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 similarity

Host translation inhibitor nsp1:

Inhibits 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 similarity

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.By similarity

Papain-like proteinase:

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.By similarity

Non-structural protein 4:

Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.By similarity

3C-like proteinase:

Cleaves 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 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.By similarity

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.By similarity

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.By similarity

Non-structural protein 9:

May participate in viral replication by acting as a ssRNA-binding protein.By similarity

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.By similarity

RNA-directed RNA polymerase:

Responsible for replication and transcription of the viral RNA genome.By similarity

Helicase:

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.By similarity

Guanine-N7 methyltransferase:

Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity.By similarity

Uridylate-specific endoribonuclease:

Mn²⁺-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.By similarity

2'-O-methyltransferase:

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.By similarity

Miscellaneous

The sequence shown is that of isolate 19572 Belgium 2004.

Catalytic activityⁱ

TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position. EC:3.4.22.69
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

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	1074	For PL1-PRO activityPROSITE-ProRule annotation	1
Active siteⁱ	1225	For PL1-PRO activityPROSITE-ProRule annotation	1
Active siteⁱ	1671	For PL2-PRO activityPROSITE-ProRule annotation	1
Active siteⁱ	1828	For PL2-PRO activityPROSITE-ProRule annotation	1
Active siteⁱ	3287	For 3CL-PRO activityPROSITE-ProRule annotation	1
Active siteⁱ	3391	For 3CL-PRO activityPROSITE-ProRule annotation	1
Metal bindingⁱ	5302	Zinc 1PROSITE-ProRule annotation	1
Metal bindingⁱ	5305	Zinc 1PROSITE-ProRule annotation	1
Metal bindingⁱ	5313	Zinc 2PROSITE-ProRule annotation	1
Metal bindingⁱ	5316	Zinc 1PROSITE-ProRule annotation	1
Metal bindingⁱ	5323	Zinc 1PROSITE-ProRule annotation	1
Metal bindingⁱ	5326	Zinc 2PROSITE-ProRule annotation	1
Metal bindingⁱ	5330	Zinc 2PROSITE-ProRule annotation	1
Metal bindingⁱ	5336	Zinc 2PROSITE-ProRule annotation	1
Metal bindingⁱ	5347	Zinc 3PROSITE-ProRule annotation	1
Metal bindingⁱ	5352	Zinc 3PROSITE-ProRule annotation	1
Metal bindingⁱ	5369	Zinc 3PROSITE-ProRule annotation	1
Metal bindingⁱ	5372	Zinc 3PROSITE-ProRule annotation	1

Regions

Feature key	Position(s)	DescriptionActions	Length
Zinc fingerⁱ	1151 – 1179	C4-type 1PROSITE-ProRule annotationAdd BLAST	29
Zinc fingerⁱ	1749 – 1785	C4-type 2PROSITE-ProRule annotationAdd BLAST	37
Zinc fingerⁱ	4306 – 4322	By similarityAdd BLAST	17
Zinc fingerⁱ	4348 – 4361	By similarityAdd BLAST	14
Nucleotide bindingⁱ	5578 – 5585	ATPBy similarity	8

GO - Molecular functionⁱ

ATP binding Source: UniProtKB-KW
cysteine-type endopeptidase activity Source: InterPro
DNA helicase activity Source: UniProtKB-EC
endonuclease activity Source: UniProtKB-KW
exonuclease 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 ubiquitinyl hydrolase activity Source: UniProtKB-EC
zinc ion binding Source: InterPro

Complete GO annotation on QuickGO ...

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 ISG15 activity Source: UniProtKB-KW
suppression by virus of host NF-kappaB transcription factor activity 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

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Endonuclease, Exonuclease, Helicase, Hydrolase, Methyltransferase, Nuclease, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase
Biological process	Activation of host autophagy by virus, Decay of host mRNAs by virus, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host ISG15 by virus, Inhibition of host NF-kappa-B by virus, Modulation of host ubiquitin pathway by viral deubiquitinase, Modulation of host ubiquitin pathway by virus, Ubl conjugation pathway, Viral immunoevasion, Viral RNA replication
Ligand	ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	C16.006

MEROPSⁱ

C16.006

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Replicase polyprotein 1ab Short name: pp1ab Alternative name(s): ORF1ab polyprotein Cleaved into the following 15 chains: Host translation inhibitor nsp1 Short name: nsp1 Alternative name(s): p28 Non-structural protein 2 Short name: nsp2 Alternative name(s): p65 Papain-like proteinase (EC:3.4.19.12, EC:3.4.22.69) Short name: PL-PRO Alternative name(s): Non-structural protein 3 Short name: nsp3 p210 Non-structural protein 4 Short name: nsp4 Alternative name(s): Peptide HD2 p44 3C-like proteinase (EC:3.4.22.-) Short name: 3CL-PRO Short name: 3CLp Alternative name(s): M-PRO nsp5 p27 Non-structural protein 6 Short name: nsp6 Non-structural protein 7 Short name: nsp7 Alternative name(s): p10 Non-structural protein 8 Short name: nsp8 Alternative name(s): p22 Non-structural protein 9 Short name: nsp9 Alternative name(s): p12 Non-structural protein 10 Short name: nsp10 Alternative name(s): Growth factor-like peptide Short name: GFL p15 RNA-directed RNA polymerase (EC:2.7.7.48) Short name: Pol Short name: RdRp Alternative name(s): nsp12 p100 Helicase (EC:3.6.4.12, EC:3.6.4.13) Short name: Hel Alternative name(s): nsp13 p67 Guanine-N7 methyltransferase (EC:2.1.1.-, EC:3.1.13.-) Short name: ExoN Alternative name(s): nsp14 Uridylate-specific endoribonuclease (EC:3.1.-.-) Alternative name(s): NendoU nsp15 p35 2'-O-methyltransferase (EC:2.1.1.-) Alternative name(s): nsp16
Gene namesⁱ	Name:rep ORF Names:1a-1b
Organismⁱ	Human coronavirus OC43 (HCoV-OC43)
Taxonomic identifierⁱ	31631 [NCBI]
Taxonomic lineageⁱ	Viruses › Riboviria › Orthornavirae › Pisuviricota › Pisoniviricetes › Nidovirales › Cornidovirineae › Coronaviridae › Orthocoronavirinae › Betacoronavirus › Embecovirus › Betacoronavirus 1
Virus hostⁱ	Homo sapiens (Human) [TaxID: 9606]
Proteomesⁱ	UP000180344 Componentⁱ: Genome UP000161137 Componentⁱ: Genome UP000159995 Componentⁱ: Genome UP000100580 Componentⁱ: Genome UP000007552 Componentⁱ: Genome

Subcellular locationⁱ

Papain-like proteinase:

Host membrane Curated; Multi-pass membrane protein Curated

Non-structural protein 4:

Host membrane Curated; Multi-pass membrane protein Curated

Non-structural protein 6:

Host membrane Curated; Multi-pass membrane protein Curated

Non-structural protein 7:

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

Non-structural protein 8:

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

Non-structural protein 9:

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

Non-structural protein 10:

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

Helicase:

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

Uridylate-specific endoribonuclease:

host perinuclear region By similarity

Topology

Feature key	Position(s)	DescriptionActions	Length
Transmembraneⁱ	2138 – 2158	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	2199 – 2219	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	2221 – 2241	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	2313 – 2333	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	2343 – 2363	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	2365 – 2385	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	2752 – 2772	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	2824 – 2844	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	3009 – 3029	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	3031 – 3051	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	3063 – 3083	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	3090 – 3110	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	3115 – 3135	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	3558 – 3578	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	3588 – 3608	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	3615 – 3635	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	3657 – 3677	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	3684 – 3704	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	3711 – 3731	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	3755 – 3775	HelicalSequence analysisAdd BLAST	21

GO - Cellular componentⁱ

host cell endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB-SubCell
host cell membrane Source: UniProtKB-SubCell
host cell perinuclear region of cytoplasm Source: UniProtKB-SubCell
integral component of membrane Source: UniProtKB-KW

Complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Host cytoplasm, Host membrane, Membrane

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
ChainⁱPRO_0000283826	1 – 246	Host translation inhibitor nsp1By similarityAdd BLAST	246
ChainⁱPRO_0000283827	247 – 851	Non-structural protein 2By similarityAdd BLAST	605
ChainⁱPRO_0000283828	852 – 2750	Papain-like proteinaseBy similarityAdd BLAST	1899
ChainⁱPRO_0000283829	2751 – 3246	Non-structural protein 4By similarityAdd BLAST	496
ChainⁱPRO_0000283830	3247 – 3549	3C-like proteinaseBy similarityAdd BLAST	303
ChainⁱPRO_0000283831	3550 – 3836	Non-structural protein 6By similarityAdd BLAST	287
ChainⁱPRO_0000283832	3837 – 3925	Non-structural protein 7By similarityAdd BLAST	89
ChainⁱPRO_0000283833	3926 – 4122	Non-structural protein 8By similarityAdd BLAST	197
ChainⁱPRO_0000283834	4123 – 4232	Non-structural protein 9By similarityAdd BLAST	110
ChainⁱPRO_0000283835	4233 – 4369	Non-structural protein 10By similarityAdd BLAST	137
ChainⁱPRO_0000037308	4370 – 5297	RNA-directed RNA polymeraseBy similarityAdd BLAST	928
ChainⁱPRO_0000283836	5298 – 5900	HelicaseBy similarityAdd BLAST	603
ChainⁱPRO_0000283837	5901 – 6421	Guanine-N7 methyltransferaseBy similarityAdd BLAST	521
ChainⁱPRO_0000283838	6422 – 6796	Uridylate-specific endoribonucleaseBy similarityAdd BLAST	375
ChainⁱPRO_0000283839	6797 – 7095	2'-O-methyltransferaseBy similarityAdd BLAST	299

Post-translational modificationⁱ

Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed (By similarity).By similarity

Sites

Feature key	Position(s)	DescriptionActions	Length
Siteⁱ	246 – 247	Cleavage; by PL1-PROBy similarity	2
Siteⁱ	851 – 852	Cleavage; by PL1-PROBy similarity	2
Siteⁱ	2750 – 2751	Cleavage; by PL2-PROBy similarity	2
Siteⁱ	3246 – 3247	Cleavage; by 3CL-PROBy similarity	2
Siteⁱ	3549 – 3550	Cleavage; by 3CL-PROBy similarity	2
Siteⁱ	3836 – 3837	Cleavage; by 3CL-PROBy similarity	2
Siteⁱ	3925 – 3926	Cleavage; by 3CL-PROBy similarity	2
Siteⁱ	4122 – 4123	Cleavage; by 3CL-PROBy similarity	2
Siteⁱ	4232 – 4233	Cleavage; by 3CL-PROBy similarity	2
Siteⁱ	4369 – 4370	Cleavage; by 3CL-PROBy similarity	2
Siteⁱ	5297 – 5298	Cleavage; by 3CL-PROBy similarity	2
Siteⁱ	5900 – 5901	Cleavage; by 3CL-PROBy similarity	2
Siteⁱ	6421 – 6422	Cleavage; by 3CL-PROBy similarity	2
Siteⁱ	6796 – 6797	Cleavage; by 3CL-PROBy similarity	2

Proteomic databases

PRIDEⁱ	P0C6X6

PRIDEⁱ

P0C6X6

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 similarity

Structureⁱ

3D structure databases

SMRⁱ	P0C6X6
ModBaseⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	1036 – 1274	Peptidase C16 1PROSITE-ProRule annotationAdd BLAST	239
Domainⁱ	1275 – 1435	MacroPROSITE-ProRule annotationAdd BLAST	161
Domainⁱ	1631 – 1892	Peptidase C16 2PROSITE-ProRule annotationAdd BLAST	262
Domainⁱ	3247 – 3549	Peptidase C30PROSITE-ProRule annotationAdd BLAST	303
Domainⁱ	4977 – 5139	RdRp catalyticPROSITE-ProRule annotationAdd BLAST	163
Domainⁱ	5298 – 5381	CV ZBDPROSITE-ProRule annotationAdd BLAST	84
Domainⁱ	5553 – 5734	(+)RNA virus helicase ATP-bindingAdd BLAST	182
Domainⁱ	5735 – 5904	(+)RNA virus helicase C-terminalAdd BLAST	170

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	2138 – 2385	HD1By similarityAdd BLAST	248
Regionⁱ	2752 – 3135	HD2By similarityAdd BLAST	384
Regionⁱ	3319 – 3775	HD3By similarityAdd BLAST	457

Domainⁱ

The hydrophobic domains (HD) could mediate the membrane association of the replication complex and thereby alter the architecture of the host cell membrane.

Sequence similaritiesⁱ

Belongs to the coronaviruses polyprotein 1ab family.Curated

Zinc finger

Feature key	Position(s)	DescriptionActions	Length
Zinc fingerⁱ	1151 – 1179	C4-type 1PROSITE-ProRule annotationAdd BLAST	29
Zinc fingerⁱ	1749 – 1785	C4-type 2PROSITE-ProRule annotationAdd BLAST	37
Zinc fingerⁱ	4306 – 4322	By similarityAdd BLAST	17
Zinc fingerⁱ	4348 – 4361	By similarityAdd BLAST	14

Keywords - Domainⁱ

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd18808, SF1_C_Upf1, 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 2.20.25.360, 1 hit 2.40.10.10, 2 hits 2.40.10.250, 1 hit 2.40.10.290, 1 hit 3.10.20.350, 1 hit 3.10.20.540, 1 hit 3.40.220.10, 1 hit 3.40.50.11580, 1 hit 3.90.70.90, 2 hits
InterProⁱ	View protein in InterPro IPR027351, (+)RNA_virus_helicase_core_dom IPR022570, B-CoV_NSP1 IPR043609, CoV_NSP15_C IPR043608, CoV_NSP15_M IPR043606, CoV_NSP15_N IPR043613, CoV_NSP2_C IPR043611, CoV_NSP3_C IPR043612, CoV_NSP4_N IPR043610, CoV_NSP6 IPR027352, CV_ZBD IPR043502, DNA/RNA_pol_sf IPR041679, DNA2/NAM7-like_AAA IPR037227, EndoU-like IPR002589, Macro_dom IPR043472, Macro_dom-like IPR036333, NSP10_sf_CoV IPR009466, NSP15_CoV IPR043174, NSP15_middle_sf IPR042515, NSP15_N_CoV IPR009461, NSP16_CoV-like IPR032592, NSP3_NAR_bCoV IPR038083, NSP3A-like IPR032505, NSP4_C_CoV IPR038123, NSP4_C_sf_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 IPR001205, RNA-dir_pol_C IPR007094, RNA-dir_pol_PSvirus IPR009469, RNA_pol_N_coronovir IPR018995, RNA_synth_NSP10_CoV IPR029063, SAM-dependent_MTases
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF13087, AAA_12, 1 hit PF16251, bCoV_NAR, 1 hit PF06471, CoV_Methyltr_1, 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 PS51653, CV_ZBD, 1 hit PS51442, M_PRO, 1 hit PS51154, MACRO, 1 hit PS51124, PEPTIDASE_C16, 2 hits PS51657, PSRV_HELICASE, 1 hit PS50507, RDRP_SSRNA_POS, 1 hit

Sequences (2)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsⁱ produced by ribosomal frameshifting. Align Add to basket

Isoform Replicase polyprotein 1ab (identifier: P0C6X6-1) [UniParc]FASTA Add to basket

Also known as: pp1ab

This isoform has been chosen as the canonicalⁱ sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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        10         20         30         40         50
MSKINKYGLE LHWAPEFPWM FEDAEEKLDN PSSSEVDMIC STTAQKLETD 
        60         70         80         90        100
GICPENHVMV DCRRLLKQEC CVQSSLIREI VMNASPYHLE VLLQDALQSR 
       110        120        130        140        150
EAVLVTTPLG MSLEACYVRG CNPKGWTMGL FRRRSVCNTG RCTVNKHVAY 
       160        170        180        190        200
QLYMIDPAGV CLGAGQFVGW VIPLAFMPVQ SRKFIVPWVM YLRKRGEKGA 
       210        220        230        240        250
YNKDHGCGGF GHVYDFKVED AYDQVHDEPK GKFSKKAYAL IRGYRGVKPL 
       260        270        280        290        300
LYVDQYGCDY TGSLADGLEA YADKTLQEMK ALFPTWSQEL PFDVIVAWHV 
       310        320        330        340        350
VRDPRYVMRL QSAATICSVA YVANPTEDLC DGSVVIKEPV HVYADDSIIL 
       360        370        380        390        400
RQYNLFDIMS HFYMEADTVV NAFYGVALKD CGFVMQFGYI DCEQDSCDFK 
       410        420        430        440        450
GWIPGNMIDG FACTTCGHVY EVGDLIAQSS GVLPVNPVLH TKSAAGYGGF 
       460        470        480        490        500
GCKDSFTLYG QTVVYFGGCV YWSPARNIWI PILKSSVKSY DSLVYTGVLG 
       510        520        530        540        550
CKAIVKETNL ICKALYLDYV QHKCGNLHQR ELLGVSDVWH KQLLINRGVY 
       560        570        580        590        600
KPLLENIDYF NMRRAKFSLE TFTVCADGFM PFLLDDLVPR AYYLAVSGQA 
       610        620        630        640        650
FCDYADKLCH AVVSKSKELL DVSLDSLGAA IHYLNSKIVD LAQHFSDFGT 
       660        670        680        690        700
SFVSKIVHFF KTFTTSTALA FAWVLFHVLH GAYIVVESDI YFVKNIPRYA 
       710        720        730        740        750
SAVAQAFQSV AKVVLDSLRV TFIDGLSCFK IGRRRICLSG RKIYEVERGL 
       760        770        780        790        800
LHSSQLPLDV YDLTMPSQVQ KAKQKPIYLK GSGSDFSLAD SVVEVVTTSL 
       810        820        830        840        850
TPCGYSEPPK VADKICIVDN VYMAKAGDKY YPVVVDDHVG LLDQAWRVPC 
       860        870        880        890        900
AGRRVTFKEQ PTVKEIISMP KIIKVFYELD NDFNTILNTA CGVFEVDDTV 
       910        920        930        940        950
DMEEFYAVVI DAIEEKLSPC KELEGVGAKV SAFLQKLEDN PLFLFDEAGE 
       960        970        980        990       1000
EVFAPKLYCA FTAPEDDDFL EESDVEEDDV EGEETDLTIT SAGQPCVASE 
      1010       1020       1030       1040       1050
QEESSEVLED TLDDGPSVET SDSQVEEDVE MSDFVDLESV IQDYENVCFE 
      1060       1070       1080       1090       1100
FYTTEPEFVK VLGLYVPKAT RNNCWLRSVL AVMQKLPCQF KDKNLQDLWV 
      1110       1120       1130       1140       1150
LYKQQYSQLF VDTLVNKIPA NIVLPQGGYV ADFAYWFLTL CDWQCVAYWK 
      1160       1170       1180       1190       1200
CIKCDLALKL KGLDAMFFYG DVVSHICKCG ESMVLIDVDV PFTAHFALKD 
      1210       1220       1230       1240       1250
KLFCAFITKR IVYKAACVVD VNDSHSMAVV DGKQIDDHRI TSITSDKFDF 
      1260       1270       1280       1290       1300
IIGHGMSFSM TTFEIAQLYG SCITPNVCFV KGDIIKVSKL VKAEVVVNPA 
      1310       1320       1330       1340       1350
NGHMVHGGGV AKAIAVAAGQ QFVKETTNMV KSKGVCATGD CYVSTGGKLC 
      1360       1370       1380       1390       1400
KTVLNVVGPD ARTQGKQSYV LLERVYKHFN NYDCVVTTLI SAGIFSVPSD 
      1410       1420       1430       1440       1450
VSLTYLLGTA KKQVVLVSNN QEDFDLISKC QITAVEGTKK LAARLSFNVG 
      1460       1470       1480       1490       1500
RSIVYETDAN KLILINDVAF VSTFNVLQDV LSLRHDIALD DDARTFVQSN 
      1510       1520       1530       1540       1550
VDVLPEGWRV VNKFYQINGV RTVKYFECTG GIDICSQDKV FGYVQQGIFN 
      1560       1570       1580       1590       1600
KATVAQIKAL FLDKVDILLT VDGVNFTNRF VPVGESFGKS LGNVFCDGVN 
      1610       1620       1630       1640       1650
VTKHKCDINY KGKVFFQFDN LSSEDLKAVR SSFNFDQKEL LAYYNMLVNC 
      1660       1670       1680       1690       1700
FKWQVVVNGK YFTFKQANNN CFVNVSCLML QSLHLTFKIV QWQEAWLEFR 
      1710       1720       1730       1740       1750
SGRPARFVAL VLAKGGFKFG DPADSRDFLR VVFSQVDLTG AICDFEIACK 
      1760       1770       1780       1790       1800
CGVKQEQRTG LDAVMHFGTL SREDLEIGYT VDCSCGKKLI HCVRFDVPFL 
      1810       1820       1830       1840       1850
ICSNTPASVK LPKGVGSANI FIGDNVGHYV HVKCEQSYQL YDASNVKKVT 
      1860       1870       1880       1890       1900
DVTGKLSDCL YLKNLKQTFK SVLTTYYLDD VKKIEYKPDL SQYYCDGGKY 
      1910       1920       1930       1940       1950
YTQRIIKAQF KTFEKVDGVY TNFKLIGHTV CDSLNSKLGF DSSKEFVEYK 
      1960       1970       1980       1990       2000
ITEWPTATGD VVLANDDLYV KRYERGCITF GKPVIWLSHE KASLNSLTYF 
      2010       2020       2030       2040       2050
NRPLLVDDNK FDVLKVDDVD DSGDSSESGA KETKEINIIK LSGVKKPFKV 
      2060       2070       2080       2090       2100
EDSVIVNDDT SETKYVKSLS IVDVYDMWLT GCKYVVRTAN ALSRAVNVPT 
      2110       2120       2130       2140       2150
IRKFIKFGMT LVSIPIDLLN LREIKPAVNV VKAVRNKTSA CFNFIKWLFV 
      2160       2170       2180       2190       2200
LLFGWIKISA DNKVIYTTEI ASKLTCKLVA LAFKNAFLTF KWSMVARGAC 
      2210       2220       2230       2240       2250
IIATIFLLWF NFIYANVIFS DFYLPKIGFL PTFVGKIAQW IKNTFSLVTI 
      2260       2270       2280       2290       2300
CDLYSIQDVG FKNQYCNGSI ACQFCLAGFD MLDNYKAIDV VQYEADRRAF 
      2310       2320       2330       2340       2350
VDYTGVLKIV IELIVSYALY TAWFYPLFAL ISIQILTTWL PELFMLSTLH 
      2360       2370       2380       2390       2400
WSFRLLVALA NMLPAHVFMR FYIIIASFIK LFSLFKHVAY GCSKSGCLFC 
      2410       2420       2430       2440       2450
YKRNRSLRVK CSTIVGGMIR YYDVMANGGT GFCSKHQWNC IDCDSYKPGN 
      2460       2470       2480       2490       2500
TFITVEAALD LSKELKRPIQ PTDVAYHTVT DVKQVGCSMR LFYDRDGQRI 
      2510       2520       2530       2540       2550
YDDVNASLFV DYSNLLHSKV KSVPNMHVVV VENDADKANF LNAAVFYAQS 
      2560       2570       2580       2590       2600
LFRPILMVDK NLITTANTGT SVTETMFDVY VDTFLSMFDV DKKSLNALIA 
      2610       2620       2630       2640       2650
TAHSSIKQGT QIYKVLDTFL SCARKSCSID SDVDTKCLAD SVMSAVSAGL 
      2660       2670       2680       2690       2700
ELTDESCNNL VPTYLKSDNI VAADLGVLIQ NSAKHVQGNV AKIAGVSCIW 
      2710       2720       2730       2740       2750
SVDAFNQFSS DFQHKLKKAC CKTGLKLKLT YNKQMANVSV LTTPFSLKGG 
      2760       2770       2780       2790       2800
AVFSYFVYVC FVLSLVCFIG LWCLMPTYTV HKSDFQLPVY ASYKVLDNGV 
      2810       2820       2830       2840       2850
IRDVSVEDVC FANKFEQFDQ WYESTFGLSY YSNSMACPIV VAVIDQDFGS 
      2860       2870       2880       2890       2900
TVFNVPTKVL RYGYHVLHFI THALSADGVQ CYTPHSQISY SNFYASGCVL 
      2910       2920       2930       2940       2950
SSACTMFTMA DGSPQPYCYT DGLMQNASLY SSLVPHVRYN LANAKGFIRF 
      2960       2970       2980       2990       3000
PEVLREGLVR VVRTRSMSYC RVGLCEEADE GICFNFNGSW VLNNDYYRSL 
      3010       3020       3030       3040       3050
PGTFCGRDVF DLIYQLFKGL AQPVDFLALT ASSIAGAILA VIVVLVFYYL 
      3060       3070       3080       3090       3100
IKLKRAFGDY TSVVFVNVIV WCVNFMMLFV FQVYPTLSCV YAICYFYATL 
      3110       3120       3130       3140       3150
YFPSEISVIM HLQWLVMYGT IMPLWFCLLY IAVVVSNHAF WVFSYCRKLG 
      3160       3170       3180       3190       3200
TSVRSDGTFE EMALTTFMIT KDSYCKLKNS LSDVAFNRYL SLYNKYRYYS 
      3210       3220       3230       3240       3250
GKMDTAAYRE AACSQLAKAM DTFTNNNGSD VLYQPPTASV STSFLQSGIV 
      3260       3270       3280       3290       3300
KMVNPTSKVE PCVVSVTYGN MTLNGLWLDD KVYCPRHVIC SASDMTNPDY 
      3310       3320       3330       3340       3350
TNLLCRVTSS DFTVLFDRLS LTVMSYQMRG CMLVLTVTLQ NSRTPKYTFG 
      3360       3370       3380       3390       3400
VVKPGETFTV LAAYNGKPQG AFHVTMRSSY TIKGSFLCGS CGSVGYVIMG 
      3410       3420       3430       3440       3450
DCVKFVYMHQ LELSTGCHTG TDFNGDFYGP YKDAQVVQLP IQDYIQSVNF 
      3460       3470       3480       3490       3500
LAWLYAAILN NCNWFIQSDK CSVEDFNVWA LSNGFSQVKS DLVIDALASM 
      3510       3520       3530       3540       3550
TGVSLETLLA AIKRLKNGFQ GRQIMGSCSF EDELTPSDVY QQLAGIKLQS 
      3560       3570       3580       3590       3600
KRTRLFKGTV CWIMASTFLF SCIITAFVKW TMFMYVTTNM FSITFCALCV 
      3610       3620       3630       3640       3650
ISLAMLLVKH KHLYLTMYIT PVLFTLLYNN YLVVYKHTFR GYVYAWLSYY 
      3660       3670       3680       3690       3700
VPSVEYTYTD EVIYGMLLLV GMVFVTLRSI NHDLFSFIMF VGRLISVFSL 
      3710       3720       3730       3740       3750
WYKGSNLEEE ILLMLASLFG TYTWTTVLSM AVAKVIAKWV AVNVLYFTDI 
      3760       3770       3780       3790       3800
PQIKIVLLCY LFIGYIISCY WGLFSLMNSL FRMPLGVYNY KISVQELRYM 
      3810       3820       3830       3840       3850
NANGLRPPKN SFEALMLNFK LLGIGGVPII EVSQFQSKLT DVKCANVVLL 
      3860       3870       3880       3890       3900
NCLQHLHVAS NSKLWHYCST LHNEILATSD LSVAFEKLAQ LLIVLFANPA 
      3910       3920       3930       3940       3950
AVDSKCLTSI EEVCDDYAKD NTVLQALQSE FVNMASFVEY EVAKKNLDEA 
      3960       3970       3980       3990       4000
RFSGSANQQQ LKQLEKACNI AKSAYERDRA VAKKLERMAD LALTNMYKEA 
      4010       4020       4030       4040       4050
RINDKKSKVV SALQTMLFSM VRKLDNQALN SILDNAVKGC VPLNAIPSLA 
      4060       4070       4080       4090       4100
ANTLNIIVPD KSVYDQIVDN IYVTYAGNVW QIQTIQDSDG TNKQLNEISD 
      4110       4120       4130       4140       4150
DCNWPLVIIA NRYNEVSATV LQNNELMPAK LKIQVVNSGP DQTCNTPTQC 
      4160       4170       4180       4190       4200
YYNNSNNGKI VYAILSDVDG LKYTKILKDD GNFVVLELDP PCKFTVQDAK 
      4210       4220       4230       4240       4250
GLKIKYLYFV KGCNTLARGW VVGTISSTVR LQAGTATEYA SNSSILSLCA 
      4260       4270       4280       4290       4300
FSVDPKKTYL DFIQQGGTPI ANCVKMLCDH AGTGMAITVK PDATTSQDSY 
      4310       4320       4330       4340       4350
GGASVCIYCR ARVEHPDVDG LCKLRGKFVQ VPVGIKDPVS YVLTHDVCRV 
      4360       4370       4380       4390       4400
CGFWRDGSCS CVSTDTTVQS KDTNFLNRVR GASVDARLVP CASGLSTDVQ 
      4410       4420       4430       4440       4450
LRAFDIYNAS VAGIGLHLKV NCCRFQRVDE NGDKLDQFFV VKRTDLTIYN 
      4460       4470       4480       4490       4500
REMKCYERVK DCKFVAEHDF FTFDVEGSRV PHIVRKDLTK YTMLDLCYAL 
      4510       4520       4530       4540       4550
RHFDRNDCML LCDILSIYAG CEQSYFTKKD WYDFVENPDI INVYKKLGPI 
      4560       4570       4580       4590       4600
FNRALVSATE FADKLVEVGL VGVLTLDNQD LNGKWYDFGD YVIAAPGCGV 
      4610       4620       4630       4640       4650
AIADSYYSYI MPMLTMCHAL DCELYVNNAY RLFDLVQYDF TDYKLELFNK 
      4660       4670       4680       4690       4700
YFKHWSMPYH PNTVDCQDDR CIIHCANFNI LFSMVLPNTC FGPLVRQIFV 
      4710       4720       4730       4740       4750
DGVPFVVSIG YHYKELGIVM NMDVDTHRYR LSLKDLLLYA ADPALHVASA 
      4760       4770       4780       4790       4800
SALYDLRTCC FSVAAITSGV KFQTVKPGNF NQDFYDFVLS KGLLKEGSSV 
      4810       4820       4830       4840       4850
DLKHFFFTQD GNAAITDYNY YKYNLPTMVD IKQLLFVLEV VYKYFEIYDG 
      4860       4870       4880       4890       4900
GCIPASQVIV NNYDKSAGYP FNKFGKARLY YEALSFEEQD EIYAYTKRNV 
      4910       4920       4930       4940       4950
LPTLTQMNLK YAISAKNRAR TVAGVSILST MTGRMFHQKC LKSIAATRGV 
      4960       4970       4980       4990       5000
PVVIGTTKFY GGWDDMLRRL IKDVDNPVLM GWDYPKCDRA MPNILRIVSS 
      5010       5020       5030       5040       5050
LVLARKHETC CSQSDRFYRL ANECAQVLSE IVMCGGCYYV KPGGTSSGDA 
      5060       5070       5080       5090       5100
TTAFANSVFN ICQAVSANVC ALMSCNGNKI EDLSIRALQK RLYSHVYRSD 
      5110       5120       5130       5140       5150
KVDSTFVTEY YEFLNKHFSM MILSDDGVVC YNSDYASKGY IANISAFQQV 
      5160       5170       5180       5190       5200
LYYQNNVFMS ESKCWVEHDI NNGPHEFCSQ HTMLVKMDGD DVYLPYPNPS 
      5210       5220       5230       5240       5250
RILGAGCFVD DLLKTDSVLL IERFVSLAID AYPLVYHENE EYQKVFRVYL 
      5260       5270       5280       5290       5300
AYIKKLYNDL GNQILDSYSV ILSTCDGQKF TDESFYKNMY LRSAVMQSVG 
      5310       5320       5330       5340       5350
ACVVCSSQTS LRCGSCIRKP LLCCKCCYDH VMATDHKYVL SVSPYVCNAP 
      5360       5370       5380       5390       5400
GCDVNDVTKL YLGGMSYYCE DHKPQYSFKL VMNGLVFGLY KQSCTGSPYI 
      5410       5420       5430       5440       5450
DDFNRIASCK WTDVDDYILA NECTERLKLF AAETQKATEE AFKQSYASAT 
      5460       5470       5480       5490       5500
IQEIVSEREL ILSWEIGKVK PPLNKNYVFT GYHFTKNGKT VLGEYVFDKS 
      5510       5520       5530       5540       5550
ELTNGVYYRA TTTYKLSVGD VFVLTSHSVA NLSAPTLVPQ ENYSSIRFAS 
      5560       5570       5580       5590       5600
VYSVLETFQN NVVNYQHIGM KRYCTVQGPP GTGKSHLAIG LAVFYCTARV 
      5610       5620       5630       5640       5650
VYTAASHAAV DALCEKAYKF LNINDCTRIV PAKVRVECYD KFKINDTTRK 
      5660       5670       5680       5690       5700
YVFTTINALP EMVTDIVVVD EVSMLTNYEL SVINARIRAK HYVYIGDPAQ 
      5710       5720       5730       5740       5750
LPAPRVLLSK GTLEPKYFNT VTKLMCCLGP DIFLGTCYRC PKEIVDTVSA 
      5760       5770       5780       5790       5800
LVYENKLKAK NESSLLCFKV YYKGVTTHES SSAVNMQQIY LINKFLKANP 
      5810       5820       5830       5840       5850
LWHKAVFISP YNSQNFAAKR VLGLQTQTVD SAQGSEYDYV IYSQTAETAH 
      5860       5870       5880       5890       5900
SVNVNRFNVA ITRAKKGILC VMSNMQLFEA LQFTTLTLDK VPQAVETKVQ 
      5910       5920       5930       5940       5950
CSTNLFKDCS KSYSGYHPAH APSFLAVDDK YKATGDLAVC LGIGDSAVTY 
      5960       5970       5980       5990       6000
SRLISLMGFK LDVTLDGYCK LFITKEEAVK RVRAWVGFDA EGAHATLDSI 
      6010       6020       6030       6040       6050
GTNFPLQLGF STGIDFVVEA TGLFADRDGY SFKKAVAKAP PGEQFKHLIP 
      6060       6070       6080       6090       6100
LMTRGHRWDV VRPRIVQMFA DHLIDLSDCV VLVTWAANFE LTCLRYFAKV 
      6110       6120       6130       6140       6150
GREISCNVCT KRATVYNSRT GYYGCWRHSV TCDYLYNPLI VDIQQWGYIG 
      6160       6170       6180       6190       6200
SLSSNHDLYC SVHKGAHVAS SDAIMTRCLA VYDCFCNNIN WNVEYPIISN 
      6210       6220       6230       6240       6250
ELSINTSCRV LQRVILKAAM LCNRYTLCYD IGNPKGIACV KDFDFKFYDA 
      6260       6270       6280       6290       6300
QPIVKSVKTL LYSFEAHKDS FKDGLCMFWN CNVDKYPPNA VVCRFDTRVL 
      6310       6320       6330       6340       6350
NNLNLPGCNG GSLYVNKHAF HTKPFARAAF EHLKPMPFFY YSDTPCVYMD 
      6360       6370       6380       6390       6400
GMDAKQVDYV PLKSATCITR CNLGGAVCLK HAEEYREYLE SYNTATTAGF 
      6410       6420       6430       6440       6450
TFWVYKTFDF YNLWNTFTKL QSLENVVYNL VKTGHYTGQA GEMPCAIIND 
      6460       6470       6480       6490       6500
KVVTKIDKED VVIFINNTTY PTNVAVELFA KRSVRHHPEL KLFRNLNIDV 
      6510       6520       6530       6540       6550
CWKHVIWDYA RESIFCSNTY GVCMYTDLKF IDKLNVLFDG RDNGAFEAFK 
      6560       6570       6580       6590       6600
RSNNGVYIST TKVKSLSMIR GPPRAELNGV VVDKVGDTDC VFYFAVRKEG 
      6610       6620       6630       6640       6650
QDVIFSQFDS LGVSSNQSPQ GNLGSNGKPG NVGGNDALSI STIFTQSRVI 
      6660       6670       6680       6690       6700
SSFTCRTDME KDFIALDQDV FIQKYGLEDY AFEHIVYGNF NQKIIGGLHL 
      6710       6720       6730       6740       6750
LIGLYRRQQT SNLVVQEFVS YDSSIHSYFI TDEKSGGSKS VCTVIDILLD 
      6760       6770       6780       6790       6800
DFVTLVKSLN LNCVSKVVNV NVDFKDFQFM LWCNDEKVMT FYPRLQAASD 
      6810       6820       6830       6840       6850
WKPGYSMPVL YKYLNSPMER VSLWNYGKPV TLPTGCMMNV AKYTQLCQYL 
      6860       6870       6880       6890       6900
NTTTLAVPVN MRVLHLGAGS EKGVAPGSAV LRQWLPAGTI LVDNDLYPFV 
      6910       6920       6930       6940       6950
SDSVATYFGD CITLPFDCQW DLIISDMYDP ITKNIGEYNV SKDGFFTYIC 
      6960       6970       6980       6990       7000
HMIRDKLALG GSVAIKITEF SWNAELYKLM GYFAFWTVFC TNANASSSEG 
      7010       7020       7030       7040       7050
FLIGINYLCK PKVEIDGNVM HANYLFWRNS TVWNGGAYSL FDMAKFPLKL 
      7060       7070       7080       7090 
AGTAVINLRA DQINDMVYSL LEKGKLLIRD TNKEVFVGDS LVNVI

Note: Produced by -1 ribosomal frameshifting at the 1a-1b genes boundary.

Length:7,095

Mass (Da):797,914

Last modified:June 10, 2008 - v1

Checksum:ⁱ157CDEBD4CE45D4A

GO

Isoform Replicase polyprotein 1a (identifier: P0C6U7-1) [UniParc]FASTA Add to basket

Also known as: pp1a, ORF1a polyprotein

The sequence of this isoform can be found in the external entry P0C6U7.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Length:4,383

Mass (Da):491,305

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	426	I → M in AAT84359 (PubMed:15650185).Curated	1
Sequence conflictⁱ	426	I → M in AAT84351 (PubMed:15650185).Curated	1
Sequence conflictⁱ	813	D → A in AAT84359 (PubMed:15650185).Curated	1
Sequence conflictⁱ	813	D → A in AAT84351 (PubMed:15650185).Curated	1
Sequence conflictⁱ	4376 – 4377	LN → FK in AAR01012 (PubMed:15280490).Curated	2

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱ	88	H → D in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	207	C → R in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	291	P → L in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	317	C → R in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	356	F → V in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	545	I → L in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	762	D → N in strain: Isolate 87309 Belgium 2003.	1
Natural variantⁱ	953	F → L in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.	1
Natural variantⁱ	989	I → V in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.	1
Natural variantⁱ	1305	V → A in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.	1
Natural variantⁱ	1328	N → D in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	1379	F → L in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	1504	L → V in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	1740	G → E in strain: Isolate 87309 Belgium 2003.	1
Natural variantⁱ	1825	N → K in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	1936	S → A in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.	1
Natural variantⁱ	1965	N → T in strain: ATCC VR-759, Isolate clinical OC43-Paris.	1
Natural variantⁱ	2004	L → S in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.	1
Natural variantⁱ	2022	S → G in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	2138 – 2140	TSA → ISV in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	3
Natural variantⁱ	2256	I → M in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	2257	Q → H in strain: Isolate 87309 Belgium 2003.	1
Natural variantⁱ	2386	K → R in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	2500	I → T in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.	1
Natural variantⁱ	2921	D → E in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	2961	V → I in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	3086	T → I in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	3440	P → L in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	3451	L → V in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	3466	I → V in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	4067	I → V in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	4071	I → V in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.	1
Natural variantⁱ	4382	A → T in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	4994	I → L in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate Tulsa 1999 and Isolate 87309 Belgium 2003.	1
Natural variantⁱ	5014 – 5015	SD → RT in strain: Isolate Tulsa 1999.	2
Natural variantⁱ	5765	L → S in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.	1
Natural variantⁱ	5997	L → R in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	6236	G → A in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	6454	T → A in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1
Natural variantⁱ	6546	F → L in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.	1
Natural variantⁱ	6636	D → E in strain: Isolate 87309 Belgium 2003.	1
Natural variantⁱ	6665	A → T in strain: Isolate 87309 Belgium 2003.	1
Natural variantⁱ	6754	T → A in strain: ATCC VR-759 and Isolate clinical OC43-Paris.	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AY903459 Genomic RNA Translation: AAX85666.1 AY903460 Genomic RNA Translation: AAX85675.1 AY585228 Genomic RNA Translation: AAT84351.1 AY585229 Genomic RNA Translation: AAT84359.1 AY391777 Genomic RNA Translation: AAR01012.1 AF124989 Genomic RNA Translation: AAD32993.1

Select the link destinations:
EMBLⁱ
GenBankⁱ
DDBJⁱ

Links Updated

AY903459 Genomic RNA Translation: AAX85666.1
AY903460 Genomic RNA Translation: AAX85675.1
AY585228 Genomic RNA Translation: AAT84351.1
AY585229 Genomic RNA Translation: AAT84359.1
AY391777 Genomic RNA Translation: AAR01012.1
AF124989 Genomic RNA Translation: AAD32993.1

Keywords - Coding sequence diversityⁱ

Ribosomal frameshifting

Protein	Similar proteins		Species	Score	Length	Source
P0C6X6	RNA-dependent RNA polymerase (Fragment)		unidentified human coronavirus		415	UniRef100_P0C6X6
ORF1ab polyprotein (Fragment)		CVHOC		139
ORF1ab polyprotein (Fragment)		CVHOC		193
ORF1ab polyprotein (Fragment)		CVHOC		120
ORF1ab polyprotein (Fragment)		CVHOC		120
+207

Protein	Similar proteins		Species	Score	Length	Source
P0C6X6	Replicase polyprotein 1ab		CVBM		7094	UniRef90_P0C6X6
Replicase polyprotein 1ab		CVBLU		7094
Replicase polyprotein 1ab		CVBEN		7094
Replicase polyprotein 1ab		CVBQ		7059
RNA-dependent RNA polymerase (Fragment)		unidentified human coronavirus		415
+587

Protein	Similar proteins		Species	Score	Length	Source
P0C6X6	Replicase polyprotein 1ab		CVBM		7094	UniRef50_P0C6X6
Replicase polyprotein 1ab		CVBEN		7094
Replicase polyprotein 1ab		CVBLU		7094
Replicase polyprotein 1ab		CVBQ		7059
Replicase polyprotein 1ab		CVM2		7124
+990

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AY903459 Genomic RNA Translation: AAX85666.1 AY903460 Genomic RNA Translation: AAX85675.1 AY585228 Genomic RNA Translation: AAT84351.1 AY585229 Genomic RNA Translation: AAT84359.1 AY391777 Genomic RNA Translation: AAR01012.1 AF124989 Genomic RNA Translation: AAD32993.1

Select the link destinations:
EMBLⁱ
GenBankⁱ
DDBJⁱ

Links Updated

AY903459 Genomic RNA Translation: AAX85666.1
AY903460 Genomic RNA Translation: AAX85675.1
AY585228 Genomic RNA Translation: AAT84351.1
AY585229 Genomic RNA Translation: AAT84359.1
AY391777 Genomic RNA Translation: AAR01012.1
AF124989 Genomic RNA Translation: AAD32993.1

3D structure databases

SMRⁱ	P0C6X6
ModBaseⁱ	Search...

Protein family/group databases

MEROPSⁱ	C16.006

MEROPSⁱ

C16.006

Proteomic databases

PRIDEⁱ	P0C6X6

PRIDEⁱ

P0C6X6

Family and domain databases

CDDⁱ	cd18808, SF1_C_Upf1, 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 2.20.25.360, 1 hit 2.40.10.10, 2 hits 2.40.10.250, 1 hit 2.40.10.290, 1 hit 3.10.20.350, 1 hit 3.10.20.540, 1 hit 3.40.220.10, 1 hit 3.40.50.11580, 1 hit 3.90.70.90, 2 hits
InterProⁱ	View protein in InterPro IPR027351, (+)RNA_virus_helicase_core_dom IPR022570, B-CoV_NSP1 IPR043609, CoV_NSP15_C IPR043608, CoV_NSP15_M IPR043606, CoV_NSP15_N IPR043613, CoV_NSP2_C IPR043611, CoV_NSP3_C IPR043612, CoV_NSP4_N IPR043610, CoV_NSP6 IPR027352, CV_ZBD IPR043502, DNA/RNA_pol_sf IPR041679, DNA2/NAM7-like_AAA IPR037227, EndoU-like IPR002589, Macro_dom IPR043472, Macro_dom-like IPR036333, NSP10_sf_CoV IPR009466, NSP15_CoV IPR043174, NSP15_middle_sf IPR042515, NSP15_N_CoV IPR009461, NSP16_CoV-like IPR032592, NSP3_NAR_bCoV IPR038083, NSP3A-like IPR032505, NSP4_C_CoV IPR038123, NSP4_C_sf_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 IPR001205, RNA-dir_pol_C IPR007094, RNA-dir_pol_PSvirus 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_Methyltr_1, 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 PS51653, CV_ZBD, 1 hit PS51442, M_PRO, 1 hit PS51154, MACRO, 1 hit PS51124, PEPTIDASE_C16, 2 hits PS51657, PSRV_HELICASE, 1 hit PS50507, RDRP_SSRNA_POS, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	R1AB_CVHOC
Accessionⁱ	P0C6X6Primary (citable) accession number: P0C6X6 Secondary accession number(s): Q4VID8 , Q4VIE7, Q696Q1, Q6TNG2, Q9WAC3
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
	Last sequence update:	June 10, 2008
	Last modified:	October 7, 2020
	This is version 94 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Viral Protein Annotation Program

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UniProtKB - P0C6X6 (R1AB_CVHOC)

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Replicase polyprotein 1ab

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

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GO - Biological processi

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

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GO - Cellular componenti

Keywords - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

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Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

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<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

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Family and domain databases

Experimental Info

Natural variant

Sequence databases

Keywords - Coding sequence diversityi

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Sequence databases

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

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Keywords - Technical termⁱ