ID C8YR34_9ALPC Unreviewed; 2680 AA.
AC C8YR34;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=ORF1ab polyprotein {ECO:0000256|PROSITE-ProRule:PRU01344};
DE Flags: Fragment;
OS Transmissible gastroenteritis virus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Tegacovirus; Alphacoronavirus 1.
OX NCBI_TaxID=11149 {ECO:0000313|EMBL:ACN71195.1, ECO:0000313|Proteomes:UP000111647};
RN [1] {ECO:0000313|EMBL:ACN71195.1, ECO:0000313|Proteomes:UP000111647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H16 {ECO:0000313|EMBL:ACN71195.1};
RX PubMed=20229183; DOI=10.1007/s11262-010-0467-6;
RA Wang C., Chen J., Shi H., Qiu H., Xue F., Liu C., Zhu Y., Liu S.,
RA Almazan F., Enjuanes L., Feng L.;
RT "Molecular characterization of a Chinese vaccine strain of transmissible
RT gastroenteritis virus: mutations that may contribute to attenuation.";
RL Virus Genes 40:403-409(2010).
CC -!- FUNCTION: Forms a primer, NSP9-pU, which is utilized by the polymerase
CC for the initiation of RNA chains. Interacts with ribosome signal
CC recognition particle RNA (SRP). Together with NSP8, suppress protein
CC integration into the cell membrane, thereby disrupting host immune
CC defenses. {ECO:0000256|ARBA:ARBA00043928}.
CC -!- FUNCTION: RNA-directed RNA polymerase that catalyzes the transcription
CC of viral genomic and subgenomic RNAs. Acts in complex with nsp7 and
CC nsp8 to transcribe both the minus and positive strands of genomic RNA.
CC The kinase-like NiRAN domain of NSP12 attaches one or more nucleotides
CC to the amino terminus of NSP9, forming a covalent RNA-protein
CC intermediate that serves as transcription/replication primer.
CC Subgenomic RNAs (sgRNAs) are formed by discontinuous transcription: The
CC polymerase has the ability to pause at transcription-regulating
CC sequences (TRS) and jump to the leader TRS, resulting in a major
CC deletion. This creates a series of subgenomic RNAs that are replicated,
CC transcribed and translated. In addition, Nsp12 is a subunit of the
CC viral RNA capping enzyme that catalyzes the RNA guanylyltransferase
CC reaction for genomic and sub-genomic RNAs. Subsequently, the NiRAN
CC domain transfers RNA to GDP, and forms the core cap structure GpppA-
CC RNA. {ECO:0000256|ARBA:ARBA00043918}.
CC -!- FUNCTION: The replicase polyprotein of coronaviruses is a
CC multifunctional protein: it contains the activities necessary for the
CC transcription of negative stranded RNA, leader RNA, subgenomic mRNAs
CC and progeny virion RNA as well as proteinases responsible for the
CC cleavage of the polyprotein into functional products.
CC {ECO:0000256|ARBA:ARBA00003368}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SUBCELLULAR LOCATION: Host cytoplasm, host perinuclear region
CC {ECO:0000256|ARBA:ARBA00004407}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC {ECO:0000256|ARBA:ARBA00008087, ECO:0000256|PROSITE-ProRule:PRU01299}.
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DR EMBL; FJ755618; ACN71195.1; -; Genomic_RNA.
DR Proteomes; UP000111647; Genome.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd21409; 1B_cv_Nsp13-like; 1.
DR CDD; cd21723; alphaCoV_Nsp13-helicase; 1.
DR CDD; cd21660; alphaCoV_Nsp14; 1.
DR CDD; cd21588; alphaCoV_RdRp; 1.
DR CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
DR CDD; cd21167; M_alpha_beta_cv_Nsp15-like; 1.
DR CDD; cd21161; NendoU_cv_Nsp15-like; 1.
DR CDD; cd21171; NTD_alpha_betaCoV_Nsp15-like; 1.
DR CDD; cd21689; stalk_CoV_Nsp13-like; 1.
DR CDD; cd21401; ZBD_cv_Nsp13-like; 1.
DR Gene3D; 3.40.50.11580; -; 1.
DR Gene3D; 3.30.160.820; Nsp15 N-terminal domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR046440; AV_NSP11N_COV_NSP15M.
DR InterPro; IPR043608; CoV_NSP15_M.
DR InterPro; IPR043606; CoV_NSP15_N.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR037227; EndoU-like.
DR InterPro; IPR046435; N7_MTase_CoV.
DR InterPro; IPR043609; NendoU_nidovirus.
DR InterPro; IPR044863; NIRAN.
DR InterPro; IPR046438; NIV_2_O_MTASE.
DR InterPro; IPR046436; NIV_EXON.
DR InterPro; IPR047570; NSP12_IF_CoV.
DR InterPro; IPR044343; NSP13_1B_dom_CoV.
DR InterPro; IPR047912; Nsp13_helicase_alphaCoV.
DR InterPro; IPR048673; NSP13_stalk_CoV.
DR InterPro; IPR048672; NSP13_ZBD_CoV.
DR InterPro; IPR027352; NSP13_ZBD_CoV-like.
DR InterPro; IPR044313; NSP14_alphaCoV.
DR InterPro; IPR009466; NSP14_CoV.
DR InterPro; IPR044330; NSP15_alpha_betaCoV_N.
DR InterPro; IPR044322; NSP15_M_alpha_beta_CoV.
DR InterPro; IPR043174; NSP15_middle_sf.
DR InterPro; IPR042515; NSP15_N_CoV.
DR InterPro; IPR044401; NSP15_NendoU_CoV.
DR InterPro; IPR009461; NSP16_CoV-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR044356; RdRp_alphaCoV.
DR InterPro; IPR046441; RdRp_CoV.
DR InterPro; IPR009469; RdRp_N_CoV.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43788:SF8; HELICASE WITH ZINC FINGER 2; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF13245; AAA_19; 1.
DR Pfam; PF06471; CoV_ExoN; 1.
DR Pfam; PF06460; CoV_Methyltr_2; 1.
DR Pfam; PF20631; CoV_NSP13_1B; 1.
DR Pfam; PF20633; CoV_NSP13_stalk; 1.
DR Pfam; PF20632; CoV_NSP13_ZBD; 1.
DR Pfam; PF19215; CoV_NSP15_C; 1.
DR Pfam; PF19216; CoV_NSP15_M; 1.
DR Pfam; PF19219; CoV_NSP15_N; 1.
DR Pfam; PF06478; CoV_RPol_N; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF142877; EndoU-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 1.
DR PROSITE; PS51954; COV_N7_MTASE; 1.
DR PROSITE; PS52000; COV_NSP12_IF; 1.
DR PROSITE; PS51948; COV_NSP12_RDRP; 1.
DR PROSITE; PS51960; COV_NSP15_NTD; 1.
DR PROSITE; PS51653; CV_ZBD; 1.
DR PROSITE; PS51958; NENDOU; 1.
DR PROSITE; PS51947; NIRAN; 1.
DR PROSITE; PS51955; NIV_2_O_MTASE; 1.
DR PROSITE; PS51953; NIV_EXON; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|PROSITE-
KW ProRule:PRU01303}; Exonuclease {ECO:0000256|PROSITE-ProRule:PRU01298};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01303}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01299};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PROSITE-
KW ProRule:PRU01298}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01299};
KW Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00986};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00986}.
FT DOMAIN 2..251
FT /note="NiRAN"
FT /evidence="ECO:0000259|PROSITE:PS51947"
FT DOMAIN 257..355
FT /note="Nsp12 Interface"
FT /evidence="ECO:0000259|PROSITE:PS52000"
FT DOMAIN 356..923
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000259|PROSITE:PS51948"
FT DOMAIN 924..1007
FT /note="CV ZBD"
FT /evidence="ECO:0000259|PROSITE:PS51653"
FT DOMAIN 1171..1532
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51657"
FT DOMAIN 1594..1808
FT /note="ExoN"
FT /evidence="ECO:0000259|PROSITE:PS51953"
FT DOMAIN 1817..2038
FT /note="N7-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51954"
FT DOMAIN 2042..2102
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000259|PROSITE:PS51960"
FT DOMAIN 2103..2220
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000259|PROSITE:PS51961"
FT DOMAIN 2237..2377
FT /note="NendoU"
FT /evidence="ECO:0000259|PROSITE:PS51958"
FT DOMAIN 2381..2677
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51955"
FT REGION 1929..1943
FT /note="GpppA-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299"
FT ACT_SITE 1612
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 1614
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 1713
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 1789
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 1794
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 2267
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 2282
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 2323
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT BINDING 1852..1858
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACN71195.1"
SQ SEQUENCE 2680 AA; 303061 MW; B4B68B981AB0BF3D CRC64;
KLFKRVRGSS AARLEPCNGT DPDHVSRAFD IYNKDVACIG KFLKTNCSRF RNLDKHDAYY
IVKRCTKTVM DHEQVCYNDL KDSGAVAEHD FFTYKEGRCE FGNVARRNLT KYTMMDLCYA
IRNFDEKNCE VLKEILVTVG ACTEEFFENK DWFDPVENEA IHEVYAKLGP IVANAMLKCV
AFCDAIVEKG YIGVITLDNQ DLNGNFYDFG DFVKTAPGFG CACVTSYYSY MMPLMGMTSC
LESENFVKSD IYGSDYKQYD LLAYDFTEHK EHLFQKYFKY WDRTYHPNCS DCTSDECIIH
CANFNTLFSM TIPMTAFGPL VRKVHIDGVP VVVTAGYHFK QLGIVWNLDV KLDTMKLSMT
DLLRFVTDPT LLVASSPALL DQRTVCFSIA ALSTGITYQT VKPGHFNKDF YDFITERGFF
EEGSELTLKH FFFAQGGEAA MTDFNYYRYN RVTVLDICHA QFVYKIVGKY FECYDGGCIS
AREVVVTNYD KSAGYPLNKF GKARLYYETL SYEEQDALFA LTKRNVLPTM TQMNLKYAIS
GKARARTVGG VSLLSTMTTR QYHQKHLKSI AATRNATVVI GSTKFYGGWD NMLKNLMRDV
DNGCLMGWDY PKCDRALPNM IRMASAMILG SKHVGCCTHN DRFYRLSNEL AQVLTEVVHC
TGGFYFKPGG TTSGDGTTAY ANSAFNIFQA VSANVNKLLG VDSNACNNVT VKSIQRKVYD
NCYRSSSIDE EFVVEYFSYL RKHFSMMILS DDGVVCYNKD YADLGYVADI NAFKATLYYQ
NNVFMSTSKC WVEPDLSVGP HEFCSQHTLQ IVGPDGDYYL PYPDPSRILS AGVFVDDIVK
TDNVIMLERY VSLAIDAYPL TKHPKPAYQK VFYTLLDWVK HLQKNLNAGV LDSFSVTMLE
EGQDKFWSEE FYTSLYEKST VLQAAGMCVV CGSQTVLRCG DCLRRPLLCT KCAYDHVMGT
KHKFIMSITP YVCSFNGCNV NDVTKLFLGG LSYYCMNHKP QLSFPLCANG NVFGLYKSSA
VGSEAVEDFN KLAVSDWTNV EDYKLANNVK ESLKIFAAET VKAKEESVKS EYAYAVLKEV
IGPKEIVLQW EASKTKPPLN RNSVFTCFQI SKDTKIQLGE FVFEQSEYGS DSVYYKSTST
YKLTPGMIFV LTSHNVSPLK APILVNQEKY NTISKLYPVF NIAEAYNTLV PYYQMIGKQK
FTTIQGPPGS GKSHCVIGLG LYYPQARIVY TACSHAAVDA LCEKAAKNFN VDRCSRIIPQ
RIRVDCYTGF KPNNTNAQYL FCTVNALPEV SCDIVVVDEV SMCTNYDLSV INSRLSYKHI
VYVGDPQQLP APRTLINKGV LQPQDYNVVT KRMCTLGPDV FLHKCYRCPA EIVKTVSALV
YENKFVPVNP ESKQCFKMFV KGQVQIESNS SINNKQLEVV KAFLAHNPKW RKAVFISPYN
SQNYVARRLL GLQTQTVDSA QGSEYDYVIY TQTSDTQHST NVNRFNVAIT RAKVGILCIM
CDRTMYENLD FYELKDSKIG LQAKPETCGL FKDCSKSEQY IPPAYATTYM SLSDNFKTSD
GLAVNIGTKD VKYANVISYM GFRFEANIPG YHTLFCTRDF AMRNVRAWLG FDVEGAHVCG
DNVGTNVPLQ LGFSNGVDFV VQTEGCVITE KGNSIEVVKA RAPPGEQFAH LIPLMRKGQP
WHIVRRRIVQ MVCDYFDGLS DILIFVLWAG GLELTTMRYF VKIGRPQKCE CGKSATCYSS
SQSVYACFKH ALGCDYLYNP YCIDIQQWGY TGSLSMNHHE VCNIHRNEHV ASGDAIMTRC
LAIHDCFVKR VDWSIVYPFI DNEEKINKAG RIVQSHVMKA ALKIFNPAAI HDVGNPKGIR
CATTPIPWFC YDRDPINNNV RCLDYDYMVH GQMNGLMLFW NCNVDMYPEF SIVCRFDTRT
RSKLSLEGCN GGALYVNNHA FHTPAYDRRA FAKLKPTPFF YYDDSNCELV DGQPNYVPLK
SNVCITKCNI GGAVCKKHAA LYRAYVEDYN IFMQAGFTIW CPQNFDTYML WHGFVNSKAL
QSLENVAFNV VKKGAFTGLK GDLPTAVIAD KIMVRDGPTD RCIFTNKTSL PTNVAFELYA
KRKLGLTPPL TILRNLGVVA TYNFVLWDYE AERPFSNFTK QVCSYTDLDS EVVTCFDNSI
AGSFERFTTT RDAVLISNNA VKGLSAIKLQ YGLLNDLPVS TVGNKPVTWY IYVRKNGEYV
EQIDSYYTHG RTFETFKPRS TMEEDFLSMD TTLFIQKYGL EDYGFEHVVF GDVSKTTIGG
MHLLISQVRL AKMGLFSVQE FMNNSDSTLK SCCITYADDP SSKNVCTYMD ILLDDFVTII
KSLDLNVVSK VVDVIVDCKA WRWMLWCENS HIKTFYPQLQ SAEWNPGYSM PTLYKIQRMC
LERCNLYNYG AQVKLPDGIT TNVVKYTQLC QYLNTTTLCV PHKMRVLHLG AAGASGVAPG
STVLRRWLPD DAILVDNDLR DYVSDADFSV TGDCTSLYIE DKFDLLVSDL YDGSTKSIDG
ENTSKDGFFT YINGFIKEKL SLGGSVAIKI TEFSWNKDLY ELIQRFEYWT VFCTSVNTSS
SEGFLIGINY LGPYCDKAIV DGNIMHANYI FWRNSTIMAL SHNSVLDTPK FKCRCNNALI
VNLKEKELNE MVIGLLRKGK LLIRNNGKLL NFGNHFVNTP
//
