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Conserved domains on  [gi|1842008944|ref|YP_009796119|]
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tail spike protein [Escherichia phage VEc3]

Protein Classification

tail fiber domain-containing protein( domain architecture ID 14409641)

tail fiber domain-containing protein similar to Enterobacteria phage long tail fiber protein p37, a structural component of the distal-half tail fiber, and to the C-terminal chaperone domain of Escherichia coli phage K1F endosialidase, a S74 family serine endopeptidase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_S74_CIMCD cd10144
Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F ...
 505-618 4.91e-51

Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F endosialidase and related proteins; This peptidase S74 family includes C-terminal intramolecular chaperone domain (CIMCD) of Escherichia coli phage K1F endosialidase, Bacillus phage GA-1 neck appendage protein, and Bacteriophage T5 L-shaped tail fibre. This domain acts as a molecular chaperone; during virus particle assembly, the CIMCD of phage tailspike proteins induces the homo-trimerization of phage tailspike proteins by chaperoning the formation of a triple beta-helix. Homo-trimeric phage tailspike proteins are then auto-cleaved by the CIMCD domain. This family also includes the peptidase S74 Intramolecular Chaperone Auto-processing (ICA) domain of mammalian Myrf. The ICA domain drives the homo-oligomerization of Myrf in the endoplasmic reticulum (ER) membrane. The homo-oligomeric Myrf is proteolyzed by the ICA domain, releasing its N-terminal fragments from the ER membrane.


:

Pssm-ID: 381748 [Multi-domain]  Cd Length: 113  Bit Score: 171.74  E-value: 4.91e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842008944 505 SDARCKTEPLTISDALLDAWSEVDFVQFQYLDRVEEKGaDSARWHFGIIAQRAKEAFERHGIDAHRYGFLCFDSWDDVYE 584
Cdd:cd10144     1 SDARLKTEIREIDDAELDAWKKVRFVQYKWKEAVAEKG-DDARLHFGVIAQEVIAAFEDAGLDAGKYGILCYDEWDAVTD 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1842008944 585 EDANgSRKLITPAGSRYGIRYEEVLILEAALMRR 618
Cdd:cd10144    80 EVIT-MENVGIEAGERYGTRYDELLIFEAAAQRR 112
 
Name Accession Description Interval E-value
Peptidase_S74_CIMCD cd10144
Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F ...
 505-618 4.91e-51

Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F endosialidase and related proteins; This peptidase S74 family includes C-terminal intramolecular chaperone domain (CIMCD) of Escherichia coli phage K1F endosialidase, Bacillus phage GA-1 neck appendage protein, and Bacteriophage T5 L-shaped tail fibre. This domain acts as a molecular chaperone; during virus particle assembly, the CIMCD of phage tailspike proteins induces the homo-trimerization of phage tailspike proteins by chaperoning the formation of a triple beta-helix. Homo-trimeric phage tailspike proteins are then auto-cleaved by the CIMCD domain. This family also includes the peptidase S74 Intramolecular Chaperone Auto-processing (ICA) domain of mammalian Myrf. The ICA domain drives the homo-oligomerization of Myrf in the endoplasmic reticulum (ER) membrane. The homo-oligomeric Myrf is proteolyzed by the ICA domain, releasing its N-terminal fragments from the ER membrane.


Pssm-ID: 381748 [Multi-domain]  Cd Length: 113  Bit Score: 171.74  E-value: 4.91e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842008944 505 SDARCKTEPLTISDALLDAWSEVDFVQFQYLDRVEEKGaDSARWHFGIIAQRAKEAFERHGIDAHRYGFLCFDSWDDVYE 584
Cdd:cd10144     1 SDARLKTEIREIDDAELDAWKKVRFVQYKWKEAVAEKG-DDARLHFGVIAQEVIAAFEDAGLDAGKYGILCYDEWDAVTD 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1842008944 585 EDANgSRKLITPAGSRYGIRYEEVLILEAALMRR 618
Cdd:cd10144    80 EVIT-MENVGIEAGERYGTRYDELLIFEAAAQRR 112
Peptidase_S74 pfam13884
Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the ...
 505-562 5.78e-13

Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the bacteriophage protein endosialidase. It releases itself, via the serine-lysine dyad at the N-terminus, from the remainder of the end-tail-spike. Cleavage occurs after the threonine which is the final residue of the End-tail-spike family, pfam12219. The endosialidase protein forms homotrimeric molecules in bacteriophages. The catalytic dyad allows this portion of the molecule to be cleaved from the more N-terminal region such that the latter can fold and bind to polysialic acid in the bacterial outer envelope.


Pssm-ID: 404724  Cd Length: 56  Bit Score: 63.80  E-value: 5.78e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1842008944 505 SDARCKTEPLTISDALLDAWSEVDFVQFQYLDrveEKGADSARWHFGIIAQRAKEAFE 562
Cdd:pfam13884   1 SDRRLKTNIKPIDENALDKIEQLEPVSYDYKD---EKGEDGARRHIGVIAQEVEEVFP 55
 
Name Accession Description Interval E-value
Peptidase_S74_CIMCD cd10144
Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F ...
 505-618 4.91e-51

Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F endosialidase and related proteins; This peptidase S74 family includes C-terminal intramolecular chaperone domain (CIMCD) of Escherichia coli phage K1F endosialidase, Bacillus phage GA-1 neck appendage protein, and Bacteriophage T5 L-shaped tail fibre. This domain acts as a molecular chaperone; during virus particle assembly, the CIMCD of phage tailspike proteins induces the homo-trimerization of phage tailspike proteins by chaperoning the formation of a triple beta-helix. Homo-trimeric phage tailspike proteins are then auto-cleaved by the CIMCD domain. This family also includes the peptidase S74 Intramolecular Chaperone Auto-processing (ICA) domain of mammalian Myrf. The ICA domain drives the homo-oligomerization of Myrf in the endoplasmic reticulum (ER) membrane. The homo-oligomeric Myrf is proteolyzed by the ICA domain, releasing its N-terminal fragments from the ER membrane.


Pssm-ID: 381748 [Multi-domain]  Cd Length: 113  Bit Score: 171.74  E-value: 4.91e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842008944 505 SDARCKTEPLTISDALLDAWSEVDFVQFQYLDRVEEKGaDSARWHFGIIAQRAKEAFERHGIDAHRYGFLCFDSWDDVYE 584
Cdd:cd10144     1 SDARLKTEIREIDDAELDAWKKVRFVQYKWKEAVAEKG-DDARLHFGVIAQEVIAAFEDAGLDAGKYGILCYDEWDAVTD 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1842008944 585 EDANgSRKLITPAGSRYGIRYEEVLILEAALMRR 618
Cdd:cd10144    80 EVIT-MENVGIEAGERYGTRYDELLIFEAAAQRR 112
Peptidase_S74 pfam13884
Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the ...
 505-562 5.78e-13

Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the bacteriophage protein endosialidase. It releases itself, via the serine-lysine dyad at the N-terminus, from the remainder of the end-tail-spike. Cleavage occurs after the threonine which is the final residue of the End-tail-spike family, pfam12219. The endosialidase protein forms homotrimeric molecules in bacteriophages. The catalytic dyad allows this portion of the molecule to be cleaved from the more N-terminal region such that the latter can fold and bind to polysialic acid in the bacterial outer envelope.


Pssm-ID: 404724  Cd Length: 56  Bit Score: 63.80  E-value: 5.78e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1842008944 505 SDARCKTEPLTISDALLDAWSEVDFVQFQYLDrveEKGADSARWHFGIIAQRAKEAFE 562
Cdd:pfam13884   1 SDRRLKTNIKPIDENALDKIEQLEPVSYDYKD---EKGEDGARRHIGVIAQEVEEVFP 55
 
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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