| IED ID | IndEnz0002013793 |
| Enzyme Type ID | protease013793 |
| 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 p14 ; 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 ; Putative 2'-O-methyl transferase EC 2.1.1.57 nsp16 |
| Gene Name | rep 1a-1b |
| Organism | Bat coronavirus 512/2005 (BtCoV) (BtCoV/512/2005) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Nidovirales Cornidovirineae Coronaviridae Orthocoronavirinae Alphacoronavirus Pedacovirus Bat coronavirus 512/2005 (BtCoV) (BtCoV/512/2005) |
| Enzyme Sequence | MASNHISLAFANDEEISAIGFGSVEEAVSYYSDAAVNGFDQCRFVSLGLQDAVVGVEDDDVVMLITGVTQLRAYLGTFGDRPLNLRGWLLFSNCNYFLEELDLVFGRCGGTTIPVDQFMCGADGAPVIQEGDWTFMDYFQDSNQFTLNGITYVKAWDVDRKPNDYAKQNVTCIRRITYITDHRHVLADGTTMKTARHPKVNKSVVLDSPFDQIYKEVGSPFMGNGSTFVEMLKDPAFFHALITCECGRSEWTVGDWKGYNSLCCNIKCKPITIVTPKAVPGAVVITKAGIGAGLKCYNNVFLKHIIDLVVPGTNLGWGVWRIAKVQSKDDVATSGNVLVDDPEDRLDPCYFGNDGPFATKFKFQLLANSFDDEVKGAIVQGVVHVNTAICDVVKDILGLPWFVKKLGSLVTVMWDQFVAGVQSMKICTLKVVQLAKALSCATMSVVKGVITLVAEVPEIFKRLFYTLTSALKSLCTSSCDALVVAGKSFAKIGDYVLLPSALVRLVSSKVKGKAQSGIKQLQFATVVLGDTHKVESDRVEFSSVNLKMVDEEFPLNPVGHTVAVGNQAFFCSDGLYRFMADRDLVITSPIFKPELELEPIFECDAIPGFPKVAASNVAELCVKVDTLLFNYDKIYKKYSTIIKGDRCYIQCTHTFKAPSYYFDDDEFVELCTKYYKLPDFDAFYNAVHAATDMDQFCALCTSGFEVFIPRVPDCPPILNDIDGGSIWTSFILSVRSATDFIKTLKIDLGLNGVVVFVTKKFRKAGALLQKLYNAFLDTVTSFIKVAGVAFKYCATCVPKIVINGCYHTVTRLFAKDLQIPTEDGVADFNTFNHCVFPVNPTRIETDSLELEEVDFVEPGVDGKLVILDDYSFYSDGTNYYPSDGKGVVASCFKKKGGGVVTISDEVQVRTIDPVYKVRLEYEFEDETLVKVCEKAIGTKLKVTGDWSNLLETLEKAMDVVRQHLDVPDYFVYDEEGGTDLNLTIMVSQWPLSSDSEDDFKAVDDEPNANTDETVDTFAEDVAETQNVQQDVTQDEVEAVCDLVVKATEEGPIEHEELSEDQKEVQQALAFIEDKPVVVKPDVFAFSYASYGGLKVLNQSSNNCWVSSALVQLQLTGLLDSDEMQLFNAGRVSPMVKRCYESQRAIFGSLGDVSACLESLLKDRDGMSITCTIDCGCGPGVRVYENAIFRFTPLKTAFPMGRCLICSKTLMHTITQMKGTGIFCRDATALDVDTLVVKPLCAAVYVGAQDGGHYLTNMYDANMAVDGHGRHPIKFNTINTLCYKDVDWEVSNGSCDVKPFLTYKNIEFYQGELSALLSVNHDFVVNAANEQLSHGGGIAKALDDLTKGELQVLSNQYVSRNGSIKVGSGVLIKCKEHSILNVVGPRKGKHAAELLTKAYTFVFKQKGVPLMPLLSVGIFKVPITESLAAFLACVGDRVCKCFCYTDKERLAIQNFVTSFQTEQPVEPLPVIQEVKGVQLEKPVPDVKVENPCEPFRIEGDAKFYDLTPSMVQSLQVTRLVSFTNSDLCLGSFVRDCDGYVQGSLGGAIANYKKSNPVLPAGNCVTLKCDGFISFTFVILPKEGDTNYEKNFNRAIAKFLKLKGSLLVVVEDSSVFNKISHASVAGYVAKPALVDTLFEAKPVQVVVTQDQRSFHTVELSTSQTYGQQLGDCVVEDKKVTNLKPVSKDKVVSVVPNVDWDKHYGFVDAGIFHTLDHTMFVFDNNVVNGKRVLRTSDNNCWINAVCLQLQFANAKFKPKGLQQLWESYCTGDVAMFVHWLYWITGVEKGEPSDAENTLNIISRFLKPQGSVEMLRATSTTCDGTCSTKRVVSTPVVNASVLKVGLDDGNCVHGLPLVDRVVSVNGTVIITNVGDTPGKPVVATENLLLDGVSYTVFQDSTTGVGHYTVFDKEAKLMFDGDVLKPCDLNVSPVTSVVVCNNKKIVVQDPVKRVELDASKFLDTMNVASEKFFTFGDFVSRNIIVLIVYLFSLLAICFRALKKRDMKVMAGVPERTGIILKRSVKYNYKALKFFFRLKFQYIKVFLKFSLVLYTLYALMFMFIRFTPVGTPICKRYTDGYANSTFDKNDYCGNVLCKICLYGYEELSDFTHTRVIWQHLKDPLIGNILPLFYLVFLIIFGGFFVRIGITYFIMQYINAAGVALGYQDNVWLLHLLPFNSMGNIIVVAFIVTRILLFLKHVLFGCDKPSCIACSKSAKLTRVPLQTILQGVTKSFYVNANGGKKFCKKHNFFCVDCDSYGYGCTFINDVIAPELSNVTKLNVIPTGPATIIIDKVEFSNGFYYLYSGSTFWKYNFDITEAKYACKDVLKNCNILTDFVVFNNSGSNVTQVKNACVYFSQLLCKPIKLVDSALLASLNVDFSANLHKAFVEVLSNSFGKDLSNCSNMNECRESLGLSDVPEEEFSAAVSEAHRYDVLISDVSFNNLIVSYAKPEEKLAVHDIANCMRVGAKVVNHNVLTKDNVPVVWLAKDFIALSEEARKYIVRTTKTKGINFMLTFNDRRMHLTIPTISVANKKGAGLPSLFTRLYSFFWHLCVLIVVLFVATSLLDFSAQVTSDTQYDFKYIENGVLKVFEKPLDCVHNAFVNFNEWHNAKFGSIPTNSRRCPIVVGTSDEVRYIPGVPAGVFLYGKSLIFAMSTIFGTSGLCFDDRGLTDPDSCIFNSACTTLSGIGGRNVYCYREGVVDNAKLYSSLLPHSYYRLMDGNHIVLPEIITRGFGIRTIKTQAMTYCRTGECIDSQAGVCVGLDRFFVYSKTPGSDYVCGTGFFSLLFNVIGMFSNSIPVTVMSGQILLNCVVAFTAVMACFAFTKFKRLFGDMSFGVLSVGLCTVVNNLSYVVTQNSIGMLAYATLYFLCTKGVRYSWVWHVGFAISYCFLAPWWVVLAYLICALLEFLPNLFKLKVSTQLFEGDKFVGSFESAASGTFVLDMHSYQKLANSISTEKLKQYCASYNRYKYYSGSASEADYRLACFAHLAKAMSDFANDHMDKLYTPPTVSYNSTLQAGLRKMAQPSGIVEGCIVRVSYGNLTLNGLWLGDTVICPRHVIASNTTNVIDYDHAMSLVRLHNFSISSGNMFLGVISASMRGTLLHIKVNQSNVNTPNYTYKVLKPGDSFNILACYDGSAAGVYGVNMRTNYTIRGSFISGACGSPGYNINNGVVEFCYMHHLELGSGCHVGSDMDGTMYGKYEDQPTLQIEGASNLVTENVCSWLYGALINGDRWWLSSVSVGVDTYNEWALRNGMTALKNVDCFSLLVAKTGVDVGRLLASIQKLHGNFGGKSILGCTSLCDEFTLSEVVKQMYGVTLQSGKVSRAFRNASIVCCLLFLFLSEMLNHSKLFWINPGYITPVFLAIIVASSALMLLVKHKLLFLQLYLLPSLCIVSGYNIFKDYHFYTYMLEEFDYKVPFGGFNVTGVLNISLCCFVMGLHTFRFLQTPNKIFSYVVAVLTVLYTYYYSTDVLGLILTSMSGFTNYWFIGTATYKLATYVLPHTSLLDSFDAIKAVVFLYLLLGYCNCVYYGSLYWINRFCKLTLGCYEFKVSAAEFKYMVANGLRAPTGVFDALILSLKLIGVGGRKTIKISSVQSKLTDLKCTNVVLLGCLSNMNIAANSREWAYCVDLHNKINLCNDAEAAQEMLLALLAFFLSKNSAFGVDELLDSYFNDSSVLQSVAATYVNLPSYLAYETARQSYEDALANGSPPQLVKQLRHAMNVAKSEFDREASTQRKLDRMAEQAASQMYKEARAVNRKSKVVSAMHSLLFGMLRRLDMSSVDTILSLAKDGVVPLSIIPAVSATKLNIVVSDIESYSKIQREGCVHYAGVIWSVVDIKDNDGKPVHAKEVVTSNVESLAWPLFLNCERIIKLQNNEIIPSKIKQRPIKAEGEGVVADGNALYSNEGGRTFMYAFISDKPDLKVVKWEFDGGSNAIELEPPCKFLVEAPSGPVVKYLYFVRNLNNLRRGAVLGFIGATVRLQAGKQTEQATNSSLLTLCAFAVDPPKTYLDAVKSGHRPVGNCVKMLANGSGNGQAITNGVEASTNQDSYGGASVCLYCRAHVEHPDMDGFCKLRGKYVQVPLGTLDPIRFVLENTVCKVCGCWQANGCTCDRAVIQSVDSGYLNRVRGSSAARLEPLNGSDTHHVFRAFDVYNRDVACISKFLKVNCVRLKNLDKHDAFWIVKKCTKSVMEHEQSIYNLISDCGAVAKHDFFTWKEGRSVYGNVCRQDLTEYTMMDLCYALRNFDENNCETLKKILVVVGACDESYFDNKLWFDPVENEDVHRVYAKLGTIVARAMLKCVKYCDAMVEQGIVGVITLDNQDLNGDFYDFGDFVTSVKGMGVPICTSYYSYMMPVMGMTNCLASECFIKSDIFGEDFRTFDLLAYDFTEHKVNLFNKYFKHWGQTYHPNCEDCHDESCIVHCANFNTLFATTIPITAFGPLCRKCWIDGVPLVTTAGYHFKQLGIVWNKDLNLHSSRLTINELLQFCADPSLLIASSPALVDKRTVCFSVAALGTGMTNQTVKPGHFNREFYDFLRSQGFFEEGSELTLKHFFFAQKGDAAVRDFDYYRYNRTTVLDICQARVVYQIVQCYFGMYEGGCITAKEVIVNNLNKSAGYPFNKFGKAGLYYDSLSYEEQDDLYAYTKRNIIPTMTQLNLKYAISGKDRARTVGGVSLLSTMTTRQYHQKHLKSIVNTRGASVVIGTTKFYGGWDNMLKTLIKDVENPHLMGWDYPKCDRALPNMIRMISAMILGSKHVNCCSSSDRYYRLCNELAQVLTEMVYSNGGFYVKPGGTTSGDATTAYANSVFNIFQATSANVNRLLSVDSNTCNNIEVKQLQRKLYDCCYRSSSVDQSFVEEYFGYLRKHFSMMILSDDGVVCYNSEYAALGYVADLNAFKAVLYYQNNVFMSASKCWIEPDINKGPHEFCSQHTMQIVDKDGTYYLPYPDPSRILSAGVFVDDIVKTDPVILLERYVSLAIDAYPLSKHDNPEYRRVFTVMLDWVKHLYKTLNQGVLDSFSVTLLEDATAKFWDESFYASMYEQSSVLQSAGLCVVCSSQTVLRCGDCIRRPMLCTKCAYDHVVSTSHKFILAITPYVCCSSGCGVSDVTKLYLGGLSYWCVDHKPRLSFPLCSSGNVFGLYKNSATGSPDVDDFNTLATSDWTDVKDYKLANDVKDSLRLFAAETIKAKEESVKSSYACATIHEVVGPKELVLKWEVGKPRPPLSRNSVFTCYHITKNTKFQVGEFTFEKLDYDNDAVSYKSTATTKLVPGMVFVLTSHNVQPLRAPTIINQERYSTLHKLRPAFNIHEDYSNLIPYYQLIGKQKLTTIQGPPGSGKSHCVIGLGLYFPGARIVFTACSHAAVDSLCVKAATAYSSDRCSRIIPQKARIECYDGFKSNNTSAQYLFSTVNALPEVNADICVVDEVSMCTNYDLSVINQRVNYRHIVYVGDPQQLPAPRVMITRGVLVPEDYNVVTRRMCVLKPDIFLHKCYRCPAEIVNTVSEMVYENQFVPVKSESKECFKIYCRGNVQVDNGSSINRRQLEVVRMFLAKNPKWAKAVFISPYNSQNYVAGRVLGLQIQTVDSSQGSEYDYVIYTQTSDTAHASNVNRFNVAITRAKKGILCIMCDRELFDILKFYELKLSDLQVGDGCGLFKDCYKGEDNLPPSHAPTFMSLSDNFKTDKDLAVQIGVNGPVKYEHVISFMGFRFDINVPNQHTLFCTRDFAMRNARGWLGFDVEGAHVIGSNVGTNVPLQLGFSNGVDFVVRPEGCVSTEVGDVIQPVRARAPPGDQFTHLLPLLRKGQPWSVIRRRIVQMCSDYLANLSDTLIFVLWSGGLELTTMRYFVKLGPVQTCDCGKRATCYNSTNHTFSCFRHALGSDYIYNCYCIDIQQWGYTGSLSMNHHEVCNIHRNEHVASGDAAMTRCLAIHDCFVKNVDWSITYPFIANEQAINKSGRLVQSHVMRAVLKLYNPKAIHDVGNPKGIRCVVTDASWYCYDKNPTNTNVKMLEYDYITHGQLDGLCLFWNCNVDMYPEFSVVCRFDTRMRSTLNLEGCNGGSLYVNNHAFHTPAYDKRAFAKLKAMPFFFYDDSECEKLQDAVNYVPLRASNCITRCNVGGAVCSKHCALYHNYVMAYNTFTTAGFTIWVPNSFDMFNLWQTFKNSNVQGLENIAYNVVKKGSFVGVEGELPVAVVNDKVMVRDGVSDNVVFVNNTSLPTNVAFELYAKRKVGLTPPLTILKNLGVVCTSKCVLWDYEASRPLTTFTKDVCKYTDFDGDVCTLFDNSVPGAFERFTVTKNAVLISLTAVKKLTAIKLTYGYLNGVPVFTHEDKPFTWYIYTRKDGAFVEYPDGYFTQGRVISDFQPRSNMEEDFLNMDMGLFISKYGLEDYGFEHVVFGDVSKTTLGGLHLLISQIRLSKIGVLKVEDFVSSSDSTLKSCTVTYVDNPSSKMVCTYVDLLLDDFVNILKSVDLSVVSKVHEVVIDCKVWRWMLWCKDHKVQTFYPQLQSAEWKCGYSMPSIYKIQRMCLEPCNLYNYGSGLKLPDGIMFNVVKYTQLCQYLNSTTMCVPHHMRVLHLGAGSDKGVAPGTAVLRRWLPLDAVIVDNDVNDYVSDADFSYTGDCASMYLTDKFDLVISDMYDGRTKSCDGDNVSKEGFFPYINGVITEKLALGGTVAIKITEFSWNKKLYELIQKFEYWTLFCTSVNTSSSEAFLIGVHFLGDFSTNAIIDGNIMHANYIFWRNSTIMTMSYNSVLDLSKFSCKHKATVVVNLKDSSVTDLVLGLLKNGKLLIRNNGVVCGFSNHLVNSTK |
| Enzyme Length | 6793 |
| Uniprot Accession Number | P0C6W0 |
| Absorption | |
| Active Site | ACT_SITE 1103; /note=For PL1-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00444; ACT_SITE 1252; /note=For PL1-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00444; ACT_SITE 1737; /note=For PL2-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00444; ACT_SITE 1902; /note=For PL2-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00444; ACT_SITE 3053; /note=For 3CL-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00772; ACT_SITE 3156; /note=For 3CL-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00772; ACT_SITE 4865; /evidence=ECO:0000255|PROSITE-ProRule:PRU01293; ACT_SITE 4866; /evidence=ECO:0000255|PROSITE-ProRule:PRU01293; ACT_SITE 4867; /evidence=ECO:0000255|PROSITE-ProRule:PRU01293; ACT_SITE 5725; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 5727; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 5826; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 5902; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 5907; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 6379; /evidence=ECO:0000255|PROSITE-ProRule:PRU01303; ACT_SITE 6394; /evidence=ECO:0000255|PROSITE-ProRule:PRU01303; ACT_SITE 6435; /evidence=ECO:0000255|PROSITE-ProRule:PRU01303; ACT_SITE 6537; /evidence=ECO:0000255|PROSITE-ProRule:PRU01300; ACT_SITE 6621; /evidence=ECO:0000255|PROSITE-ProRule:PRU01300; ACT_SITE 6661; /evidence=ECO:0000255|PROSITE-ProRule:PRU01300; ACT_SITE 6694; /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. ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G) (By similarity). {ECO:0000250}.; 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 5321..5328; /note=ATP; /evidence=ECO:0000250 |
| Features | Active site (21); Chain (15); Domain (24); Metal binding (32); Nucleotide binding (1); Region (5); Site (14); Transmembrane (19); Zinc finger (3) |
| Keywords | 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 | |
| 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 (By similarity). {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 757,262 |
| Kinetics | |
| Metal Binding | METAL 4050; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4053; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4059; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4066; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4092; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4095; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4103; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4105; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 5043; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5046; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5054; /note=Zinc 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5057; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5064; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5067; /note=Zinc 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5071; /note=Zinc 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5077; /note=Zinc 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5088; /note=Zinc 5; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5093; /note=Zinc 5; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5110; /note=Zinc 5; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5113; /note=Zinc 5; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5842; /note=Zinc 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5844; /note=Zinc 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5860; /note=Zinc 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5863; /note=Zinc 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5891; /note=Zinc 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5895; /note=Zinc 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5898; /note=Zinc 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5913; /note=Zinc 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 6080; /note=Zinc 8; /evidence=ECO:0000255|PROSITE-ProRule:PRU01299; METAL 6097; /note=Zinc 8; /evidence=ECO:0000255|PROSITE-ProRule:PRU01299; METAL 6108; /note=Zinc 8; /evidence=ECO:0000255|PROSITE-ProRule:PRU01299; METAL 6111; /note=Zinc 8; /evidence=ECO:0000255|PROSITE-ProRule:PRU01299 |
| Rhea ID | RHEA:21248; RHEA:13065; RHEA:67020; RHEA:67732 |
| Cross Reference Brenda |