NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2553414608|ref|WP_303048165|]
View 

major outer sheath C-terminal domain-containing protein, partial [Treponema pallidum]

Protein Classification

MOSP_C domain-containing protein( domain architecture ID 10497896)

MOSP_C domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MOSP_C pfam02722
Major Outer Sheath Protein C-terminal domain; This is a family of spirochete major outer ...
 162-360 2.11e-115

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: 333.32  E-value: 2.11e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553414608 162 DALLTAQWTYVSAGLYGATAGTNVFGKRVLPALQSWHFDFAGFLKLETKSGDPYTHLLTGLNAGVEARVYIPLTYIRYRN 241
Cdd:pfam02722   1 DALLTLQWRWLSSGAYFATAPANVFGKRVFPRTMSDHFDCAAFLKLETKSGDPYTHLLTGLDAGVEARLYIPLTHGLYKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553414608 242 NGGYPLNGVVPPGTINMPILGKAWCSYRIPLGSHAWLTPHTSVLGTTNRFNVINPA-------YTLLNERALQYQVGLTF 314
Cdd:pfam02722  81 NGGYALPPVHPGGHINLPVVGKVWLSYRIPLGEHAWLKPYVSVYGTTNRFNGNSKAtngaagaTKLLAEYCLQYQVGVTV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2553414608 315 SPFEKVELSAQWEQGVLADAPYMGIAESMWSERyFGTFICGVKVVW 360
Cdd:pfam02722 161 SPIEKVELSAQWEQGMLADAPYMVIEENVTSRK-FGTFVCGCKLIW 205
MOSP_N super family cl03668
Major Outer Sheath Protein N-terminal region; This is a family of spirochete major outer ...
 1-29 1.15e-11

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: 63.29  E-value: 1.15e-11
                          10        20
                  ....*....|....*....|....*....
gi 2553414608   1 TALLWGVGGRLTLEPGAGFRFSFALDAGN 29
Cdd:pfam02707 168 DTLLWNVGGRLTLTPGAGFRFVLALDAGN 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 ...
 162-360 2.11e-115

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: 333.32  E-value: 2.11e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553414608 162 DALLTAQWTYVSAGLYGATAGTNVFGKRVLPALQSWHFDFAGFLKLETKSGDPYTHLLTGLNAGVEARVYIPLTYIRYRN 241
Cdd:pfam02722   1 DALLTLQWRWLSSGAYFATAPANVFGKRVFPRTMSDHFDCAAFLKLETKSGDPYTHLLTGLDAGVEARLYIPLTHGLYKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553414608 242 NGGYPLNGVVPPGTINMPILGKAWCSYRIPLGSHAWLTPHTSVLGTTNRFNVINPA-------YTLLNERALQYQVGLTF 314
Cdd:pfam02722  81 NGGYALPPVHPGGHINLPVVGKVWLSYRIPLGEHAWLKPYVSVYGTTNRFNGNSKAtngaagaTKLLAEYCLQYQVGVTV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2553414608 315 SPFEKVELSAQWEQGVLADAPYMGIAESMWSERyFGTFICGVKVVW 360
Cdd:pfam02722 161 SPIEKVELSAQWEQGMLADAPYMVIEENVTSRK-FGTFVCGCKLIW 205
msp_porin NF033926
MSP porin; Members of this HMM are MSP porins (major outer sheath proteins) in Treponema. They ...
 159-360 2.57e-34

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: 132.22  E-value: 2.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553414608 159 FNADALLTAQWTYVSAGLYGATAGTNVFGKRVLPALQSwhfDFAGFLKLETKSGDPYTHLLTGLNAGVEARVYIPLTYIR 238
Cdd:NF033926  320 FAWDAVFTAGYKWVGAGVYVGSAGTPYAGNNKSNKAGT---DMAAFAAFETKGDGDDTNLVEGLDAGVDVRMYHLLSKIS 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553414608 239 YRNNGGYplngvvppgtINMPILGKAWCSYRIPLGSHAWLTPHTSVLGTTNRFNVINPAYTLLNERALQYQVGLTFSPFE 318
Cdd:NF033926  397 DEDRVKY----------AKFPLGLKVWGSYKYNLTDSMWVKPYANFWGETNHDHVDPDKSKDKLYFGLAYEVGVTFSPVE 466

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2553414608 319 KVELSAQWEQGVLADAPYMG----IAESMWSERYFGTFICGVKVVW 360
Cdd:NF033926  467 KVEIDASWEHGKLNKNKYEGgtsmIKTPVNDKTHNGTFVLSLKVTY 512
MOSP_N pfam02707
Major Outer Sheath Protein N-terminal region; This is a family of spirochete major outer ...
 1-29 1.15e-11

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: 63.29  E-value: 1.15e-11
                          10        20
                  ....*....|....*....|....*....
gi 2553414608   1 TALLWGVGGRLTLEPGAGFRFSFALDAGN 29
Cdd:pfam02707 168 DTLLWNVGGRLTLTPGAGFRFVLALDAGN 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 ...
 162-360 2.11e-115

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: 333.32  E-value: 2.11e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553414608 162 DALLTAQWTYVSAGLYGATAGTNVFGKRVLPALQSWHFDFAGFLKLETKSGDPYTHLLTGLNAGVEARVYIPLTYIRYRN 241
Cdd:pfam02722   1 DALLTLQWRWLSSGAYFATAPANVFGKRVFPRTMSDHFDCAAFLKLETKSGDPYTHLLTGLDAGVEARLYIPLTHGLYKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553414608 242 NGGYPLNGVVPPGTINMPILGKAWCSYRIPLGSHAWLTPHTSVLGTTNRFNVINPA-------YTLLNERALQYQVGLTF 314
Cdd:pfam02722  81 NGGYALPPVHPGGHINLPVVGKVWLSYRIPLGEHAWLKPYVSVYGTTNRFNGNSKAtngaagaTKLLAEYCLQYQVGVTV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2553414608 315 SPFEKVELSAQWEQGVLADAPYMGIAESMWSERyFGTFICGVKVVW 360
Cdd:pfam02722 161 SPIEKVELSAQWEQGMLADAPYMVIEENVTSRK-FGTFVCGCKLIW 205
msp_porin NF033926
MSP porin; Members of this HMM are MSP porins (major outer sheath proteins) in Treponema. They ...
 159-360 2.57e-34

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: 132.22  E-value: 2.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553414608 159 FNADALLTAQWTYVSAGLYGATAGTNVFGKRVLPALQSwhfDFAGFLKLETKSGDPYTHLLTGLNAGVEARVYIPLTYIR 238
Cdd:NF033926  320 FAWDAVFTAGYKWVGAGVYVGSAGTPYAGNNKSNKAGT---DMAAFAAFETKGDGDDTNLVEGLDAGVDVRMYHLLSKIS 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553414608 239 YRNNGGYplngvvppgtINMPILGKAWCSYRIPLGSHAWLTPHTSVLGTTNRFNVINPAYTLLNERALQYQVGLTFSPFE 318
Cdd:NF033926  397 DEDRVKY----------AKFPLGLKVWGSYKYNLTDSMWVKPYANFWGETNHDHVDPDKSKDKLYFGLAYEVGVTFSPVE 466

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2553414608 319 KVELSAQWEQGVLADAPYMG----IAESMWSERYFGTFICGVKVVW 360
Cdd:NF033926  467 KVEIDASWEHGKLNKNKYEGgtsmIKTPVNDKTHNGTFVLSLKVTY 512
MOSP_N pfam02707
Major Outer Sheath Protein N-terminal region; This is a family of spirochete major outer ...
 1-29 1.15e-11

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: 63.29  E-value: 1.15e-11
                          10        20
                  ....*....|....*....|....*....
gi 2553414608   1 TALLWGVGGRLTLEPGAGFRFSFALDAGN 29
Cdd:pfam02707 168 DTLLWNVGGRLTLTPGAGFRFVLALDAGN 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH