protein 6 | |||
Sequence: SGVRKVTYGTAHWLFATLVSTYVIILQATKFTLWNYLFETIPTQLFPLLFVTMAFVMLLVKHKHTFLTLFLLPVAICLTYANIVYEPTTPISSALIAVANWLAPTNAYMRTTHTDIGVYISMSLVLVIVVKRLYNPSLSNFALALCSGVMWLYTYSIGEASSPIAYLVFVTTLTSDYTITVFVTVNLAKVCTYAIFAYSPQLTLVFPEVKMILLLYTCLGFMCTCYFGVFSLLNLKLRAPMGVYDFKVSTQEFRFMTANNLTAPRNSWEAMALNFKLIGIGGTPCIKVAAMQ | ||||||
Chain | PRO_0000422445 | 3846-3928 | Non-structural protein 7 | |||
Sequence: SKLTDLKCTSVVLLSVLQQLHLEANSRAWAFCVKCHNDILAATDPSEAFEKFVSLFATLMTFSGNVDLDALASDIFDTPSVLQ | ||||||
Chain | PRO_0000422446 | 3929-4127 | Non-structural protein 8 | |||
Sequence: ATLSEFSHLATFAELEAAQKAYQEAMDSGDTSPQVLKALQKAVNIAKNAYEKDKAVARKLERMADQAMTSMYKQARAEDKKAKIVSAMQTMLFGMIKKLDNDVLNGIISNARNGCIPLSVIPLCASNKLRVVIPDFTVWNQVVTYPSLNYAGALWDITVINNVDNEIVKSSDVVDSNENLTWPLVLECTRASTSAVKLQ | ||||||
Chain | PRO_0000422447 | 4128-4237 | Viral protein genome-linked nsp9 | |||
Sequence: NNEIKPSGLKTMVVSAGQEQTNCNTSSLAYYEPVQGRKMLMALLSDNAYLKWARVEGKDGFVSVELQPPCKFLIAGPKGPEIRYLYFVKNLNNLHRGQVLGHIAATVRLQ | ||||||
Chain | PRO_0000422448 | 4238-4377 | Non-structural protein 10 | |||
Sequence: AGSNTEFASNSSVLSLVNFTVDPQKAYLDFVNAGGAPLTNCVKMLTPKTGTGIAISVKPESTADQETYGGASVCLYCRAHIEHPDVSGVCKYKGKFVQIPAQCVRDPVGFCLSNTPCNVCQYWIGYGCNCDSLRQAALPQ | ||||||
Chain | PRO_0000422449 | 4378-5310 | RNA-directed RNA polymerase nsp12 | |||
Sequence: SKDSNFLKRVRGSIVNARIEPCSSGLSTDVVFRAFDICNYKAKVAGIGKYYKTNTCRFVELDDQGHHLDSYFVVKRHTMENYELEKHCYDLLRDCDAVAPHDFFIFDVDKVKTPHIVRQRLTEYTMMDLVYALRHFDQNSEVLKAILVKYGCCDVTYFENKLWFDFVENPSVIGVYHKLGERVRQAILNTVKFCDHMVKAGLVGVLTLDNQDLNGKWYDFGDFVITQPGSGVAIVDSYYSYLMPVLSMTDCLAAETHRDCDFNKPLIEWPLTEYDFTDYKVQLFEKYFKYWDQTYHANCVNCTDDRCVLHCANFNVLFAMTMPKTCFGPIVRKIFVDGVPFVVSCGYHYKELGLVMNMDVSLHRHRLSLKELMMYAADPAMHIASSNAFLDLRTSCFSVAALTTGLTFQTVRPGNFNQDFYDFVVSKGFFKEGSSVTLKHFFFAQDGNAAITDYNYYSYNLPTMCDIKQMLFCMEVVNKYFEIYDGGCLNASEVVVNNLDKSAGHPFNKFGKARVYYESMSYQEQDELFAMTKRNVIPTMTQMNLKYAISAKNRARTVAGVSILSTMTNRQYHQKMLKSMAATRGATCVIGTTKFYGGWDFMLKTLYKDVDNPHLMGWDYPKCDRAMPNMCRIFASLILARKHGTCCTTRDRFYRLANECAQVLSEYVLCGGGYYVKPGGTSSGDATTAYANSVFNILQATTANVSALMGANGNKIVDKEVKDMQFDLYVNVYRSTSPDPKFVDKYYAFLNKHFSMMILSDDGVVCYNSDYAAKGYIAGIQNFKETLYYQNNVFMSEAKCWVETDLKKGPHEFCSQHTLYIKDGDDGYFLPYPDPSRILSAGCFVDDIVKTDGTLMVERFVSLAIDAYPLTKHEDIEYQNVFWVYLQYIEKLYKDLTGHMLDSYSVMLCGDNSAKFWEEAFYRDLYSSPTTLQ | ||||||
Chain | PRO_0000422450 | 5311-5908 | Helicase nsp13 | |||
Sequence: AVGSCVVCHSQTSLRCGTCIRRPFLCCKCCYDHVIATPHKMVLSVSPYVCNAPGCGVSDVTKLYLGGMSYFCVDHRPVCSFPLCANGLVFGLYKNMCTGSPSIVEFNRLATCDWTESGDYTLANTTTEPLKLFAAETLRATEEASKQSYAIATIKEIVGERQLLLVWEAGKSKPPLNRNYVFTGYHITKNSKVQLGEYIFERIDYSDAVSYKSSTTYKLTVGDIFVLTSHSVATLTAPTIVNQERYVKITGLYPTITVPEEFASHVANFQKSGYSKYVTVQGPPGTGKSHFAIGLAIYYPTARVVYTACSHAAVDALCEKAFKYLNIAKCSRIIPAKARVECYDRFKVNETNSQYLFSTINALPETSADILVVDEVSMCTNYDLSIINARIKAKHIVYVGDPAQLPAPRTLLTRGTLEPENFNSVTRLMCNLGPDIFLSMCYRCPKEIVSTVSALVYNNKLLAKKELSGQCFKILYKGNVTHDASSAINRPQLTFVKNFITANPAWSKAVFISPYNSQNAVARSMLGLTTQTVDSSQGSEYQYVIFCQTADTAHANNINRFNVAITRAQKGILCVMTSQALFESLEFTELSFTNYKLQ | ||||||
Chain | PRO_0000422451 | 5909-6432 | Guanine-N7 methyltransferase nsp14 | |||
Sequence: SQIVTGLFKDCSRETSGLSPAYAPTYVSVDDKYKTSDELCVNLNLPANVPYSRVISRMGFKLDATVPGYPKLFITREEAVRQVRSWIGFDVEGAHASRNACGTNVPLQLGFSTGVNFVVQPVGVVDTEWGNMLTGIAARPPPGEQFKHLVPLMHKGAAWPIVRRRIVQMLSDTLDKLSDYCTFVCWAHGFELTSASYFCKIGKEQKCCMCNRRAAAYSSPLQSYACWTHSCGYDYVYNPFFVDVQQWGYVGNLATNHDRYCSVHQGAHVASNDAIMTRCLAIHSCFIERVDWDIEYPYISHEKKLNSCCRIVERNVVRAALLAGSFDKVYDIGNPKGIPIVDDPVVDWHYFDAQPLTRKVQQLFYTEDMASRFADGLCLFWNCNVPKYPNNAIVCRFDTRVHSEFNLPGCDGGSLYVNKHAFHTPAYDVSAFRDLKPLPFFYYSTTPCEVHGNGSMIEDIDYVPLKSAVCITACNLGGAVCRKHATEYREYMEAYNLVSASGFRLWCYKTFDIYNLWSTFTKVQ | ||||||
Chain | PRO_0000422452 | 6433-6775 | Uridylate-specific endoribonuclease nsp15 | |||
Sequence: GLENIAFNFVKQGHFIGVEGELPVAVVNDKIFTKSGVNDICMFENKTTLPTNIAFELYAKRAVRSHPDFKLLHNLQADICYKFVLWDYERSNIYGTATIGVCKYTDIDVNSALNICFDIRDNGSLEKFMSTPNAIFISDRKIKKYPCMVGPDYAYFNGAIIRDSDVVKQPVKFYLYKKVNNEFIDPTECIYTQSRSCSDFLPLSDMEKDFLSFDSDVFIKKYGLENYAFEHVVYGDFSHTTLGGLHLLIGLYKKQQEGHIIMEEMLKGSSTIHNYFITETNTAAFKAVCSVIDLKLDDFVMILKSQDLGVVSKVVKVPIDLTMIEFMLWCKDGQVQTFYPRLQ | ||||||
Chain | PRO_0000422453 | 6776-7078 | 2'-O-methyltransferase nsp16 | |||
Sequence: ASADWKPGHAMPSLFKVQNVNLERCELANYKQSIPMPRGVHMNIAKYMQLCQYLNTCTLAVPANMRVIHFGAGSDKGIAPGTSVLRQWLPTDAIIIDNDLNEFVSDADITLFGDCVTVRVGQQVDLVISDMYDPTTKNVTGSNESKALFFTYLCNLINNNLALGGSVAIKITEHSWSVELYELMGKFAWWTVFCTNANASSSEGFLLGINYLGTIKENIDGGAMHANYIFWRNSTPMNLSTYSLFDLSKFQLKLKGTPVLQLKESQINELVISLLSQGKLLIRDNDTLSVSTDVLVNTYRKLR |
Post-translational modification
Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed (By similarity).
Keywords
- PTM
PTM databases
Interaction
Subunit
Non-structural protein 2
Interacts with host PHB and PHB2.
Non-structural protein 4
Interacts with papain-like protease nsp3 and non-structural protein 6.
3C-like proteinase nsp5
Monomer. Homodimer. Only the homodimer shows catalytic activity.
Non-structural protein 7
Interacts with nsp8 and nsp12 to form the replication-transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up to two subunits of nsp13.
Non-structural protein 8
Interacts with nsp7, nsp13 and nsp12 to form the replication-transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up to two subunits of nsp13.
Viral protein genome-linked nsp9
Interacts with nsp12.
Non-structural protein 10
Interacts with proofreading exoribonuclease nsp14 and 2'-O-methyltransferase nsp16; these interactions enhance nsp14 and nsp16 enzymatic activities.
RNA-directed RNA polymerase nsp12
Interacts with nsp7 and nsp8 to form the replication-transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up to two subunits of nsp13. Interacts with nsp9.
Helicase nsp13
Interacts with nsp8 to form the replication-transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up to two subunits of nsp13.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | PRO_0000422452 | rep PRO_0000422446 K9N7C7 | 2 | EBI-25592093, EBI-25592080 | |
BINARY | PRO_0000422452 | rep PRO_0000422452 K9N7C7 | 2 | EBI-25592093, EBI-25592093 | |
XENO | PRO_0000422441 | ISG15 P05161 | 4 | EBI-25592237, EBI-746466 | |
XENO | PRO_0000422441 | RCHY1 Q96PM5 | 2 | EBI-25592237, EBI-947779 |
Protein-protein interaction databases
Chemistry
Family & Domains
Features
Showing features for domain, region, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 25-149 | CoV Nsp1 globular | ||||
Sequence: HQDHVSLTVPLCGSGNLVEKLSPWFMDGENAYEVVKAMLLKKEPLLYVPIRLAGHTRHLPGPRVYLVERLIACENPFMVNQLAYSSSANGSLVGTTLQGKPIGMFFPYDIELVTGKQNILLRKYG | ||||||
Domain | 165-193 | BetaCoV Nsp1 C-terminal | ||||
Sequence: TSCPEWMDDFEADPKGKYAQNLLKKLIGG | ||||||
Domain | 195-475 | CoV Nsp2 N-terminal | ||||
Sequence: VTPVDQYMCGVDGKPISAYAFLMAKDGITKLADVEADVAARADDEGFITLKNNLYRLVWHVERKDVPYPKQSIFTINSVVQKDGVENTPPHYFTLGCKILTLTPRNKWSGVSDLSLKQKLLYTFYGKESLENPTYIYHSAFIECGSCGNDSWLTGNAIQGFACGCGASYTANDVEVQSSGMIKPNALLCATCPFAKGDSCSSNCKHSVAQLVSYLSERCNVIADSKSFTLIFGGVAYAYFGCEEGTMYFVPRAKSVVSRIGDSIFTGCTGSWNKVTQIANM | ||||||
Region | 338-359 | C4 | ||||
Sequence: CGSCGNDSWLTGNAIQGFACGC | ||||||
Region | 383-436 | C2HC | ||||
Sequence: CATCPFAKGDSCSSNCKHSVAQLVSYLSERCNVIADSKSFTLIFGGVAYAYFGC | ||||||
Domain | 481-715 | CoV Nsp2 middle | ||||
Sequence: QHSLNFVGEFVVNDVVLAILSGTTTNVDKIRQLLKGVTLDKLRDYLADYDVAVTAGPFMDNAINVGGTGLQYAAITAPYVVLTGLGESFKKVATIPYKVCNSVKDTLTYYAHSVLYRVFPYDMDSGVSSFSELLFDCVDLSVASTYFLVRLLQDKTGDFMSTIITSCQTAVSKLLDTCFEATEATFNFLLDLAGLFRIFLRNAYVYTSQGFVVVNGKVSTLVKQVLDLLNKGMQL | ||||||
Domain | 717-853 | CoV Nsp2 C-terminal | ||||
Sequence: HTKVSWAGSNISAVIYSGRESLIFPSGTYYCVTTKAKSVQQDLDVILPGEFSKKQLGLLQPTDNSTTVSVTVSSNMVETVVGQLEQTNMHSPDVIVGDYVIISEKLFVRSKEEDGFAFYPACTNGHAVPTLFRLKGG | ||||||
Domain | 857-966 | Ubiquitin-like 1 | ||||
Sequence: KKVAFGGDQVHEVAAVRSVTVEYNIHAVLDTLLASSSLRTFVVDKSLSIEEFADVVKEQVSDLLVKLLRGMPIPDFDLDDFIDAPCYCFNAEGDASWSSTMIFSLHPVEC | ||||||
Domain | 1110-1276 | Macro 1 | ||||
Sequence: PLSNFEHKVITECVTIVLGDAIQVAKCYGESVLVNAANTHLKHGGGIAGAINAASKGAVQKESDEYILAKGPLQVGDSVLLQGHSLAKNILHVVGPDARAKQDVSLLSKCYKAMNAYPLVVTPLVSAGIFGVKPAVSFDYLIREAKTRVLVVVNSQDVYKSLTIVDI | ||||||
Domain | 1278-1404 | Macro 2 | ||||
Sequence: QSLTFSYDGLRGAIRKAKDYGFTVFVCTDNSANTKVLRNKGVDYTKKFLTVDGVQYYCYTSKDTLDDILQQANKSVGIISMPLGYVSHGLDLIQAGSVVRRVNVPYVCLLANKEQEAILMSEDVKLN | ||||||
Domain | 1404-1477 | DPUP | ||||
Sequence: NPSEDFIKHVRTNGGYNSWHLVEGELLVQDLRLNKLLHWSDQTICYKDSVFYVVKNSTAFPFETLSACRAYLDS | ||||||
Domain | 1482-1537 | Ubiquitin-like 2 | ||||
Sequence: QLTIEVLVTVDGVNFRTVVLNNKNTYRSQLGCVFFNGADISDTIPDEKQNGHSLYL | ||||||
Domain | 1552-1823 | Peptidase C16 | ||||
Sequence: LYGPVDPTFLHRFYSLKAAVHKWKMVVCDKVRSLKLSDNNCYLNAVIMTLDLLKDIKFVIPALQHAFMKHKGGDSTDFIALIMAYGNCTFGAPDDASRLLHTVLAKAELCCSARMVWREWCNVCGIKDVVLQGLKACCYVGVQTVEDLRARMTYVCQCGGERHRQIVEHTTPWLLLSGTPNEKLVTTSTAPDFVAFNVFQGIETAVGHYVHARLKGGLILKFDSGTVSKTSDWKCKVTDVLFPGQKYSSDCNVVRYSLDGNFRTEVDPDLSA | ||||||
Zinc finger | 1672-1709 | C4-type | ||||
Sequence: CNVCGIKDVVLQGLKACCYVGVQTVEDLRARMTYVCQC | ||||||
Domain | 1837-1954 | Nucleic acid-binding | ||||
Sequence: PVTYSPATILAGSVYTNSCLVSSDGQPGGDAISLSFNNLLGFDSSKPVTKKYTYSFLPKEDGDVLLAEFDTYDPIYKNGAMYKGKPILWVNKASYDTNLNKFNRASLRQIFDVAPIEL | ||||||
Domain | 1967-2088 | G2M | ||||
Sequence: PVEPPTVDVVALQQEMTIVKCKGLNKPFVKDNVSFVADDSGTPVVEYLSKEDLHTLYVDPKYQVIVLKDNVLSSMLRLHTVESGDINVVAASGSLTRKVKLLFRASFYFKEFATRTFTATTA | ||||||
Region | 2040-2363 | HD1 | ||||
Sequence: SMLRLHTVESGDINVVAASGSLTRKVKLLFRASFYFKEFATRTFTATTAVGSCIKSVVRHLGVTKGILTGCFSFVKMLFMLPLAYFSDSKLGTTEVKVSALKTAGVVTGNVVKQCCTAAVDLSMDKLRRVDWKSTLRLLLMLCTTMVLLSSVYHLYVFNQVLSSDVMFEDAQGLKKFYKEVRAYLGISSACDGLASAYRANSFDVPTFCANRSAMCNWCLISQDSITHYPALKMVQTHLSHYVLNIDWLWFAFETGLAYMLYTSAFNWLLLAGTLHYFFAQTSIFVDWRSYNYAVSSAFWLFTHIPMAGLVRMYNLLACLWLLR | ||||||
Domain | 2214-2280 | 3Ecto | ||||
Sequence: KKFYKEVRAYLGISSACDGLASAYRANSFDVPTFCANRSAMCNWCLISQDSITHYPALKMVQTHLSH | ||||||
Region | 2364-2454 | Y1 | ||||
Sequence: KFYQHVINGCKDTACLLCYKRNRLTRVEASTVVCGGKRTFYITANGGISFCRRHNWNCVDCDTAGVGNTFICEEVANDLTTALRRPINATD | ||||||
Domain | 2364-2737 | CoV Nsp3 Y | ||||
Sequence: KFYQHVINGCKDTACLLCYKRNRLTRVEASTVVCGGKRTFYITANGGISFCRRHNWNCVDCDTAGVGNTFICEEVANDLTTALRRPINATDRSHYYVDSVTVKETVVQFNYRRDGQPFYERFPLCAFTNLDKLKFKEVCKTTTGIPEYNFIIYDSSDRGQESLARSACVYYSQVLCKSILLVDSSLVTSVGDSSEIATKMFDSFVNSFVSLYNVTRDKLEKLISTARDGVRRGDNFHSVLTTFIDAARGPAGVESDVETNEIVDSVQYAHKHDIQITNESYNNYVPSYVKPDSVSTSDLGSLIDCNAASVNQIVLRNSNGACIWNAAAYMKLSDALKRQIRIACRKCNLAFRLTTSKLRANDNILSVRFTANKI | ||||||
Region | 2368-2381 | ZF1 | ||||
Sequence: HVINGCKDTACLLC | ||||||
Region | 2414-2424 | ZF2 | ||||
Sequence: CRRHNWNCVDC | ||||||
Region | 2455-2553 | Y2 | ||||
Sequence: RSHYYVDSVTVKETVVQFNYRRDGQPFYERFPLCAFTNLDKLKFKEVCKTTTGIPEYNFIIYDSSDRGQESLARSACVYYSQVLCKSILLVDSSLVTSV | ||||||
Region | 2455-2737 | CoV-Y | ||||
Sequence: RSHYYVDSVTVKETVVQFNYRRDGQPFYERFPLCAFTNLDKLKFKEVCKTTTGIPEYNFIIYDSSDRGQESLARSACVYYSQVLCKSILLVDSSLVTSVGDSSEIATKMFDSFVNSFVSLYNVTRDKLEKLISTARDGVRRGDNFHSVLTTFIDAARGPAGVESDVETNEIVDSVQYAHKHDIQITNESYNNYVPSYVKPDSVSTSDLGSLIDCNAASVNQIVLRNSNGACIWNAAAYMKLSDALKRQIRIACRKCNLAFRLTTSKLRANDNILSVRFTANKI | ||||||
Region | 2554-2636 | Y3 | ||||
Sequence: GDSSEIATKMFDSFVNSFVSLYNVTRDKLEKLISTARDGVRRGDNFHSVLTTFIDAARGPAGVESDVETNEIVDSVQYAHKHD | ||||||
Region | 2637-2737 | Y4 | ||||
Sequence: IQITNESYNNYVPSYVKPDSVSTSDLGSLIDCNAASVNQIVLRNSNGACIWNAAAYMKLSDALKRQIRIACRKCNLAFRLTTSKLRANDNILSVRFTANKI | ||||||
Region | 2761-3171 | HD2 | ||||
Sequence: IIVFLCAVLMYLCLPTFSMVPVEFYEDRILDFKVLDNGIIRDVNPDDKCFANKHRSFTQWYHEHVGGVYDNSITCPLTVAVIAGVAGARIPDVPTTLAWVNNQIIFFVSRVFANTGSVCYTPIDEIPYKSFSDSGCILPSECTMFRDAEGRMTPYCHDPTVLPGAFAYSQMRPHVRYDLYDGNMFIKFPEVVFESTLRITRTLSTQYCRFGSCEYAQEGVCITTNGSWAIFNDHHLNRPGVYCGSDFIDIVRRLAVSLFQPITYFQLTTSLVLGIGLCAFLTLLFYYINKVKRAFADYTQCAVIAVVAAVLNSLCICFVASIPLCIVPYTALYYYATFYFTNEPAFIMHVSWYIMFGPIVPIWMTCVYTVAMCFRHFFWVLAYFSKKHVEVFTDGKLNCSFQDAASNIFVI | ||||||
Domain | 3151-3247 | Nsp4C | ||||
Sequence: VFTDGKLNCSFQDAASNIFVINKDTYAALRNSLTNDAYSRFLGLFNKYKYFSGAMETAAYREAAACHLAKALQTYSETGSDLLYQPPNCSITSGVLQ | ||||||
Domain | 3248-3553 | Peptidase C30 | ||||
Sequence: SGLVKMSHPSGDVEACMVQVTCGSMTLNGLWLDNTVWCPRHVMCPADQLSDPNYDALLISMTNHSFSVQKHIGAPANLRVVGHAMQGTLLKLTVDVANPSTPAYTFTTVKPGAAFSVLACYNGRPTGTFTVVMRPNYTIKGSFLCGSCGSVGYTKEGSVINFCYMHQMELANGTHTGSAFDGTMYGAFMDKQVHQVQLTDKYCSVNVVAWLYAAILNGCAWFVKPNRTSVVSFNEWALANQFTEFVGTQSVDMLAVKTGVAIEQLLYAIQQLYTGFQGKQILGSTMLEDEFTPEDVNMQIMGVVMQ | ||||||
Region | 3571-3785 | HD3 | ||||
Sequence: LVSTYVIILQATKFTLWNYLFETIPTQLFPLLFVTMAFVMLLVKHKHTFLTLFLLPVAICLTYANIVYEPTTPISSALIAVANWLAPTNAYMRTTHTDIGVYISMSLVLVIVVKRLYNPSLSNFALALCSGVMWLYTYSIGEASSPIAYLVFVTTLTSDYTITVFVTVNLAKVCTYAIFAYSPQLTLVFPEVKMILLLYTCLGFMCTCYFGVFSL | ||||||
Domain | 3846-3928 | RdRp Nsp7 cofactor | ||||
Sequence: SKLTDLKCTSVVLLSVLQQLHLEANSRAWAFCVKCHNDILAATDPSEAFEKFVSLFATLMTFSGNVDLDALASDIFDTPSVLQ | ||||||
Domain | 3929-4127 | RdRp Nsp8 cofactor | ||||
Sequence: ATLSEFSHLATFAELEAAQKAYQEAMDSGDTSPQVLKALQKAVNIAKNAYEKDKAVARKLERMADQAMTSMYKQARAEDKKAKIVSAMQTMLFGMIKKLDNDVLNGIISNARNGCIPLSVIPLCASNKLRVVIPDFTVWNQVVTYPSLNYAGALWDITVINNVDNEIVKSSDVVDSNENLTWPLVLECTRASTSAVKLQ | ||||||
Domain | 4128-4237 | Nsp9 ssRNA-binding | ||||
Sequence: NNEIKPSGLKTMVVSAGQEQTNCNTSSLAYYEPVQGRKMLMALLSDNAYLKWARVEGKDGFVSVELQPPCKFLIAGPKGPEIRYLYFVKNLNNLHRGQVLGHIAATVRLQ | ||||||
Domain | 4238-4377 | ExoN/MTase coactivator | ||||
Sequence: AGSNTEFASNSSVLSLVNFTVDPQKAYLDFVNAGGAPLTNCVKMLTPKTGTGIAISVKPESTADQETYGGASVCLYCRAHIEHPDVSGVCKYKGKFVQIPAQCVRDPVGFCLSNTPCNVCQYWIGYGCNCDSLRQAALPQ | ||||||
Zinc finger | 4311-4327 | |||||
Sequence: CLYCRAHIEHPDVSGVC | ||||||
Zinc finger | 4354-4367 | |||||
Sequence: CNVCQYWIGYGCNC | ||||||
Domain | 4383-4639 | NiRAN | ||||
Sequence: FLKRVRGSIVNARIEPCSSGLSTDVVFRAFDICNYKAKVAGIGKYYKTNTCRFVELDDQGHHLDSYFVVKRHTMENYELEKHCYDLLRDCDAVAPHDFFIFDVDKVKTPHIVRQRLTEYTMMDLVYALRHFDQNSEVLKAILVKYGCCDVTYFENKLWFDFVENPSVIGVYHKLGERVRQAILNTVKFCDHMVKAGLVGVLTLDNQDLNGKWYDFGDFVITQPGSGVAIVDSYYSYLMPVLSMTDCLAAETHRDCDF | ||||||
Domain | 4644-4742 | Nsp12 Interface | ||||
Sequence: IEWPLTEYDFTDYKVQLFEKYFKYWDQTYHANCVNCTDDRCVLHCANFNVLFAMTMPKTCFGPIVRKIFVDGVPFVVSCGYHYKELGLVMNMDVSLHRH | ||||||
Domain | 4743-5310 | Nsp12 RNA-dependent RNA polymerase | ||||
Sequence: RLSLKELMMYAADPAMHIASSNAFLDLRTSCFSVAALTTGLTFQTVRPGNFNQDFYDFVVSKGFFKEGSSVTLKHFFFAQDGNAAITDYNYYSYNLPTMCDIKQMLFCMEVVNKYFEIYDGGCLNASEVVVNNLDKSAGHPFNKFGKARVYYESMSYQEQDELFAMTKRNVIPTMTQMNLKYAISAKNRARTVAGVSILSTMTNRQYHQKMLKSMAATRGATCVIGTTKFYGGWDFMLKTLYKDVDNPHLMGWDYPKCDRAMPNMCRIFASLILARKHGTCCTTRDRFYRLANECAQVLSEYVLCGGGYYVKPGGTSSGDATTAYANSVFNILQATTANVSALMGANGNKIVDKEVKDMQFDLYVNVYRSTSPDPKFVDKYYAFLNKHFSMMILSDDGVVCYNSDYAAKGYIAGIQNFKETLYYQNNVFMSEAKCWVETDLKKGPHEFCSQHTLYIKDGDDGYFLPYPDPSRILSAGCFVDDIVKTDGTLMVERFVSLAIDAYPLTKHEDIEYQNVFWVYLQYIEKLYKDLTGHMLDSYSVMLCGDNSAKFWEEAFYRDLYSSPTTLQ | ||||||
Region | 4745-4959 | RdRp Fingers N-ter | ||||
Sequence: SLKELMMYAADPAMHIASSNAFLDLRTSCFSVAALTTGLTFQTVRPGNFNQDFYDFVVSKGFFKEGSSVTLKHFFFAQDGNAAITDYNYYSYNLPTMCDIKQMLFCMEVVNKYFEIYDGGCLNASEVVVNNLDKSAGHPFNKFGKARVYYESMSYQEQDELFAMTKRNVIPTMTQMNLKYAISAKNRARTVAGVSILSTMTNRQYHQKMLKSMAA | ||||||
Region | 4960-4998 | RdRp Palm N-ter | ||||
Sequence: TRGATCVIGTTKFYGGWDFMLKTLYKDVDNPHLMGWDYP | ||||||
Domain | 4990-5152 | RdRp catalytic | ||||
Sequence: PHLMGWDYPKCDRAMPNMCRIFASLILARKHGTCCTTRDRFYRLANECAQVLSEYVLCGGGYYVKPGGTSSGDATTAYANSVFNILQATTANVSALMGANGNKIVDKEVKDMQFDLYVNVYRSTSPDPKFVDKYYAFLNKHFSMMILSDDGVVCYNSDYAAKG | ||||||
Region | 4999-5057 | RdRp Fingers C-ter | ||||
Sequence: KCDRAMPNMCRIFASLILARKHGTCCTTRDRFYRLANECAQVLSEYVLCGGGYYVKPGG | ||||||
Region | 5058-5193 | RdRp Palm C-ter | ||||
Sequence: TSSGDATTAYANSVFNILQATTANVSALMGANGNKIVDKEVKDMQFDLYVNVYRSTSPDPKFVDKYYAFLNKHFSMMILSDDGVVCYNSDYAAKGYIAGIQNFKETLYYQNNVFMSEAKCWVETDLKKGPHEFCSQ | ||||||
Region | 5194-5310 | RdRp Thumb | ||||
Sequence: HTLYIKDGDDGYFLPYPDPSRILSAGCFVDDIVKTDGTLMVERFVSLAIDAYPLTKHEDIEYQNVFWVYLQYIEKLYKDLTGHMLDSYSVMLCGDNSAKFWEEAFYRDLYSSPTTLQ | ||||||
Domain | 5311-5423 | CV ZBD | ||||
Sequence: AVGSCVVCHSQTSLRCGTCIRRPFLCCKCCYDHVIATPHKMVLSVSPYVCNAPGCGVSDVTKLYLGGMSYFCVDHRPVCSFPLCANGLVFGLYKNMCTGSPSIVEFNRLATCD | ||||||
Domain | 5980-6195 | ExoN | ||||
Sequence: LFITREEAVRQVRSWIGFDVEGAHASRNACGTNVPLQLGFSTGVNFVVQPVGVVDTEWGNMLTGIAARPPPGEQFKHLVPLMHKGAAWPIVRRRIVQMLSDTLDKLSDYCTFVCWAHGFELTSASYFCKIGKEQKCCMCNRRAAAYSSPLQSYACWTHSCGYDYVYNPFFVDVQQWGYVGNLATNHDRYCSVHQGAHVASNDAIMTRCLAIHSCFI | ||||||
Domain | 6204-6432 | N7-MTase | ||||
Sequence: YPYISHEKKLNSCCRIVERNVVRAALLAGSFDKVYDIGNPKGIPIVDDPVVDWHYFDAQPLTRKVQQLFYTEDMASRFADGLCLFWNCNVPKYPNNAIVCRFDTRVHSEFNLPGCDGGSLYVNKHAFHTPAYDVSAFRDLKPLPFFYYSTTPCEVHGNGSMIEDIDYVPLKSAVCITACNLGGAVCRKHATEYREYMEAYNLVSASGFRLWCYKTFDIYNLWSTFTKVQ | ||||||
Region | 6318-6332 | GpppA-binding | ||||
Sequence: CDGGSLYVNKHAFHT | ||||||
Domain | 6433-6493 | Nsp15 N-terminal oligomerization | ||||
Sequence: GLENIAFNFVKQGHFIGVEGELPVAVVNDKIFTKSGVNDICMFENKTTLPTNIAFELYAKR | ||||||
Domain | 6494-6616 | AV-Nsp11N/CoV-Nsp15M | ||||
Sequence: AVRSHPDFKLLHNLQADICYKFVLWDYERSNIYGTATIGVCKYTDIDVNSALNICFDIRDNGSLEKFMSTPNAIFISDRKIKKYPCMVGPDYAYFNGAIIRDSDVVKQPVKFYLYKKVNNEFI | ||||||
Domain | 6633-6772 | NendoU | ||||
Sequence: LPLSDMEKDFLSFDSDVFIKKYGLENYAFEHVVYGDFSHTTLGGLHLLIGLYKKQQEGHIIMEEMLKGSSTIHNYFITETNTAAFKAVCSVIDLKLDDFVMILKSQDLGVVSKVVKVPIDLTMIEFMLWCKDGQVQTFYP | ||||||
Domain | 6777-7071 | Nidovirus-type SAM-dependent 2'-O-MTase | ||||
Sequence: SADWKPGHAMPSLFKVQNVNLERCELANYKQSIPMPRGVHMNIAKYMQLCQYLNTCTLAVPANMRVIHFGAGSDKGIAPGTSVLRQWLPTDAIIIDNDLNEFVSDADITLFGDCVTVRVGQQVDLVISDMYDPTTKNVTGSNESKALFFTYLCNLINNNLALGGSVAIKITEHSWSVELYELMGKFAWWTVFCTNANASSSEGFLLGINYLGTIKENIDGGAMHANYIFWRNSTPMNLSTYSLFDLSKFQLKLKGTPVLQLKESQINELVISLLSQGKLLIRDNDTLSVSTDVLV |
Domain
The hydrophobic domains (HD) could mediate the membrane association of the replication complex and thereby alter the architecture of the host cell membrane.
Sequence similarities
Belongs to the coronaviruses polyprotein 1ab family.
Keywords
- Domain
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Ribosomal frameshifting.
K9N7C7-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameReplicase polyprotein 1ab
- Synonymspp1ab
- NoteProduced by -1 ribosomal frameshifting at the 1a-1b genes boundary.
- Length7,078
- Mass (Da)789,563
- Last updated2013-03-06 v1
- ChecksumA944AF691D57A1E0
K9N638-1
The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
View isoform- NameReplicase polyprotein 1a
- Synonymspp1a, ORF1a polyprotein
- NoteProduced by -1 ribosomal frameshifting at the 1a-1b genes boundary.
Keywords
- Coding sequence diversity
- Technical term