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Conserved domains on  [gi|2781191]
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Chain B, FIBRITIN

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Fibritin_C super family cl44324
Fibritin C-terminal region; This family features sequences bearing similarity to the ...
 1-70 1.59e-12

Fibritin C-terminal region; This family features sequences bearing similarity to the C-terminal portion of the bacteriophage T4 protein fibritin. This protein is responsible for attachment of long tail fibres to virus particle, and forms the 'whiskers' or fibres on the neck of the virion. The region seen in this family contains an N-terminal coiled-coil portion and the C-terminal globular foldon domain (residues 457-486), which is essential for fibritin trimerization and folding. This domain consists of a beta-hairpin; three such hairpins come together in a beta-propeller-like arrangement in the trimer, which is stabilized by hydrogen bonds, salt bridges and hydrophobic interactions.


The actual alignment was detected with superfamily member pfam07921:

Pssm-ID: 254516 [Multi-domain]  Cd Length: 93  Bit Score: 57.08  E-value: 1.59e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781191     1 VEESGLTNKIKAIETDIAsvrqevntakgnisslqgdVQALQEAGYIPEAPRDGQAYVRKDGEWVLLSTF 70
Cdd:pfam07921 43 FEERGIKKTVKDLETTIG-------------------VQALQESGKIDDAPDDGRWYVRKDGAWVLLSSI 93
 
Name Accession Description Interval E-value
Fibritin_C pfam07921
Fibritin C-terminal region; This family features sequences bearing similarity to the ...
 1-70 1.59e-12

Fibritin C-terminal region; This family features sequences bearing similarity to the C-terminal portion of the bacteriophage T4 protein fibritin. This protein is responsible for attachment of long tail fibres to virus particle, and forms the 'whiskers' or fibres on the neck of the virion. The region seen in this family contains an N-terminal coiled-coil portion and the C-terminal globular foldon domain (residues 457-486), which is essential for fibritin trimerization and folding. This domain consists of a beta-hairpin; three such hairpins come together in a beta-propeller-like arrangement in the trimer, which is stabilized by hydrogen bonds, salt bridges and hydrophobic interactions.


Pssm-ID: 254516 [Multi-domain]  Cd Length: 93  Bit Score: 57.08  E-value: 1.59e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781191     1 VEESGLTNKIKAIETDIAsvrqevntakgnisslqgdVQALQEAGYIPEAPRDGQAYVRKDGEWVLLSTF 70
Cdd:pfam07921 43 FEERGIKKTVKDLETTIG-------------------VQALQESGKIDDAPDDGRWYVRKDGAWVLLSSI 93
wac PHA02607
fibritin; Provisional
 1-74 6.47e-11

fibritin; Provisional


Pssm-ID: 177432 [Multi-domain]  Cd Length: 454  Bit Score: 55.80  E-value: 6.47e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2781191     1 VEESGLTNKIKAIETDIAsvrqevntakgnisslqgdvqalqeaGYIPEAPRDGQAYVRKDGEWVLLSTFLSPA 74
Cdd:PHA02607 407 FEERGLKKTVKDLETQIA--------------------------GKLDDAPSDGSWYVRKNGAWVEVSTGLSPV 454
 
Name Accession Description Interval E-value
Fibritin_C pfam07921
Fibritin C-terminal region; This family features sequences bearing similarity to the ...
 1-70 1.59e-12

Fibritin C-terminal region; This family features sequences bearing similarity to the C-terminal portion of the bacteriophage T4 protein fibritin. This protein is responsible for attachment of long tail fibres to virus particle, and forms the 'whiskers' or fibres on the neck of the virion. The region seen in this family contains an N-terminal coiled-coil portion and the C-terminal globular foldon domain (residues 457-486), which is essential for fibritin trimerization and folding. This domain consists of a beta-hairpin; three such hairpins come together in a beta-propeller-like arrangement in the trimer, which is stabilized by hydrogen bonds, salt bridges and hydrophobic interactions.


Pssm-ID: 254516 [Multi-domain]  Cd Length: 93  Bit Score: 57.08  E-value: 1.59e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781191     1 VEESGLTNKIKAIETDIAsvrqevntakgnisslqgdVQALQEAGYIPEAPRDGQAYVRKDGEWVLLSTF 70
Cdd:pfam07921 43 FEERGIKKTVKDLETTIG-------------------VQALQESGKIDDAPDDGRWYVRKDGAWVLLSSI 93
wac PHA02607
fibritin; Provisional
 1-74 6.47e-11

fibritin; Provisional


Pssm-ID: 177432 [Multi-domain]  Cd Length: 454  Bit Score: 55.80  E-value: 6.47e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2781191     1 VEESGLTNKIKAIETDIAsvrqevntakgnisslqgdvqalqeaGYIPEAPRDGQAYVRKDGEWVLLSTFLSPA 74
Cdd:PHA02607 407 FEERGLKKTVKDLETQIA--------------------------GKLDDAPSDGSWYVRKNGAWVEVSTGLSPV 454
 
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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