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Conserved domains on  [gi|2553414138|ref|WP_303047698|]
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major outer sheath C-terminal domain-containing protein, partial [Treponema pallidum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MOSP_C super family cl03676
Major Outer Sheath Protein C-terminal domain; This is a family of spirochete major outer ...
 297-336 8.09e-19

Major Outer Sheath Protein C-terminal domain; This is a family of spirochete major outer sheath protein C-terminal regions. These proteins are present on the bacterial cell surface. In T. denticola the major outer sheath protein (Msp) binds immobilized laminin and fibronectin supporting the hypothesis that Msp mediates the extracellular matrix binding activity of T. denticola. This domain forms an amphipathic beta rich structure with channel forming activity.


The actual alignment was detected with superfamily member pfam02722:

Pssm-ID: 280819  Cd Length: 205  Bit Score: 83.32  E-value: 8.09e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2553414138 297 DALLTAQWKWLSSGIYFATAPANVFGTRVLDNTIASCGDF 336
Cdd:pfam02722   1 DALLTLQWRWLSSGAYFATAPANVFGKRVFPRTMSDHFDC 40
MOSP_N super family cl03668
Major Outer Sheath Protein N-terminal region; This is a family of spirochete major outer ...
 1-32 4.11e-15

Major Outer Sheath Protein N-terminal region; This is a family of spirochete major outer sheath protein N-terminal regions. These proteins are present on the bacterial cell surface. In T. denticola the major outer sheath protein (Msp) binds immobilized laminin and fibronectin supporting the hypothesis that Msp mediates the extracellular matrix binding activity of T. denticola.


The actual alignment was detected with superfamily member pfam02707:

Pssm-ID: 280810  Cd Length: 196  Bit Score: 72.92  E-value: 4.11e-15
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2553414138   1 QNKDKLLWNVGGRLTLEPGAGFRFSFALDAGN 32
Cdd:pfam02707 165 QNKDTLLWNVGGRLTLTPGAGFRFVLALDAGN 196
 
Name Accession Description Interval E-value
MOSP_C pfam02722
Major Outer Sheath Protein C-terminal domain; This is a family of spirochete major outer ...
 297-336 8.09e-19

Major Outer Sheath Protein C-terminal domain; This is a family of spirochete major outer sheath protein C-terminal regions. These proteins are present on the bacterial cell surface. In T. denticola the major outer sheath protein (Msp) binds immobilized laminin and fibronectin supporting the hypothesis that Msp mediates the extracellular matrix binding activity of T. denticola. This domain forms an amphipathic beta rich structure with channel forming activity.


Pssm-ID: 280819  Cd Length: 205  Bit Score: 83.32  E-value: 8.09e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2553414138 297 DALLTAQWKWLSSGIYFATAPANVFGTRVLDNTIASCGDF 336
Cdd:pfam02722   1 DALLTLQWRWLSSGAYFATAPANVFGKRVFPRTMSDHFDC 40
MOSP_N pfam02707
Major Outer Sheath Protein N-terminal region; This is a family of spirochete major outer ...
 1-32 4.11e-15

Major Outer Sheath Protein N-terminal region; This is a family of spirochete major outer sheath protein N-terminal regions. These proteins are present on the bacterial cell surface. In T. denticola the major outer sheath protein (Msp) binds immobilized laminin and fibronectin supporting the hypothesis that Msp mediates the extracellular matrix binding activity of T. denticola.


Pssm-ID: 280810  Cd Length: 196  Bit Score: 72.92  E-value: 4.11e-15
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2553414138   1 QNKDKLLWNVGGRLTLEPGAGFRFSFALDAGN 32
Cdd:pfam02707 165 QNKDTLLWNVGGRLTLTPGAGFRFVLALDAGN 196
 
Name Accession Description Interval E-value
MOSP_C pfam02722
Major Outer Sheath Protein C-terminal domain; This is a family of spirochete major outer ...
 297-336 8.09e-19

Major Outer Sheath Protein C-terminal domain; This is a family of spirochete major outer sheath protein C-terminal regions. These proteins are present on the bacterial cell surface. In T. denticola the major outer sheath protein (Msp) binds immobilized laminin and fibronectin supporting the hypothesis that Msp mediates the extracellular matrix binding activity of T. denticola. This domain forms an amphipathic beta rich structure with channel forming activity.


Pssm-ID: 280819  Cd Length: 205  Bit Score: 83.32  E-value: 8.09e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2553414138 297 DALLTAQWKWLSSGIYFATAPANVFGTRVLDNTIASCGDF 336
Cdd:pfam02722   1 DALLTLQWRWLSSGAYFATAPANVFGKRVFPRTMSDHFDC 40
MOSP_N pfam02707
Major Outer Sheath Protein N-terminal region; This is a family of spirochete major outer ...
 1-32 4.11e-15

Major Outer Sheath Protein N-terminal region; This is a family of spirochete major outer sheath protein N-terminal regions. These proteins are present on the bacterial cell surface. In T. denticola the major outer sheath protein (Msp) binds immobilized laminin and fibronectin supporting the hypothesis that Msp mediates the extracellular matrix binding activity of T. denticola.


Pssm-ID: 280810  Cd Length: 196  Bit Score: 72.92  E-value: 4.11e-15
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2553414138   1 QNKDKLLWNVGGRLTLEPGAGFRFSFALDAGN 32
Cdd:pfam02707 165 QNKDTLLWNVGGRLTLTPGAGFRFVLALDAGN 196
 
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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