Collagen alpha-2(IV) chain [Caenorhabditis elegans]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| C4 | pfam01413 | C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1641-1751 | 1.49e-63 | |||||
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome. : Pssm-ID: 460201 Cd Length: 110 Bit Score: 211.30 E-value: 1.49e-63
|
|||||||||
| C4 | pfam01413 | C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1533-1638 | 8.30e-60 | |||||
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome. : Pssm-ID: 460201 Cd Length: 110 Bit Score: 200.51 E-value: 8.30e-60
|
|||||||||
| gly_rich_SclB super family | cl45768 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1003-1239 | 4.10e-26 | |||||
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: 113.85 E-value: 4.10e-26
|
|||||||||
| gly_rich_SclB super family | cl45768 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
725-961 | 2.50e-23 | |||||
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: 105.37 E-value: 2.50e-23
|
|||||||||
| gly_rich_SclB super family | cl45768 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
389-606 | 3.59e-20 | |||||
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: 95.74 E-value: 3.59e-20
|
|||||||||
| gly_rich_SclB super family | cl45768 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1283-1504 | 1.38e-18 | |||||
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: 90.73 E-value: 1.38e-18
|
|||||||||
| gly_rich_SclB super family | cl45768 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
601-833 | 3.44e-14 | |||||
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: 76.87 E-value: 3.44e-14
|
|||||||||
| gly_rich_SclB super family | cl45768 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
63-317 | 3.68e-13 | |||||
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: 73.79 E-value: 3.68e-13
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| C4 | pfam01413 | C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1641-1751 | 1.49e-63 | |||||
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome. Pssm-ID: 460201 Cd Length: 110 Bit Score: 211.30 E-value: 1.49e-63
|
|||||||||
| C4 | pfam01413 | C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1533-1638 | 8.30e-60 | |||||
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome. Pssm-ID: 460201 Cd Length: 110 Bit Score: 200.51 E-value: 8.30e-60
|
|||||||||
| C4 | smart00111 | C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1640-1753 | 5.86e-59 | |||||
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome. Pssm-ID: 128421 Cd Length: 114 Bit Score: 198.38 E-value: 5.86e-59
|
|||||||||
| C4 | smart00111 | C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1532-1639 | 8.21e-55 | |||||
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome. Pssm-ID: 128421 Cd Length: 114 Bit Score: 186.44 E-value: 8.21e-55
|
|||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1003-1239 | 4.10e-26 | |||||
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: 113.85 E-value: 4.10e-26
|
|||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
976-1189 | 6.98e-26 | |||||
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: 113.08 E-value: 6.98e-26
|
|||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1022-1252 | 1.36e-25 | |||||
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: 112.31 E-value: 1.36e-25
|
|||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
725-961 | 2.50e-23 | |||||
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: 105.37 E-value: 2.50e-23
|
|||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
811-1053 | 7.74e-23 | |||||
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: 103.83 E-value: 7.74e-23
|
|||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1101-1370 | 2.14e-22 | |||||
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: 102.29 E-value: 2.14e-22
|
|||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
389-606 | 3.59e-20 | |||||
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: 95.74 E-value: 3.59e-20
|
|||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
709-946 | 3.82e-20 | |||||
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: 95.36 E-value: 3.82e-20
|
|||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1283-1504 | 1.38e-18 | |||||
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: 90.73 E-value: 1.38e-18
|
|||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
494-728 | 1.73e-17 | |||||
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: 87.27 E-value: 1.73e-17
|
|||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
644-898 | 1.97e-15 | |||||
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: 81.10 E-value: 1.97e-15
|
|||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1296-1512 | 5.81e-15 | |||||
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: 79.56 E-value: 5.81e-15
|
|||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
223-528 | 1.79e-14 | |||||
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: 78.02 E-value: 1.79e-14
|
|||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
601-833 | 3.44e-14 | |||||
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: 76.87 E-value: 3.44e-14
|
|||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
63-317 | 3.68e-13 | |||||
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: 73.79 E-value: 3.68e-13
|
|||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
824-879 | 2.01e-05 | |||||
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: 43.64 E-value: 2.01e-05
|
|||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
41-218 | 2.93e-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: 48.75 E-value: 2.93e-05
|
|||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1338-1392 | 8.04e-05 | |||||
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: 42.10 E-value: 8.04e-05
|
|||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1075-1131 | 1.28e-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: 41.33 E-value: 1.28e-04
|
|||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
473-531 | 2.28e-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: 37.86 E-value: 2.28e-03
|
|||||||||
| PRK14959 | PRK14959 | DNA polymerase III subunits gamma and tau; Provisional |
818-947 | 2.49e-03 | |||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 42.74 E-value: 2.49e-03
|
|||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
180-228 | 5.92e-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: 36.70 E-value: 5.92e-03
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||||||
| C4 | pfam01413 | C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1641-1751 | 1.49e-63 | |||||||||
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome. Pssm-ID: 460201 Cd Length: 110 Bit Score: 211.30 E-value: 1.49e-63
|
|||||||||||||
| C4 | pfam01413 | C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1533-1638 | 8.30e-60 | |||||||||
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome. Pssm-ID: 460201 Cd Length: 110 Bit Score: 200.51 E-value: 8.30e-60
|
|||||||||||||
| C4 | smart00111 | C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1640-1753 | 5.86e-59 | |||||||||
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome. Pssm-ID: 128421 Cd Length: 114 Bit Score: 198.38 E-value: 5.86e-59
|
|||||||||||||
| C4 | smart00111 | C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1532-1639 | 8.21e-55 | |||||||||
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome. Pssm-ID: 128421 Cd Length: 114 Bit Score: 186.44 E-value: 8.21e-55
|
|||||||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1003-1239 | 4.10e-26 | |||||||||
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: 113.85 E-value: 4.10e-26
|
|||||||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
976-1189 | 6.98e-26 | |||||||||
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: 113.08 E-value: 6.98e-26
|
|||||||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1022-1252 | 1.36e-25 | |||||||||
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: 112.31 E-value: 1.36e-25
|
|||||||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
725-961 | 2.50e-23 | |||||||||
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: 105.37 E-value: 2.50e-23
|
|||||||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
811-1053 | 7.74e-23 | |||||||||
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: 103.83 E-value: 7.74e-23
|
|||||||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1101-1370 | 2.14e-22 | |||||||||
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: 102.29 E-value: 2.14e-22
|
|||||||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
389-606 | 3.59e-20 | |||||||||
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: 95.74 E-value: 3.59e-20
|
|||||||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
709-946 | 3.82e-20 | |||||||||
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: 95.36 E-value: 3.82e-20
|
|||||||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1283-1504 | 1.38e-18 | |||||||||
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: 90.73 E-value: 1.38e-18
|
|||||||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
494-728 | 1.73e-17 | |||||||||
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: 87.27 E-value: 1.73e-17
|
|||||||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
644-898 | 1.97e-15 | |||||||||
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: 81.10 E-value: 1.97e-15
|
|||||||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1296-1512 | 5.81e-15 | |||||||||
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: 79.56 E-value: 5.81e-15
|
|||||||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
223-528 | 1.79e-14 | |||||||||
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: 78.02 E-value: 1.79e-14
|
|||||||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
601-833 | 3.44e-14 | |||||||||
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: 76.87 E-value: 3.44e-14
|
|||||||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
63-317 | 3.68e-13 | |||||||||
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: 73.79 E-value: 3.68e-13
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
824-879 | 2.01e-05 | |||||||||
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: 43.64 E-value: 2.01e-05
|
|||||||||||||
| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
41-218 | 2.93e-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: 48.75 E-value: 2.93e-05
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
902-958 | 7.07e-05 | |||||||||
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: 42.10 E-value: 7.07e-05
|
|||||||||||||
| Glutenin_hmw | pfam03157 | High molecular weight glutenin subunit; Members of this family include high molecular weight ... |
725-1299 | 7.71e-05 | |||||||||
High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm. Pssm-ID: 367362 [Multi-domain] Cd Length: 786 Bit Score: 47.63 E-value: 7.71e-05
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1338-1392 | 8.04e-05 | |||||||||
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: 42.10 E-value: 8.04e-05
|
|||||||||||||
| Glutenin_hmw | pfam03157 | High molecular weight glutenin subunit; Members of this family include high molecular weight ... |
726-1350 | 8.91e-05 | |||||||||
High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm. Pssm-ID: 367362 [Multi-domain] Cd Length: 786 Bit Score: 47.63 E-value: 8.91e-05
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1075-1131 | 1.28e-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: 41.33 E-value: 1.28e-04
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1311-1367 | 1.49e-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: 41.33 E-value: 1.49e-04
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1007-1061 | 1.70e-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: 40.94 E-value: 1.70e-04
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
863-919 | 1.73e-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: 40.94 E-value: 1.73e-04
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1072-1128 | 1.75e-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: 40.94 E-value: 1.75e-04
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1350-1405 | 1.82e-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: 40.94 E-value: 1.82e-04
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
854-908 | 1.87e-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: 40.94 E-value: 1.87e-04
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
851-907 | 1.95e-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: 40.94 E-value: 1.95e-04
|
|||||||||||||
| Glutenin_hmw | pfam03157 | High molecular weight glutenin subunit; Members of this family include high molecular weight ... |
835-1405 | 1.98e-04 | |||||||||
High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm. Pssm-ID: 367362 [Multi-domain] Cd Length: 786 Bit Score: 46.48 E-value: 1.98e-04
|
|||||||||||||
| Glutenin_hmw | pfam03157 | High molecular weight glutenin subunit; Members of this family include high molecular weight ... |
673-1268 | 2.36e-04 | |||||||||
High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm. Pssm-ID: 367362 [Multi-domain] Cd Length: 786 Bit Score: 46.09 E-value: 2.36e-04
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
887-943 | 3.03e-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: 40.17 E-value: 3.03e-04
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
839-895 | 4.03e-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: 39.78 E-value: 4.03e-04
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
893-947 | 4.32e-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: 39.78 E-value: 4.32e-04
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
866-920 | 4.58e-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: 39.78 E-value: 4.58e-04
|
|||||||||||||
| Glutenin_hmw | pfam03157 | High molecular weight glutenin subunit; Members of this family include high molecular weight ... |
667-1245 | 4.77e-04 | |||||||||
High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm. Pssm-ID: 367362 [Multi-domain] Cd Length: 786 Bit Score: 44.94 E-value: 4.77e-04
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1084-1139 | 5.58e-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: 39.40 E-value: 5.58e-04
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1093-1149 | 8.43e-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: 39.01 E-value: 8.43e-04
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1329-1383 | 9.30e-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: 39.01 E-value: 9.30e-04
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1326-1378 | 1.08e-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: 38.63 E-value: 1.08e-03
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1019-1070 | 1.78e-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: 38.24 E-value: 1.78e-03
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1296-1350 | 1.91e-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: 37.86 E-value: 1.91e-03
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
473-531 | 2.28e-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: 37.86 E-value: 2.28e-03
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1120-1176 | 2.30e-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: 37.86 E-value: 2.30e-03
|
|||||||||||||
| PRK14959 | PRK14959 | DNA polymerase III subunits gamma and tau; Provisional |
818-947 | 2.49e-03 | |||||||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 42.74 E-value: 2.49e-03
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1290-1344 | 2.97e-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: 37.47 E-value: 2.97e-03
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1359-1406 | 3.92e-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: 37.09 E-value: 3.92e-03
|
|||||||||||||
| Med15 | pfam09606 | ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
661-958 | 4.05e-03 | |||||||||
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development. Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 41.92 E-value: 4.05e-03
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1138-1189 | 4.91e-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: 36.70 E-value: 4.91e-03
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1204-1253 | 5.06e-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: 36.70 E-value: 5.06e-03
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1293-1349 | 5.87e-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: 36.70 E-value: 5.87e-03
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
180-228 | 5.92e-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: 36.70 E-value: 5.92e-03
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
460-511 | 6.35e-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: 36.70 E-value: 6.35e-03
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1096-1150 | 7.81e-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: 36.32 E-value: 7.81e-03
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1111-1166 | 8.12e-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: 36.32 E-value: 8.12e-03
|
|||||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1326-1382 | 9.79e-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: 35.93 E-value: 9.79e-03
|
|||||||||||||
| Med15 | pfam09606 | ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
393-738 | 9.95e-03 | |||||||||
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development. Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 40.76 E-value: 9.95e-03
|
|||||||||||||
| Blast search parameters | ||||
|
