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Conserved domains on  [gi|1370481825|ref|XP_024307918|]
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complement C1q tumor necrosis factor-related protein 6 isoform X1 [Homo sapiens]

Protein Classification

complement C1q tumor necrosis factor-related protein( domain architecture ID 10476476)

complement C1q tumor necrosis factor-related protein (C1q/TNF) plays diverse and important roles in immune, endocrine, skeletal, neuronal, reproductive, sensory, and vascular systems

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 145-273 1.74e-53

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: 1.74e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481825 145 AFSVGRKTALHSGEDfQTLLFERVFVNLDGCFDMATGQFAAPLRGIYFFSLNVHSWNYKETYVHIMHNQKEAVILYAQPS 224
Cdd:pfam00386   1 AFSAGRTTGLTAPNE-QPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDGKSLYVSLVKNGQEVVSFYDQPQ 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370481825 225 ERS-IMQSQSVMLDLAYGDRVWVRLFKrqrENAIYSNDFDTYITFSGHLI 273
Cdd:pfam00386  80 KGSlDVASGSVVLELQRGDEVWLQLTG---YNGLYYDGSDTDSTFSGFLL 126
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 100-138 3.49e-10

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: 54.42  E-value: 3.49e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1370481825 100 GDPGPMGLPGYMGREGPQGEPGPQGSKGDKGEMGSPGAP 138
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPP 39
 
Name Accession Description Interval E-value
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 145-273 1.74e-53

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: 1.74e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481825 145 AFSVGRKTALHSGEDfQTLLFERVFVNLDGCFDMATGQFAAPLRGIYFFSLNVHSWNYKETYVHIMHNQKEAVILYAQPS 224
Cdd:pfam00386   1 AFSAGRTTGLTAPNE-QPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDGKSLYVSLVKNGQEVVSFYDQPQ 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370481825 225 ERS-IMQSQSVMLDLAYGDRVWVRLFKrqrENAIYSNDFDTYITFSGHLI 273
Cdd:pfam00386  80 KGSlDVASGSVVLELQRGDEVWLQLTG---YNGLYYDGSDTDSTFSGFLL 126
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 145-273 1.03e-17

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: 77.34  E-value: 1.03e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481825  145 AFSVGRKTALHSGedFQTLLFERVFVNLDGCFDMATGQFAAPLRGIYFFSLNVHSWnYKETYVHIMHNQKEAVILYAQPS 224
Cdd:smart00110   9 AFSVIRSNRPPPP--GQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESK-GRNVKVSLMKNGIQVMSTYDEYQ 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1370481825  225 ERSIMQ-SQSVMLDLAYGDRVWVRLFKRQreNAIYSnDFDTYITFSGHLI 273
Cdd:smart00110  86 KGLYDVaSGGALLQLRQGDQVWLELPDEK--NGLYA-GEYVDSTFSGFLL 132
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 100-138 3.49e-10

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: 54.42  E-value: 3.49e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1370481825 100 GDPGPMGLPGYMGREGPQGEPGPQGSKGDKGEMGSPGAP 138
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPP 39
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 97-141 8.29e-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: 55.68  E-value: 8.29e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1370481825  97 GDKGDPGPMGLPGYMGREGPQGEPGPQGSKGDKGEMGSPGAPCQK 141
Cdd:NF038329  147 GPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 91-141 3.35e-08

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 54.14  E-value: 3.35e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370481825  91 NITILKGD--KGDPGPMGLPGYMGREGPQGEPGPQGSKGDKGEMGSPGAPCQK 141
Cdd:NF038329  109 GLQQLKGDgeKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEK 161
 
Name Accession Description Interval E-value
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 145-273 1.74e-53

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: 1.74e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481825 145 AFSVGRKTALHSGEDfQTLLFERVFVNLDGCFDMATGQFAAPLRGIYFFSLNVHSWNYKETYVHIMHNQKEAVILYAQPS 224
Cdd:pfam00386   1 AFSAGRTTGLTAPNE-QPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDGKSLYVSLVKNGQEVVSFYDQPQ 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370481825 225 ERS-IMQSQSVMLDLAYGDRVWVRLFKrqrENAIYSNDFDTYITFSGHLI 273
Cdd:pfam00386  80 KGSlDVASGSVVLELQRGDEVWLQLTG---YNGLYYDGSDTDSTFSGFLL 126
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 145-273 1.03e-17

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: 77.34  E-value: 1.03e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481825  145 AFSVGRKTALHSGedFQTLLFERVFVNLDGCFDMATGQFAAPLRGIYFFSLNVHSWnYKETYVHIMHNQKEAVILYAQPS 224
Cdd:smart00110   9 AFSVIRSNRPPPP--GQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESK-GRNVKVSLMKNGIQVMSTYDEYQ 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1370481825  225 ERSIMQ-SQSVMLDLAYGDRVWVRLFKRQreNAIYSnDFDTYITFSGHLI 273
Cdd:smart00110  86 KGLYDVaSGGALLQLRQGDQVWLELPDEK--NGLYA-GEYVDSTFSGFLL 132
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 100-138 3.49e-10

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: 54.42  E-value: 3.49e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1370481825 100 GDPGPMGLPGYMGREGPQGEPGPQGSKGDKGEMGSPGAP 138
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPP 39
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 97-138 2.16e-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: 2.16e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1370481825  97 GDKGDPGPMGLPGYMGREGPQGEPGPQGSKGDKGEMGSPGAP 138
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPP 45
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 96-138 2.34e-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: 52.11  E-value: 2.34e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370481825  96 KGDKGDPGPMGLPGYMGREGPQGEPGPQGSKGDKGEMGSPGAP 138
Cdd:pfam01391  15 PGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 97-138 4.62e-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: 51.34  E-value: 4.62e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1370481825  97 GDKGDPGPMGLPGYMGREGPQGEPGPQGSKGDKGEMGSPGAP 138
Cdd:pfam01391  10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 97-138 7.23e-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: 50.96  E-value: 7.23e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1370481825  97 GDKGDPGPMGLPGYMGREGPQGEPGPQGSKGDKGEMGSPGAP 138
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPP 42
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 97-141 8.29e-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: 55.68  E-value: 8.29e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1370481825  97 GDKGDPGPMGLPGYMGREGPQGEPGPQGSKGDKGEMGSPGAPCQK 141
Cdd:NF038329  147 GPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 96-138 9.47e-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: 50.57  E-value: 9.47e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370481825  96 KGDKGDPGPMGLPGYMGREGPQGEPGPQGSKGDKGEMGSPGAP 138
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 91-141 3.35e-08

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 54.14  E-value: 3.35e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370481825  91 NITILKGD--KGDPGPMGLPGYMGREGPQGEPGPQGSKGDKGEMGSPGAPCQK 141
Cdd:NF038329  109 GLQQLKGDgeKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEK 161
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 96-138 3.85e-08

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: 49.03  E-value: 3.85e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370481825  96 KGDKGDPGPMGLPGYMGREGPQGEPGPQGSKGDKGEMGSPGAP 138
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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