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Conserved domains on  [gi|1035745627|ref|WP_064580073|]
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phage tail assembly chaperone G, partial [Escherichia coli]

Protein Classification

phage minor tail protein G( domain architecture ID 10019799)

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_lambda_G TIGR01674
phage minor tail protein G; This model describes a family of bacteriophage proteins including ...
 1-130 8.21e-65

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: 193.60  E-value: 8.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035745627   1 ESFEHNGVTVTLSELSALQRIEHLALMKRQAEQAESDSNRKFTVEDAIRTGAFLVAMSLWHNHPQK-TKLPSMNEAVKQI 79
Cdd:TIGR01674   6 ETFECNGSSVTLFELSALQRIEHLEFLKRQTEKVEVDSDFQAEAEFTVRSGAYLVAMSLWHWHPSKsLQNENASQDVATI 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1035745627  80 EQEVLTTWPTEAISHAENVVYRLSGMYEFVVNDAPEQAEDAGS-AEPVSAGK 130
Cdd:TIGR01674  86 QQEVMTTWPTEALAAAEEKVLLLSGMIAPVIDEATENAEDRGEpAEPVTAEK 137
 
Name Accession Description Interval E-value
phage_lambda_G TIGR01674
phage minor tail protein G; This model describes a family of bacteriophage proteins including ...
 1-130 8.21e-65

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: 193.60  E-value: 8.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035745627   1 ESFEHNGVTVTLSELSALQRIEHLALMKRQAEQAESDSNRKFTVEDAIRTGAFLVAMSLWHNHPQK-TKLPSMNEAVKQI 79
Cdd:TIGR01674   6 ETFECNGSSVTLFELSALQRIEHLEFLKRQTEKVEVDSDFQAEAEFTVRSGAYLVAMSLWHWHPSKsLQNENASQDVATI 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1035745627  80 EQEVLTTWPTEAISHAENVVYRLSGMYEFVVNDAPEQAEDAGS-AEPVSAGK 130
Cdd:TIGR01674  86 QQEVMTTWPTEALAAAEEKVLLLSGMIAPVIDEATENAEDRGEpAEPVTAEK 137
Phage_TAC_2 pfam06894
Bacteriophage lambda tail assembly chaperone, TAC, protein G; This family consists of ...
 1-121 1.30e-64

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: 192.44  E-value: 1.30e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035745627   1 ESFEHNGVTVTLSELSALQRIEHLALMKRQAEQAESDSNRKFTVEDAIRTGAFLVAMSLWHNHPQKTKLPSMNEAVKQIE 80
Cdd:pfam06894   6 ETFECNGSSVTLFELSALQRIEHLEFIKRQTEAYEVDADRQAAIQMAVKIGAWLVAMSLWHGHPLKGQGENAAEEVAKIY 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1035745627  81 QEVLTTWPTEAISHAENVVYRLSGMYEFVVNDAPEQAEDAG 121
Cdd:pfam06894  86 QEVMQTWPTEALAEAEYKVLLLSGMAPVIDEPASSGEESGE 126
 
Name Accession Description Interval E-value
phage_lambda_G TIGR01674
phage minor tail protein G; This model describes a family of bacteriophage proteins including ...
 1-130 8.21e-65

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: 193.60  E-value: 8.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035745627   1 ESFEHNGVTVTLSELSALQRIEHLALMKRQAEQAESDSNRKFTVEDAIRTGAFLVAMSLWHNHPQK-TKLPSMNEAVKQI 79
Cdd:TIGR01674   6 ETFECNGSSVTLFELSALQRIEHLEFLKRQTEKVEVDSDFQAEAEFTVRSGAYLVAMSLWHWHPSKsLQNENASQDVATI 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1035745627  80 EQEVLTTWPTEAISHAENVVYRLSGMYEFVVNDAPEQAEDAGS-AEPVSAGK 130
Cdd:TIGR01674  86 QQEVMTTWPTEALAAAEEKVLLLSGMIAPVIDEATENAEDRGEpAEPVTAEK 137
Phage_TAC_2 pfam06894
Bacteriophage lambda tail assembly chaperone, TAC, protein G; This family consists of ...
 1-121 1.30e-64

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: 192.44  E-value: 1.30e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035745627   1 ESFEHNGVTVTLSELSALQRIEHLALMKRQAEQAESDSNRKFTVEDAIRTGAFLVAMSLWHNHPQKTKLPSMNEAVKQIE 80
Cdd:pfam06894   6 ETFECNGSSVTLFELSALQRIEHLEFIKRQTEAYEVDADRQAAIQMAVKIGAWLVAMSLWHGHPLKGQGENAAEEVAKIY 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1035745627  81 QEVLTTWPTEAISHAENVVYRLSGMYEFVVNDAPEQAEDAG 121
Cdd:pfam06894  86 QEVMQTWPTEALAEAEYKVLLLSGMAPVIDEPASSGEESGE 126
 
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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