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Conserved domains on  [gi|2553414234|ref|WP_303047794|]
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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 ...
 2-103 1.82e-39

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: 129.93  E-value: 1.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553414234   2 RTYMPVHYKVLKaQARAGAAVPAAVNNDIYFPVYGKVWGSYRHDMGEYGWVKVYANLYGGTNKKNDAAP--------TKW 73
Cdd:pfam02722  68 RLYIPLTHGLYK-NNGGYALPPVHPGGHINLPVVGKVWLSYRIPLGEHAWLKPYVSVYGTTNRFNGNSKatngaagaTKL 146

                          90       100       110
                  ....*....|....*....|....*....|
gi 2553414234  74 SKEYCGYYECGVVVSPLEKVEIRLSWEQGK 103
Cdd:pfam02722 147 LAEYCLQYQVGVTVSPIEKVELSAQWEQGM 176
 
Name Accession Description Interval E-value
MOSP_C pfam02722
Major Outer Sheath Protein C-terminal domain; This is a family of spirochete major outer ...
 2-103 1.82e-39

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: 129.93  E-value: 1.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553414234   2 RTYMPVHYKVLKaQARAGAAVPAAVNNDIYFPVYGKVWGSYRHDMGEYGWVKVYANLYGGTNKKNDAAP--------TKW 73
Cdd:pfam02722  68 RLYIPLTHGLYK-NNGGYALPPVHPGGHINLPVVGKVWLSYRIPLGEHAWLKPYVSVYGTTNRFNGNSKatngaagaTKL 146

                          90       100       110
                  ....*....|....*....|....*....|
gi 2553414234  74 SKEYCGYYECGVVVSPLEKVEIRLSWEQGK 103
Cdd:pfam02722 147 LAEYCLQYQVGVTVSPIEKVELSAQWEQGM 176
msp_porin NF033926
MSP porin; Members of this HMM are MSP porins (major outer sheath proteins) in Treponema. They ...
 28-103 4.78e-32

MSP porin; Members of this HMM are MSP porins (major outer sheath proteins) in Treponema. They may play a role in immune evasion and persistence.


Pssm-ID: 468249 [Multi-domain]  Cd Length: 512  Bit Score: 116.82  E-value: 4.78e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553414234  28 NDIYFPVYGKVWGSYRHDMGEYGWVKVYANLYGGTNKKNDAAPTKWSKEYCG-YYECGVVVSPLEKVEIRLSWEQGK 103
Cdd:NF033926  402 KYAKFPLGLKVWGSYKYNLTDSMWVKPYANFWGETNHDHVDPDKSKDKLYFGlAYEVGVTFSPVEKVEIDASWEHGK 478
 
Name Accession Description Interval E-value
MOSP_C pfam02722
Major Outer Sheath Protein C-terminal domain; This is a family of spirochete major outer ...
 2-103 1.82e-39

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: 129.93  E-value: 1.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553414234   2 RTYMPVHYKVLKaQARAGAAVPAAVNNDIYFPVYGKVWGSYRHDMGEYGWVKVYANLYGGTNKKNDAAP--------TKW 73
Cdd:pfam02722  68 RLYIPLTHGLYK-NNGGYALPPVHPGGHINLPVVGKVWLSYRIPLGEHAWLKPYVSVYGTTNRFNGNSKatngaagaTKL 146

                          90       100       110
                  ....*....|....*....|....*....|
gi 2553414234  74 SKEYCGYYECGVVVSPLEKVEIRLSWEQGK 103
Cdd:pfam02722 147 LAEYCLQYQVGVTVSPIEKVELSAQWEQGM 176
msp_porin NF033926
MSP porin; Members of this HMM are MSP porins (major outer sheath proteins) in Treponema. They ...
 28-103 4.78e-32

MSP porin; Members of this HMM are MSP porins (major outer sheath proteins) in Treponema. They may play a role in immune evasion and persistence.


Pssm-ID: 468249 [Multi-domain]  Cd Length: 512  Bit Score: 116.82  E-value: 4.78e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553414234  28 NDIYFPVYGKVWGSYRHDMGEYGWVKVYANLYGGTNKKNDAAPTKWSKEYCG-YYECGVVVSPLEKVEIRLSWEQGK 103
Cdd:NF033926  402 KYAKFPLGLKVWGSYKYNLTDSMWVKPYANFWGETNHDHVDPDKSKDKLYFGlAYEVGVTFSPVEKVEIDASWEHGK 478
 
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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