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Conserved domains on  [gi|446125470|ref|WP_000203325|]
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MULTISPECIES: exosporium glycoprotein BclB-related protein [Bacillus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
exospore_TM TIGR03721
BclB C-terminal domain; This domain occurs as the C-terminal region in a number of proteins ...
 257-416 2.34e-51

BclB C-terminal domain; This domain occurs as the C-terminal region in a number of proteins that have extensive collagen-like triple helix repeat regions. Member domains are predicted by TmHMM to have four or five transmembrane helices. Members are found mostly in the Firmicutes, but also in Acanthamoeba polyphaga mimivirus. Members include spore surface glycoprotein BclB from Bacillus anthracis, a protein of the exosporium. The exosporium is an additional outermost spore layer, lacking in B. subtilis and most other spore formers, consisting of a basal layer and, above it, a nap of fine filaments.


:

Pssm-ID: 274746 [Multi-domain]  Cd Length: 165  Bit Score: 170.07  E-value: 2.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125470  257 IIPFASGTTPSALVNAL-IANTGTLLGFGFSQPGIALTGGTsITLALGIGDYAFVAPRDGIITSLAGFFSATAALAPLSP 335
Cdd:TIGR03721   1 IIPFASGTTLALTTNAGgLAGTPGLIGFGSSAPGLSLVGGT-IDLAGGLTNYAFSMPRDGIITSLAAYFSATAALALLGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125470  336 VQVQIQILTAPPASNTFT-VQGAPLLLTPAFA-AIAIGSTASGIIA-EAIPVTAGDKILLYVSLTA--ASPIAAVAGFVS 410
Cdd:TIGR03721  80 VTITAQLYIAPAPSNVFTpVPGAPVTLTPPITgPIAVGSTASGIITgLNIPVTAGDRLLLVVSATAsgLSPIATVAGYVS 159


                  ....*.
gi 446125470  411 AGINIV 416
Cdd:TIGR03721 160 AGLAIV 165
N_to_GlyXaaXaa NF033172
collagen-like repeat preface domain; All protein sequence used in the seed alignment for this ...
 31-133 3.13e-17

collagen-like repeat preface domain; All protein sequence used in the seed alignment for this model comes from the N-terminal region of proteins with extended collagen-like Gly-rich repeat regions, and occur in Firmicutes.


:

Pssm-ID: 467978  Cd Length: 122  Bit Score: 77.33  E-value: 3.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125470  31 ITSEQLGRLITLLNSLISAIAAFFANPSDANRLALLNLFTQLLN-LLNELPPSPEGNYLKQLIQSIINVLQSPNPDLSQL 109
Cdd:NF033172   1 ISKSQLTRLISLLQELTTLIPAVFTNPTPSNISALQNLLRQLLKfLNSLNLSSAEKAALLSIIENLITILESPPFSPGAL 80

                         90       100
                 ....*....|....*....|....
gi 446125470 110 LSLLQQFYSALAPFFFSLIIDPAS 133
Cdd:NF033172  81 AILLQQLLNALLSIVLLFKIDPCI 104
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 202-242 2.20e-07

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: 47.49  E-value: 2.20e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 446125470  202 GPTGPTGDTGATGPTGPTGDTGATGPTGPTGDTGPTGATGP 242
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGP 41
 
Name Accession Description Interval E-value
exospore_TM TIGR03721
BclB C-terminal domain; This domain occurs as the C-terminal region in a number of proteins ...
 257-416 2.34e-51

BclB C-terminal domain; This domain occurs as the C-terminal region in a number of proteins that have extensive collagen-like triple helix repeat regions. Member domains are predicted by TmHMM to have four or five transmembrane helices. Members are found mostly in the Firmicutes, but also in Acanthamoeba polyphaga mimivirus. Members include spore surface glycoprotein BclB from Bacillus anthracis, a protein of the exosporium. The exosporium is an additional outermost spore layer, lacking in B. subtilis and most other spore formers, consisting of a basal layer and, above it, a nap of fine filaments.


Pssm-ID: 274746 [Multi-domain]  Cd Length: 165  Bit Score: 170.07  E-value: 2.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125470  257 IIPFASGTTPSALVNAL-IANTGTLLGFGFSQPGIALTGGTsITLALGIGDYAFVAPRDGIITSLAGFFSATAALAPLSP 335
Cdd:TIGR03721   1 IIPFASGTTLALTTNAGgLAGTPGLIGFGSSAPGLSLVGGT-IDLAGGLTNYAFSMPRDGIITSLAAYFSATAALALLGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125470  336 VQVQIQILTAPPASNTFT-VQGAPLLLTPAFA-AIAIGSTASGIIA-EAIPVTAGDKILLYVSLTA--ASPIAAVAGFVS 410
Cdd:TIGR03721  80 VTITAQLYIAPAPSNVFTpVPGAPVTLTPPITgPIAVGSTASGIITgLNIPVTAGDRLLLVVSATAsgLSPIATVAGYVS 159


                  ....*.
gi 446125470  411 AGINIV 416
Cdd:TIGR03721 160 AGLAIV 165
N_to_GlyXaaXaa NF033172
collagen-like repeat preface domain; All protein sequence used in the seed alignment for this ...
 31-133 3.13e-17

collagen-like repeat preface domain; All protein sequence used in the seed alignment for this model comes from the N-terminal region of proteins with extended collagen-like Gly-rich repeat regions, and occur in Firmicutes.


Pssm-ID: 467978  Cd Length: 122  Bit Score: 77.33  E-value: 3.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125470  31 ITSEQLGRLITLLNSLISAIAAFFANPSDANRLALLNLFTQLLN-LLNELPPSPEGNYLKQLIQSIINVLQSPNPDLSQL 109
Cdd:NF033172   1 ISKSQLTRLISLLQELTTLIPAVFTNPTPSNISALQNLLRQLLKfLNSLNLSSAEKAALLSIIENLITILESPPFSPGAL 80

                         90       100
                 ....*....|....*....|....
gi 446125470 110 LSLLQQFYSALAPFFFSLIIDPAS 133
Cdd:NF033172  81 AILLQQLLNALLSIVLLFKIDPCI 104
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 202-242 2.20e-07

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: 47.49  E-value: 2.20e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 446125470  202 GPTGPTGDTGATGPTGPTGDTGATGPTGPTGDTGPTGATGP 242
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGP 41
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 199-242 1.09e-05

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: 47.21  E-value: 1.09e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446125470 199 GATGPTGPTGDTGATGPTGPTGDTGATGPTGPTGDTGPTGATGP 242
Cdd:NF038329 168 GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 182-242 1.22e-05

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: 47.21  E-value: 1.22e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125470 182 DTGATGPTGPTGPTGDTGATGPTGPTGDTGATGPTGPTGD---TGATGPTGPTGDTGPTGATGP 242
Cdd:NF038329 139 DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKdgeAGAKGPAGEKGPQGPRGETGP 202
 
Name Accession Description Interval E-value
exospore_TM TIGR03721
BclB C-terminal domain; This domain occurs as the C-terminal region in a number of proteins ...
 257-416 2.34e-51

BclB C-terminal domain; This domain occurs as the C-terminal region in a number of proteins that have extensive collagen-like triple helix repeat regions. Member domains are predicted by TmHMM to have four or five transmembrane helices. Members are found mostly in the Firmicutes, but also in Acanthamoeba polyphaga mimivirus. Members include spore surface glycoprotein BclB from Bacillus anthracis, a protein of the exosporium. The exosporium is an additional outermost spore layer, lacking in B. subtilis and most other spore formers, consisting of a basal layer and, above it, a nap of fine filaments.


Pssm-ID: 274746 [Multi-domain]  Cd Length: 165  Bit Score: 170.07  E-value: 2.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125470  257 IIPFASGTTPSALVNAL-IANTGTLLGFGFSQPGIALTGGTsITLALGIGDYAFVAPRDGIITSLAGFFSATAALAPLSP 335
Cdd:TIGR03721   1 IIPFASGTTLALTTNAGgLAGTPGLIGFGSSAPGLSLVGGT-IDLAGGLTNYAFSMPRDGIITSLAAYFSATAALALLGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125470  336 VQVQIQILTAPPASNTFT-VQGAPLLLTPAFA-AIAIGSTASGIIA-EAIPVTAGDKILLYVSLTA--ASPIAAVAGFVS 410
Cdd:TIGR03721  80 VTITAQLYIAPAPSNVFTpVPGAPVTLTPPITgPIAVGSTASGIITgLNIPVTAGDRLLLVVSATAsgLSPIATVAGYVS 159


                  ....*.
gi 446125470  411 AGINIV 416
Cdd:TIGR03721 160 AGLAIV 165
N_to_GlyXaaXaa NF033172
collagen-like repeat preface domain; All protein sequence used in the seed alignment for this ...
 31-133 3.13e-17

collagen-like repeat preface domain; All protein sequence used in the seed alignment for this model comes from the N-terminal region of proteins with extended collagen-like Gly-rich repeat regions, and occur in Firmicutes.


Pssm-ID: 467978  Cd Length: 122  Bit Score: 77.33  E-value: 3.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125470  31 ITSEQLGRLITLLNSLISAIAAFFANPSDANRLALLNLFTQLLN-LLNELPPSPEGNYLKQLIQSIINVLQSPNPDLSQL 109
Cdd:NF033172   1 ISKSQLTRLISLLQELTTLIPAVFTNPTPSNISALQNLLRQLLKfLNSLNLSSAEKAALLSIIENLITILESPPFSPGAL 80

                         90       100
                 ....*....|....*....|....
gi 446125470 110 LSLLQQFYSALAPFFFSLIIDPAS 133
Cdd:NF033172  81 AILLQQLLNALLSIVLLFKIDPCI 104
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 202-242 2.20e-07

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: 47.49  E-value: 2.20e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 446125470  202 GPTGPTGDTGATGPTGPTGDTGATGPTGPTGDTGPTGATGP 242
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGP 41
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 202-242 3.32e-07

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: 46.72  E-value: 3.32e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 446125470  202 GPTGPTGDTGATGPTGPTGDTGATGPTGPTGDTGPTGATGP 242
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 200-242 6.54e-07

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: 45.95  E-value: 6.54e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 446125470  200 ATGPTGPTGDTGATGPTGPTGDTGATGPTGPTGDTGPTGATGP 242
Cdd:pfam01391  11 PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 202-242 2.85e-06

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: 44.41  E-value: 2.85e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 446125470  202 GPTGPTGDTGATGPTGPTGDTGATGPTGPTGDTGPTGATGP 242
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGP 44
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 200-242 2.90e-06

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: 44.02  E-value: 2.90e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 446125470  200 ATGPTGPTGDTGATGPTGPTGDTGATGPTGPTGDTGPTGATGP 242
Cdd:pfam01391   8 PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 202-242 7.82e-06

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: 42.87  E-value: 7.82e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 446125470  202 GPTGPTGDTGATGPTGPTGDTGATGPTGPTGDTGPTGATGP 242
Cdd:pfam01391  16 GPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 199-242 1.09e-05

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: 47.21  E-value: 1.09e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446125470 199 GATGPTGPTGDTGATGPTGPTGDTGATGPTGPTGDTGPTGATGP 242
Cdd:NF038329 168 GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 182-242 1.22e-05

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: 47.21  E-value: 1.22e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125470 182 DTGATGPTGPTGPTGDTGATGPTGPTGDTGATGPTGPTGD---TGATGPTGPTGDTGPTGATGP 242
Cdd:NF038329 139 DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKdgeAGAKGPAGEKGPQGPRGETGP 202
 
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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