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Conserved domains on  [gi|350280644|gb|AEQ25561|]
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read-through protein [Enterobacteria phage SP]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Levi_coat super family cl28115
Levivirus coat protein; The Levivirus coat protein forms the bacteriophage coat that ...
2-132 5.63e-63

Levivirus coat protein; The Levivirus coat protein forms the bacteriophage coat that encapsidates the viral RNA. 180 copies of this protein form the virion shell. The MS2 bacteriophage coat protein controls two distinct processes: sequence-specific RNA encapsidation and repression of replicase translation-by binding to an RNA stem-loop structure of 19 nucleotides containing the initiation codon of the replicase gene. The binding of a coat protein dimer to this hairpin shuts off synthesis of the viral replicase, switching the viral replication cycle to virion assembly rather than continued replication.


The actual alignment was detected with superfamily member pfam01819:

Pssm-ID: 421570  Cd Length: 132  Bit Score: 196.10  E-value: 5.63e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350280644    2 AKLNQVTLSEIGKNGDQTLTLTPRGVNPTNGVASLSEAGAVPALEKRVTVSVAQPSRNRKNFKVQIKLQNPTACTKDA-C 80
Cdd:pfam01819   1 AKFQAFTLSDIGGNGDVTLALNPRGVNFANGVAALIEAGARPAAEKRVTCSVRQPSANNKKYKIKVEIPKPASCTAGGtC 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 350280644   81 DPSVTRSAFADVTLSFTSYSTDEERALIRTELAALLADPLIVDAIDNLNPAY 132
Cdd:pfam01819  81 DPSAARRAYADMEFSFPIFATDEDCALIRKALKALLADGMLIDAADAANPAI 132
Read-through super family cl25129
Read-through domain; The Enterobacteria phage minor coat protein A1 is a C-terminally extended ...
163-329 1.49e-48

Read-through domain; The Enterobacteria phage minor coat protein A1 is a C-terminally extended version of the coat protein formed when ribosomes read-through a leaky stop codon. This is the C-terminal read-through domain of A1.


The actual alignment was detected with superfamily member pfam16814:

Pssm-ID: 293419  Cd Length: 182  Bit Score: 161.03  E-value: 1.49e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350280644  163 GTGRYKCPFACYRLGSIYEVGKDG-SPDIYERGDEVSVTFDYALEDFLGNTNWRNWDQRLSdydIANRRRCRGNGYIDLD 241
Cdd:pfam16814  15 GTGSYTCPFRIWDLSSIYEAANSShSWDIYNAVELSPRKFDVTLDDLLGNTDWRDWDGRLR---YTTFRGSRGNGYIDLD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350280644  242 ATAMQSDDFVLSGRYAVRKVKFPGAFGSIKYLLNIQG-DAWLDLSEVTAYRSYGMVIGFWAD-SKSPQLPTDYTQFNSAN 319
Cdd:pfam16814  92 ATSLMQDEYLTSSKYLVREGKRPGAFGSIERFVYLKSiNAYCSLSDITAYHSDGVVVGFWRDpSSGGAIPFDFSEFDSNK 171
                         170
                  ....*....|
gi 350280644  320 CPVQTVIIIP 329
Cdd:pfam16814 172 CPIQAVIVVP 181
 
Name Accession Description Interval E-value
Levi_coat pfam01819
Levivirus coat protein; The Levivirus coat protein forms the bacteriophage coat that ...
2-132 5.63e-63

Levivirus coat protein; The Levivirus coat protein forms the bacteriophage coat that encapsidates the viral RNA. 180 copies of this protein form the virion shell. The MS2 bacteriophage coat protein controls two distinct processes: sequence-specific RNA encapsidation and repression of replicase translation-by binding to an RNA stem-loop structure of 19 nucleotides containing the initiation codon of the replicase gene. The binding of a coat protein dimer to this hairpin shuts off synthesis of the viral replicase, switching the viral replication cycle to virion assembly rather than continued replication.


Pssm-ID: 396403  Cd Length: 132  Bit Score: 196.10  E-value: 5.63e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350280644    2 AKLNQVTLSEIGKNGDQTLTLTPRGVNPTNGVASLSEAGAVPALEKRVTVSVAQPSRNRKNFKVQIKLQNPTACTKDA-C 80
Cdd:pfam01819   1 AKFQAFTLSDIGGNGDVTLALNPRGVNFANGVAALIEAGARPAAEKRVTCSVRQPSANNKKYKIKVEIPKPASCTAGGtC 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 350280644   81 DPSVTRSAFADVTLSFTSYSTDEERALIRTELAALLADPLIVDAIDNLNPAY 132
Cdd:pfam01819  81 DPSAARRAYADMEFSFPIFATDEDCALIRKALKALLADGMLIDAADAANPAI 132
Read-through pfam16814
Read-through domain; The Enterobacteria phage minor coat protein A1 is a C-terminally extended ...
163-329 1.49e-48

Read-through domain; The Enterobacteria phage minor coat protein A1 is a C-terminally extended version of the coat protein formed when ribosomes read-through a leaky stop codon. This is the C-terminal read-through domain of A1.


Pssm-ID: 293419  Cd Length: 182  Bit Score: 161.03  E-value: 1.49e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350280644  163 GTGRYKCPFACYRLGSIYEVGKDG-SPDIYERGDEVSVTFDYALEDFLGNTNWRNWDQRLSdydIANRRRCRGNGYIDLD 241
Cdd:pfam16814  15 GTGSYTCPFRIWDLSSIYEAANSShSWDIYNAVELSPRKFDVTLDDLLGNTDWRDWDGRLR---YTTFRGSRGNGYIDLD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350280644  242 ATAMQSDDFVLSGRYAVRKVKFPGAFGSIKYLLNIQG-DAWLDLSEVTAYRSYGMVIGFWAD-SKSPQLPTDYTQFNSAN 319
Cdd:pfam16814  92 ATSLMQDEYLTSSKYLVREGKRPGAFGSIERFVYLKSiNAYCSLSDITAYHSDGVVVGFWRDpSSGGAIPFDFSEFDSNK 171
                         170
                  ....*....|
gi 350280644  320 CPVQTVIIIP 329
Cdd:pfam16814 172 CPIQAVIVVP 181
 
Name Accession Description Interval E-value
Levi_coat pfam01819
Levivirus coat protein; The Levivirus coat protein forms the bacteriophage coat that ...
2-132 5.63e-63

Levivirus coat protein; The Levivirus coat protein forms the bacteriophage coat that encapsidates the viral RNA. 180 copies of this protein form the virion shell. The MS2 bacteriophage coat protein controls two distinct processes: sequence-specific RNA encapsidation and repression of replicase translation-by binding to an RNA stem-loop structure of 19 nucleotides containing the initiation codon of the replicase gene. The binding of a coat protein dimer to this hairpin shuts off synthesis of the viral replicase, switching the viral replication cycle to virion assembly rather than continued replication.


Pssm-ID: 396403  Cd Length: 132  Bit Score: 196.10  E-value: 5.63e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350280644    2 AKLNQVTLSEIGKNGDQTLTLTPRGVNPTNGVASLSEAGAVPALEKRVTVSVAQPSRNRKNFKVQIKLQNPTACTKDA-C 80
Cdd:pfam01819   1 AKFQAFTLSDIGGNGDVTLALNPRGVNFANGVAALIEAGARPAAEKRVTCSVRQPSANNKKYKIKVEIPKPASCTAGGtC 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 350280644   81 DPSVTRSAFADVTLSFTSYSTDEERALIRTELAALLADPLIVDAIDNLNPAY 132
Cdd:pfam01819  81 DPSAARRAYADMEFSFPIFATDEDCALIRKALKALLADGMLIDAADAANPAI 132
Read-through pfam16814
Read-through domain; The Enterobacteria phage minor coat protein A1 is a C-terminally extended ...
163-329 1.49e-48

Read-through domain; The Enterobacteria phage minor coat protein A1 is a C-terminally extended version of the coat protein formed when ribosomes read-through a leaky stop codon. This is the C-terminal read-through domain of A1.


Pssm-ID: 293419  Cd Length: 182  Bit Score: 161.03  E-value: 1.49e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350280644  163 GTGRYKCPFACYRLGSIYEVGKDG-SPDIYERGDEVSVTFDYALEDFLGNTNWRNWDQRLSdydIANRRRCRGNGYIDLD 241
Cdd:pfam16814  15 GTGSYTCPFRIWDLSSIYEAANSShSWDIYNAVELSPRKFDVTLDDLLGNTDWRDWDGRLR---YTTFRGSRGNGYIDLD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350280644  242 ATAMQSDDFVLSGRYAVRKVKFPGAFGSIKYLLNIQG-DAWLDLSEVTAYRSYGMVIGFWAD-SKSPQLPTDYTQFNSAN 319
Cdd:pfam16814  92 ATSLMQDEYLTSSKYLVREGKRPGAFGSIERFVYLKSiNAYCSLSDITAYHSDGVVVGFWRDpSSGGAIPFDFSEFDSNK 171
                         170
                  ....*....|
gi 350280644  320 CPVQTVIIIP 329
Cdd:pfam16814 172 CPIQAVIVVP 181
 
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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