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Conserved domains on  [gi|446401298|ref|WP_000479153|]
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MULTISPECIES: phage tail assembly chaperone G [Bacteria]

Protein Classification

phage minor tail protein G( domain architecture ID 10536437)

phage minor tail protein G promotes tail assembly by creating a scaffold for the tail tube proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Phage_TAC_2 pfam06894
Bacteriophage lambda tail assembly chaperone, TAC, protein G; This family consists of ...
 1-126 1.78e-72

Bacteriophage lambda tail assembly chaperone, TAC, protein G; This family consists of Bacteriophage lambda minor tail protein G and related sequences. The construction of phage tails involves a stage of tail-tube formation, and tail-tube polymerization requires two additional proteins, gpG and gpGT. The open reading frames, ORFs, for gpG and gpGT are overlapping and are related by a programmed translational frameshift. During virion morphogenesis, gpG is expressed in large amounts, and about 3.5% of the time, a -1 translational frameshift leads to the production of the larger fusion protein, gpGT. The correct ratio of gpG to gpGT, as determined by the frequency of frameshifting, is crucial for tail assembly. Since gpG accumulates to high levels during a lambda infection and yet is not found in mature phage particles it is believed to act as a chaperone.


:

Pssm-ID: 284344  Cd Length: 126  Bit Score: 212.48  E-value: 1.78e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401298    1 MFLKTESFEHNGVTVTLSELSALQRIEHLALMKRQAEQAESDSNRKFTVEDAIRTGAFLVAMSLWHNHPQKTQMPSMNEA 80
Cdd:pfam06894   1 MFLKTETFECNGSSVTLFELSALQRIEHLEFIKRQTEAYEVDADRQAAIQMAVKIGAWLVAMSLWHGHPLKGQGENAAEE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 446401298   81 VKQIEQEVLTTWPTEAISHAENVVYRLSGMYEFVVNNAPEQTEDAG 126
Cdd:pfam06894  81 VAKIYQEVMQTWPTEALAEAEYKVLLLSGMAPVIDEPASSGEESGE 126
 
Name Accession Description Interval E-value
Phage_TAC_2 pfam06894
Bacteriophage lambda tail assembly chaperone, TAC, protein G; This family consists of ...
 1-126 1.78e-72

Bacteriophage lambda tail assembly chaperone, TAC, protein G; This family consists of Bacteriophage lambda minor tail protein G and related sequences. The construction of phage tails involves a stage of tail-tube formation, and tail-tube polymerization requires two additional proteins, gpG and gpGT. The open reading frames, ORFs, for gpG and gpGT are overlapping and are related by a programmed translational frameshift. During virion morphogenesis, gpG is expressed in large amounts, and about 3.5% of the time, a -1 translational frameshift leads to the production of the larger fusion protein, gpGT. The correct ratio of gpG to gpGT, as determined by the frequency of frameshifting, is crucial for tail assembly. Since gpG accumulates to high levels during a lambda infection and yet is not found in mature phage particles it is believed to act as a chaperone.


Pssm-ID: 284344  Cd Length: 126  Bit Score: 212.48  E-value: 1.78e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401298    1 MFLKTESFEHNGVTVTLSELSALQRIEHLALMKRQAEQAESDSNRKFTVEDAIRTGAFLVAMSLWHNHPQKTQMPSMNEA 80
Cdd:pfam06894   1 MFLKTETFECNGSSVTLFELSALQRIEHLEFIKRQTEAYEVDADRQAAIQMAVKIGAWLVAMSLWHGHPLKGQGENAAEE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 446401298   81 VKQIEQEVLTTWPTEAISHAENVVYRLSGMYEFVVNNAPEQTEDAG 126
Cdd:pfam06894  81 VAKIYQEVMQTWPTEALAEAEYKVLLLSGMAPVIDEPASSGEESGE 126
phage_lambda_G TIGR01674
phage minor tail protein G; This model describes a family of bacteriophage proteins including ...
 1-135 5.38e-72

phage minor tail protein G; This model describes a family of bacteriophage proteins including G of phage lambda. This protein has been described as undergoing a translational frameshift at a Gly-Lys dipeptide near the C-terminus of protein G from phage lambda, with about 4 % efficiency, to produce tail assembly protein G-T. The Lys of the Gly-Lys pair is the conserved second-to-last residue of seed alignment for this family. [Mobile and extrachromosomal element functions, Prophage functions]


Pssm-ID: 273748  Cd Length: 138  Bit Score: 211.71  E-value: 5.38e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401298    1 MFLKTESFEHNGVTVTLSELSALQRIEHLALMKRQAEQAESDSNRKFTVEDAIRTGAFLVAMSLWHNHPQK-TQMPSMNE 79
Cdd:TIGR01674   1 MFLKSETFECNGSSVTLFELSALQRIEHLEFLKRQTEKVEVDSDFQAEAEFTVRSGAYLVAMSLWHWHPSKsLQNENASQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446401298   80 AVKQIEQEVLTTWPTEAISHAENVVYRLSGMYEFVVNNAPEQTEDAG-PAEPVSAGK 135
Cdd:TIGR01674  81 DVATIQQEVMTTWPTEALAAAEEKVLLLSGMIAPVIDEATENAEDRGePAEPVTAEK 137
 
Name Accession Description Interval E-value
Phage_TAC_2 pfam06894
Bacteriophage lambda tail assembly chaperone, TAC, protein G; This family consists of ...
 1-126 1.78e-72

Bacteriophage lambda tail assembly chaperone, TAC, protein G; This family consists of Bacteriophage lambda minor tail protein G and related sequences. The construction of phage tails involves a stage of tail-tube formation, and tail-tube polymerization requires two additional proteins, gpG and gpGT. The open reading frames, ORFs, for gpG and gpGT are overlapping and are related by a programmed translational frameshift. During virion morphogenesis, gpG is expressed in large amounts, and about 3.5% of the time, a -1 translational frameshift leads to the production of the larger fusion protein, gpGT. The correct ratio of gpG to gpGT, as determined by the frequency of frameshifting, is crucial for tail assembly. Since gpG accumulates to high levels during a lambda infection and yet is not found in mature phage particles it is believed to act as a chaperone.


Pssm-ID: 284344  Cd Length: 126  Bit Score: 212.48  E-value: 1.78e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401298    1 MFLKTESFEHNGVTVTLSELSALQRIEHLALMKRQAEQAESDSNRKFTVEDAIRTGAFLVAMSLWHNHPQKTQMPSMNEA 80
Cdd:pfam06894   1 MFLKTETFECNGSSVTLFELSALQRIEHLEFIKRQTEAYEVDADRQAAIQMAVKIGAWLVAMSLWHGHPLKGQGENAAEE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 446401298   81 VKQIEQEVLTTWPTEAISHAENVVYRLSGMYEFVVNNAPEQTEDAG 126
Cdd:pfam06894  81 VAKIYQEVMQTWPTEALAEAEYKVLLLSGMAPVIDEPASSGEESGE 126
phage_lambda_G TIGR01674
phage minor tail protein G; This model describes a family of bacteriophage proteins including ...
 1-135 5.38e-72

phage minor tail protein G; This model describes a family of bacteriophage proteins including G of phage lambda. This protein has been described as undergoing a translational frameshift at a Gly-Lys dipeptide near the C-terminus of protein G from phage lambda, with about 4 % efficiency, to produce tail assembly protein G-T. The Lys of the Gly-Lys pair is the conserved second-to-last residue of seed alignment for this family. [Mobile and extrachromosomal element functions, Prophage functions]


Pssm-ID: 273748  Cd Length: 138  Bit Score: 211.71  E-value: 5.38e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446401298    1 MFLKTESFEHNGVTVTLSELSALQRIEHLALMKRQAEQAESDSNRKFTVEDAIRTGAFLVAMSLWHNHPQK-TQMPSMNE 79
Cdd:TIGR01674   1 MFLKSETFECNGSSVTLFELSALQRIEHLEFLKRQTEKVEVDSDFQAEAEFTVRSGAYLVAMSLWHWHPSKsLQNENASQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446401298   80 AVKQIEQEVLTTWPTEAISHAENVVYRLSGMYEFVVNNAPEQTEDAG-PAEPVSAGK 135
Cdd:TIGR01674  81 DVATIQQEVMTTWPTEALAAAEEKVLLLSGMIAPVIDEATENAEDRGePAEPVTAEK 137
 
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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