collagen alpha-2(XI) chain isoform X7 [Rattus norvegicus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| COLFI | smart00038 | Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1596-1791 | 1.41e-99 | |||||
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc. : Pssm-ID: 197483 Cd Length: 232 Bit Score: 319.42 E-value: 1.41e-99
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| TSPN | smart00210 | Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
169-350 | 1.32e-60 | |||||
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin : Pssm-ID: 214560 Cd Length: 184 Bit Score: 206.05 E-value: 1.32e-60
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| gly_rich_SclB super family | cl45768 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
564-830 | 2.78e-34 | |||||
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: 138.11 E-value: 2.78e-34
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| gly_rich_SclB super family | cl45768 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1278-1500 | 7.49e-31 | |||||
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: 128.10 E-value: 7.49e-31
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| gly_rich_SclB super family | cl45768 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
433-667 | 3.77e-21 | |||||
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: 98.82 E-value: 3.77e-21
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| gly_rich_SclB super family | cl45768 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
756-1059 | 4.86e-19 | |||||
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: 92.28 E-value: 4.86e-19
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| gly_rich_SclB super family | cl45768 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
956-1224 | 9.06e-10 | |||||
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: 63.00 E-value: 9.06e-10
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| gly_rich_SclB super family | cl45768 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1464-1561 | 3.29e-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. The actual alignment was detected with superfamily member NF038329: Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 48.36 E-value: 3.29e-05
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| Name | Accession | Description | Interval | E-value | ||||||
| COLFI | smart00038 | Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1596-1791 | 1.41e-99 | ||||||
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc. Pssm-ID: 197483 Cd Length: 232 Bit Score: 319.42 E-value: 1.41e-99
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| COLFI | pfam01410 | Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1595-1790 | 1.93e-76 | ||||||
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc. Pssm-ID: 460199 Cd Length: 233 Bit Score: 253.42 E-value: 1.93e-76
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| TSPN | smart00210 | Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
169-350 | 1.32e-60 | ||||||
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin Pssm-ID: 214560 Cd Length: 184 Bit Score: 206.05 E-value: 1.32e-60
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
564-830 | 2.78e-34 | ||||||
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: 138.11 E-value: 2.78e-34
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
644-917 | 3.44e-32 | ||||||
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: 131.95 E-value: 3.44e-32
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
542-769 | 4.71e-31 | ||||||
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: 128.48 E-value: 4.71e-31
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1278-1500 | 7.49e-31 | ||||||
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: 128.10 E-value: 7.49e-31
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1344-1503 | 1.72e-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: 111.92 E-value: 1.72e-25
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1352-1540 | 6.31e-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: 109.99 E-value: 6.31e-25
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
433-667 | 3.77e-21 | ||||||
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: 98.82 E-value: 3.77e-21
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1104-1412 | 1.14e-19 | ||||||
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: 94.20 E-value: 1.14e-19
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
756-1059 | 4.86e-19 | ||||||
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: 92.28 E-value: 4.86e-19
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
843-1059 | 3.20e-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: 89.58 E-value: 3.20e-18
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1054-1428 | 2.47e-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: 80.72 E-value: 2.47e-15
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| LamG | cd00110 | Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
196-347 | 3.59e-10 | ||||||
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules. Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 60.12 E-value: 3.59e-10
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
956-1224 | 9.06e-10 | ||||||
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: 63.00 E-value: 9.06e-10
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| Laminin_G_2 | pfam02210 | Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
227-347 | 2.17e-09 | ||||||
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily. Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 57.04 E-value: 2.17e-09
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| SPT5 | COG5164 | Transcription elongation factor SPT5 [Transcription]; |
1184-1439 | 8.11e-09 | ||||||
Transcription elongation factor SPT5 [Transcription]; Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 60.04 E-value: 8.11e-09
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1365-1420 | 3.79e-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: 45.56 E-value: 3.79e-06
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
711-766 | 7.17e-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: 44.79 E-value: 7.17e-06
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1464-1561 | 3.29e-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: 48.36 E-value: 3.29e-05
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| GGGWT_bact | NF040941 | fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ... |
1626-1665 | 1.03e-04 | ||||||
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV. Pssm-ID: 468872 [Multi-domain] Cd Length: 46 Bit Score: 41.39 E-value: 1.03e-04
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
864-918 | 1.25e-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: 1.25e-04
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| PHA03169 | PHA03169 | hypothetical protein; Provisional |
1266-1422 | 6.23e-04 | ||||||
hypothetical protein; Provisional Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 44.19 E-value: 6.23e-04
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| SPT5 | COG5164 | Transcription elongation factor SPT5 [Transcription]; |
825-1017 | 9.45e-03 | ||||||
Transcription elongation factor SPT5 [Transcription]; Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 40.78 E-value: 9.45e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| COLFI | smart00038 | Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1596-1791 | 1.41e-99 | ||||||
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc. Pssm-ID: 197483 Cd Length: 232 Bit Score: 319.42 E-value: 1.41e-99
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| COLFI | pfam01410 | Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1595-1790 | 1.93e-76 | ||||||
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc. Pssm-ID: 460199 Cd Length: 233 Bit Score: 253.42 E-value: 1.93e-76
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| TSPN | smart00210 | Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
169-350 | 1.32e-60 | ||||||
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin Pssm-ID: 214560 Cd Length: 184 Bit Score: 206.05 E-value: 1.32e-60
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
564-830 | 2.78e-34 | ||||||
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: 138.11 E-value: 2.78e-34
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
644-917 | 3.44e-32 | ||||||
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: 131.95 E-value: 3.44e-32
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
542-769 | 4.71e-31 | ||||||
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: 128.48 E-value: 4.71e-31
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1278-1500 | 7.49e-31 | ||||||
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: 128.10 E-value: 7.49e-31
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1344-1503 | 1.72e-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: 111.92 E-value: 1.72e-25
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1352-1540 | 6.31e-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: 109.99 E-value: 6.31e-25
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
433-667 | 3.77e-21 | ||||||
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: 98.82 E-value: 3.77e-21
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1104-1412 | 1.14e-19 | ||||||
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: 94.20 E-value: 1.14e-19
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
756-1059 | 4.86e-19 | ||||||
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: 92.28 E-value: 4.86e-19
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
843-1059 | 3.20e-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: 89.58 E-value: 3.20e-18
|
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1054-1428 | 2.47e-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: 80.72 E-value: 2.47e-15
|
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| LamG | smart00282 | Laminin G domain; |
227-347 | 6.66e-13 | ||||||
Laminin G domain; Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 67.36 E-value: 6.66e-13
|
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| LamG | cd00110 | Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
196-347 | 3.59e-10 | ||||||
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules. Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 60.12 E-value: 3.59e-10
|
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
956-1224 | 9.06e-10 | ||||||
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: 63.00 E-value: 9.06e-10
|
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| Laminin_G_2 | pfam02210 | Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
227-347 | 2.17e-09 | ||||||
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily. Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 57.04 E-value: 2.17e-09
|
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| SPT5 | COG5164 | Transcription elongation factor SPT5 [Transcription]; |
1184-1439 | 8.11e-09 | ||||||
Transcription elongation factor SPT5 [Transcription]; Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 60.04 E-value: 8.11e-09
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1365-1420 | 3.79e-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: 45.56 E-value: 3.79e-06
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1347-1403 | 6.25e-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: 6.25e-06
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
711-766 | 7.17e-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: 44.79 E-value: 7.17e-06
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1368-1422 | 1.40e-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: 44.02 E-value: 1.40e-05
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1344-1397 | 2.40e-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: 43.25 E-value: 2.40e-05
|
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1464-1561 | 3.29e-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: 48.36 E-value: 3.29e-05
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
558-614 | 3.81e-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: 3.81e-05
|
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
552-608 | 4.04e-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: 42.87 E-value: 4.04e-05
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
573-629 | 4.28e-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: 4.28e-05
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1386-1442 | 6.34e-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: 6.34e-05
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
720-776 | 7.28e-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: 7.28e-05
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
606-661 | 8.69e-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: 8.69e-05
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
541-594 | 9.12e-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: 9.12e-05
|
||||||||||
| GGGWT_bact | NF040941 | fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ... |
1626-1665 | 1.03e-04 | ||||||
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV. Pssm-ID: 468872 [Multi-domain] Cd Length: 46 Bit Score: 41.39 E-value: 1.03e-04
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1383-1438 | 1.07e-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: 41.71 E-value: 1.07e-04
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
864-918 | 1.25e-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: 1.25e-04
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
594-648 | 1.41e-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: 1.41e-04
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
600-656 | 1.43e-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: 41.33 E-value: 1.43e-04
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
732-786 | 2.37e-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: 40.55 E-value: 2.37e-04
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1380-1436 | 2.41e-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: 40.55 E-value: 2.41e-04
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
849-905 | 5.20e-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: 5.20e-04
|
||||||||||
| PHA03169 | PHA03169 | hypothetical protein; Provisional |
1266-1422 | 6.23e-04 | ||||||
hypothetical protein; Provisional Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 44.19 E-value: 6.23e-04
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
723-777 | 6.99e-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: 6.99e-04
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
726-780 | 7.71e-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: 7.71e-04
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
738-793 | 8.18e-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: 8.18e-04
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
828-884 | 8.50e-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: 8.50e-04
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
816-870 | 1.03e-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: 39.01 E-value: 1.03e-03
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
747-801 | 1.52e-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: 1.52e-03
|
||||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
813-867 | 3.12e-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: 37.47 E-value: 3.12e-03
|
||||||||||
| PHA03169 | PHA03169 | hypothetical protein; Provisional |
1263-1419 | 3.31e-03 | ||||||
hypothetical protein; Provisional Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 41.88 E-value: 3.31e-03
|
||||||||||
| PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
1269-1427 | 3.64e-03 | ||||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.28 E-value: 3.64e-03
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
786-841 | 9.04e-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: 9.04e-03
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| SPT5 | COG5164 | Transcription elongation factor SPT5 [Transcription]; |
825-1017 | 9.45e-03 | ||||||
Transcription elongation factor SPT5 [Transcription]; Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 40.78 E-value: 9.45e-03
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