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Conserved domains on  [gi|1806621599|ref|WP_162257391|]
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Cna B-type domain-containing protein, partial [Pediococcus claussenii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CollagenBindB cd00222
Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates ...
 13-113 2.31e-19

Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates bacterial adherence to collagen; the primary sequence has a non-repetitive, collagen-binding A region, followed by instances of this B region repetitive unit. The B region has one to four 23 kDa repeat units (B1-B4), which have been suggested to serve as 'stalks' that project the A region from the bacterial surface and thus facilitate bacterial adherence to collagen. Each B repeat unit has two highly similar domains (D1 and D2) placed side-by-side; both D1 and D2 are included in this model. They exhibit a unique inverse IgG-like domain fold.


:

Pssm-ID: 212461 [Multi-domain]  Cd Length: 92  Bit Score: 78.10  E-value: 2.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806621599  13 ITFKGTKQWDDDNNKYGERPEDLEVQLQRrlsDDAdwENYKTQDIDAENVdldehiWEFEFTDLPKENNAGQTYQYRVIE 92
Cdd:cd00222     1 TDITVTKTWDDDDNQDGKRPESITVQLLA---NGK--ETGDTVTLTASND------WTYTFTNLPKYDENGKEITYTVKE 69

                          90       100
                  ....*....|....*....|...
gi 1806621599  93 NDVPNNYAE--TLVDNHTIINKH 113
Cdd:cd00222    70 VPVPGYTTTvtGDDGGFTITNTH 92
SpaA pfam17802
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
 128-177 8.59e-09

Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.


:

Pssm-ID: 465513 [Multi-domain]  Cd Length: 72  Bit Score: 49.89  E-value: 8.59e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1806621599 128 KGESLAGAEFKLTDSEGKTIEKDGSS--TDS--KFVWKELDVGEYTLEETKAPD 177
Cdd:pfam17802   2 TGKPLAGAEFTLYDADGTVDGKVVGTltTDEdgKATFDGLPPGTYTLKETKAPD 55
 
Name Accession Description Interval E-value
CollagenBindB cd00222
Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates ...
 13-113 2.31e-19

Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates bacterial adherence to collagen; the primary sequence has a non-repetitive, collagen-binding A region, followed by instances of this B region repetitive unit. The B region has one to four 23 kDa repeat units (B1-B4), which have been suggested to serve as 'stalks' that project the A region from the bacterial surface and thus facilitate bacterial adherence to collagen. Each B repeat unit has two highly similar domains (D1 and D2) placed side-by-side; both D1 and D2 are included in this model. They exhibit a unique inverse IgG-like domain fold.


Pssm-ID: 212461 [Multi-domain]  Cd Length: 92  Bit Score: 78.10  E-value: 2.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806621599  13 ITFKGTKQWDDDNNKYGERPEDLEVQLQRrlsDDAdwENYKTQDIDAENVdldehiWEFEFTDLPKENNAGQTYQYRVIE 92
Cdd:cd00222     1 TDITVTKTWDDDDNQDGKRPESITVQLLA---NGK--ETGDTVTLTASND------WTYTFTNLPKYDENGKEITYTVKE 69

                          90       100
                  ....*....|....*....|...
gi 1806621599  93 NDVPNNYAE--TLVDNHTIINKH 113
Cdd:cd00222    70 VPVPGYTTTvtGDDGGFTITNTH 92
Cna_B pfam05738
Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding ...
 16-110 1.03e-16

Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding surface protein. The structure of the repetitive B-region has been solved and forms a beta sandwich structure.


Pssm-ID: 461726 [Multi-domain]  Cd Length: 88  Bit Score: 71.12  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806621599  16 KGTKQWDDDNNKYGERPEDLEVQLQRrlsDDAdwENYKTQDIDAENVdldehiWEFEFTDLPKENNAGQTYQYRVIENDV 95
Cdd:pfam05738   2 SVTKVWDDNNNQDGIRPESITVQLLA---NGQ--KVGVTKELTAANN------WTYTFTDLPKYDENGKEITYTVEEDAV 70

                          90
                  ....*....|....*
gi 1806621599  96 PNNYAETLVDNHTII 110
Cdd:pfam05738  71 PGYTTTVDAKDGFTI 85
SpaA pfam17802
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
 128-177 8.59e-09

Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.


Pssm-ID: 465513 [Multi-domain]  Cd Length: 72  Bit Score: 49.89  E-value: 8.59e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1806621599 128 KGESLAGAEFKLTDSEGKTIEKDGSS--TDS--KFVWKELDVGEYTLEETKAPD 177
Cdd:pfam17802   2 TGKPLAGAEFTLYDADGTVDGKVVGTltTDEdgKATFDGLPPGTYTLKETKAPD 55
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
 70-177 1.37e-08

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 53.44  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806621599  70 EFEFTDLPKENnagqtyqYRVIENDVPNNYAETLVDNHTIINKHVQHHFDY------------EVNKVDA--KGESLAGA 135
Cdd:COG4932   305 SYTFTDLPPGT-------YTVTETKAPAGYDLDGEAVKVTITAGQTTTVTVtngnnevktgsvTLTKVDAddGEAPLAGA 377

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1806621599 136 EFKLTDSEGKTIEKDGSSTDSKFVWKELDVGEYTLEETKAPD 177
Cdd:COG4932   378 EFTLTDADGTVVATITTDADGTASFKGLAPGTYTLTETKAPE 419
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
 121-177 4.36e-06

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 46.12  E-value: 4.36e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1806621599 121 EVNKVDAK-GESLAGAEFKLTDSEGK-TIEKDGSSTDS--KFVWKELDVGEYTLEETKAPD 177
Cdd:COG4932   265 TVTKTDADtGEPLAGATFTLTDADGNtVVTTTVTVTDAdgSYTFTDLPPGTYTVTETKAPA 325
iso_D2_wall_anc NF033902
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
 70-177 2.41e-03

SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits whose structure includes an LPXTG motif-containing signal (see TIGR01167) near the C-terminus, for processing by sortases. Most contain a recognizable D2-type fimbrial isopeptide formation domain (see TIGR04226), in which Lys-to-Asn isopeptide bond formation provides additional structural integrity to support adhesion despite shear. For proper members of this subfamily, lengths fall typically in the range of 460 to 640 amino acids in length. Many members of this family contribute to the virulence of certain Gram-positive pathogens, including SpaA, SpaD, and SpaH from Corynebacterium diphtheriae, and EbpB and EbpC from Enterococcus faecalis.


Pssm-ID: 468234 [Multi-domain]  Cd Length: 533  Bit Score: 37.81  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806621599  70 EFEFT---DLPKENNAGQTYQYRVIENDVPNNYAETLVDNHTIINKHVQ-HHFDYEVNKVDAKGES--LAGAEFKL--TD 141
Cdd:NF033902  320 TFKTKvtkTAKGGTNGEITNKAGLIPNNPGPNTPEPTTPGTPDPTPTVKtYFGKLKIKKVDADDTSkkLKGAEFKVyaCE 399

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806621599 142 SEGKTIEKDGSSTDSKFVWKELDVG------------------------EYTLEETKAPD 177
Cdd:NF033902  400 ADAAAACVNAIGINGKTTFTTGADGtvsidglhvtdledgasvkaaagkDYCLVETKAPA 459
 
Name Accession Description Interval E-value
CollagenBindB cd00222
Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates ...
 13-113 2.31e-19

Repeat unit of collagen-binding protein domain B; The collagen-binding protein mediates bacterial adherence to collagen; the primary sequence has a non-repetitive, collagen-binding A region, followed by instances of this B region repetitive unit. The B region has one to four 23 kDa repeat units (B1-B4), which have been suggested to serve as 'stalks' that project the A region from the bacterial surface and thus facilitate bacterial adherence to collagen. Each B repeat unit has two highly similar domains (D1 and D2) placed side-by-side; both D1 and D2 are included in this model. They exhibit a unique inverse IgG-like domain fold.


Pssm-ID: 212461 [Multi-domain]  Cd Length: 92  Bit Score: 78.10  E-value: 2.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806621599  13 ITFKGTKQWDDDNNKYGERPEDLEVQLQRrlsDDAdwENYKTQDIDAENVdldehiWEFEFTDLPKENNAGQTYQYRVIE 92
Cdd:cd00222     1 TDITVTKTWDDDDNQDGKRPESITVQLLA---NGK--ETGDTVTLTASND------WTYTFTNLPKYDENGKEITYTVKE 69

                          90       100
                  ....*....|....*....|...
gi 1806621599  93 NDVPNNYAE--TLVDNHTIINKH 113
Cdd:cd00222    70 VPVPGYTTTvtGDDGGFTITNTH 92
Cna_B pfam05738
Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding ...
 16-110 1.03e-16

Cna protein B-type domain; This domain is found in Staphylococcus aureus collagen-binding surface protein. The structure of the repetitive B-region has been solved and forms a beta sandwich structure.


Pssm-ID: 461726 [Multi-domain]  Cd Length: 88  Bit Score: 71.12  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806621599  16 KGTKQWDDDNNKYGERPEDLEVQLQRrlsDDAdwENYKTQDIDAENVdldehiWEFEFTDLPKENNAGQTYQYRVIENDV 95
Cdd:pfam05738   2 SVTKVWDDNNNQDGIRPESITVQLLA---NGQ--KVGVTKELTAANN------WTYTFTDLPKYDENGKEITYTVEEDAV 70

                          90
                  ....*....|....*
gi 1806621599  96 PNNYAETLVDNHTII 110
Cdd:pfam05738  71 PGYTTTVDAKDGFTI 85
SpaA pfam17802
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
 128-177 8.59e-09

Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.


Pssm-ID: 465513 [Multi-domain]  Cd Length: 72  Bit Score: 49.89  E-value: 8.59e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1806621599 128 KGESLAGAEFKLTDSEGKTIEKDGSS--TDS--KFVWKELDVGEYTLEETKAPD 177
Cdd:pfam17802   2 TGKPLAGAEFTLYDADGTVDGKVVGTltTDEdgKATFDGLPPGTYTLKETKAPD 55
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
 70-177 1.37e-08

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 53.44  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806621599  70 EFEFTDLPKENnagqtyqYRVIENDVPNNYAETLVDNHTIINKHVQHHFDY------------EVNKVDA--KGESLAGA 135
Cdd:COG4932   305 SYTFTDLPPGT-------YTVTETKAPAGYDLDGEAVKVTITAGQTTTVTVtngnnevktgsvTLTKVDAddGEAPLAGA 377

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1806621599 136 EFKLTDSEGKTIEKDGSSTDSKFVWKELDVGEYTLEETKAPD 177
Cdd:COG4932   378 EFTLTDADGTVVATITTDADGTASFKGLAPGTYTLTETKAPE 419
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
 121-177 4.36e-06

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 46.12  E-value: 4.36e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1806621599 121 EVNKVDAK-GESLAGAEFKLTDSEGK-TIEKDGSSTDS--KFVWKELDVGEYTLEETKAPD 177
Cdd:COG4932   265 TVTKTDADtGEPLAGATFTLTDADGNtVVTTTVTVTDAdgSYTFTDLPPGTYTVTETKAPA 325
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
 44-177 8.69e-05

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 42.27  E-value: 8.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806621599  44 SDDADWENYKTQDIDAENVDLDEHIWEFEFTDLPKENNAGQTYQYRVIENDVPNNYAETLVDNHTIINKHVQHHFDYEVN 123
Cdd:COG4932    90 DATVTTTANVAKVTNGAAANLTVNADGTASNAGTLAKGAETATGNLDGDAGDVTVTAAATDGVNDVDGNGASVTDSVTLK 169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1806621599 124 KVDAK--GESLAGAEFKLTDSEGKTIEKDGSSTDSKFVWKELDVGEYTLEETKAPD 177
Cdd:COG4932   170 KVDDGdtGKPLPGATFTLYDSDGTLVKTVTTDADGKYTFTDLPPGTYTLTETKAPE 225
iso_D2_wall_anc NF033902
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
 70-177 2.41e-03

SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits whose structure includes an LPXTG motif-containing signal (see TIGR01167) near the C-terminus, for processing by sortases. Most contain a recognizable D2-type fimbrial isopeptide formation domain (see TIGR04226), in which Lys-to-Asn isopeptide bond formation provides additional structural integrity to support adhesion despite shear. For proper members of this subfamily, lengths fall typically in the range of 460 to 640 amino acids in length. Many members of this family contribute to the virulence of certain Gram-positive pathogens, including SpaA, SpaD, and SpaH from Corynebacterium diphtheriae, and EbpB and EbpC from Enterococcus faecalis.


Pssm-ID: 468234 [Multi-domain]  Cd Length: 533  Bit Score: 37.81  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806621599  70 EFEFT---DLPKENNAGQTYQYRVIENDVPNNYAETLVDNHTIINKHVQ-HHFDYEVNKVDAKGES--LAGAEFKL--TD 141
Cdd:NF033902  320 TFKTKvtkTAKGGTNGEITNKAGLIPNNPGPNTPEPTTPGTPDPTPTVKtYFGKLKIKKVDADDTSkkLKGAEFKVyaCE 399

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806621599 142 SEGKTIEKDGSSTDSKFVWKELDVG------------------------EYTLEETKAPD 177
Cdd:NF033902  400 ADAAAACVNAIGINGKTTFTTGADGtvsidglhvtdledgasvkaaagkDYCLVETKAPA 459
 
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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