| IED ID | IndEnz0002001199 |
| Enzyme Type ID | protease001199 |
| Protein Name |
Replicase polyprotein 1ab pp1ab ORF1ab polyprotein Cleaved into: Non-structural protein 1 nsp1 p9 ; Non-structural protein 2 nsp2 p87 ; Non-structural protein 3 nsp3 EC 3.4.19.12 EC 3.4.22.- PL1-PRO/PL2-PRO PLP1/PLP2 Papain-like proteinases 1/2 p195 ; Non-structural protein 4 nsp4 Peptide HD2 ; 3C-like proteinase 3CL-PRO 3CLp EC 3.4.22.- M-PRO nsp5 p34 ; Non-structural protein 6 nsp6 ; Non-structural protein 7 nsp7 p5 ; Non-structural protein 8 nsp8 p23 ; Non-structural protein 9 nsp9 p12 ; Non-structural protein 10 nsp10 Growth factor-like peptide GFL p16 ; RNA-directed RNA polymerase Pol RdRp EC 2.7.7.48 nsp12 p100 ; Helicase Hel EC 3.6.4.12 EC 3.6.4.13 nsp13 p66 p66-HEL ; Exoribonuclease ExoN EC 3.1.13.- nsp14 ; Uridylate-specific endoribonuclease EC 4.6.1.- NendoU nsp15 p41 ; Putative 2'-O-methyl transferase EC 2.1.1.57 nsp16 |
| Gene Name | rep 1a-1b |
| Organism | Human coronavirus 229E (HCoV-229E) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Nidovirales Cornidovirineae Coronaviridae Orthocoronavirinae Alphacoronavirus Duvinacovirus Human coronavirus 229E (HCoV-229E) |
| Enzyme Sequence | MACNRVTLAVASDSEISANGCSTIAQAVRRYSEAASNGFRACRFVSLDLQDCIVGIADDTYVMGLHGNQTLFCNIMKFSDRPFMLHGWLVFSNSNYLLEEFDVVFGKRGGGNVTYTDQYLCGADGKPVMSEDLWQFVDHFGENEEIIINGHTYVCAWLTKRKPLDYKRQNNLAIEEIEYVHGDALHTLRNGSVLEMAKEVKTSSKVVLSDALDKLYKVFGSPVMTNGSNILEAFTKPVFISALVQCTCGTKSWSVGDWTGFKSSCCNVISNKLCVVPGNVKPGDAVITTQQAGAGIKYFCGMTLKFVANIEGVSVWRVIALQSVDCFVASSTFVEEEHVNRMDTFCFNVRNSVTDECRLAMLGAEMTSNVRRQVASGVIDISTGWFDVYDDIFAESKPWFVRKAEDIFGPCWSALASALKQLKVTTGELVRFVKSICNSAVAVVGGTIQILASVPEKFLNAFDVFVTAIQTVFDCAVETCTIAGKAFDKVFDYVLLDNALVKLVTTKLKGVRERGLNKVKYATVVVGSTEEVKSSRVERSTAVLTIANNYSKLFDEGYTVVIGDVAYFVSDGYFRLMASPNSVLTTAVYKPLFAFNVNVMGTRPEKFPTTVTCENLESAVLFVNDKITEFQLDYSIDVIDNEIIVKPNISLCVPLYVRDYVDKWDDFCRQYSNESWFEDDYRAFISVLDITDAAVKAAESKAFVDTIVPPCPSILKVIDGGKIWNGVIKNVNSVRDWLKSLKLNLTQQGLLGTCAKRFKRWLGILLEAYNAFLDTVVSTVKIGGLTFKTYAFDKPYIVIRDIVCKVENKTEAEWIELFPHNDRIKSFSTFESAYMPIADPTHFDIEEVELLDAEFVEPGCGGILAVIDEHVFYKKDGVYYPSNGTNILPVAFTKAAGGKVSFSDDVEVKDIEPVYRVKLCFEFEDEKLVDVCEKAIGKKIKHEGDWDSFCKTIQSALSVVSCYVNLPTYYIYDEEGGNDLSLPVMISEWPLSVQQAQQEATLPDIAEDVVDQVEEVNSIFDIETVDVKHDVSPFEMPFEELNGLKILKQLDNNCWVNSVMLQIQLTGILDGDYAMQFFKMGRVAKMIERCYTAEQCIRGAMGDVGLCMYRLLKDLHTGFMVMDYKCSCTSGRLEESGAVLFCTPTKKAFPYGTCLNCNAPRMCTIRQLQGTIIFVQQKPEPVNPVSFVVKPVCSSIFRGAVSCGHYQTNIYSQNLCVDGFGVNKIQPWTNDALNTICIKDADYNAKVEISVTPIKNTVDTTPKEEFVVKEKLNAFLVHDNVAFYQGDVDTVVNGVDFDFIVNAANENLAHGGGLAKALDVYTKGKLQRLSKEHIGLAGKVKVGTGVMVECDSLRIFNVVGPRKGKHERDLLIKAYNTINNEQGTPLTPILSCGIFGIKLETSLEVLLDVCNTKEVKVFVYTDTEVCKVKDFVSGLVNVQKVEQPKIEPKPVSVIKVAPKPYRVDGKFSYFTEDLLCVADDKPIVLFTDSMLTLDDRGLALDNALSGVLSAAIKDCVDINKAIPSGNLIKFDIGSVVVYMCVVPSEKDKHLDNNVQRCTRKLNRLMCDIVCTIPADYILPLVLSSLTCNVSFVGELKAAEAKVITIKVTEDGVNVHDVTVTTDKSFEQQVGVIADKDKDLSGAVPSDLNTSELLTKAIDVDWVEFYGFKDAVTFATVDHSAFAYESAVVNGIRVLKTSDNNCWVNAVCIALQYSKPHFISQGLDAAWNKFVLGDVEIFVAFVYYVARLMKGDKGDAEDTLTKLSKYLANEAQVQLEHYSSCVECDAKFKNSVASINSAIVCASVKRDGVQVGYCVHGIKYYSRVRSVRGRAIIVSVEQLEPCAQSRLLSGVAYTAFSGPVDKGHYTVYDTAKKSMYDGDRFVKHDLSLLSVTSVVMVGGYVAPVNTVKPKPVINQLDEKAQKFFDFGDFLIHNFVIFFTWLLSMFTLCKTAVTTGDVKIMAKAPQRTGVVLKRSLKYNLKASAAVLKSKWWLLAKFTKLLLLIYTLYSVVLLCVRFGPFNFCSETVNGYAKSNFVKDDYCDGSLGCKMCLFGYQELSQFSHLDVVWKHITDPLFSNMQPFIVMVLLLIFGDNYLRCFLLYFVAQMISTVGVFLGYKETNWFLHFIPFDVICDELLVTVIVIKVISFVRHVLFGCENPDCIACSKSARLKRFPVNTIVNGVQRSFYVNANGGSKFCKKHRFFCVDCDSYGYGSTFITPEVSRELGNITKTNVQPTGPAYVMIDKVEFENGFYRLYSCETFWRYNFDITESKYSCKEVFKNCNVLDDFIVFNNNGTNVTQVKNASVYFSQLLCRPIKLVDSELLSTLSVDFNGVLHKAYIDVLRNSFGKDLNANMSLAECKRALGLSISDHEFTSAISNAHRCDVLLSDLSFNNFVSSYAKPEEKLSAYDLACCMRAGAKVVNANVLTKDQTPIVWHAKDFNSLSAEGRKYIVKTSKAKGLTFLLTINENQAVTQIPATSIVAKQGAGDAGHSLTWLWLLCGLVCLIQFYLCFFMPYFMYDIVSSFEGYDFKYIENGQLKNFEAPLKCVRNVFENFEDWHYAKFGFTPLNKQSCPIVVGVSEIVNTVAGIPSNVYLVGKTLIFTLQAAFGNAGVCYDIFGVTTPEKCIFTSACTRLEGLGGNNVYCYNTALMEGSLPYSSIQANAYYKYDNGNFIKLPEVIAQGFGFRTVRTIATKYCRVGECVESNAGVCFGFDKWFVNDGRVANGYVCGTGLWNLVFNILSMFSSSFSVAAMSGQILLNCALGAFAIFCCFLVTKFRRMFGDLSVGVCTVVVAVLLNNVSYIVTQNLVTMIAYAILYFFATRSLRYAWIWCAAYLIAYISFAPWWLCAWYFLAMLTGLLPSLLKLKVSTNLFEGDKFVGTFESAAAGTFVIDMRSYEKLANSISPEKLKSYAASYNRYKYYSGNANEADYRCACYAYLAKAMLDFSRDHNDILYTPPTVSYGSTLQAGLRKMAQPSGFVEKCVVRVCYGNTVLNGLWLGDIVYCPRHVIASNTTSAIDYDHEYSIMRLHNFSIISGTAFLGVVGATMHGVTLKIKVSQTNMHTPRHSFRTLKSGEGFNILACYDGCAQGVFGVNMRTNWTIRGSFINGACGSPGYNLKNGEVEFVYMHQIELGSGSHVGSSFDGVMYGGFEDQPNLQVESANQMLTVNVVAFLYAAILNGCTWWLKGEKLFVEHYNEWAQANGFTAMNGEDAFSILAAKTGVCVERLLHAIQVLNNGFGGKQILGYSSLNDEFSINEVVKQMFGVNLQSGKTTSMFKSISLFAGFFVMFWAELFVYTTTIWVNPGFLTPFMILLVALSLCLTFVVKHKVLFLQVFLLPSIIVAAIQNCAWDYHVTKVLAEKFDYNVSVMQMDIQGFVNIFICLFVALLHTWRFAKERCTHWCTYLFSLIAVLYTALYSYDYVSLLVMLLCAISNEWYIGAIIFRICRFGVAFLPVEYVSYFDGVKTVLLFYMLLGFVSCMYYGLLYWINRFCKCTLGVYDFCVSPAEFKYMVANGLNAPNGPFDALFLSFKLMGIGGPRTIKVSTVQSKLTDLKCTNVVLMGILSNMNIASNSKEWAYCVEMHNKINLCDDPETAQELLLALLAFFLSKHSDFGLGDLVDSYFENDSILQSVASSFVGMPSFVAYETARQEYENAVANGSSPQIIKQLKKAMNVAKAEFDRESSVQKKINRMAEQAAAAMYKEARAVNRKSKVVSAMHSLLFGMLRRLDMSSVDTILNMARNGVVPLSVIPATSAARLVVVVPDHDSFVKMMVDGFVHYAGVVWTLQEVKDNDGKNVHLKDVTKENQEILVWPLILTCERVVKLQNNEIMPGKMKVKATKGEGDGGITSEGNALYNNEGGRAFMYAYVTTKPGMKYVKWEHDSGVVTVELEPPCRFVIDTPTGPQIKYLYFVKNLNNLRRGAVLGYIGATVRLQAGKQTEFVSNSHLLTHCSFAVDPAAAYLDAVKQGAKPVGNCVKMLTNGSGSGQAITCTIDSNTTQDTYGGASVCIYCRAHVAHPTMDGFCQYKGKWVQVPIGTNDPIRFCLENTVCKVCGCWLNHGCTCDRTAIQSFDNSYLNRVRGSSAARLEPCNGTDIDYCVRAFDVYNKDASFIGKNLKSNCVRFKNVDKDDAFYIVKRCIKSVMDHEQSMYNLLKGCNAVAKHDFFTWHEGRTIYGNVSRQDLTKYTMMDLCFALRNFDEKDCEVFKEILVLTGCCSTDYFEMKNWFDPIENEDIHRVYAALGKVVANAMLKCVAFCDEMVLKGVVGVLTLDNQDLNGNFYDFGDFVLCPPGMGIPYCTSYYSYMMPVMGMTNCLASECFMKSDIFGQDFKTFDLLKYDFTEHKEVLFNKYFKYWGQDYHPDCVDCHDEMCILHCSNFNTLFATTIPNTAFGPLCRKVFIDGVPVVATAGYHFKQLGLVWNKDVNTHSTRLTITELLQFVTDPTLIVASSPALVDKRTVCFSVAALSTGLTSQTVKPGHFNKEFYDFLRSQGFFDEGSELTLKHFFFTQKGDAAIKDFDYYRYNRPTMLDIGQARVAYQVAARYFDCYEGGCITSREVVVTNLNKSAGWPLNKFGKAGLYYESISYEEQDAIFSLTKRNILPTMTQLNLKYAISGKERARTVGGVSLLATMTTRQFHQKCLKSIVATRNATVVIGTTKFYGGWDNMLKNLMADVDDPKLMGWDYPKCDRAMPSMIRMLSAMILGSKHVTCCTASDKFYRLSNELAQVLTEVVYSNGGFYFKPGGTTSGDATTAYANSVFNIFQAVSSNINCVLSVNSSNCNNFNVKKLQRQLYDNCYRNSNVDESFVDDFYGYLQKHFSMMILSDDSVVCYNKTYAGLGYIADISAFKATLYYQNGVFMSTAKCWTEEDLSIGPHEFCSQHTMQIVDENGKYYLPYPDPSRIISAGVFVDDITKTDAVILLERYVSLAIDAYPLSKHPKPEYRKVFYALLDWVKHLNKTLNEGVLESFSVTLLDEHESKFWDESFYASMYEKSTVLQAAGLCVVCGSQTVLRCGDCLRRPMLCTKCAYDHVFGTDHKFILAITPYVCNTSGCNVNDVTKLYLGGLNYYCVDHKPHLSFPLCSAGNVFGLYKSSALGSMDIDVFNKLSTSDWSDIRDYKLANDAKESLRLFAAETVKAKEESVKSSYAYATLKEIVGPKELLLLWESGKAKPPLNRNSVFTCFQITKDSKFQVGEFVFEKVDYGSDTVTYKSTATTKLVPGMLFILTSHNVAPLRAPTMANQEKYSTIYKLHPSFNVSDAYANLVPYYQLIGKQRITTIQGPPGSGKSHCSIGIGVYYPGARIVFTACSHAAVDSLCAKAVTAYSVDKCTRIIPARARVECYSGFKPNNNSAQYVFSTVNALPEVNADIVVVDEVSMCTNYDLSVINQRISYKHIVYVGDPQQLPAPRVLISKGVMEPIDYNVVTQRMCAIGPDVFLHKCYRCPAEIVNTVSELVYENKFVPVKEASKQCFKIFERGSVQVDNGSSINRRQLDVVKRFIHKNSTWSKAVFISPYNSQNYVAARLLGLQTQTVDSAQGSEYDYVIFAQTSDTAHACNANRFNVAITRAKKGIFCIMSDRTLFDALKFFEITMTDLQSESSCGLFKDCARNPIDLPPSHATTYLSLSDRFKTSGDLAVQIGNNNVCTYEHVISYMGFRFDVSMPGSHSLFCTRDFAMRHVRGWLGMDVEGAHVTGDNVGTNVPLQVGFSNGVDFVAQPEGCVLTNTGSVVKPVRARAPPGEQFTHIVPLLRKGQPWSVLRKRIVQMIADFLAGSSDVLVFVLWAGGLELTTMRYFVKIGAVKHCQCGTVATCYNSVSNDYCCFKHALGCDYVYNPYVIDIQQWGYVGSLSTNHHAICNVHRNEHVASGDAIMTRCLAVYDCFVKNVDWSITYPMIANENAINKGGRTVQSHIMRAAIKLYNPKAIHDIGNPKGIRCAVTDAKWYCYDKNPINSNVKTLEYDYMTHGQMDGLCLFWNCNVDMYPEFSIVCRFDTRTRSTLNLEGVNGGSLYVNNHAFHTPAYDKRAMAKLKPAPFFYYDDGSCEVVHDQVNYVPLRATNCITKCNIGGAVCSKHANLYRAYVESYNIFTQAGFNIWVPTTFDCYNLWQTFTEVNLQGLENIAFNVVNKGSFVGADGELPVAISGDKVFVRDGNTDNLVFVNKTSLPTNIAFELFAKRKVGLTPPLSILKNLGVVATYKFVLWDYEAERPLTSFTKSVCGYTDFAEDVCTCYDNSIQGSYERFTLSTNAVLFSATAVKTGGKSLPAIKLNFGMLNGNAIATVKSEDGNIKNINWFVYVRKDGKPVDHYDGFYTQGRNLQDFLPRSTMEEDFLNMDIGVFIQKYGLEDFNFEHVVYGDVSKTTLGGLHLLISQVRLSKMGILKAEEFVAASDITLKCCTVTYLNDPSSKTVCTYMDLLLDDFVSVLKSLDLTVVSKVHEVIIDNKPWRWMLWCKDNAVATFYPQLQSAEWKCGYSMPGIYKTQRMCLEPCNLYNYGAGLKLPSGIMFNVVKYTQLCQYFNSTTLCVPHNMRVLHLGAGSDYGVAPGTAVLKRWLPHDAIVVDNDVVDYVSDADFSVTGDCATVYLEDKFDLLISDMYDGRTKAIDGENVSKEGFFTYINGFICEKLAIGGSIAIKVTEYSWNKKLYELVQRFSFWTMFCTSVNTSSSEAFVVGINYLGDFAQGPFIDGNIIHANYVFWRNSTVMSLSYNSVLDLSKFNCKHKATVVVQLKDSDINEMVLSLVRSGKLLVRGNGKCLSFSNHLVSTK |
| Enzyme Length | 6758 |
| Uniprot Accession Number | P0C6X1 |
| Absorption | |
| Active Site | ACT_SITE 1054; /note=For PL1-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00444; ACT_SITE 1205; /note=For PL1-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00444; ACT_SITE 1701; /note=For PL2-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00444; ACT_SITE 1863; /note=For PL2-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00444; ACT_SITE 3006; /note=For 3CL-PRO activity; ACT_SITE 3109; /note=For 3CL-PRO activity; ACT_SITE 4822; /evidence=ECO:0000255|PROSITE-ProRule:PRU01293; ACT_SITE 4823; /evidence=ECO:0000255|PROSITE-ProRule:PRU01293; ACT_SITE 4824; /evidence=ECO:0000255|PROSITE-ProRule:PRU01293; ACT_SITE 5682; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 5684; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 5783; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 5859; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 5864; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 6345; /evidence=ECO:0000255|PROSITE-ProRule:PRU01303; ACT_SITE 6360; /evidence=ECO:0000255|PROSITE-ProRule:PRU01303; ACT_SITE 6401; /evidence=ECO:0000255|PROSITE-ProRule:PRU01303; ACT_SITE 6503; /evidence=ECO:0000255|PROSITE-ProRule:PRU01300; ACT_SITE 6587; /evidence=ECO:0000255|PROSITE-ProRule:PRU01300; ACT_SITE 6627; /evidence=ECO:0000255|PROSITE-ProRule:PRU01300; ACT_SITE 6660; /evidence=ECO:0000255|PROSITE-ProRule:PRU01300 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: [Non-structural protein 3]: Reaction=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; CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: [Helicase]: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; CATALYTIC ACTIVITY: [Helicase]: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; CATALYTIC ACTIVITY: [Putative 2'-O-methyl transferase]: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167, Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609; EC=2.1.1.57; Evidence={ECO:0000250|UniProtKB:P0C6X7}; CATALYTIC ACTIVITY: [Uridylate-specific endoribonuclease]: Reaction=uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-RNA; Xref=Rhea:RHEA:67732, Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:17334, Rhea:RHEA-COMP:17335, ChEBI:CHEBI:138284, ChEBI:CHEBI:173079, ChEBI:CHEBI:173080; Evidence={ECO:0000250|UniProtKB:P0C6X7}; |
| DNA Binding | |
| EC Number | 3.4.19.12; 3.4.22.-; 3.4.22.-; 2.7.7.48; 3.6.4.12; 3.6.4.13; 3.1.13.-; 4.6.1.-; 2.1.1.57 |
| Enzyme 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.; FUNCTION: 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 (By similarity). {ECO:0000250}.; FUNCTION: [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}.; FUNCTION: The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Its ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G).; FUNCTION: The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction. {ECO:0000250}.; FUNCTION: Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}.; FUNCTION: Nsp9 is a ssRNA-binding protein. {ECO:0000250}.; FUNCTION: [Uridylate-specific endoribonuclease]: 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). {ECO:0000250|UniProtKB:P0C6X7}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 5278..5285; /note=ATP; /evidence=ECO:0000305 |
| Features | Active site (21); Beta strand (37); Chain (15); Domain (24); Helix (19); Metal binding (32); Mutagenesis (31); Nucleotide binding (1); Region (5); Sequence conflict (4); Site (14); Transmembrane (17); Turn (6); Zinc finger (4) |
| Keywords | 3D-structure;ATP-binding;Activation of host autophagy by virus;Endonuclease;Exonuclease;Helicase;Host cytoplasm;Host membrane;Host-virus interaction;Hydrolase;Inhibition of host IRF3 by virus;Inhibition of host RLR pathway by virus;Inhibition of host innate immune response by virus;Lyase;Membrane;Metal-binding;Methyltransferase;Modulation of host ubiquitin pathway by viral deubiquitinase;Modulation of host ubiquitin pathway by virus;Nuclease;Nucleotide-binding;Nucleotidyltransferase;Protease;RNA-binding;RNA-directed RNA polymerase;Reference proteome;Repeat;Ribosomal frameshifting;Thiol protease;Transferase;Transmembrane;Transmembrane helix;Ubl conjugation pathway;Viral RNA replication;Viral immunoevasion;Zinc;Zinc-finger |
| Interact With | P0C6X1; Itself |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}.; SUBCELLULAR LOCATION: [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed. {ECO:0000269|PubMed:11431476, ECO:0000269|PubMed:11842254, ECO:0000269|PubMed:9847320}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 1P9S; 2J97; 2J98; 3EJG; 4RS4; 4S1T; |
| Mapped Pubmed ID | 18694760; 19177346; |
| Motif | |
| Gene Encoded By | |
| Mass | 754,163 |
| Kinetics | |
| Metal Binding | METAL 4007; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4010; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4016; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4023; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4049; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4052; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4060; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4062; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 5000; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5003; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5011; /note=Zinc 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5014; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5021; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5024; /note=Zinc 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5028; /note=Zinc 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5034; /note=Zinc 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5045; /note=Zinc 5; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5050; /note=Zinc 5; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5067; /note=Zinc 5; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5070; /note=Zinc 5; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5799; /note=Zinc 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5801; /note=Zinc 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5817; /note=Zinc 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5820; /note=Zinc 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5848; /note=Zinc 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5852; /note=Zinc 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5855; /note=Zinc 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5870; /note=Zinc 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 6037; /note=Zinc 8; /evidence=ECO:0000255|PROSITE-ProRule:PRU01299; METAL 6054; /note=Zinc 8; /evidence=ECO:0000255|PROSITE-ProRule:PRU01299; METAL 6065; /note=Zinc 8; /evidence=ECO:0000255|PROSITE-ProRule:PRU01299; METAL 6068; /note=Zinc 8; /evidence=ECO:0000255|PROSITE-ProRule:PRU01299 |
| Rhea ID | RHEA:21248; RHEA:13065; RHEA:67020; RHEA:67732 |
| Cross Reference Brenda | 3.4.22.B14;3.6.4.12;3.6.4.13; |