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Conserved domains on  [gi|2243697453|gb|URC19712|]
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RNA-dependent RNA polymerase, partial [Murine coronavirus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CoV_Nsp14 super family cl40464
nonstructural protein 14 of coronavirus; Nonstructural protein 14 (Nsp14) of coronavirus (CoV) ...
 1-96 4.84e-67

nonstructural protein 14 of coronavirus; Nonstructural protein 14 (Nsp14) of coronavirus (CoV) plays an important role in viral replication and transcription. It consists of 2 domains with different enzymatic activities: an N-terminal exoribonuclease (ExoN) domain and a C-terminal cap (guanine-N7) methyltransferase (N7-MTase) domain. ExoN is important for proofreading and therefore, the prevention of lethal mutations. The association of Nsp14 with Nsp10 stimulates its ExoN activity; the complex hydrolyzes double-stranded RNA in a 3' to 5' direction as well as a single mismatched nucleotide at the 3'-end mimicking an erroneous replication product. The Nsp10/Nsp14 complex may function in a replicative mismatch repair mechanism. N7-MTase functions in mRNA capping. Nsp14 can methylate GTP, dGTP as well as cap analogs GpppG, GpppA and m7GpppG. The accumulation of m7GTP or Nsp14 has been found to interfere with protein translation of cellular mRNAs.


The actual alignment was detected with superfamily member cd21659:

Pssm-ID: 424095  Cd Length: 519  Bit Score: 209.19  E-value: 4.84e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243697453   1 KHLIPLISRGQRWDVVRIRIVQMLSDHLVDLADSVVLVTWAASFELTCLRYFAKIGKEVVCNVCNKRATCFNSRTGYYGC 80
Cdd:cd21659   144 KHLIPLMSKGQPWDVVRIRIVQMLSDTLDDLSDSVVFVTWAHGFELTSLRYFAKIGKERTCCMCTKRATCYSSRTGYYGC 223

                          90
                  ....*....|....*.
gi 2243697453  81 WRHSYSCDYLYNPLIV 96
Cdd:cd21659   224 WRHSVGCDYVYNPFIV 239
 
Name Accession Description Interval E-value
betaCoV_Nsp14 cd21659
nonstructural protein 14 of betacoronavirus; Nonstructural protein 14 (Nsp14) of coronavirus ...
 1-96 4.84e-67

nonstructural protein 14 of betacoronavirus; Nonstructural protein 14 (Nsp14) of coronavirus (CoV) plays an important role in viral replication and transcription. It consists of 2 domains with different enzymatic activities: an N-terminal exoribonuclease (ExoN) domain and a C-terminal cap (guanine-N7) methyltransferase (N7-MTase) domain. ExoN is important for proofreading and therefore, the prevention of lethal mutations. The association of Nsp14 with Nsp10 stimulates its ExoN activity; the complex hydrolyzes double-stranded RNA in a 3' to 5' direction as well as a single mismatched nucleotide at the 3'-end mimicking an erroneous replication product. The Nsp10/Nsp14 complex may function in a replicative mismatch repair mechanism. N7-MTase functions in mRNA capping. Nsp14 can methylate GTP, dGTP as well as cap analogs GpppG, GpppA and m7GpppG. The accumulation of m7GTP or Nsp14 has been found to interfere with protein translation of cellular mRNAs.


Pssm-ID: 394958  Cd Length: 519  Bit Score: 209.19  E-value: 4.84e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243697453   1 KHLIPLISRGQRWDVVRIRIVQMLSDHLVDLADSVVLVTWAASFELTCLRYFAKIGKEVVCNVCNKRATCFNSRTGYYGC 80
Cdd:cd21659   144 KHLIPLMSKGQPWDVVRIRIVQMLSDTLDDLSDSVVFVTWAHGFELTSLRYFAKIGKERTCCMCTKRATCYSSRTGYYGC 223

                          90
                  ....*....|....*.
gi 2243697453  81 WRHSYSCDYLYNPLIV 96
Cdd:cd21659   224 WRHSVGCDYVYNPFIV 239
CoV_ExoN pfam06471
Coronavirus proofreading exoribonuclease; This region of coronavirus polyproteins encodes the ...
 1-96 9.54e-52

Coronavirus proofreading exoribonuclease; This region of coronavirus polyproteins encodes the NSP14 protein. Its N-terminal exoribonuclease (ExoN) domain plays a proofreading role for prevention of lethal mutagenesis, and the C-terminal domain functions as a (guanine-N7) methyl transferase (N7-MTase) for mRNA capping. NSP14 forms the nsp14-nsp10 complex involved in RNA viral proofreading.


Pssm-ID: 399465  Cd Length: 515  Bit Score: 169.17  E-value: 9.54e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243697453   1 KHLIPLISRGQRWDVVRIRIVQMLSDHLVDLADSVVLVTWAASFELTCLRYFAKIGKEVVCNvCNKRATCFNSRTGYYGC 80
Cdd:pfam06471 146 KHLIPLMRKGQPWHVVRIRIVQMLADTLAGLSDRVVFVLWAHGLELTTMRYFVKIGREQVCS-CGKRATCFNSSTDTYAC 224

                          90
                  ....*....|....*.
gi 2243697453  81 WRHSYSCDYLYNPLIV 96
Cdd:pfam06471 225 WKHSLGCDYVYNPFLI 240
 
Name Accession Description Interval E-value
betaCoV_Nsp14 cd21659
nonstructural protein 14 of betacoronavirus; Nonstructural protein 14 (Nsp14) of coronavirus ...
 1-96 4.84e-67

nonstructural protein 14 of betacoronavirus; Nonstructural protein 14 (Nsp14) of coronavirus (CoV) plays an important role in viral replication and transcription. It consists of 2 domains with different enzymatic activities: an N-terminal exoribonuclease (ExoN) domain and a C-terminal cap (guanine-N7) methyltransferase (N7-MTase) domain. ExoN is important for proofreading and therefore, the prevention of lethal mutations. The association of Nsp14 with Nsp10 stimulates its ExoN activity; the complex hydrolyzes double-stranded RNA in a 3' to 5' direction as well as a single mismatched nucleotide at the 3'-end mimicking an erroneous replication product. The Nsp10/Nsp14 complex may function in a replicative mismatch repair mechanism. N7-MTase functions in mRNA capping. Nsp14 can methylate GTP, dGTP as well as cap analogs GpppG, GpppA and m7GpppG. The accumulation of m7GTP or Nsp14 has been found to interfere with protein translation of cellular mRNAs.


Pssm-ID: 394958  Cd Length: 519  Bit Score: 209.19  E-value: 4.84e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243697453   1 KHLIPLISRGQRWDVVRIRIVQMLSDHLVDLADSVVLVTWAASFELTCLRYFAKIGKEVVCNVCNKRATCFNSRTGYYGC 80
Cdd:cd21659   144 KHLIPLMSKGQPWDVVRIRIVQMLSDTLDDLSDSVVFVTWAHGFELTSLRYFAKIGKERTCCMCTKRATCYSSRTGYYGC 223

                          90
                  ....*....|....*.
gi 2243697453  81 WRHSYSCDYLYNPLIV 96
Cdd:cd21659   224 WRHSVGCDYVYNPFIV 239
CoV_ExoN pfam06471
Coronavirus proofreading exoribonuclease; This region of coronavirus polyproteins encodes the ...
 1-96 9.54e-52

Coronavirus proofreading exoribonuclease; This region of coronavirus polyproteins encodes the NSP14 protein. Its N-terminal exoribonuclease (ExoN) domain plays a proofreading role for prevention of lethal mutagenesis, and the C-terminal domain functions as a (guanine-N7) methyl transferase (N7-MTase) for mRNA capping. NSP14 forms the nsp14-nsp10 complex involved in RNA viral proofreading.


Pssm-ID: 399465  Cd Length: 515  Bit Score: 169.17  E-value: 9.54e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243697453   1 KHLIPLISRGQRWDVVRIRIVQMLSDHLVDLADSVVLVTWAASFELTCLRYFAKIGKEVVCNvCNKRATCFNSRTGYYGC 80
Cdd:pfam06471 146 KHLIPLMRKGQPWHVVRIRIVQMLADTLAGLSDRVVFVLWAHGLELTTMRYFVKIGREQVCS-CGKRATCFNSSTDTYAC 224

                          90
                  ....*....|....*.
gi 2243697453  81 WRHSYSCDYLYNPLIV 96
Cdd:pfam06471 225 WKHSLGCDYVYNPFLI 240
CoV_Nsp14 cd21528
nonstructural protein 14 of coronavirus; Nonstructural protein 14 (Nsp14) of coronavirus (CoV) ...
 1-96 1.69e-40

nonstructural protein 14 of coronavirus; Nonstructural protein 14 (Nsp14) of coronavirus (CoV) plays an important role in viral replication and transcription. It consists of 2 domains with different enzymatic activities: an N-terminal exoribonuclease (ExoN) domain and a C-terminal cap (guanine-N7) methyltransferase (N7-MTase) domain. ExoN is important for proofreading and therefore, the prevention of lethal mutations. The association of Nsp14 with Nsp10 stimulates its ExoN activity; the complex hydrolyzes double-stranded RNA in a 3' to 5' direction as well as a single mismatched nucleotide at the 3'-end mimicking an erroneous replication product. The Nsp10/Nsp14 complex may function in a replicative mismatch repair mechanism. N7-MTase functions in mRNA capping. Nsp14 can methylate GTP, dGTP as well as cap analogs GpppG, GpppA and m7GpppG. The accumulation of m7GTP or Nsp14 has been found to interfere with protein translation of cellular mRNAs.


Pssm-ID: 394955  Cd Length: 518  Bit Score: 139.13  E-value: 1.69e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243697453   1 KHLIPLISRGQRWDVVRIRIVQMLSDHLVDLADSVVLVTWAASFELTCLRYFAKIGKEVVCNvCNKRATCFNSRTGYYGC 80
Cdd:cd21528   145 KHLIPLMRKALPWSVVRKRIVQMLADTLKGLSDRVVFVLWAHGLELTTMRYFVKIGPEKKCC-CGKRATCYNSSSDTYAC 223

                          90
                  ....*....|....*.
gi 2243697453  81 WRHSYSCDYLYNPLIV 96
Cdd:cd21528   224 WNHSLGCDYVYNPYII 239
alphaCoV_Nsp14 cd21660
nonstructural protein 14 of alphacoronavirus; Nonstructural protein 14 (Nsp14) of coronavirus ...
 2-96 1.82e-38

nonstructural protein 14 of alphacoronavirus; Nonstructural protein 14 (Nsp14) of coronavirus (CoV) plays an important role in viral replication and transcription. It consists of 2 domains with different enzymatic activities: an N-terminal exoribonuclease (ExoN) domain and a C-terminal cap (guanine-N7) methyltransferase (N7-MTase) domain. ExoN is important for proofreading and therefore, the prevention of lethal mutations. The association of Nsp14 with Nsp10 stimulates its ExoN activity; the complex hydrolyzes double-stranded RNA in a 3' to 5' direction as well as a single mismatched nucleotide at the 3'-end mimicking an erroneous replication product. The Nsp10/Nsp14 complex may function in a replicative mismatch repair mechanism. N7-MTase functions in mRNA capping. Nsp14 can methylate GTP, dGTP as well as cap analogs GpppG, GpppA and m7GpppG. The accumulation of m7GTP or Nsp14 has been found to interfere with protein translation of cellular mRNAs.


Pssm-ID: 394959  Cd Length: 510  Bit Score: 133.62  E-value: 1.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243697453   2 HLIPLISRGQRWDVVRIRIVQMLSDHLVDLADSVVLVTWAASFELTCLRYFAKIGKEVVCNvCNKRATCFNSRTGYYGCW 81
Cdd:cd21660   144 HLIPLMRKGQPWSVVRKRIVQMCCDYLKGLSDILIFVLWAGGLELTTMRYFVKIGPVKHCH-CGKEATCYNSVSHAYCCF 222

                          90
                  ....*....|....*
gi 2243697453  82 RHSYSCDYLYNPLIV 96
Cdd:cd21660   223 KHALGCDYLYNPYVI 237
gammaCoV_Nsp14 cd21658
nonstructural protein 14 of gammacoronavirus; Nonstructural protein 14 (Nsp14) of coronavirus ...
 2-96 4.87e-35

nonstructural protein 14 of gammacoronavirus; Nonstructural protein 14 (Nsp14) of coronavirus (CoV) plays an important role in viral replication and transcription. It consists of 2 domains with different enzymatic activities: an N-terminal exoribonuclease (ExoN) domain and a C-terminal cap (guanine-N7) methyltransferase (N7-MTase) domain. ExoN is important for proofreading and therefore, the prevention of lethal mutations. The association of Nsp14 with Nsp10 stimulates its ExoN activity; the complex hydrolyzes double-stranded RNA in a 3' to 5' direction as well as a single mismatched nucleotide at the 3'-end mimicking an erroneous replication product. The Nsp10/Nsp14 complex may function in a replicative mismatch repair mechanism. N7-MTase functions in mRNA capping. Nsp14 can methylate GTP, dGTP as well as cap analogs GpppG, GpppA and m7GpppG. The accumulation of m7GTP or Nsp14 has been found to interfere with protein translation of cellular mRNAs.


Pssm-ID: 394957  Cd Length: 518  Bit Score: 124.59  E-value: 4.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243697453   2 HLIPLISRGQRWDVVRIRIVQMLSDHLVDLADSVVLVTWAASFELTCLRYFAKIGKEVVCNvCNKRATCFNSRTGYYGCW 81
Cdd:cd21658   146 HLRALFKSAKPWHVIRPRIVQMLADNLCNVSDCVVFVTWCHGLELTTLRYFVKIGKEQVCS-CGSRATTFNSHTQAYACW 224

                          90
                  ....*....|....*
gi 2243697453  82 RHSYSCDYLYNPLIV 96
Cdd:cd21658   225 KHCLGFDFVYNPLLV 239
deltaCoV_Nsp14 cd21657
nonstructural protein 14 of deltacoronavirus; Nonstructural protein 14 (Nsp14) of coronavirus ...
 1-96 1.76e-19

nonstructural protein 14 of deltacoronavirus; Nonstructural protein 14 (Nsp14) of coronavirus (CoV) plays an important role in viral replication and transcription. It consists of 2 domains with different enzymatic activities: an N-terminal exoribonuclease (ExoN) domain and a C-terminal cap (guanine-N7) methyltransferase (N7-MTase) domain. ExoN is important for proofreading and therefore, the prevention of lethal mutations. The association of Nsp14 with Nsp10 stimulates its ExoN activity; the complex hydrolyzes double-stranded RNA in a 3' to 5' direction as well as a single mismatched nucleotide at the 3'-end mimicking an erroneous replication product. The Nsp10/Nsp14 complex may function in a replicative mismatch repair mechanism. N7-MTase functions in mRNA capping. Nsp14 can methylate GTP, dGTP as well as cap analogs GpppG, GpppA and m7GpppG. The accumulation of m7GTP or Nsp14 has been found to interfere with protein translation of cellular mRNAs.


Pssm-ID: 394956  Cd Length: 508  Bit Score: 81.06  E-value: 1.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2243697453   1 KHLIPLISRGQRWDVVRIRIVQMLSDHLVDlADSVVLVTWAASFELTCLRYFAKIGKEVVCNvCNKRAtCFNSRTGyYGC 80
Cdd:cd21657   145 RHLKKDMRQARPWKVVRREIAAHLAEVAPH-TDYICFVTWAHQLELATMRYFVKIGMEEKCF-CGRRA-CFTNGTE-FAC 220

                          90       100
                  ....*....|....*....|
gi 2243697453  81 WRH----SYSCDYLYNPLIV 96
Cdd:cd21657   221 KAHhsltTPQCDYVYNPFLI 240
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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