collagen alpha-1(XXVII) chain A precursor [Danio rerio]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| COLFI super family | cl02436 | Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1589-1783 | 1.17e-40 | |||||
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. The actual alignment was detected with superfamily member smart00038: Pssm-ID: 470578 Cd Length: 232 Bit Score: 150.70 E-value: 1.17e-40
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| gly_rich_SclB super family | cl45768 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1261-1493 | 2.47e-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: 138.50 E-value: 2.47e-34
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| gly_rich_SclB super family | cl45768 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
654-875 | 7.49e-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: 136.96 E-value: 7.49e-34
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| gly_rich_SclB super family | cl45768 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1072-1325 | 1.52e-33 | |||||
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: 136.19 E-value: 1.52e-33
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| gly_rich_SclB super family | cl45768 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
893-1162 | 6.20e-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. The actual alignment was detected with superfamily member NF038329: Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 131.18 E-value: 6.20e-32
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| LamG super family | cl22861 | Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
41-220 | 7.58e-15 | |||||
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. The actual alignment was detected with superfamily member smart00210: Pssm-ID: 473984 Cd Length: 184 Bit Score: 74.70 E-value: 7.58e-15
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| PHA03247 super family | cl33720 | large tegument protein UL36; Provisional |
329-525 | 7.10e-11 | |||||
large tegument protein UL36; Provisional The actual alignment was detected with superfamily member PHA03247: Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 68.04 E-value: 7.10e-11
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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 ... |
1589-1783 | 1.17e-40 | |||||
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: 150.70 E-value: 1.17e-40
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| COLFI | pfam01410 | Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1589-1782 | 7.08e-40 | |||||
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: 148.26 E-value: 7.08e-40
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1261-1493 | 2.47e-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: 138.50 E-value: 2.47e-34
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
654-875 | 7.49e-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: 136.96 E-value: 7.49e-34
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1072-1325 | 1.52e-33 | |||||
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: 136.19 E-value: 1.52e-33
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
893-1162 | 6.20e-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: 131.18 E-value: 6.20e-32
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
700-953 | 1.26e-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: 130.41 E-value: 1.26e-31
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
764-1047 | 5.65e-30 | |||||
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: 125.40 E-value: 5.65e-30
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1344-1527 | 3.62e-27 | |||||
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: 116.93 E-value: 3.62e-27
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
548-820 | 3.62e-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: 110.77 E-value: 3.62e-25
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1398-1529 | 2.12e-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: 90.35 E-value: 2.12e-18
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| TSPN | smart00210 | Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
41-220 | 7.58e-15 | |||||
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin Pssm-ID: 214560 Cd Length: 184 Bit Score: 74.70 E-value: 7.58e-15
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| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
329-525 | 7.10e-11 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 68.04 E-value: 7.10e-11
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| SPT5 | COG5164 | Transcription elongation factor SPT5 [Transcription]; |
704-959 | 8.49e-10 | |||||
Transcription elongation factor SPT5 [Transcription]; Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 63.51 E-value: 8.49e-10
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| PspC_subgroup_2 | NF033839 | pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
334-521 | 2.66e-08 | |||||
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 58.63 E-value: 2.66e-08
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| LamG | cd00110 | Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
69-210 | 2.27e-07 | |||||
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: 52.04 E-value: 2.27e-07
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| PspC_subgroup_2 | NF033839 | pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
328-481 | 5.64e-07 | |||||
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 54.39 E-value: 5.64e-07
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| PspC_subgroup_2 | NF033839 | pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
324-489 | 1.69e-06 | |||||
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 52.85 E-value: 1.69e-06
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
689-745 | 5.37e-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: 5.37e-06
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| Herpes_BLLF1 | pfam05109 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
330-534 | 1.30e-05 | |||||
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo. Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 50.30 E-value: 1.30e-05
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1272-1326 | 1.66e-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: 1.66e-05
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
989-1043 | 3.30e-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: 3.30e-05
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| Laminin_G_2 | pfam02210 | Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
107-210 | 1.26e-04 | |||||
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: 43.56 E-value: 1.26e-04
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| SPT5 | COG5164 | Transcription elongation factor SPT5 [Transcription]; |
890-1143 | 1.34e-04 | |||||
Transcription elongation factor SPT5 [Transcription]; Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 46.56 E-value: 1.34e-04
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| PspC_subgroup_2 | NF033839 | pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
359-529 | 2.69e-04 | |||||
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 45.53 E-value: 2.69e-04
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1124-1180 | 1.33e-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: 1.33e-03
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| PHA03169 | PHA03169 | hypothetical protein; Provisional |
1001-1179 | 2.12e-03 | |||||
hypothetical protein; Provisional Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 42.65 E-value: 2.12e-03
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| PHA03169 | PHA03169 | hypothetical protein; Provisional |
1343-1494 | 2.27e-03 | |||||
hypothetical protein; Provisional Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 42.65 E-value: 2.27e-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 ... |
1589-1783 | 1.17e-40 | |||||
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: 150.70 E-value: 1.17e-40
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| COLFI | pfam01410 | Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1589-1782 | 7.08e-40 | |||||
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: 148.26 E-value: 7.08e-40
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1261-1493 | 2.47e-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: 138.50 E-value: 2.47e-34
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
654-875 | 7.49e-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: 136.96 E-value: 7.49e-34
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1072-1325 | 1.52e-33 | |||||
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: 136.19 E-value: 1.52e-33
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
893-1162 | 6.20e-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: 131.18 E-value: 6.20e-32
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
700-953 | 1.26e-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: 130.41 E-value: 1.26e-31
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
764-1047 | 5.65e-30 | |||||
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: 125.40 E-value: 5.65e-30
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1344-1527 | 3.62e-27 | |||||
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: 116.93 E-value: 3.62e-27
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
548-820 | 3.62e-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: 110.77 E-value: 3.62e-25
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| gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1398-1529 | 2.12e-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: 90.35 E-value: 2.12e-18
|
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| TSPN | smart00210 | Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
41-220 | 7.58e-15 | |||||
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin Pssm-ID: 214560 Cd Length: 184 Bit Score: 74.70 E-value: 7.58e-15
|
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| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
329-525 | 7.10e-11 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 68.04 E-value: 7.10e-11
|
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| SPT5 | COG5164 | Transcription elongation factor SPT5 [Transcription]; |
704-959 | 8.49e-10 | |||||
Transcription elongation factor SPT5 [Transcription]; Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 63.51 E-value: 8.49e-10
|
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| PTZ00449 | PTZ00449 | 104 kDa microneme/rhoptry antigen; Provisional |
322-526 | 1.56e-08 | |||||
104 kDa microneme/rhoptry antigen; Provisional Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 59.70 E-value: 1.56e-08
|
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| PspC_subgroup_2 | NF033839 | pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
334-521 | 2.66e-08 | |||||
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 58.63 E-value: 2.66e-08
|
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| LamG | smart00282 | Laminin G domain; |
95-210 | 4.80e-08 | |||||
Laminin G domain; Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 53.50 E-value: 4.80e-08
|
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| LamG | cd00110 | Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
69-210 | 2.27e-07 | |||||
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: 52.04 E-value: 2.27e-07
|
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| PspC_subgroup_2 | NF033839 | pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
328-481 | 5.64e-07 | |||||
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 54.39 E-value: 5.64e-07
|
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| PspC_subgroup_2 | NF033839 | pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
324-489 | 1.69e-06 | |||||
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 52.85 E-value: 1.69e-06
|
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
689-745 | 5.37e-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: 5.37e-06
|
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| PHA02682 | PHA02682 | ORF080 virion core protein; Provisional |
318-524 | 7.64e-06 | |||||
ORF080 virion core protein; Provisional Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 49.86 E-value: 7.64e-06
|
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| SPT5 | COG5164 | Transcription elongation factor SPT5 [Transcription]; |
655-893 | 7.89e-06 | |||||
Transcription elongation factor SPT5 [Transcription]; Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 50.41 E-value: 7.89e-06
|
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
656-712 | 1.01e-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: 44.41 E-value: 1.01e-05
|
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| PTZ00449 | PTZ00449 | 104 kDa microneme/rhoptry antigen; Provisional |
319-549 | 1.02e-05 | |||||
104 kDa microneme/rhoptry antigen; Provisional Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 50.46 E-value: 1.02e-05
|
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| Herpes_BLLF1 | pfam05109 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
330-534 | 1.30e-05 | |||||
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo. Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 50.30 E-value: 1.30e-05
|
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1272-1326 | 1.66e-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: 1.66e-05
|
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
701-757 | 1.98e-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: 1.98e-05
|
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
989-1043 | 3.30e-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: 3.30e-05
|
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1410-1464 | 4.52e-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: 42.48 E-value: 4.52e-05
|
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| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
331-521 | 5.37e-05 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.40 E-value: 5.37e-05
|
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| HC2 | pfam07382 | Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ... |
322-479 | 5.64e-05 | |||||
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles. Pssm-ID: 369339 [Multi-domain] Cd Length: 187 Bit Score: 45.93 E-value: 5.64e-05
|
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
695-746 | 7.24e-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: 7.24e-05
|
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1413-1467 | 1.03e-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: 41.71 E-value: 1.03e-04
|
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| Laminin_G_2 | pfam02210 | Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
107-210 | 1.26e-04 | |||||
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: 43.56 E-value: 1.26e-04
|
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| SPT5 | COG5164 | Transcription elongation factor SPT5 [Transcription]; |
890-1143 | 1.34e-04 | |||||
Transcription elongation factor SPT5 [Transcription]; Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 46.56 E-value: 1.34e-04
|
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| Laminin_G_1 | pfam00054 | Laminin G domain; |
121-212 | 1.61e-04 | |||||
Laminin G domain; Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 43.46 E-value: 1.61e-04
|
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
704-758 | 1.74e-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: 1.74e-04
|
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| KAR9 | pfam08580 | Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal ... |
312-537 | 1.95e-04 | |||||
Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal protein required for karyogamy, correct positioning of the mitotic spindle and for orientation of cytoplasmic microtubules. KAR9 localizes at the shmoo tip in mating cells and at the tip of the growing bud in anaphase. Pssm-ID: 430088 [Multi-domain] Cd Length: 684 Bit Score: 46.36 E-value: 1.95e-04
|
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| Herpes_BLLF1 | pfam05109 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
315-534 | 1.98e-04 | |||||
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo. Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 46.45 E-value: 1.98e-04
|
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1269-1324 | 2.36e-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: 2.36e-04
|
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
692-746 | 2.45e-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: 2.45e-04
|
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| Atrophin-1 | pfam03154 | Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
322-524 | 2.69e-04 | |||||
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity. Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 45.91 E-value: 2.69e-04
|
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| PspC_subgroup_2 | NF033839 | pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
359-529 | 2.69e-04 | |||||
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 45.53 E-value: 2.69e-04
|
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| PRK07003 | PRK07003 | DNA polymerase III subunit gamma/tau; |
334-524 | 2.71e-04 | |||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 46.00 E-value: 2.71e-04
|
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1422-1478 | 2.73e-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: 40.55 E-value: 2.73e-04
|
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1392-1447 | 2.78e-04 | |||||
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins. Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 40.55 E-value: 2.78e-04
|
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
677-731 | 2.92e-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: 2.92e-04
|
|||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1269-1316 | 3.13e-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: 3.13e-04
|
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| Herpes_BLLF1 | pfam05109 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
397-531 | 3.26e-04 | |||||
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo. Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 45.68 E-value: 3.26e-04
|
|||||||||
| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
336-525 | 4.17e-04 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.70 E-value: 4.17e-04
|
|||||||||
| PRK12323 | PRK12323 | DNA polymerase III subunit gamma/tau; |
333-537 | 4.61e-04 | |||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 45.25 E-value: 4.61e-04
|
|||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1401-1457 | 6.12e-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: 6.12e-04
|
|||||||||
| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
334-524 | 7.26e-04 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 7.26e-04
|
|||||||||
| DUF5585 | pfam17823 | Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
329-547 | 1.21e-03 | |||||
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 43.41 E-value: 1.21e-03
|
|||||||||
| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1124-1180 | 1.33e-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: 1.33e-03
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
719-773 | 1.62e-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: 1.62e-03
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| PLN03237 | PLN03237 | DNA topoisomerase 2; Provisional |
329-501 | 1.90e-03 | |||||
DNA topoisomerase 2; Provisional Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 43.31 E-value: 1.90e-03
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1440-1494 | 1.93e-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: 1.93e-03
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| PRK14950 | PRK14950 | DNA polymerase III subunits gamma and tau; Provisional |
431-537 | 2.04e-03 | |||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 42.87 E-value: 2.04e-03
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| PHA03169 | PHA03169 | hypothetical protein; Provisional |
1001-1179 | 2.12e-03 | |||||
hypothetical protein; Provisional Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 42.65 E-value: 2.12e-03
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| PRK10819 | PRK10819 | transport protein TonB; Provisional |
394-524 | 2.13e-03 | |||||
transport protein TonB; Provisional Pssm-ID: 236768 [Multi-domain] Cd Length: 246 Bit Score: 41.98 E-value: 2.13e-03
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| PHA03169 | PHA03169 | hypothetical protein; Provisional |
1343-1494 | 2.27e-03 | |||||
hypothetical protein; Provisional Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 42.65 E-value: 2.27e-03
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1368-1424 | 2.50e-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: 2.50e-03
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| DUF4045 | pfam13254 | Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ... |
326-487 | 2.74e-03 | |||||
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length. Pssm-ID: 433066 [Multi-domain] Cd Length: 415 Bit Score: 42.08 E-value: 2.74e-03
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1142-1197 | 2.78e-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: 37.47 E-value: 2.78e-03
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
986-1036 | 2.95e-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: 2.95e-03
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1115-1170 | 2.95e-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: 2.95e-03
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
776-826 | 3.07e-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: 3.07e-03
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1377-1432 | 3.63e-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: 3.63e-03
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| PLN03209 | PLN03209 | translocon at the inner envelope of chloroplast subunit 62; Provisional |
318-524 | 4.90e-03 | |||||
translocon at the inner envelope of chloroplast subunit 62; Provisional Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 41.45 E-value: 4.90e-03
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| PRK10819 | PRK10819 | transport protein TonB; Provisional |
316-457 | 5.08e-03 | |||||
transport protein TonB; Provisional Pssm-ID: 236768 [Multi-domain] Cd Length: 246 Bit Score: 40.82 E-value: 5.08e-03
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1136-1190 | 8.23e-03 | |||||
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins. Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.32 E-value: 8.23e-03
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
728-782 | 9.08e-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: 36.32 E-value: 9.08e-03
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| Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
767-822 | 9.54e-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: 9.54e-03
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| Blast search parameters | ||||
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