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Conserved domains on  [gi|447012750|ref|WP_001090006|]
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tail assembly protein [Escherichia coli]

Protein Classification

tail assembly protein( domain architecture ID 10008749)

tail assembly protein similar to Enterobacteria phage tail tip assembly protein I (TAPI), which plays a role in distal tail tip complex assembly

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4723 COG4723
Phage-related protein, tail assembly protein I [Mobilome: prophages, transposons];
2-181 1.12e-56

Phage-related protein, tail assembly protein I [Mobilome: prophages, transposons];


:

Pssm-ID: 443758  Cd Length: 197  Bit Score: 177.41  E-value: 1.12e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447012750   2 NTAAEAIRALSLQVPGFRRQMNEG-----WYQIRIRGEDTAPEAvyarLHEPLGeGAVIHIVPRLAGAGKGGL-QIVLGA 75
Cdd:COG4723   24 ASPAEAIRALCVTIPGFEQFMRTShkrglTYAVFRGKRNIGEDE----LELPVG-GADIRIVPVIIGAKRGGLfQTILGA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447012750  76 AAIVGSFFTAGASMALWGSALAAggfsattMLFSLGASMILGGVAQMLAPKAKVPEYKSTDNGRQNTYFSSLDNMIAQGN 155
Cdd:COG4723   99 ALIVAAFFFGGGSLAAFGGGAAG-------ALAMLGASMALGGVVQMLSPQPKGLSSRQSPDNKPSYAFGGPVNTTAQGN 171

                        170       180
                 ....*....|....*....|....*.
gi 447012750 156 PMPVPYGEMLVGSRRISQDISTRDEG 181
Cdd:COG4723  172 PVPLLYGERRIGGAVISAGIYAEDQQ 197
 
Name Accession Description Interval E-value
COG4723 COG4723
Phage-related protein, tail assembly protein I [Mobilome: prophages, transposons];
2-181 1.12e-56

Phage-related protein, tail assembly protein I [Mobilome: prophages, transposons];


Pssm-ID: 443758  Cd Length: 197  Bit Score: 177.41  E-value: 1.12e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447012750   2 NTAAEAIRALSLQVPGFRRQMNEG-----WYQIRIRGEDTAPEAvyarLHEPLGeGAVIHIVPRLAGAGKGGL-QIVLGA 75
Cdd:COG4723   24 ASPAEAIRALCVTIPGFEQFMRTShkrglTYAVFRGKRNIGEDE----LELPVG-GADIRIVPVIIGAKRGGLfQTILGA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447012750  76 AAIVGSFFTAGASMALWGSALAAggfsattMLFSLGASMILGGVAQMLAPKAKVPEYKSTDNGRQNTYFSSLDNMIAQGN 155
Cdd:COG4723   99 ALIVAAFFFGGGSLAAFGGGAAG-------ALAMLGASMALGGVVQMLSPQPKGLSSRQSPDNKPSYAFGGPVNTTAQGN 171

                        170       180
                 ....*....|....*....|....*.
gi 447012750 156 PMPVPYGEMLVGSRRISQDISTRDEG 181
Cdd:COG4723  172 PVPLLYGERRIGGAVISAGIYAEDQQ 197
Lambda_tail_I pfam06805
Bacteriophage lambda tail assembly protein I; This family consists of tail assembly proteins ...
 3-64 2.47e-04

Bacteriophage lambda tail assembly protein I; This family consists of tail assembly proteins from lambdoid and T1 phages and related prophages, e.g. the tail assembly protein I (TAPI). Members of this family contain a core ubiquitin fold domain. The exact function of TAPI is not clear but it is not incorporated into the mature tail. Gene neighborhoods reveal that TAPI co-occurs with genes encoding the host-specificity protein TapJ, and TapK, which contains a JAB metallopeptidase fused to an NlpC/P60 peptidase. It is proposed that the TAPI protein is processed by the peptidase domains of TapK.


Pssm-ID: 284272  Cd Length: 82  Bit Score: 38.32  E-value: 2.47e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447012750    3 TAAEAIRALSLQVPGFRRqmnegWYQIRIRGEDTAPEAVYARLHEPLGEGAVIHIVPRLAGA 64
Cdd:pfam06805  26 TLGEAIRALGIQEDCFEA-----LSDGPEAGVDGMTVPVGIYAVETIVDGEVVTIVPWPAGG 82
ClyA_AhlB-like cd22652
Aeromonas hydrophila hemolytic component B (AhlB), and similar proteins; This model includes ...
 62-100 9.22e-03

Aeromonas hydrophila hemolytic component B (AhlB), and similar proteins; This model includes Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). It consists of three proteins, AhlA, AhlB and AhlC, encoded by one operon containing the three genes. Functional and mutagenic studies support a model of pore assembly where the soluble tetrameric form of AhlC first disassociates into monomers, binds a single membrane leaflet, and then recruits AhlB to promote soluble to pore transition; AhlA then binds to form the active hydrophilic lined pore. The structure of AhlB shows an elongated, almost entirely alpha-helical protein, including a hydrophobic beta-hairpin known as a beta-tongue to shield membrane inserting hydrophobic residues. The head domain of AhlB undergoes a large conformational change involving the beta tongue becoming an extended alpha helix, and the tail domain helices sliding relative to one another as AhlB assembles into a hydrophobic pore.


Pssm-ID: 439150 [Multi-domain]  Cd Length: 332  Bit Score: 36.05  E-value: 9.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 447012750  62 AGAGKGGLQIVLGAAAI----VGSFFTAGASMAL--WGSALAAGG 100
Cdd:cd22652  173 AGIVLSGLAIIGGVFMIavgaVASFVTAGTSTPLviGGVAVVAAG 217
 
Name Accession Description Interval E-value
COG4723 COG4723
Phage-related protein, tail assembly protein I [Mobilome: prophages, transposons];
2-181 1.12e-56

Phage-related protein, tail assembly protein I [Mobilome: prophages, transposons];


Pssm-ID: 443758  Cd Length: 197  Bit Score: 177.41  E-value: 1.12e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447012750   2 NTAAEAIRALSLQVPGFRRQMNEG-----WYQIRIRGEDTAPEAvyarLHEPLGeGAVIHIVPRLAGAGKGGL-QIVLGA 75
Cdd:COG4723   24 ASPAEAIRALCVTIPGFEQFMRTShkrglTYAVFRGKRNIGEDE----LELPVG-GADIRIVPVIIGAKRGGLfQTILGA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447012750  76 AAIVGSFFTAGASMALWGSALAAggfsattMLFSLGASMILGGVAQMLAPKAKVPEYKSTDNGRQNTYFSSLDNMIAQGN 155
Cdd:COG4723   99 ALIVAAFFFGGGSLAAFGGGAAG-------ALAMLGASMALGGVVQMLSPQPKGLSSRQSPDNKPSYAFGGPVNTTAQGN 171

                        170       180
                 ....*....|....*....|....*.
gi 447012750 156 PMPVPYGEMLVGSRRISQDISTRDEG 181
Cdd:COG4723  172 PVPLLYGERRIGGAVISAGIYAEDQQ 197
Lambda_tail_I pfam06805
Bacteriophage lambda tail assembly protein I; This family consists of tail assembly proteins ...
 3-64 2.47e-04

Bacteriophage lambda tail assembly protein I; This family consists of tail assembly proteins from lambdoid and T1 phages and related prophages, e.g. the tail assembly protein I (TAPI). Members of this family contain a core ubiquitin fold domain. The exact function of TAPI is not clear but it is not incorporated into the mature tail. Gene neighborhoods reveal that TAPI co-occurs with genes encoding the host-specificity protein TapJ, and TapK, which contains a JAB metallopeptidase fused to an NlpC/P60 peptidase. It is proposed that the TAPI protein is processed by the peptidase domains of TapK.


Pssm-ID: 284272  Cd Length: 82  Bit Score: 38.32  E-value: 2.47e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447012750    3 TAAEAIRALSLQVPGFRRqmnegWYQIRIRGEDTAPEAVYARLHEPLGEGAVIHIVPRLAGA 64
Cdd:pfam06805  26 TLGEAIRALGIQEDCFEA-----LSDGPEAGVDGMTVPVGIYAVETIVDGEVVTIVPWPAGG 82
ClyA_AhlB-like cd22652
Aeromonas hydrophila hemolytic component B (AhlB), and similar proteins; This model includes ...
 62-100 9.22e-03

Aeromonas hydrophila hemolytic component B (AhlB), and similar proteins; This model includes Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). It consists of three proteins, AhlA, AhlB and AhlC, encoded by one operon containing the three genes. Functional and mutagenic studies support a model of pore assembly where the soluble tetrameric form of AhlC first disassociates into monomers, binds a single membrane leaflet, and then recruits AhlB to promote soluble to pore transition; AhlA then binds to form the active hydrophilic lined pore. The structure of AhlB shows an elongated, almost entirely alpha-helical protein, including a hydrophobic beta-hairpin known as a beta-tongue to shield membrane inserting hydrophobic residues. The head domain of AhlB undergoes a large conformational change involving the beta tongue becoming an extended alpha helix, and the tail domain helices sliding relative to one another as AhlB assembles into a hydrophobic pore.


Pssm-ID: 439150 [Multi-domain]  Cd Length: 332  Bit Score: 36.05  E-value: 9.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 447012750  62 AGAGKGGLQIVLGAAAI----VGSFFTAGASMAL--WGSALAAGG 100
Cdd:cd22652  173 AGIVLSGLAIIGGVFMIavgaVASFVTAGTSTPLviGGVAVVAAG 217
 
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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