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Database: UniProt
Entry: C3VPE7_CVMA5
LinkDB: C3VPE7_CVMA5
Original site: C3VPE7_CVMA5 
ID   C3VPE7_CVMA5            Unreviewed;      2733 AA.
AC   C3VPE7;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=ORF1ab polyprotein {ECO:0000256|PROSITE-ProRule:PRU01344};
DE   Flags: Fragment;
OS   Murine coronavirus (strain A59) (MHV-A59) (Murine hepatitis virus).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Betacoronavirus; Embecovirus; Murine coronavirus.
OX   NCBI_TaxID=11142 {ECO:0000313|EMBL:ACO72882.1, ECO:0000313|Proteomes:UP000180349};
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1] {ECO:0000313|EMBL:ACO72882.1, ECO:0000313|Proteomes:UP000180349}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A59 {ECO:0000313|EMBL:ACO72882.1};
RX   PubMed=8392595;
RA   Gombold J.L., Hingley S.T., Weiss S.R.;
RT   "Fusion-defective mutants of mouse hepatitis virus A59 contain a mutation
RT   in the spike protein cleavage signal.";
RL   J. Virol. 67:4504-4512(1993).
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; FJ884686; ACO72882.1; -; Genomic_RNA.
DR   Proteomes; UP000180349; 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   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   CDD; cd21409; 1B_cv_Nsp13-like; 1.
DR   CDD; cd21722; betaCoV_Nsp13-helicase; 1.
DR   CDD; cd21659; betaCoV_Nsp14; 1.
DR   CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
DR   CDD; cd21593; HCoV_HKU1-like_RdRp; 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; IPR048673; NSP13_stalk_CoV.
DR   InterPro; IPR048672; NSP13_ZBD_CoV.
DR   InterPro; IPR027352; NSP13_ZBD_CoV-like.
DR   InterPro; IPR044315; NSP14_betaCoV.
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; IPR046441; RdRp_CoV.
DR   InterPro; IPR044347; RdRp_HCoV_HKU1-like.
DR   InterPro; IPR009469; RdRp_N_CoV.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
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; PF13604; AAA_30; 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.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 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   Protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758};
KW   RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01299}; Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
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          17..272
FT                   /note="NiRAN"
FT                   /evidence="ECO:0000259|PROSITE:PS51947"
FT   DOMAIN          273..371
FT                   /note="Nsp12 Interface"
FT                   /evidence="ECO:0000259|PROSITE:PS52000"
FT   DOMAIN          372..939
FT                   /note="Nsp12 RNA-dependent RNA polymerase"
FT                   /evidence="ECO:0000259|PROSITE:PS51948"
FT   DOMAIN          619..781
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   DOMAIN          940..1023
FT                   /note="CV ZBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51653"
FT   DOMAIN          1195..1546
FT                   /note="(+)RNA virus helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51657"
FT   DOMAIN          1610..1825
FT                   /note="ExoN"
FT                   /evidence="ECO:0000259|PROSITE:PS51953"
FT   DOMAIN          1834..2060
FT                   /note="N7-MTase"
FT                   /evidence="ECO:0000259|PROSITE:PS51954"
FT   DOMAIN          2061..2121
FT                   /note="Nsp15 N-terminal oligomerization"
FT                   /evidence="ECO:0000259|PROSITE:PS51960"
FT   DOMAIN          2122..2242
FT                   /note="AV-Nsp11N/CoV-Nsp15M"
FT                   /evidence="ECO:0000259|PROSITE:PS51961"
FT   DOMAIN          2292..2431
FT                   /note="NendoU"
FT                   /evidence="ECO:0000259|PROSITE:PS51958"
FT   DOMAIN          2436..2730
FT                   /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT                   /evidence="ECO:0000259|PROSITE:PS51955"
FT   REGION          1947..1961
FT                   /note="GpppA-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01299"
FT   ACT_SITE        1628
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        1630
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        1729
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        1806
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        1811
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT   ACT_SITE        2322
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        2337
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT   ACT_SITE        2377
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT   BINDING         1869..1875
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:ACO72882.1"
SQ   SEQUENCE   2733 AA;  309167 MW;  55B4CCB931745D46 CRC64;
     LFLCRHRLPV SVKRHELFKR VRGTSVNARL VPCASGLDTD VQLRAFDICN ANRAGIGLYY
     KVNCCRFQRV DEDGNKLDKF FVVKRTNLEV YNKEKECYEL TKECGVVAEH EFFTFDVEGS
     RVPHIVRKDL SKFTMLDLCY ALRHFDRNDC STLKEILLTY AECEESYFQK KDWYDFVENP
     DIINVYKKLG PIFNRALLNT AKFADALVEA GLVGVLTLDN QDLYGQWYDF GDFVKTVPGC
     GVAVADSYYS YMMPMLTMCH ALDSELFVNG TYREFDLVQY DFTDFKLELF TKYFKHWSMT
     YHPNTCECED DRCIIHCANF NILFSMVLPK TCFGPLVRQI FVDGVPFVVS IGYHYKELGV
     VMNMDVDTHR YRLSLKDLLL YAADPALHVA SASALLDLRT CCFSVAAITS GVKFQTVKPG
     NFNQDFYEFI LSKGLLKEGS SVDLKHFFFT QDGNAAITDY NYYKYNLPTM VDIKQLLFVL
     EVVNKYFEIY EGGCTPATQV IVNNYDKSAG YPFNKFGKAR LYYEALSFEE QDEIYAYTKR
     NVLPTLTQMN LKYAISAKNR ARTVAGVSIL STMTGRMFHQ KCLKSIAATR GVPVVIGTTK
     FYGGWDDMLR RLIKDVDSPV LMGWDYPKCD RAMPNILRIV SSLVLARKHD SCCSHTDRFY
     RLANECAQVL SEIVMCGGCY YVKPGGTSSG DATTAFANSV FNICQAVSAN VCSLMACNGH
     KIEDLSIREL QKRLYSNVYR ADHVDPAFVS EYYEFLNKHF SMMILSDDGV VCYNSEFASK
     GYIANISAFQ QVLYYQNNVF MSEAKCWVET DIEKGPHEFC SQHTMLVKMD GDEVYLPYPD
     PSRILGAGCF VDDLLKTDSV LLIERFVSLA IDAYPLVYHE NPEYQNVFRV YLEYIKKLYN
     DLGNQILDSY SVILSTCDGQ KFTDETFYKN MYLRSAVLQS VGACVVCSSQ TSLRCGSCIR
     KPLLCCKCAY DHVMSTDHKY VLSVSPYVCN SPGCDVNDVT KLYLGGMSYY CEDHKPQYSF
     KLVMNGMVFG LYKQSCTGSP YIEDFNKIAS CKWTEVDDYV LANECTERLK LFAAETQKAT
     EEAFKQCYAS ATIREIVSDR ELILSWEIGK VRPPLNKNYV FTGYHFTNNG KTVLGEYVFD
     KSELTNGVYY RATTTYKLSV GDVFILTSHA VSSLSAPTLV PQENYTSIRF ASVYSVPETF
     QNNVPNYQHI GMKRYCTVQG PPGTGKSHLA IGLAVYYCTA RVVYTAASHA AVDALCEKAH
     KFLNINDCTR IVPAKVRVDC YDKFKVNDTT RKYVFTTINA LPELVTDIIV VDEVSMLTNY
     ELSVINSRVR AKHYVYIGDP AQLPAPRVLL NKGTLEPRYF NSVTKLMCCL GPDIFLGTCY
     RCPKEIVDTV SALVYNNKLK AKNDNSSMCF KVYYKGQTTH ESSSAVNMQQ IHLISKFLKA
     NPSWSNAVFI SPYNSQNYVA KRVLGLQTQT VDSAQGSEYD FVIYSQTAET AHSVNVNRFN
     VAITRAKKGI LCVMSSMQLF ESLNFTTLTL DKINNPRLQC TTNLFKDCSR SYVGYHPAHA
     PSFLAVDDKY KVGGDLAVCL NVADSAVTYS RLISLMGFKL DLTLDGYCKL FITRDEAIKR
     VRAWVGFDAE GAHAIRDSIG TNFPLQLGFS TGIDFVVEAT GMFAERDGYV FKKAAARAPP
     GEQFKHLIPL MSRGQKWDVV RIRIVQMLSD HLADLADSVV LVTWAASFEL TCLRYFAKVG
     REVVCSVCTK RATCFNSRTG YYGCWRHSYS CDYLYNPLIV DIQQWGYTGS LTSNHDPICS
     VHKGAHVASS DAIMTRCLAV HDCFCKSVNW NLEYPIISNE VSVNTSCRLL QRVMFRAAML
     CNRYDVCYDI GNPKGLACVK GYDFKFYDAS PVVKSVKQFV YKYEAHKDQF LDGLCMFWNC
     NVDKYPANAV VCRFDTRVLN KLNLPGCNGG SLYVNKHAFH TSPFTRAAFE NLKPMPFFYY
     SDTPCVYMEG MESKQVDYVP LRSATCITRC NLGGAVCLKH AEEYREYLES YNTATTAGFT
     FWVYKTFDFY NLWNTFTRLQ SLENVVYNLV NAGHFDGRAG ELPCAVIGEK VIAKIQNEDV
     VVFKNNTPFP TNVAVELFAK RSIRPHPELK LFRNLNIDVC WSHVLWDYAK DSVFCSSTYK
     VCKYTDLQCI ESLNVLFDGR DNGALEAFKK CRNGVYINTT KIKSLSMIKG PQRADLNGVV
     VEKVGDSDVE FWFAVRKDGD DVIFSRTGSL EPSHYRSPQG NPGGNRVGDL SGNEALARGT
     IFTQSRLLSS FTPRSEMEKD FMDLDDDVFI AKYSLQDYAF EHVVYGSFNQ KIIGGLHLLI
     GLARRQQKSN LVIQEFVTYD SSIHSYFITD ENSGSSKSVC TVIDLLLDDF VDIVKSLNLK
     CVSKVVNVNV DFKDFQFMLW CNEEKVMTFY PRLQAAADWK PGYVMPVLYK YLESPLERVN
     LWNYGKPITL PTGCMMNVAK YTQLCQYLST TTLAVPANMR VLHLGAGSDK GVAPGSAVLR
     QWLPAGSILV DNDVNPFVSD SVASYYGNCI TLPFDCQWDL IISDMYDPLT KNIGEYNVSK
     DGFFTYLCHL IRDKLALGGS VAIKITEFSW NAELYSLMGK FAFWTIFCTN VNASSSEGFL
     IGINWLNKTR TEIDGKTMHA NYLFWRNSTM WNGGAYSLFD MSKFPLKAAG TAVVSLKPDQ
     INDLVLSLIE KGKLLVRDTR KEVFVGDSLV NVK
//
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