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Conserved domains on  [gi|1778827620|ref|WP_154975031|]
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collagen-like protein, partial [Priestia megaterium]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BclA_C pfam18573
BclA C-terminal domain; This is the C-terminal domain of BclA (Bacillus collagen-like protein ...
 45-179 4.44e-31

BclA C-terminal domain; This is the C-terminal domain of BclA (Bacillus collagen-like protein of anthracis) which is expressed on spores of Bacillus species. Trimers of the C-terminal domain (CTD) form the tips of the spore's hair-like nap and are the immunodominant target of vertebrate antibodies and drive trimerization. Structure analysis indicate the C-terminal region of the peptide folding into an all-beta structure with a jelly-fold topology, similar to the first human complement C1q, a member of the tumor necrosis factor (TNF)-like family. The C-terminal globular domain has been shown to be located on the exterior of the exosporium, and therefore is critical in determining the immunogenicity of the spore in a mammalian host.


:

Pssm-ID: 436587 [Multi-domain]  Cd Length: 127  Bit Score: 109.29  E-value: 4.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778827620  45 FACNTTGSVIPVALGGSNsIPLPNNQNLDGFIANGPNTIFTVPATGRYYITYQINTTAALGVgaGSRILLNStTPIPGSI 124
Cdd:pfam18573   1 YAANTSGSTIAVVLGGTP-VPLPNNQNLSGITVNGTNTTFTVNEAGRYYISYQVNTTAALLV--GLRLLVNG-TPVPGSI 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1778827620 125 LSPVLSTSTFNNDVIVNLSAGNTISLQLFSsillIATLLSAGGSVGAALTIIRLQ 179
Cdd:pfam18573  77 ITPALSTSSYSNSVIVTLTAGDTISLQLFG----LAGAATLGGGTGASLTIIRLA 127
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 3-37 1.90e-04

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 41.04  E-value: 1.90e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1778827620   3 GVTGPTGPTGATGVTGPTGPTGATGVTGPTGPTGE 37
Cdd:NF038329  141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP 175
 
Name Accession Description Interval E-value
BclA_C pfam18573
BclA C-terminal domain; This is the C-terminal domain of BclA (Bacillus collagen-like protein ...
 45-179 4.44e-31

BclA C-terminal domain; This is the C-terminal domain of BclA (Bacillus collagen-like protein of anthracis) which is expressed on spores of Bacillus species. Trimers of the C-terminal domain (CTD) form the tips of the spore's hair-like nap and are the immunodominant target of vertebrate antibodies and drive trimerization. Structure analysis indicate the C-terminal region of the peptide folding into an all-beta structure with a jelly-fold topology, similar to the first human complement C1q, a member of the tumor necrosis factor (TNF)-like family. The C-terminal globular domain has been shown to be located on the exterior of the exosporium, and therefore is critical in determining the immunogenicity of the spore in a mammalian host.


Pssm-ID: 436587 [Multi-domain]  Cd Length: 127  Bit Score: 109.29  E-value: 4.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778827620  45 FACNTTGSVIPVALGGSNsIPLPNNQNLDGFIANGPNTIFTVPATGRYYITYQINTTAALGVgaGSRILLNStTPIPGSI 124
Cdd:pfam18573   1 YAANTSGSTIAVVLGGTP-VPLPNNQNLSGITVNGTNTTFTVNEAGRYYISYQVNTTAALLV--GLRLLVNG-TPVPGSI 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1778827620 125 LSPVLSTSTFNNDVIVNLSAGNTISLQLFSsillIATLLSAGGSVGAALTIIRLQ 179
Cdd:pfam18573  77 ITPALSTSSYSNSVIVTLTAGDTISLQLFG----LAGAATLGGGTGASLTIIRLA 127
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 3-37 1.90e-04

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 41.04  E-value: 1.90e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1778827620   3 GVTGPTGPTGATGVTGPTGPTGATGVTGPTGPTGE 37
Cdd:NF038329  141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP 175
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 3-37 4.58e-04

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 39.89  E-value: 4.58e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1778827620   3 GVTGPTGPTGATGVTGPTGPTGATGVTGPTGPTGE 37
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGP 151
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 3-37 5.21e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.70  E-value: 5.21e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1778827620   3 GVTGPTGPTGATGVTGPTGPTGATGVTGPTGPTGE 37
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGP 41
 
Name Accession Description Interval E-value
BclA_C pfam18573
BclA C-terminal domain; This is the C-terminal domain of BclA (Bacillus collagen-like protein ...
 45-179 4.44e-31

BclA C-terminal domain; This is the C-terminal domain of BclA (Bacillus collagen-like protein of anthracis) which is expressed on spores of Bacillus species. Trimers of the C-terminal domain (CTD) form the tips of the spore's hair-like nap and are the immunodominant target of vertebrate antibodies and drive trimerization. Structure analysis indicate the C-terminal region of the peptide folding into an all-beta structure with a jelly-fold topology, similar to the first human complement C1q, a member of the tumor necrosis factor (TNF)-like family. The C-terminal globular domain has been shown to be located on the exterior of the exosporium, and therefore is critical in determining the immunogenicity of the spore in a mammalian host.


Pssm-ID: 436587 [Multi-domain]  Cd Length: 127  Bit Score: 109.29  E-value: 4.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778827620  45 FACNTTGSVIPVALGGSNsIPLPNNQNLDGFIANGPNTIFTVPATGRYYITYQINTTAALGVgaGSRILLNStTPIPGSI 124
Cdd:pfam18573   1 YAANTSGSTIAVVLGGTP-VPLPNNQNLSGITVNGTNTTFTVNEAGRYYISYQVNTTAALLV--GLRLLVNG-TPVPGSI 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1778827620 125 LSPVLSTSTFNNDVIVNLSAGNTISLQLFSsillIATLLSAGGSVGAALTIIRLQ 179
Cdd:pfam18573  77 ITPALSTSSYSNSVIVTLTAGDTISLQLFG----LAGAATLGGGTGASLTIIRLA 127
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 3-37 1.90e-04

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 41.04  E-value: 1.90e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1778827620   3 GVTGPTGPTGATGVTGPTGPTGATGVTGPTGPTGE 37
Cdd:NF038329  141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP 175
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 3-37 4.58e-04

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 39.89  E-value: 4.58e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1778827620   3 GVTGPTGPTGATGVTGPTGPTGATGVTGPTGPTGE 37
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGP 151
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 3-37 5.21e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.70  E-value: 5.21e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1778827620   3 GVTGPTGPTGATGVTGPTGPTGATGVTGPTGPTGE 37
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGP 41
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 3-36 6.78e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 6.78e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1778827620   3 GVTGPTGPTGATGVTGPTGPTGATGVTGPTGPTG 36
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPG 37
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 6-37 8.14e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.93  E-value: 8.14e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1778827620   6 GPTGPTGATGVTGPTGPTGATGVTGPTGPTGE 37
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGE 32
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 3-37 9.19e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.93  E-value: 9.19e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1778827620   3 GVTGPTGPTGATGVTGPTGPTGATGVTGPTGPTGE 37
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGP 35
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1-36 9.19e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.93  E-value: 9.19e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1778827620   1 ATGVTGPTGPTGATGVTGPTGPTGATGVTGPTGPTG 36
Cdd:pfam01391   8 PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPG 43
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1-37 1.23e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.55  E-value: 1.23e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1778827620   1 ATGVTGPTGPTGATGVTGPTGPTGATGVTGPTGPTGE 37
Cdd:pfam01391  11 PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
 
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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