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collagen alpha-1(IX) chain isoform 2 precursor [Homo sapiens]
collagen-like domain-containing protein( domain architecture ID 1903237)
collagen-like domain-containing protein such as collagens, which are extracellular structural proteins involved in formation of connective tissue structure
List of domain hits
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Name | Accession | Description | Interval | E-value | |||||
gly_rich_SclB super family | cl45768 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
184-474 | 2.47e-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. The actual alignment was detected with superfamily member NF038329: Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 109.61 E-value: 2.47e-25
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gly_rich_SclB super family | cl45768 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
358-622 | 4.54e-12 | |||||
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: 68.78 E-value: 4.54e-12
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Name | Accession | Description | Interval | E-value | ||||||
gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
184-474 | 2.47e-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: 109.61 E-value: 2.47e-25
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gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
173-378 | 2.45e-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: 103.45 E-value: 2.45e-23
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gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
46-354 | 6.01e-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: 83.80 E-value: 6.01e-17
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gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
323-516 | 1.54e-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: 73.40 E-value: 1.54e-13
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gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
211-552 | 1.84e-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: 73.02 E-value: 1.84e-13
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gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
358-622 | 4.54e-12 | ||||||
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: 68.78 E-value: 4.54e-12
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gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
454-640 | 4.92e-08 | ||||||
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: 55.68 E-value: 4.92e-08
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gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
364-640 | 5.23e-08 | ||||||
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: 55.68 E-value: 5.23e-08
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
253-309 | 8.03e-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: 46.33 E-value: 8.03e-07
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PRK14959 | PRK14959 | DNA polymerase III subunits gamma and tau; Provisional |
258-379 | 4.47e-03 | ||||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 40.05 E-value: 4.47e-03
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Name | Accession | Description | Interval | E-value | ||||||
gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
184-474 | 2.47e-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: 109.61 E-value: 2.47e-25
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gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
173-378 | 2.45e-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: 103.45 E-value: 2.45e-23
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gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
46-354 | 6.01e-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: 83.80 E-value: 6.01e-17
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gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
323-516 | 1.54e-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: 73.40 E-value: 1.54e-13
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gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
211-552 | 1.84e-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: 73.02 E-value: 1.84e-13
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gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
358-622 | 4.54e-12 | ||||||
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: 68.78 E-value: 4.54e-12
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gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
454-640 | 4.92e-08 | ||||||
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: 55.68 E-value: 4.92e-08
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gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
364-640 | 5.23e-08 | ||||||
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: 55.68 E-value: 5.23e-08
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
253-309 | 8.03e-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: 46.33 E-value: 8.03e-07
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
244-298 | 8.43e-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: 46.33 E-value: 8.43e-07
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
340-396 | 2.16e-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: 45.18 E-value: 2.16e-06
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
214-270 | 5.18e-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: 5.18e-06
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
238-292 | 8.29e-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: 43.64 E-value: 8.29e-06
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
220-276 | 1.36e-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: 42.87 E-value: 1.36e-05
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
241-297 | 1.57e-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: 42.87 E-value: 1.57e-05
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
235-290 | 2.57e-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: 2.57e-05
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
232-288 | 4.19e-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: 41.71 E-value: 4.19e-05
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
331-386 | 8.43e-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: 40.55 E-value: 8.43e-05
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
328-384 | 8.85e-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: 40.55 E-value: 8.85e-05
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
262-310 | 1.31e-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: 1.31e-04
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
223-278 | 1.89e-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: 1.89e-04
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
175-229 | 5.15e-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: 38.63 E-value: 5.15e-04
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
349-397 | 5.46e-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: 38.24 E-value: 5.46e-04
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
211-267 | 8.26e-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: 37.86 E-value: 8.26e-04
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
259-310 | 9.48e-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: 37.86 E-value: 9.48e-04
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
208-264 | 1.09e-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: 1.09e-03
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
324-375 | 1.29e-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: 1.29e-03
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PRK14959 | PRK14959 | DNA polymerase III subunits gamma and tau; Provisional |
258-379 | 4.47e-03 | ||||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 40.05 E-value: 4.47e-03
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Blast search parameters | ||||
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