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Conserved domains on  [gi|515667813|ref|WP_017100413|]
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MULTISPECIES: major capsid protein P2 [Vibrio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P2_N pfam18628
Viral coat protein P2 N-terminal domain; P2 (30.2 kDa) is the major outer-coat protein of the ...
 5-133 6.41e-39

Viral coat protein P2 N-terminal domain; P2 (30.2 kDa) is the major outer-coat protein of the marine lipid-containing bacteriophage PM2. Each sub-unit of P2 is composed of two beta barrel jelly rolls, disposed normal to the surface of the capsid, which lend pseudo-6-fold symmetry to the molecules, facilitating their close packing within the capsid. There is a Ca2+ ion located between the two beta barrels of P2 that helps PM2 molecular organizations stabilization. This entry represents the N-terminal jelly roll domain of P2.


:

Pssm-ID: 436633  Cd Length: 127  Bit Score: 132.40  E-value: 6.41e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667813    5 PIKLNSMVGASWGQKGTLPIPNGPTYHELVLETNASA-ADMQRIAITLNAEEIYVLTGEELVMLERYKQRDATAGHFVIP 83
Cdd:pfam18628   1 PQKLPSFSNVVAGGTATLTLPIGPTYHRIELELGGTTkADITDIRVKLNGKPIIQVTGQDLDKLNAYKGLYADAGRLVID 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 515667813   84 FSDIVARTKNGVRYTGLVTELGDNIHLDIQFKGKAANATplsIQVHAWVS 133
Cdd:pfam18628  81 FTDISARTLEGQRLGALVTTNIDNFTLEITIAGAATAPT---LKAWAEVS 127
 
Name Accession Description Interval E-value
P2_N pfam18628
Viral coat protein P2 N-terminal domain; P2 (30.2 kDa) is the major outer-coat protein of the ...
 5-133 6.41e-39

Viral coat protein P2 N-terminal domain; P2 (30.2 kDa) is the major outer-coat protein of the marine lipid-containing bacteriophage PM2. Each sub-unit of P2 is composed of two beta barrel jelly rolls, disposed normal to the surface of the capsid, which lend pseudo-6-fold symmetry to the molecules, facilitating their close packing within the capsid. There is a Ca2+ ion located between the two beta barrels of P2 that helps PM2 molecular organizations stabilization. This entry represents the N-terminal jelly roll domain of P2.


Pssm-ID: 436633  Cd Length: 127  Bit Score: 132.40  E-value: 6.41e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667813    5 PIKLNSMVGASWGQKGTLPIPNGPTYHELVLETNASA-ADMQRIAITLNAEEIYVLTGEELVMLERYKQRDATAGHFVIP 83
Cdd:pfam18628   1 PQKLPSFSNVVAGGTATLTLPIGPTYHRIELELGGTTkADITDIRVKLNGKPIIQVTGQDLDKLNAYKGLYADAGRLVID 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 515667813   84 FSDIVARTKNGVRYTGLVTELGDNIHLDIQFKGKAANATplsIQVHAWVS 133
Cdd:pfam18628  81 FTDISARTLEGQRLGALVTTNIDNFTLEITIAGAATAPT---LKAWAEVS 127
 
Name Accession Description Interval E-value
P2_N pfam18628
Viral coat protein P2 N-terminal domain; P2 (30.2 kDa) is the major outer-coat protein of the ...
 5-133 6.41e-39

Viral coat protein P2 N-terminal domain; P2 (30.2 kDa) is the major outer-coat protein of the marine lipid-containing bacteriophage PM2. Each sub-unit of P2 is composed of two beta barrel jelly rolls, disposed normal to the surface of the capsid, which lend pseudo-6-fold symmetry to the molecules, facilitating their close packing within the capsid. There is a Ca2+ ion located between the two beta barrels of P2 that helps PM2 molecular organizations stabilization. This entry represents the N-terminal jelly roll domain of P2.


Pssm-ID: 436633  Cd Length: 127  Bit Score: 132.40  E-value: 6.41e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515667813    5 PIKLNSMVGASWGQKGTLPIPNGPTYHELVLETNASA-ADMQRIAITLNAEEIYVLTGEELVMLERYKQRDATAGHFVIP 83
Cdd:pfam18628   1 PQKLPSFSNVVAGGTATLTLPIGPTYHRIELELGGTTkADITDIRVKLNGKPIIQVTGQDLDKLNAYKGLYADAGRLVID 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 515667813   84 FSDIVARTKNGVRYTGLVTELGDNIHLDIQFKGKAANATplsIQVHAWVS 133
Cdd:pfam18628  81 FTDISARTLEGQRLGALVTTNIDNFTLEITIAGAATAPT---LKAWAEVS 127
 
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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