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Conserved domains on  [gi|835428317|ref|WP_047502771|]
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hypothetical protein, partial [Citrobacter braakii]

Protein Classification

tail fiber domain-containing protein( domain architecture ID 82077)

tail fiber domain-containing protein similar to Enterobacteria phage long tail fiber protein p37, a structural component of the distal-half tail fiber

Gene Ontology:  GO:0098024|GO:0019062|GO:0046718
MEROPS:  S74
PubMed:  17158460

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_S74_CIMCD super family cl16452
Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F ...
22-73 6.71e-05

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.


The actual alignment was detected with superfamily member cd10144:

Pssm-ID: 418048 [Multi-domain]  Cd Length: 113  Bit Score: 38.46  E-value: 6.71e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 835428317  22 DALQYKLVN-DEFVPEIEEVEEtvMIPVRKSAGIRLGLRYTECLIFEAAYQRS 73
Cdd:cd10144   62 DAGKYGILCyDEWDAVTDEVIT--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 ...
22-73 6.71e-05

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: 38.46  E-value: 6.71e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 835428317  22 DALQYKLVN-DEFVPEIEEVEEtvMIPVRKSAGIRLGLRYTECLIFEAAYQRS 73
Cdd:cd10144   62 DAGKYGILCyDEWDAVTDEVIT--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 ...
22-73 6.71e-05

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: 38.46  E-value: 6.71e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 835428317  22 DALQYKLVN-DEFVPEIEEVEEtvMIPVRKSAGIRLGLRYTECLIFEAAYQRS 73
Cdd:cd10144   62 DAGKYGILCyDEWDAVTDEVIT--MENVGIEAGERYGTRYDELLIFEAAAQRR 112
 
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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