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Conserved domains on  [gi|1563816334|dbj|BBI32738|]
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hypothetical protein KCTCHS21_21370 [Cohnella abietis]

Protein Classification

S-layer homology domain-containing protein( domain architecture ID 10171019)

SLH (S-layer homology) domain-containing protein similar to S-layer proteins that are major cell-wall components which form a paracrystalline mono-layered assembly that coats the surface of bacteria

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Type_II_cohesin cd08547
Type II cohesin domain, interaction partner of dockerin; Bacterial cohesin domains bind to a ...
 35-153 2.16e-12

Type II cohesin domain, interaction partner of dockerin; Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type II cohesins; their interactions with dockerin mediate attachment of the cellulosome complex to the bacterial cell wall.


:

Pssm-ID: 260084  Cd Length: 136  Bit Score: 63.58  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563816334  35 TTDKPAGGKVVVTLSGKGIKDLYGYEARFTFDPDQLELVESKSSLDGFSVSPI----IKKNEIIIAHTKIGNVTGESGDI 110
Cdd:cd08547     9 ETDVKVGETFTVTVKVNNATNLAGYDFTLSYDPSVLEFVSVTTGSLSGGGGVIanedAPPGTVRVAGSSTGGAGGVSGSG 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1563816334 111 VIGSLTFKIKKNGTSNVKWESMKAVDHNLSAQTYPIGKSVSVT 153
Cdd:cd08547    89 TLATLTFKAKAAGTSTISLTDSNTTLSDADGSTIPTFVGGGLE 131
SLH pfam00395
S-layer homology domain;
218-259 1.07e-11

S-layer homology domain;


:

Pssm-ID: 459798 [Multi-domain]  Cd Length: 42  Bit Score: 58.76  E-value: 1.07e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1563816334 218 FTDVAPASWYKDVINSAYSAGIIQGLTDTKFAPERNITREEM 259
Cdd:pfam00395   1 FKDVKSVAAWAEAVAALAELGIISGYPDGTFRPNEPITRAEA 42
SLH pfam00395
S-layer homology domain;
159-199 2.51e-07

S-layer homology domain;


:

Pssm-ID: 459798 [Multi-domain]  Cd Length: 42  Bit Score: 46.43  E-value: 2.51e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1563816334 159 FLDLEGHWAKAD-IEVLASKGIIEGIDEDHFAPENHVTRAQF 199
Cdd:pfam00395   1 FKDVKSVAAWAEaVAALAELGIISGYPDGTFRPNEPITRAEA 42
SLH pfam00395
S-layer homology domain;
286-328 2.24e-06

S-layer homology domain;


:

Pssm-ID: 459798 [Multi-domain]  Cd Length: 42  Bit Score: 43.73  E-value: 2.24e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1563816334 286 FADSADISKWArEGVQAAVRSGIIKGKAGLKFDPQGKASRAEA 328
Cdd:pfam00395   1 FKDVKSVAAWA-EAVAALAELGIISGYPDGTFRPNEPITRAEA 42
 
Name Accession Description Interval E-value
Type_II_cohesin cd08547
Type II cohesin domain, interaction partner of dockerin; Bacterial cohesin domains bind to a ...
 35-153 2.16e-12

Type II cohesin domain, interaction partner of dockerin; Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type II cohesins; their interactions with dockerin mediate attachment of the cellulosome complex to the bacterial cell wall.


Pssm-ID: 260084  Cd Length: 136  Bit Score: 63.58  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563816334  35 TTDKPAGGKVVVTLSGKGIKDLYGYEARFTFDPDQLELVESKSSLDGFSVSPI----IKKNEIIIAHTKIGNVTGESGDI 110
Cdd:cd08547     9 ETDVKVGETFTVTVKVNNATNLAGYDFTLSYDPSVLEFVSVTTGSLSGGGGVIanedAPPGTVRVAGSSTGGAGGVSGSG 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1563816334 111 VIGSLTFKIKKNGTSNVKWESMKAVDHNLSAQTYPIGKSVSVT 153
Cdd:cd08547    89 TLATLTFKAKAAGTSTISLTDSNTTLSDADGSTIPTFVGGGLE 131
SLH pfam00395
S-layer homology domain;
218-259 1.07e-11

S-layer homology domain;


Pssm-ID: 459798 [Multi-domain]  Cd Length: 42  Bit Score: 58.76  E-value: 1.07e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1563816334 218 FTDVAPASWYKDVINSAYSAGIIQGLTDTKFAPERNITREEM 259
Cdd:pfam00395   1 FKDVKSVAAWAEAVAALAELGIISGYPDGTFRPNEPITRAEA 42
SLH pfam00395
S-layer homology domain;
159-199 2.51e-07

S-layer homology domain;


Pssm-ID: 459798 [Multi-domain]  Cd Length: 42  Bit Score: 46.43  E-value: 2.51e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1563816334 159 FLDLEGHWAKAD-IEVLASKGIIEGIDEDHFAPENHVTRAQF 199
Cdd:pfam00395   1 FKDVKSVAAWAEaVAALAELGIISGYPDGTFRPNEPITRAEA 42
SLH pfam00395
S-layer homology domain;
286-328 2.24e-06

S-layer homology domain;


Pssm-ID: 459798 [Multi-domain]  Cd Length: 42  Bit Score: 43.73  E-value: 2.24e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1563816334 286 FADSADISKWArEGVQAAVRSGIIKGKAGLKFDPQGKASRAEA 328
Cdd:pfam00395   1 FKDVKSVAAWA-EAVAALAELGIISGYPDGTFRPNEPITRAEA 42
Cohesin pfam00963
Cohesin domain; Cohesin domains interact with a complementary domain, termed the dockerin ...
 35-153 9.67e-05

Cohesin domain; Cohesin domains interact with a complementary domain, termed the dockerin domain. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome.


Pssm-ID: 395769  Cd Length: 139  Bit Score: 42.00  E-value: 9.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563816334  35 TTDKPAGGKVVVTLSGKGI--KDLYGYEARFTFDPDQLELVE------SKSSLDGFSVSPIIKKNEIIIAHTKIGNVTGE 106
Cdd:pfam00963   7 KVSGKVGDTVTVPVTVSNVpkNGVAAADFTINYDPTVLEVVSvtpgsiVDNPNVNFGSNVLVEPGKIKFLFLDLTSLGSS 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1563816334 107 --SGDIVIGSLTFKIKKN---GTSNVKWESMKAVDHNLSAQTYPIGKSVSVT 153
Cdd:pfam00963  87 giAKDGVFATITFKVKSDaaaGTTPIKISGTLSFGDGGLNEIKVTLTDGSIN 138
 
Name Accession Description Interval E-value
Type_II_cohesin cd08547
Type II cohesin domain, interaction partner of dockerin; Bacterial cohesin domains bind to a ...
 35-153 2.16e-12

Type II cohesin domain, interaction partner of dockerin; Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type II cohesins; their interactions with dockerin mediate attachment of the cellulosome complex to the bacterial cell wall.


Pssm-ID: 260084  Cd Length: 136  Bit Score: 63.58  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563816334  35 TTDKPAGGKVVVTLSGKGIKDLYGYEARFTFDPDQLELVESKSSLDGFSVSPI----IKKNEIIIAHTKIGNVTGESGDI 110
Cdd:cd08547     9 ETDVKVGETFTVTVKVNNATNLAGYDFTLSYDPSVLEFVSVTTGSLSGGGGVIanedAPPGTVRVAGSSTGGAGGVSGSG 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1563816334 111 VIGSLTFKIKKNGTSNVKWESMKAVDHNLSAQTYPIGKSVSVT 153
Cdd:cd08547    89 TLATLTFKAKAAGTSTISLTDSNTTLSDADGSTIPTFVGGGLE 131
SLH pfam00395
S-layer homology domain;
218-259 1.07e-11

S-layer homology domain;


Pssm-ID: 459798 [Multi-domain]  Cd Length: 42  Bit Score: 58.76  E-value: 1.07e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1563816334 218 FTDVAPASWYKDVINSAYSAGIIQGLTDTKFAPERNITREEM 259
Cdd:pfam00395   1 FKDVKSVAAWAEAVAALAELGIISGYPDGTFRPNEPITRAEA 42
SLH pfam00395
S-layer homology domain;
159-199 2.51e-07

S-layer homology domain;


Pssm-ID: 459798 [Multi-domain]  Cd Length: 42  Bit Score: 46.43  E-value: 2.51e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1563816334 159 FLDLEGHWAKAD-IEVLASKGIIEGIDEDHFAPENHVTRAQF 199
Cdd:pfam00395   1 FKDVKSVAAWAEaVAALAELGIISGYPDGTFRPNEPITRAEA 42
SLH pfam00395
S-layer homology domain;
286-328 2.24e-06

S-layer homology domain;


Pssm-ID: 459798 [Multi-domain]  Cd Length: 42  Bit Score: 43.73  E-value: 2.24e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1563816334 286 FADSADISKWArEGVQAAVRSGIIKGKAGLKFDPQGKASRAEA 328
Cdd:pfam00395   1 FKDVKSVAAWA-EAVAALAELGIISGYPDGTFRPNEPITRAEA 42
Cohesin pfam00963
Cohesin domain; Cohesin domains interact with a complementary domain, termed the dockerin ...
 35-153 9.67e-05

Cohesin domain; Cohesin domains interact with a complementary domain, termed the dockerin domain. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome.


Pssm-ID: 395769  Cd Length: 139  Bit Score: 42.00  E-value: 9.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563816334  35 TTDKPAGGKVVVTLSGKGI--KDLYGYEARFTFDPDQLELVE------SKSSLDGFSVSPIIKKNEIIIAHTKIGNVTGE 106
Cdd:pfam00963   7 KVSGKVGDTVTVPVTVSNVpkNGVAAADFTINYDPTVLEVVSvtpgsiVDNPNVNFGSNVLVEPGKIKFLFLDLTSLGSS 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1563816334 107 --SGDIVIGSLTFKIKKN---GTSNVKWESMKAVDHNLSAQTYPIGKSVSVT 153
Cdd:pfam00963  87 giAKDGVFATITFKVKSDaaaGTTPIKISGTLSFGDGGLNEIKVTLTDGSIN 138
 
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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