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Conserved domains on  [gi|1802476809|ref|YP_009725301|]
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3C-like proteinase [Severe acute respiratory syndrome coronavirus 2]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
betaCoV_Nsp5_Mpro cd21666
betacoronavirus non-structural protein 5, also called Main protease (Mpro); This subfamily ...
 4-300 0e+00

betacoronavirus non-structural protein 5, also called Main protease (Mpro); This subfamily contains the coronavirus (CoV) non-structural protein 5 (Nsp5) also called the Main protease (Mpro), or 3C-like protease (3CLpro), found in betacoronaviruses. CoVs utilize a multi-subunit replication/transcription machinery. A set of non-structural proteins (Nsps) generated as cleavage products of the ORF1a and ORF1ab viral polyproteins assemble to facilitate viral replication and transcription. Mpro/Nsp5 is a key enzyme in this process, making it a high value target for the development of anti-coronavirus therapeutics. These enzymes belong to the MEROPS peptidase C30 family, where the active site residues His and Cys form a catalytic dyad. The structures of Mpro/Nsp5 consist of three domains with the first two containing anti-parallel beta barrels and the third consisting of an arrangement of alpha-helices. The catalytic residues are found in a cleft between the first two domains. Mpro requires a Gln residue in the P1 position of the substrate and space for only small amino-acid residues such as Gly, Ala, or Ser in the P1' position; since there is no known human protease with a specificity for Gln at the cleavage site of the substrate, these viral proteases are suitable targets for the development of antiviral drugs.


:

Pssm-ID: 394887  Cd Length: 297  Bit Score: 565.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809   4 RKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQ 83
Cdd:cd21666     1 RKMAFPSGKVEGCMVQVTCGTMTLNGLWLDDTVYCPRHVICTAEDMLNPNYEDLLIRKTNHSFLVQAGNVQLRVIGHSMQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809  84 NCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMH 163
Cdd:cd21666    81 GCLLRLTVDTSNPKTPKYKFVRVKPGQTFSVLACYNGSPSGVYQCAMRPNHTIKGSFLCGSCGSVGYNIDGDCVSFCYMH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809 164 HMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLT 243
Cdd:cd21666   161 QMELPTGVHTGTDLEGKFYGPFVDRQTAQAAGTDTTITLNVLAWLYAAVLNGDRWFVNRFTTTLNDFNLWAMKYNYEPLT 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1802476809 244 QDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQC 300
Cdd:cd21666   241 QDHVDILDPLAAQTGIAVEDMLAALKELLQGGMQGRTILGSTILEDEFTPFDVVRQC 297
 
Name Accession Description Interval E-value
betaCoV_Nsp5_Mpro cd21666
betacoronavirus non-structural protein 5, also called Main protease (Mpro); This subfamily ...
 4-300 0e+00

betacoronavirus non-structural protein 5, also called Main protease (Mpro); This subfamily contains the coronavirus (CoV) non-structural protein 5 (Nsp5) also called the Main protease (Mpro), or 3C-like protease (3CLpro), found in betacoronaviruses. CoVs utilize a multi-subunit replication/transcription machinery. A set of non-structural proteins (Nsps) generated as cleavage products of the ORF1a and ORF1ab viral polyproteins assemble to facilitate viral replication and transcription. Mpro/Nsp5 is a key enzyme in this process, making it a high value target for the development of anti-coronavirus therapeutics. These enzymes belong to the MEROPS peptidase C30 family, where the active site residues His and Cys form a catalytic dyad. The structures of Mpro/Nsp5 consist of three domains with the first two containing anti-parallel beta barrels and the third consisting of an arrangement of alpha-helices. The catalytic residues are found in a cleft between the first two domains. Mpro requires a Gln residue in the P1 position of the substrate and space for only small amino-acid residues such as Gly, Ala, or Ser in the P1' position; since there is no known human protease with a specificity for Gln at the cleavage site of the substrate, these viral proteases are suitable targets for the development of antiviral drugs.


Pssm-ID: 394887  Cd Length: 297  Bit Score: 565.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809   4 RKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQ 83
Cdd:cd21666     1 RKMAFPSGKVEGCMVQVTCGTMTLNGLWLDDTVYCPRHVICTAEDMLNPNYEDLLIRKTNHSFLVQAGNVQLRVIGHSMQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809  84 NCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMH 163
Cdd:cd21666    81 GCLLRLTVDTSNPKTPKYKFVRVKPGQTFSVLACYNGSPSGVYQCAMRPNHTIKGSFLCGSCGSVGYNIDGDCVSFCYMH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809 164 HMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLT 243
Cdd:cd21666   161 QMELPTGVHTGTDLEGKFYGPFVDRQTAQAAGTDTTITLNVLAWLYAAVLNGDRWFVNRFTTTLNDFNLWAMKYNYEPLT 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1802476809 244 QDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQC 300
Cdd:cd21666   241 QDHVDILDPLAAQTGIAVEDMLAALKELLQGGMQGRTILGSTILEDEFTPFDVVRQC 297
Peptidase_C30 pfam05409
Coronavirus endopeptidase C30; This Coronavirus (CoV) domain, peptidase C30, is also known as ...
 29-306 2.34e-176

Coronavirus endopeptidase C30; This Coronavirus (CoV) domain, peptidase C30, is also known as 3C-like proteinase (3CL-pro), or CoV main protease (M-pro) domain. CoV M-pro is a dimer where each subunit is composed of three domains I, II and III,,. Domains I and II consist of six-stranded antiparallel beta barrels and together resemble the architecture of chymotrypsin, and of picornaviruses 3C proteinases. The substrate-binding site is located in a cleft between these two domains. The catalytic site is situated at the centre of the cleft. A long loop connects domain II to the C-terminal domain (domain III). This latter domain has been implicated in the proteolytic activity of M-pro. In the active site of M-pro, Cys and His form a catalytic dyad,.


Pssm-ID: 398852  Cd Length: 274  Bit Score: 488.10  E-value: 2.34e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809  29 GLWLDDVVYCPRHVICTSEDMLnPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQP 108
Cdd:pfam05409   1 GLWLGDTVYCPRHVIGSFTGML-PQYEHLLSIARNHDFCVVSGGVQLTVVSAKMQGAILVLKVHTNNPNTPKYKFVRLKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809 109 GQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGNFYGPFVDR 188
Cdd:pfam05409  80 GESFTILAAYDGCPQGVYHVTMRSNHTIKGSFLNGACGSVGYNLKGGTVCFVYMHHLELPNGSHTGTDLEGVFYGPYVDE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809 189 QTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVdiLGPLSAQTGIAVLDMCASL 268
Cdd:pfam05409 160 EVAQLEGTDQTYTDNVVAWLYAAIINGPRWFLASTTVSLEDFNAWAMTNGFTPFPCEDA--ILGLAAKTGVSVERLLAAI 237

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1802476809 269 KElLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ 306
Cdd:pfam05409 238 KV-LNNGFGGRTILGSPSLEDEFTPEDVYNQMAGVTLQ 274
 
Name Accession Description Interval E-value
betaCoV_Nsp5_Mpro cd21666
betacoronavirus non-structural protein 5, also called Main protease (Mpro); This subfamily ...
 4-300 0e+00

betacoronavirus non-structural protein 5, also called Main protease (Mpro); This subfamily contains the coronavirus (CoV) non-structural protein 5 (Nsp5) also called the Main protease (Mpro), or 3C-like protease (3CLpro), found in betacoronaviruses. CoVs utilize a multi-subunit replication/transcription machinery. A set of non-structural proteins (Nsps) generated as cleavage products of the ORF1a and ORF1ab viral polyproteins assemble to facilitate viral replication and transcription. Mpro/Nsp5 is a key enzyme in this process, making it a high value target for the development of anti-coronavirus therapeutics. These enzymes belong to the MEROPS peptidase C30 family, where the active site residues His and Cys form a catalytic dyad. The structures of Mpro/Nsp5 consist of three domains with the first two containing anti-parallel beta barrels and the third consisting of an arrangement of alpha-helices. The catalytic residues are found in a cleft between the first two domains. Mpro requires a Gln residue in the P1 position of the substrate and space for only small amino-acid residues such as Gly, Ala, or Ser in the P1' position; since there is no known human protease with a specificity for Gln at the cleavage site of the substrate, these viral proteases are suitable targets for the development of antiviral drugs.


Pssm-ID: 394887  Cd Length: 297  Bit Score: 565.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809   4 RKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQ 83
Cdd:cd21666     1 RKMAFPSGKVEGCMVQVTCGTMTLNGLWLDDTVYCPRHVICTAEDMLNPNYEDLLIRKTNHSFLVQAGNVQLRVIGHSMQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809  84 NCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMH 163
Cdd:cd21666    81 GCLLRLTVDTSNPKTPKYKFVRVKPGQTFSVLACYNGSPSGVYQCAMRPNHTIKGSFLCGSCGSVGYNIDGDCVSFCYMH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809 164 HMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLT 243
Cdd:cd21666   161 QMELPTGVHTGTDLEGKFYGPFVDRQTAQAAGTDTTITLNVLAWLYAAVLNGDRWFVNRFTTTLNDFNLWAMKYNYEPLT 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1802476809 244 QDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQC 300
Cdd:cd21666   241 QDHVDILDPLAAQTGIAVEDMLAALKELLQGGMQGRTILGSTILEDEFTPFDVVRQC 297
CoV_Nsp5_Mpro cd21646
coronavirus non-structural protein 5, also called Main protease (Mpro); This family contains ...
 4-299 0e+00

coronavirus non-structural protein 5, also called Main protease (Mpro); This family contains the coronavirus (CoV) non-structural protein 5 (Nsp5) also called the Main protease (Mpro), or 3C-like protease (3CLpro). CoVs utilize a multi-subunit replication/transcription machinery. A set of non-structural proteins (Nsps) generated as cleavage products of the ORF1a and ORF1ab viral polyproteins assemble to facilitate viral replication and transcription. Mpro/Nsp5 is a key enzyme in this process, making it a high value target for the development of anti-coronavirus therapeutics. These enzymes belong to the MEROPS peptidase C30 family, where the active site residues His and Cys form a catalytic dyad. The structures of Mpro/Nsp5 consist of three domains with the first two containing anti-parallel beta barrels and the third consisting of an arrangement of alpha-helices. The catalytic residues are found in a cleft between the first two domains. Mpro/Nsp5 requires a Gln residue in the P1 position of the substrate and space for only small amino-acid residues such as Gly, Ala, or Ser in the P1' position; since there is no known human protease with a specificity for Gln at the cleavage site of the substrate, these viral proteases are suitable targets for the development of antiviral drugs.


Pssm-ID: 394885  Cd Length: 292  Bit Score: 520.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809   4 RKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDmLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQ 83
Cdd:cd21646     1 KKMAQPSGKVERCMVSVTYGSTTLNGLWLDDTVYCPRHVICKSTT-SGPDYDDLLSRARNHNFSVQSGGVQLRVVGVTMQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809  84 NCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMH 163
Cdd:cd21646    80 GALLRLKVDTSNPHTPKYKFVTVKPGDSFTILACYNGSPSGVYGVNMRSNYTIKGSFLNGACGSVGYNIDGGTVEFCYMH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809 164 HMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLT 243
Cdd:cd21646   160 HLELPNGCHTGTDLTGKFYGPYVDQQVAQVEGADTLITDNVVAWLYAAIINGDRWWLNSSRTTVNDFNEWAMANGFTPVS 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1802476809 244 QdhVDILGPLSAQTGIAVLDMCASLKELLQNGmNGRTILGSALLEDEFTPFDVVRQ 299
Cdd:cd21646   240 Q--VDCLSILAAKTGVSVERLLAAIQQLHQNF-GGKQILGSTSLEDEFTPEDVVRQ 292
Peptidase_C30 pfam05409
Coronavirus endopeptidase C30; This Coronavirus (CoV) domain, peptidase C30, is also known as ...
 29-306 2.34e-176

Coronavirus endopeptidase C30; This Coronavirus (CoV) domain, peptidase C30, is also known as 3C-like proteinase (3CL-pro), or CoV main protease (M-pro) domain. CoV M-pro is a dimer where each subunit is composed of three domains I, II and III,,. Domains I and II consist of six-stranded antiparallel beta barrels and together resemble the architecture of chymotrypsin, and of picornaviruses 3C proteinases. The substrate-binding site is located in a cleft between these two domains. The catalytic site is situated at the centre of the cleft. A long loop connects domain II to the C-terminal domain (domain III). This latter domain has been implicated in the proteolytic activity of M-pro. In the active site of M-pro, Cys and His form a catalytic dyad,.


Pssm-ID: 398852  Cd Length: 274  Bit Score: 488.10  E-value: 2.34e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809  29 GLWLDDVVYCPRHVICTSEDMLnPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQP 108
Cdd:pfam05409   1 GLWLGDTVYCPRHVIGSFTGML-PQYEHLLSIARNHDFCVVSGGVQLTVVSAKMQGAILVLKVHTNNPNTPKYKFVRLKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809 109 GQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGNFYGPFVDR 188
Cdd:pfam05409  80 GESFTILAAYDGCPQGVYHVTMRSNHTIKGSFLNGACGSVGYNLKGGTVCFVYMHHLELPNGSHTGTDLEGVFYGPYVDE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809 189 QTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVdiLGPLSAQTGIAVLDMCASL 268
Cdd:pfam05409 160 EVAQLEGTDQTYTDNVVAWLYAAIINGPRWFLASTTVSLEDFNAWAMTNGFTPFPCEDA--ILGLAAKTGVSVERLLAAI 237

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1802476809 269 KElLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ 306
Cdd:pfam05409 238 KV-LNNGFGGRTILGSPSLEDEFTPEDVYNQMAGVTLQ 274
alphaCoV_Nsp5_Mpro cd21665
alphacoronavirus non-structural protein 5, also called Main protease (Mpro); This subfamily ...
 3-302 6.82e-118

alphacoronavirus non-structural protein 5, also called Main protease (Mpro); This subfamily contains the coronavirus (CoV) non-structural protein 5 (Nsp5) also called the Main protease (Mpro), or 3C-like protease (3CLpro), found in alphacoronaviruses. CoVs utilize a multi-subunit replication/transcription machinery. A set of non-structural proteins (Nsps) generated as cleavage products of the ORF1a and ORF1ab viral polyproteins assemble to facilitate viral replication and transcription. Mpro/Nsp5 is a key enzyme in this process, making it a high value target for the development of anti-coronavirus therapeutics. These enzymes belong to the MEROPS peptidase C30 family, where the active site residues His and Cys form a catalytic dyad. The structures of Mpro/Nsp5 consist of three domains with the first two containing anti-parallel beta barrels and the third consisting of an arrangement of alpha-helices. The catalytic residues are found in a cleft between the first two domains. Mpro/Nsp5 requires a Gln residue in the P1 position of the substrate and space for only small amino-acid residues such as Gly, Ala, or Ser in the P1' position; since there is no known human protease with a specificity for Gln at the cleavage site of the substrate, these viral proteases are suitable targets for the development of antiviral drugs.


Pssm-ID: 394886  Cd Length: 296  Bit Score: 340.81  E-value: 6.82e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809   3 FRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTS-EDMLNPNYEDLLIRKsnHNFLVQAGNVQLRVIGHS 81
Cdd:cd21665     1 LRKMAQPSGVVEKCVVRVSYGNMVLNGLWLGDTVYCPRHVIASDtTSTIDYDHEYSLMRL--HNFSISVGNVFLGVVGVT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809  82 MQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCY 161
Cdd:cd21665    79 MRGALLVIKVNQNNVNTPKYTFRTLKPGDSFNILACYDGVPSGVYGVNMRTNYTIKGSFINGACGSPGYNLNNGTVEFCY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809 162 MHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEP 241
Cdd:cd21665   159 MHQLELGSGCHVGSDLDGVMYGGYEDQPTLQVEGANVLVTENVVAFLYAALLNGCNWWLSSDRVTVEAFNEWAVANGFTT 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1802476809 242 LTQdhVDILGPLSAQTGIAVLDMCASLKElLQNGMNGRTILGSALLEDEFTPFDVVRQCSG 302
Cdd:cd21665   239 VSS--TDCFSILAAKTGVDVERLLAAIQR-LSKGFGGKTILGYTSLTDEFTLSEVIKQMYG 296
gammaCoV_Nsp5_Mpro cd21667
gammacoronavirus non-structural protein 5, also called Main protease (Mpro); This subfamily ...
 2-306 1.75e-94

gammacoronavirus non-structural protein 5, also called Main protease (Mpro); This subfamily contains the coronavirus (CoV) non-structural protein 5 (Nsp5) also called the Main protease (Mpro), or 3C-like protease (3CLpro), found in gammacoronaviruses. CoVs utilize a multi-subunit replication/transcription machinery. A set of non-structural proteins (Nsps) generated as cleavage products of the ORF1a and ORF1ab viral polyproteins assemble to facilitate viral replication and transcription. Mpro/Nsp5 is a key enzyme in this process, making it a high value target for the development of anti-coronavirus therapeutics. These enzymes belong to the MEROPS peptidase C30 family, where the active site residues His and Cys form a catalytic dyad. The structures of Mpro/Nsp5 consist of three domains with the first two containing anti-parallel beta barrels and the third consisting of an arrangement of alpha-helices. The catalytic residues are found in a cleft between the first two domains. Mpro/Nsp5 requires a Gln residue in the P1 position of the substrate and space for only small amino-acid residues such as Gly, Ala, or Ser in the P1' position; since there is no known human protease with a specificity for Gln at the cleavage site of the substrate, these viral proteases are suitable targets for the development of antiviral drugs.


Pssm-ID: 394888  Cd Length: 306  Bit Score: 281.68  E-value: 1.75e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809   2 GFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVI--CTSEDmlnpnYEDLLIRKSNHNFLVQAGN-VQLRVI 78
Cdd:cd21667     1 GFKKLVSPSSAVEKCIVSVSYRGNNLNGLWLGDSIYCPRHVLgkFSGDQ-----WQDVLNLANNHEFEVVTQNgVTLNVV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809  79 GHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVS 158
Cdd:cd21667    76 SRRLKGAVLILQTAVANANTPKYKFVKANCGDSFTIACSYGGTVVGLYPVTMRSNGTIRASFLAGACGSVGFNIEKGVVN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809 159 FCYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVIN---GDRWF---LNRFTTTLNDFNL 232
Cdd:cd21667   156 FFYMHHLELPNALHTGTDLMGEFYGGYVDEEVAQRVPPDNLVTNNIVAWLYAAIISvkeSSFSLpkwLESTTVSVEDYNK 235

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1802476809 233 VAMKYNYEPL-TQDHVDIlgpLSAQTGIAVLDMCASLKElLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ 306
Cdd:cd21667   236 WASDNGFTPFsTSTAITK---LSAITGVDVCKLLRTIMV-KSAQWGSDPILGQYNFEDELTPESVFNQVGGVRLQ 306
deltaCoV_Nsp5_Mpro cd21668
deltacoronavirus non-structural protein 5, also called Main protease (Mpro); This subfamily ...
 1-299 8.36e-70

deltacoronavirus non-structural protein 5, also called Main protease (Mpro); This subfamily contains the coronavirus (CoV) non-structural protein 5 (Nsp5) also called the Main protease (Mpro), or 3C-like protease (3CLpro), found in deltacoronaviruses. CoVs utilize a multi-subunit replication/transcription machinery. A set of non-structural proteins (Nsps) generated as cleavage products of the ORF1a and ORF1ab viral polyproteins assemble to facilitate viral replication and transcription. Mpro/Nsp5 is a key enzyme in this process, making it a high value target for the development of anti-coronavirus therapeutics. These enzymes belong to the MEROPS peptidase C30 family, where the active site residues His and Cys form a catalytic dyad. The structures of Mpro/Nsp5 consist of three domains with the first two containing anti-parallel beta barrels and the third consisting of an arrangement of alpha-helices. The catalytic residues are found in a cleft between the first two domains. Mpro/Nsp5 requires a Gln residue in the P1 position of the substrate and space for only small amino-acid residues such as Gly, Ala, or Ser in the P1' position; since there is no known human protease with a specificity for Gln at the cleavage site of the substrate, these viral proteases are suitable targets for the development of antiviral drugs.


Pssm-ID: 394889  Cd Length: 302  Bit Score: 218.91  E-value: 8.36e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809   1 SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVIctsEDMLNPNYEDLLIRKSNHNFLV--QAGNVQLRVI 78
Cdd:cd21668     2 AGIKILLHPSGVVERCMVSVTYNGSTLNGIWLHNVVYCPRHVI---GKYTGSQWQDMVSIADCRDFVIfcPTQGIQLTVQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809  79 GHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVS 158
Cdd:cd21668    79 SVKMVGAVLQLTVHTKNLHTPDYEFERATPGSSMTIACAYDGIVRNVYHVVLQTNNLIYASFLNGACGSVGYTLKGKTLL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802476809 159 FCYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDR---WfLNRFTTTLNDFNLVAM 235
Cdd:cd21668   159 LHYMHHLEFNNKTHGGTDLHGHFYGPYVDEEVAQHQTAFQYYTDNVVAQIYAHLLTIDAkpkW-LASQEISVEDFNEWAA 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1802476809 236 KYNYE--PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNgMNGRTILGSALLEDEFTPFDVVRQ 299
Cdd:cd21668   238 NNSFAnfPCESSNMAYLEGLAQTTKVSVGRVLNTIIQLTLN-RGGALIMGKPDFECDWTPEMVYNQ 302
 
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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