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complement component 1, q subcomponent, alpha polypeptide [Homo sapiens]
complement C1q domain-containing protein( domain architecture ID 10476615)
complement C1q domain-containing protein with an N-terminal collagen-like triple helix repeat domain similar to human C1q, which is a collagen-like hexameric glycoprotein, which associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
C1Q | smart00110 | Complement component C1q domain; Globular domain found in many collagens and eponymously in ... |
108-244 | 4.48e-67 | |||
Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor. : Pssm-ID: 128420 Cd Length: 135 Bit Score: 203.69 E-value: 4.48e-67
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
49-106 | 1.65e-09 | |||
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: 52.50 E-value: 1.65e-09
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Name | Accession | Description | Interval | E-value | |||
C1Q | smart00110 | Complement component C1q domain; Globular domain found in many collagens and eponymously in ... |
108-244 | 4.48e-67 | |||
Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor. Pssm-ID: 128420 Cd Length: 135 Bit Score: 203.69 E-value: 4.48e-67
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C1q | pfam00386 | C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ... |
116-241 | 5.82e-54 | |||
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system. Pssm-ID: 395310 [Multi-domain] Cd Length: 126 Bit Score: 169.77 E-value: 5.82e-54
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
49-106 | 1.65e-09 | |||
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: 52.50 E-value: 1.65e-09
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gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
30-107 | 2.85e-09 | |||
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: 56.84 E-value: 2.85e-09
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gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
27-90 | 2.86e-03 | |||
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: 38.35 E-value: 2.86e-03
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Name | Accession | Description | Interval | E-value | |||
C1Q | smart00110 | Complement component C1q domain; Globular domain found in many collagens and eponymously in ... |
108-244 | 4.48e-67 | |||
Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor. Pssm-ID: 128420 Cd Length: 135 Bit Score: 203.69 E-value: 4.48e-67
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C1q | pfam00386 | C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ... |
116-241 | 5.82e-54 | |||
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system. Pssm-ID: 395310 [Multi-domain] Cd Length: 126 Bit Score: 169.77 E-value: 5.82e-54
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
49-106 | 1.65e-09 | |||
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: 52.50 E-value: 1.65e-09
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gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
30-107 | 2.85e-09 | |||
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: 56.84 E-value: 2.85e-09
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Collagen | pfam01391 | Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
62-108 | 6.36e-07 | |||
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins. Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 45.18 E-value: 6.36e-07
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gly_rich_SclB | NF038329 | LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
27-90 | 2.86e-03 | |||
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: 38.35 E-value: 2.86e-03
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Blast search parameters | ||||
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