K7XK97 · K7XK97_9ALPC
- ProteinORF1a polyprotein
- Gene1a
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids4016 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter.
The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3.
Catalytic activity
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell membrane | |
Cellular Component | host cell perinuclear region of cytoplasm | |
Cellular Component | membrane | |
Molecular Function | cysteine-type deubiquitinase activity | |
Molecular Function | cysteine-type endopeptidase activity | |
Molecular Function | omega peptidase activity | |
Molecular Function | RNA binding | |
Molecular Function | transferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | induction by virus of host autophagy | |
Biological Process | proteolysis | |
Biological Process | symbiont-mediated perturbation of host ubiquitin-like protein modification | |
Biological Process | symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity | |
Biological Process | viral genome replication | |
Biological Process | viral protein processing | |
Biological Process | viral translational frameshifting | |
Biological Process | virus-mediated perturbation of host defense response |
Keywords
- Molecular function
- Biological process
- Ligand
Protein family/group databases
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Nidovirales > Cornidovirineae > Coronaviridae > Orthocoronavirinae > Alphacoronavirus > Tegacovirus > Alphacoronavirus 1
Accessions
- Primary accessionK7XK97
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 1834-1852 | Helical | ||||
Sequence: ILRFLLEVFKYLLVLFMCL | ||||||
Transmembrane | 1889-1909 | Helical | ||||
Sequence: VWRYAKLVLLLIAIYNFFYLF | ||||||
Transmembrane | 1971-1988 | Helical | ||||
Sequence: LWNRLVQLSYFAFLAVFG | ||||||
Transmembrane | 1995-2013 | Helical | ||||
Sequence: VLMYFVSQYLNLWLSYFGY | ||||||
Transmembrane | 2025-2045 | Helical | ||||
Sequence: FESISAEFVIIVIVVKAVLVL | ||||||
Transmembrane | 2400-2420 | Helical | ||||
Sequence: IVMLILAFIFIYGLCSVYSVA | ||||||
Transmembrane | 2665-2685 | Helical | ||||
Sequence: GAMLVNIIIACLAIAMCYGVL | ||||||
Transmembrane | 2690-2707 | Helical | ||||
Sequence: IFGDCTLLIVMIIVTLVV | ||||||
Transmembrane | 2713-2731 | Helical | ||||
Sequence: FVTQNTFFMIIYAIVYYFT | ||||||
Transmembrane | 2743-2767 | Helical | ||||
Sequence: AGFIIAYINMAPWYVITAYILVFLY | ||||||
Transmembrane | 3186-3205 | Helical | ||||
Sequence: FFYPIMTAMTILFAFWLEFF | ||||||
Transmembrane | 3217-3236 | Helical | ||||
Sequence: FVSIVLAVTTLISTVFVSGI | ||||||
Transmembrane | 3242-3266 | Helical | ||||
Sequence: FFMSFVLPSVILVTAHNLFWDFSYY | ||||||
Transmembrane | 3287-3306 | Helical | ||||
Sequence: GVMLTVFCFIVFVTYSVRFF | ||||||
Transmembrane | 3312-3330 | Helical | ||||
Sequence: WFSLAVTTVLVIFNMVKIF | ||||||
Transmembrane | 3370-3389 | Helical | ||||
Sequence: IAYYIVVCVMPSAFVSDFGF | ||||||
Transmembrane | 3396-3414 | Helical | ||||
Sequence: VYMACGYLFCCYYGILYWV |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 1920↔1947 | |||||
Sequence: CNGAVQAYKNSSFVKSEVCGNSILCKAC | ||||||
Disulfide bond | 1938↔1944 | |||||
Sequence: CGNSILC |
Keywords
- PTM
Interaction
Subunit
3CL-PRO exists as monomer and homodimer. Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp9 is a dimer. Nsp10 forms a dodecamer.
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-108 | CoV Nsp1 globular | ||||
Sequence: SSKQFKILVNEDYQVNVPSLPIRDVLQEIKYCYRNGFEGYVFVPEYCRDLVDCDRKDHYVIGVLGNGVSDLKPVLLTEPSVMLQGFIVRANCNGVLEDFDLKIARTG | ||||||
Domain | 111-349 | CoV Nsp2 N-terminal | ||||
Sequence: AIYVDQYMCGADGKPVIEGDFKDYFGDEDVIEFEGEEYHCAWTTVRDEKPLNQQTLFTIQEIQYNLEIPHKLPNCATRHVAPPVKKNSKIVLSEDYRKLYDIFGSPFMGNGDCLSKCFDTLHFIAATLRCPCGSESSGVGDWTGFKTACCGLSGKVKGVTLGDVKPGDAVVTSMSAGKGIKFFANCVLQHAGDVENVSIWKVIKTFTVDETVCTPDFEGELNDFIKPESKSPTACSIKR | ||||||
Domain | 378-773 | CoV Nsp2 middle | ||||
Sequence: NVGLLFKKTPWFVQKCGALFVDAWKVVEELCSSLKLTYKQIYEVVASLCTSAFTIVNYKPTFVVSDNRVKDLVDKCVKVLVKAFDVFTQTITIAGIEAKCFVLGAKYLLFNNALVKLVSVKILGKKQKGLESAFFATSLVGATVNVTPKRTETANISLNKVDDVVAPGDGYIVIVGDMAFYKSGEYYFMMASPDSVLINNVFKAARAPSYDIVYDVDDDTKSKMIAKLGSSFEYDGDIDAAIVKVNELLIEFKQQNLCFRALKDDKSIFVEAYLKKYKMPACLAKHIGLWNIIKKDSCKKSFLSLFNHLNELEDIKETNVQDIKNILCPDLLLDLDYGAIWYKCMPSCSDLSVLRSVQLLIGNGVKVVCDGCKVFANQLSNGYNKLCNAARTDIEI | ||||||
Domain | 768-879 | CoV Nsp2 C-terminal | ||||
Sequence: RTDIEIGGIPFSTFKTPTNTFIEMTDAIYSVIEQGKALSFGNADVPVVDNGTILTDDWSEPILLEPAEYVKPKNNGNIIVIAGYTFYKDEDEHFYPYGSGKIVQRMYNKMGG | ||||||
Domain | 882-983 | Ubiquitin-like | ||||
Sequence: KTVSFSEEVDVQEIAPVTRVKLEFEFDNEIVTGVLEQAIGTRYKFTGTTWEEFEDSISEELDAIFDTLANQGVELEGYFIYDTCGGFDIKNSDGIMISQYDI | ||||||
Compositional bias | 1002-1021 | Acidic residues | ||||
Sequence: VEYVEEDSETEIEASEGVEE | ||||||
Region | 1002-1039 | Disordered | ||||
Sequence: VEYVEEDSETEIEASEGVEETSSQEEVGTVEVEDVTST | ||||||
Domain | 1054-1298 | Peptidase C16 | ||||
Sequence: PWAAAVDVQEAEQIKPSLPPFKTTNLNGKIILKQQDNNCWINACCYQLQAFDFFNNESWEKFKKGDVMDFVNLCYAATTLERGHSGDAEYLLELMLNDYSTAKIVLAAKCGCGVKEIVLERTVFKLTPLKESFKYGVCGDCMQVNTCRFLSVEGSGVFVHDILSKQTPEGMFVVKPIMHAVYTGTTQNGHYMVDDIERDYCVDGMGIKPLKKRYYTSTLFINANVMTRAEKPKQEPKVEKVEQQP | ||||||
Region | 1284-1314 | Disordered | ||||
Sequence: KPKQEPKVEKVEQQPEIEEKKPSIEKEEVQS | ||||||
Domain | 1317-1488 | Macro | ||||
Sequence: NDDLILPFYKAGKLSFYQGDLDVLINFLEPDVIVNAANGDLKHMGGVARAIDVFTSGKLTERSKDYLKKNKSIAPGNAVFFENVIEHLSVLNVVGPRSGDSRVEAKLNNVYKAIAKCEGKILTPLISVGIFSVKLETSLQCLLKTVNDRELNIFVYTDQERQAVENFFSGSI | ||||||
Domain | 1485-1541 | Ubiquitin-like | ||||
Sequence: SGSIPVKVTEDNVNHERVSVSFDKTYGEQLKGTVVIKDKDVTNQLPSAFDVGQKVVK | ||||||
Domain | 1549-1802 | Peptidase C16 | ||||
Sequence: AHYGFHDAAAFSASSHDAYKFEVVTHSNFIVHKQTDNNCWINAICLALQRLKPQWKFPGVRGLWNEFLERKTQGFVHMLYHISGVKKGEPGDAELTLHKLGDLMDNDCEIIVTHTTACDKCSKVEKFTGPVVAAPLAIHGTDETCVHGVSVNVKVTQIKGTVAITSLSGPIIGEVLEATGYICYRGSSKNGHYTYYDKRNGLMIDAEKAYHFNKDLLQVTTAIASNFVVKKPQVEEKPKTRVFNRVEESPKIAQ | ||||||
Domain | 1904-1969 | 3Ecto | ||||
Sequence: NFFYLFVSIPVVHKLACNGAVQAYKNSSFVKSEVCGNSILCKACLASYDELADFQHLQVTWDFKSD | ||||||
Region | 2043-2133 | Y1 | ||||
Sequence: LVLKHIVFSCSNPSCKTCSKTARQTRIPIQVVVNGSMKTVYVHANGTGKLCKKHNFYCKNCESYGFENTFICDEIVRDLSNSVKQTVYATD | ||||||
Domain | 2043-2383 | CoV Nsp3 Y | ||||
Sequence: LVLKHIVFSCSNPSCKTCSKTARQTRIPIQVVVNGSMKTVYVHANGTGKLCKKHNFYCKNCESYGFENTFICDEIVRDLSNSVKQTVYATDRSHQEVTKVECSDGFYRFYVGDEFTSYDYDVKHKKYSSQEVLKNMLLLDDFIVYSPSGSSLANVRNACVYFSQLIGKPIKIVNSDLLEDLSVDFKGALFNAKKNVIKNSFNVDVSECKNLDECYRACNLDVSFSTFEMAVNNAHRFGILITDRSFNNFWPSKVKPGSSGVSAMDIGKCMTSDAKIVNAKVLTQRGKSVVWLSQDFAALSSTAQKVLVKTFVEEGVNFSLTFNAVGSDDDLPYERFTESVP | ||||||
Region | 2047-2060 | ZF1 | ||||
Sequence: HIVFSCSNPSCKTC | ||||||
Region | 2093-2103 | ZF2 | ||||
Sequence: CKKHNFYCKNC | ||||||
Region | 2134-2383 | CoV-Y | ||||
Sequence: RSHQEVTKVECSDGFYRFYVGDEFTSYDYDVKHKKYSSQEVLKNMLLLDDFIVYSPSGSSLANVRNACVYFSQLIGKPIKIVNSDLLEDLSVDFKGALFNAKKNVIKNSFNVDVSECKNLDECYRACNLDVSFSTFEMAVNNAHRFGILITDRSFNNFWPSKVKPGSSGVSAMDIGKCMTSDAKIVNAKVLTQRGKSVVWLSQDFAALSSTAQKVLVKTFVEEGVNFSLTFNAVGSDDDLPYERFTESVP | ||||||
Region | 2281-2383 | Y4 | ||||
Sequence: ILITDRSFNNFWPSKVKPGSSGVSAMDIGKCMTSDAKIVNAKVLTQRGKSVVWLSQDFAALSSTAQKVLVKTFVEEGVNFSLTFNAVGSDDDLPYERFTESVP | ||||||
Domain | 2782-2877 | Nsp4C | ||||
Sequence: LFEGDKFVGNFESAAMGTFVIDMRSYETIVNSTPIDRIKSYANSFNKYKYYTGSMGEADYRMACYAHLGKALMDYSVNRTDMLYTPPTVSVNSTLQ | ||||||
Domain | 2878-3179 | Peptidase C30 | ||||
Sequence: SGLRKMAQPSGLVEPCIVRVSYGNNVLNGLWLGDEVICPRHVIASDTTRVINYENEMSSVRLHNFSVSKNNVFLGVVSAKYKGVNLVLKVNQVNPNTPEHKFKSIKSGESFNILACYEGCPGSVYGVNMRSQGTIKGSFIAGTCGSVGYVLENGILYFVYMHHLELGNGSHVGSNLEGEMYGGYEDQPSMQLEGTNVMSSDNVVAFLYAALINGERWFVTNTSMSLESYNTWAKTNSFTELSSTDAFSMLAAKTGQSVEKLLDSIVRLNKGFGGRTILSYGSLCDEFTPTEVIRQMYGVNLQ | ||||||
Domain | 3474-3556 | RdRp Nsp7 cofactor | ||||
Sequence: SKLTEMKCTNVVLLGLLSKMHVESNSKEWNYCVGLHNEINLCDDPEIVLEKLLALIAFFLSKHNTCDLSELIESYFENTTILQ | ||||||
Domain | 3557-3751 | RdRp Nsp8 cofactor | ||||
Sequence: SVASAYAALPSWIALEKARADLEEAKKNDVSPQILKQLTKAFNIAKSDFEREASVQKKLDKMAEQAAASMYKEARAVDRKSKIISAMHSLLFGMLKKLDMSSVNTIIDQARNGVLPLSIIPAASATRLVVVTPSLEVFSKIRQENNVHYAGAIWTIVEVKDANGSHVHLKEITAANELNLTWPLSITCERTTKLQ | ||||||
Domain | 3752-3862 | Nsp9 ssRNA-binding | ||||
Sequence: NNEIMPGKLKERAVKASSTLDGEAFGSGKALMAAESGKSFMYAFIASENNLKYVKWESNNDIIPIELEAPLRFYVDGANGPEVKYLYFVKNLNTLRRGAVLGYIGATVRLQ | ||||||
Domain | 3863-4003 | ExoN/MTase coactivator | ||||
Sequence: AGKPTEHPSNSSLLTLCAFAPDPAKAYVDAVKRGMQPVNNCVKMLSNGAGNGMAVTNGVEANTQQDSYGGASVCIYCRCHVEHPAIDGLCRYKGKFVQIPTGTQDPIRFCIENEVCVVCGCWLNNGCMCDRTSMQSSTVDQ |
Sequence similarities
Belongs to the coronaviruses polyprotein 1ab family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length4,016
- Mass (Da)447,798
- Last updated2013-02-06 v1
- ChecksumD2BE2BF3B2F25503
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1002-1021 | Acidic residues | ||||
Sequence: VEYVEEDSETEIEASEGVEE |
Keywords
- Coding sequence diversity