A0A0K2RW65 · A0A0K2RW65_9BETC
- ProteinORF1ab polyprotein
- GeneORF1ab
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids7117 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
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).
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.
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.
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.
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.
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.
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.
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.
Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.
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.
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.
Plays a role in viral RNA synthesis through two distinct activities. The N7-guanine methyltransferase activity plays a role in the formation of the cap structure GpppA-RNA. The proofreading exoribonuclease reduces the sensitivity of the virus to RNA mutagens during replication. This activity acts on both ssRNA and dsRNA in a 3'-5' direction.
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
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
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.
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.
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.
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
- ATP + H2O = ADP + H+ + phosphate
- uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-RNA
Cofactor
Protein has several cofactor binding sites:
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 6020 | |||||
Sequence: D | ||||||
Active site | 6022 | |||||
Sequence: E | ||||||
Active site | 6121 | |||||
Sequence: E | ||||||
Active site | 6198 | |||||
Sequence: H | ||||||
Active site | 6203 | |||||
Sequence: D | ||||||
Binding site | 6261-6267 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: DIGNPKA | ||||||
Active site | 6706 | |||||
Sequence: H | ||||||
Active site | 6721 | |||||
Sequence: H | ||||||
Active site | 6761 | |||||
Sequence: K |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameORF1ab polyprotein
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Nidovirales > Cornidovirineae > Coronaviridae > Orthocoronavirinae > Betacoronavirus > Embecovirus > Betacoronavirus 1
Accessions
- Primary accessionA0A0K2RW65
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Host membrane ; Multi-pass membrane protein
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 2169-2191 | Helical | ||||
Sequence: VRNKIFACFNFIRWLFVLLFGWI | ||||||
Transmembrane | 2229-2254 | Helical | ||||
Sequence: VVARGACIIATIFLLWFNFIYANVIF | ||||||
Transmembrane | 2352-2371 | Helical | ||||
Sequence: YALYTAWFYPLFALISIQIL | ||||||
Transmembrane | 2391-2414 | Helical | ||||
Sequence: LVSLANMLPAHVFMRFYIIIASFI | ||||||
Transmembrane | 2790-2813 | Helical | ||||
Sequence: YFVYVCFVLSLVCFIGLWCLMPTY | ||||||
Transmembrane | 3061-3086 | Helical | ||||
Sequence: FLALTASSIAGAILAVIVVLVFYYLI | ||||||
Transmembrane | 3098-3119 | Helical | ||||
Sequence: IVFVNVIVWCVNFMMLFVFQVY | ||||||
Transmembrane | 3125-3147 | Helical | ||||
Sequence: VYAICYFYATLYFPSEISVIMHL | ||||||
Transmembrane | 3159-3180 | Helical | ||||
Sequence: LWFCLLYISVVVSNHAFWVFAY | ||||||
Transmembrane | 3590-3613 | Helical | ||||
Sequence: LVKGIVCWIMASTFLFSCIITAFV | ||||||
Transmembrane | 3625-3643 | Helical | ||||
Sequence: MLSITFCALCVISLAMLLV | ||||||
Transmembrane | 3650-3671 | Helical | ||||
Sequence: LTMYIIPVLFTLLYNNYLVVYK | ||||||
Transmembrane | 3691-3712 | Helical | ||||
Sequence: YTYTDEVIYGVLLLIGMVFVTL | ||||||
Transmembrane | 3719-3739 | Helical | ||||
Sequence: LFSFIMFGGRVISVVSLWYMG | ||||||
Transmembrane | 3790-3809 | Helical | ||||
Sequence: IVLICYLFIGYIISCYWGLF |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 2301↔2307 | |||||
Sequence: CNGSIAC |
Keywords
- PTM
Interaction
Subunit
Interacts with host PHB and PHB2.
Interacts with 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.
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.
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.
Interacts with nsp8 to form the replication-transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up to two subunits of nsp13.
Interacts with papain-like protease nsp3 and non-structural protein 6.
Interacts with proofreading exoribonuclease nsp14 and 2'-O-methyltransferase nsp16; these interactions enhance nsp14 and nsp16 enzymatic activities.
Monomer. Homodimer. Only the homodimer shows catalytic activity.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 54-194 | CoV Nsp1 globular | ||||
Sequence: LENHVMVDCRRLIQEGCVQSNLIREIKMNTRPDDMDRVIQDALLSREAVLIPPPRRLSIETCYKWGCCPQGWAMGLFRRCSTCYGGCDVNSHVAYQLFLIDPQGVCLGAGNFVGWVVPLAKLSKEAQAKTVPWTMWLRKRG | ||||||
Domain | 209-244 | BetaCoV Nsp1 C-terminal | ||||
Sequence: DEVCDVLLERAYDSVLDEPKGKFSAKAFALLRSYRG | ||||||
Domain | 248-512 | CoV Nsp2 N-terminal | ||||
Sequence: LLYVDQYGCDYTGSLAVGLEAYADKTLQEMKSLFGVWSQELSYDVVVAWHVVRDTRYNMKLQSAATIRSITYVANPTEDLCDGSVVIQEPVHVYAADSIILRLPKLVDIMDHFYMEEDRALDSIYGVKLEECGLVMQFGYIDCKQDSCDFRGWLPGNMIDGFVCTTCGHVYETGELLAQSSGVLPSNPVLRTKSAAGYAGFGCKDSFTLFDQTVVCFGGCVYWNPVPKIWIPILKSSVKAFDGLVYTGSVGIKSVVKETALICKA | ||||||
Domain | 522-711 | CoV Nsp2 middle | ||||
Sequence: CGNLDQRELLGLSDVWHKQLLLNRGVYKPLLDHIDYFNMRRAKFSLETFTVCSDGFMPFLVDDLVPRSYYLIKSGQAFSEKLNQFVSKSKELIEVSLDSLEAAMCYLNLKIADLAQHFSALGAVFVSKIIHYFKTFTTNTARAFAWVLFHVLHGFYMVVESSIYFVKSVPSYARSVVQAFQDVVRVVLES | ||||||
Domain | 727-845 | CoV Nsp2 C-terminal | ||||
Sequence: RKRICFSGSNVYELERGLLDLSHLPSSVYDLTMPSKIQKANQKPIYLKGVGFDFSLSDDVVEVVTASIIPCGYSKPPKIAEKICVVDNVYMAKAGDKYYPVVVDKQAGLLDQAWRIPCA | ||||||
Domain | 847-959 | Ubiquitin-like | ||||
Sequence: RHVSFKDEFVVKEISTSLKIKVCYELDVDFNSILNTACSVFEVDTTVDMEEFSAVVADAIEDKLTPCKEVDGVGAKVSAFLQKLEDNALYFFDDAGECVLASKLYCTFSAPVD | ||||||
Domain | 1041-1290 | Peptidase C16 | ||||
Sequence: DYDTFYCDTVFEFYATQQEPAFVKVLGVYVPKATRNNCWLRSVLAVFQKLPCVFKDKNLQSLWLSYKQHFDQLFIDTIMQKIPENIVVPQGGYVADFAYWLLTLCDWQATSHWRCLKCDMDLNLHGLDAIFFYGDIVSHVCKCGASMVLLKIDVPFTAHFAMKNKQFCAFTTQRRIFKAACVIDKNDRHSMAVIDGKQVDDKLVTDINSDKFDFIIGHEMTFNMSSFEIAQLYGCCITSNVCFVKGDVIR | ||||||
Domain | 1268-1439 | Macro | ||||
Sequence: EIAQLYGCCITSNVCFVKGDVIRIAQLVYADVVVNPANGHMAHGGGVAKAIANAAGQSFVKETANMVKSKGVCATGDCYVSSGGKLCKTVLNVVGPDARSQGKQSYALLEKTYKHLNKYDCSLTTLISAGIFSVPSDVSLTYLLGVVEKQVILVSNNKEDFDIISKCQITAV | ||||||
Domain | 1495-1567 | DPUP | ||||
Sequence: DDARVFVQSNMENLPADWRIVNKFDQINGVRTIKYFECPGGIDVCSQGKEFGYVRQGSFYKATVSQIKALFVD | ||||||
Domain | 1566-1621 | Ubiquitin-like | ||||
Sequence: VDKIDVLLTVDGVNFVTRYVPCGEVFGKTLGNVFCDAINVTKCKAEQKYKGKVFFQ | ||||||
Domain | 1635-1896 | Peptidase C16 | ||||
Sequence: SSFNFDQKELLAYYNVLVNCGKWQIVVNGKYFTFKQANNNCFVNVACLMLQNVNLKFVSVQWQEAWLEFRAGKPLRFVALVYAKGSFKFGDPADARDFIRVVLSQTDLADAACDYEIVCKCGVKQEQRKGIDAVMHFGTLNREDLENGYTIDCSCGDKLIHCTRIKVPFLICSNTPKDNVLPKGVICANVFTGDNVGHYTHLRCDSSYQLFDASNVKKITTVSGKITDCLYLKNLKQTFRSVLTTYYLDDVMKVEYKPDLTQ | ||||||
Domain | 1910-2011 | Nucleic acid-binding | ||||
Sequence: VKAQFRTFEKVDGAYINFKLVGHTVCDSLNAKLGFDSSKEFVEYKVTEWPTATGDVVLANDDLYVKRYERGCITFGKPVIWYNHEQASLNSLTYFNRPSLVD | ||||||
Domain | 2057-2204 | G2M | ||||
Sequence: PGNQGSYAANGLAISNNIVKLNGVKKPFKVENSIVINDSTSDTKFVKSLSIVDVYDMWLTGCRYVVNAANALSVAVNVPTIKRFIKFGMTVVSIPIDLLNLREIKPVDVVKVVRNKIFACFNFIRWLFVLLFGWIKISADNKVIYITE | ||||||
Domain | 2270-2331 | 3Ecto | ||||
Sequence: GKIVQWIKNTFSFVTICDLYSIQDVGFKNQYCNGSIACQFCLAGFDMLDNYKAIDVVQYEAD | ||||||
Region | 2418-2508 | Y1 | ||||
Sequence: SLFRHVAYGCSKPGCLFCYKRNRSLRVKCSTIVGGMIRYYDVMANGGTAFCSKHQWNCIDCDSYKPGNTFITVEAALDLSKELKRPIQPTD | ||||||
Domain | 2418-2785 | CoV Nsp3 Y | ||||
Sequence: SLFRHVAYGCSKPGCLFCYKRNRSLRVKCSTIVGGMIRYYDVMANGGTAFCSKHQWNCIDCDSYKPGNTFITVEAALDLSKELKRPIQPTDVAYHTVTDVKQVGCYMRLFYERNGQRTYDDVNASLFVDYSNLLHSKVKGVPNMHVVVVENDADKANFLNAAVFYAQSLFRPILMVDKNLITTANTGTSVTETMFDVYVDTFLSMFDVDKKSLNALIATAHSSIKQGTQICKVLDTFLSCARKSCSIDSDVDTKCLADSVMSAVSAGLELTDESCNNLVPTYLKSDNIVAADLGVLIQNSAKHVQGNVAKIAGVSCIWSVDAFNQLSSDFQHKLKKACCKTGLKLKLTYNKQMANVSVLTTPFSLKGG | ||||||
Region | 2422-2435 | ZF1 | ||||
Sequence: HVAYGCSKPGCLFC | ||||||
Region | 2468-2478 | ZF2 | ||||
Sequence: CSKHQWNCIDC | ||||||
Region | 2509-2785 | CoV-Y | ||||
Sequence: VAYHTVTDVKQVGCYMRLFYERNGQRTYDDVNASLFVDYSNLLHSKVKGVPNMHVVVVENDADKANFLNAAVFYAQSLFRPILMVDKNLITTANTGTSVTETMFDVYVDTFLSMFDVDKKSLNALIATAHSSIKQGTQICKVLDTFLSCARKSCSIDSDVDTKCLADSVMSAVSAGLELTDESCNNLVPTYLKSDNIVAADLGVLIQNSAKHVQGNVAKIAGVSCIWSVDAFNQLSSDFQHKLKKACCKTGLKLKLTYNKQMANVSVLTTPFSLKGG | ||||||
Region | 2685-2785 | Y4 | ||||
Sequence: LELTDESCNNLVPTYLKSDNIVAADLGVLIQNSAKHVQGNVAKIAGVSCIWSVDAFNQLSSDFQHKLKKACCKTGLKLKLTYNKQMANVSVLTTPFSLKGG | ||||||
Domain | 3184-3281 | Nsp4C | ||||
Sequence: LGTSVRSDGTFEEMALTTFMITKDSYCKLKNSLSDVAFNRYLSLYNKYRYYSGKMDTAAYREAACSQLAKAMDTFTNNNGSDVLYQPPTASVSTSFLQ | ||||||
Domain | 3282-3584 | Peptidase C30 | ||||
Sequence: SGIVKMVNPTSKVEPCIVSVTYGNMTLNGLWLDDKVYCPRHVICSASDMTNPDYTNLLCRVTSSDFTVLFDRLSLTVMSYQMQGCMLVLTVTLQNSRTPKYTFGVVKPGETFTVLAAYNGKPQGAFHVTMRSSYTIKGSFLCGSCGSVGYVLMGDCVKFVYMHQLELSTGCHTGTDFNGDFYGPYKDAQVVQLPVQDYIQSVNFVAWLYAAILNNCNWFVQSDKCSVEDFNVWALSNGFSQVKSDLVIDALASMTGVSLETLLAAIKRLKNGFQGRQIMGSCSFEDELTPSDVYQQLAGIKLQ | ||||||
Domain | 3872-3960 | RdRp Nsp7 cofactor | ||||
Sequence: SKLTDVKCANVVLLNCLQHLHVASNSKLWQYCSTLHNEILATSDLGVAFEKLAQLLIVLFANPAAVDSKCLTSIEEVCDDYAKDNTVLQ | ||||||
Domain | 3961-4157 | RdRp Nsp8 cofactor | ||||
Sequence: ALQSEFVNMASFVEYEVAKKNLDEARSSGSANQQQLKQLEKACNIAKSAYERDRAVARKLERMADLALTNMYKEARINDKKSKVVSALQTMLFSMVRKLDNQALNSILDNAVKGCVPLNAIPSLAANTLTIIVPDKSVYDQVVDNVYVTYAGNVWQIQTIQDSDGTNKQLNEISDDCNWPLVIIANRHNEVSATVLQ | ||||||
Domain | 4158-4267 | Nsp9 ssRNA-binding | ||||
Sequence: NNELMPAKLKTQVVNSGPDQTCNTPTQCYYNNSNNGKIVYAILSDVDGLKYTKILKDDGNFVVLELDPPCKFTVQDVKGLKIKYLYFVKGCNTLARGWVVGTISSTVRLQ | ||||||
Domain | 4268-4405 | ExoN/MTase coactivator | ||||
Sequence: AGTATEYASNSSILSLCAFSVDPKKTYLDFIQQGGTPIANCVKMLCDHAGTGMAITIKPEATTSQDSYGGASVCIYCRSRVEHPDVDGLCKLRGKFVQVPVGIKDPVSYVLTHDVCQVCGFWRDGSCSCVSTDTTVQS | ||||||
Domain | 4410-4665 | NiRAN | ||||
Sequence: FLNRVRGTSVDARLVPCASGLSTDVQLRAFDICNASVAGIGLHLKVNCCRFQRVDENGDKLDQFFVVKRTDLTIYNREMECYERVKDCKFVAEHDFFTFDVEGSRVPHIVRKDLTKYTMLDLCYALRHFDRNDCMLLCDILSIYAGCEQSYFTKKDWYDFVENPDIINVYKKLGPIFNRALVSATEFADKLVEVGLVGVLTLDNQDLNGKWYDFGDFVIATPGCGVAIADSYYSYMMPMLTMCHALDCELYINGAY | ||||||
Domain | 4666-4764 | Nsp12 Interface | ||||
Sequence: RQFDLVQYDFTDYKLELFNKYFKHWSMPYHPNTVDCQDDRCIIHCANFNILFSMVLPNTCFGPLVRQIFVDGVPFVVSIGYHYKELGIVMNMDVDTHRY | ||||||
Domain | 4765-5332 | Nsp12 RNA-dependent RNA polymerase | ||||
Sequence: RLSLKDLLLYAADPALHVASASALYDLRTCCFSVAAITSGVKFQTVKPGNFNQDFYDFILSKGLLKEGSSVDLKHFFFTQDGNAAITDYNYYKYNLPTMVDIKQLLFVLEVVYKYFEIYDGGCIPASQVIVNNYDKSAGYPFNKFGKARLYYEALSFEEQDEIYAYTKRNVLPTLTQMNLKYAISAKNRARTVAGVSILSTMTGRMFHQKCLKSIAATRGVPVVIGTTKFYGGWDDMLRRLIKDVDNPVLMGWDYPKCDRAMPNLLRIVSSLVLARKHEACCSQSDRFYRLANECAQVLSEIVMCGGCYYVKPGGTSSGDATTAFANSVFNICQAVSANVCALMSCNGNKIEDLSIRALQKRLYSHVYRSDMVDSTFVTEYYEFLNKHFSMMILSDDGVVCYNSDYASKGYIANISAFQQVLYYQNNVFMSESKCWVENNINNGPHEFCSQHTMLVKMDGDDVYLPYPDPSRILGAGCFVDDLLKTDSVLLIERFVSLAIDAYPLVYHENEEYQKVFRVYLEYIKKLYNDLGNQILDSYSVILSTCDGQKFTDESFYKNMYLRSAVMQ | ||||||
Domain | 5012-5174 | RdRp catalytic | ||||
Sequence: PVLMGWDYPKCDRAMPNLLRIVSSLVLARKHEACCSQSDRFYRLANECAQVLSEIVMCGGCYYVKPGGTSSGDATTAFANSVFNICQAVSANVCALMSCNGNKIEDLSIRALQKRLYSHVYRSDMVDSTFVTEYYEFLNKHFSMMILSDDGVVCYNSDYASKG | ||||||
Domain | 5333-5416 | CV ZBD | ||||
Sequence: SVGACVVCSSQTSLRCGSCIRKPLLCCKCCYDHVMATDHKYVLSVSPYVCNAPGCDVNDVTKLYLGGMSYYCEDHKPQYSFKLV | ||||||
Domain | 5588-5946 | +RNA virus helicase C-terminal | ||||
Sequence: SVPETFQSNVVNYQHIGMKRYCTVQGPPGTGKSHLAIGLAVYYCTARVVYTAASHAAVDALCEKAYKFLNINDCTRIVPAKVRVDCYDKFKINDTTRKYVFTTINALPEMVTDIVVVDEVSMLTNYELSVINARIRAKHYVYIGDPAQLPAPRVLLSKGSLEPKYFNTVTKLMCCLGPDIFLGTCYRCPKEIVDTVSALVYDNKLKAKNESSSLCFKVYFKGVTTHESSSAVNMQQIYLISKFLKANPLWHNAVFISPYNSQNFAAKRVLGLQTQTVDSAQGSEYDYVIYSQTAETAHSVNVNRFNVAITRAKKGILCVMCNMQLFEALQFTALTLDKVPSKLQCTTNLFKDCSKSYVG | ||||||
Domain | 6002-6217 | ExoN | ||||
Sequence: LFITKEEAVKRVRAWVGFDAEGAHATRDNIGTNFPLQLGFSTGIDFVVEATGLFSERDGYSFKKAVAKAPPGEQFKHLIPLMTRGQRWDVVRPRIVQMFSDHLVDLSDSVVLVTWAASFELTCLRYFAKLGKETCCNVCTNRATVYNSRTGYYGCWRHSVSCDYLYNPLIVDIQQWGYSGSLSSNHDMYCSIHKGAHIASSDAIMTRCLAIYDCFC | ||||||
Domain | 6226-6452 | N7-MTase | ||||
Sequence: YPIISNELSINSSCRTLQRVMLKAAMLCNRYSLCYDIGNPKAIACIKGYDFKFYDSQPIVKSVKTLVYSYEAHKDSFKDGLCMFWNCNVDKYPPNAVVCRFDTRVLNNLNLPGCNGGSLYVNKHAFHTNPFSRAAFEYLKPMPFFYYSDTPCVYMDGMDNKQVDYVPLKSATCITRCNLGGAVCLKHAEEYREYLEFYNTATTAGFTFWVYKTFDFYNLWNTFTKLQ | ||||||
Region | 6339-6353 | GpppA-binding | ||||
Sequence: CNGGSLYVNKHAFHT | ||||||
Domain | 6453-6513 | Nsp15 N-terminal oligomerization | ||||
Sequence: SLENVVYNLVKTGYYTGQAGEMPCAIINDKVVAKIEQEDVVVFTNNTTYPTNIAVELFAKR | ||||||
Domain | 6514-6634 | AV-Nsp11N/CoV-Nsp15M | ||||
Sequence: SVRHHPELKLFRNLNIDVCWKHVIWDYVRQSIYCSNTFGVCTYTDLKCIDKLNVLFDGRDNGALEAFKRSNNGVYISTTKVKSLSMIRGPPRAELNGVVVDKVGDADCAFYFAVRKDGQDV | ||||||
Domain | 6676-6815 | NendoU | ||||
Sequence: TCRTDMEKDFIALDQDVFIQKYGLEDYAFEHIVYGNFNQKIIGGLHLLIGLYRRQQTSNLVIQEFVSYDSSIHSYFITDQKSGGSKSVCTVIDILLDDFVALVKSLNLNCVSKVVNVNVDFKDFQFMLWCNDEKVMTFYP | ||||||
Domain | 6820-7114 | Nidovirus-type SAM-dependent 2'-O-MTase | ||||
Sequence: ASDWKPGYSMPVLYKYLNSPMERVSLWNYGKPVTLPTGCMMNVAKYTQLCQYLNTTTLAVPVNMRVLHLGAGSEKGVAPGSAVLRQWLPAGTILVDNDLHPFVSDSVASYFGDCITLPFDCQWDLIISDMYDPITKNIGEYNVSKDGFFTYICHMIRDNLALGGSVAIKITEFSWNAELYKLMGCFAFWTVFCTNANASSSEGFLIGINYLGKSKFDIDGNVMHANYLFWRNSTVWNGGSYSLFDMAKFPLKLAGTAVINLRADQINDMVYSLLEKGKLLIRDTSKEVFVGDSLV |
Sequence similarities
Belongs to the coronaviruses polyprotein 1ab family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length7,117
- Mass (Da)799,702
- Last updated2015-11-11 v1
- ChecksumA662F949AAF62A06
Keywords
- Coding sequence diversity
- Technical term