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Conserved domains on  [gi|116686136|ref|NP_997302|]
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complement C1q tumor necrosis factor-related protein 8 precursor [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 ...
 118-246 1.04e-49

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: 159.37  E-value: 1.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686136  118 AFSVGRREGLHSSDHfQAVPFDTELVNLDGAFDLAAGRFLCTVPGVYFLSLNVHTWNYKETYLHIMLNRRPAAVLYAQPS 197
Cdd:pfam00386   1 AFSAGRTTGLTAPNE-QPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDGKSLYVSLVKNGQEVVSFYDQPQ 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 116686136  198 ERSV-MQAQSLMLLLAAGDAVWVRMFqrdRDNAIYGEHGDLYITFSGHLV 246
Cdd:pfam00386  80 KGSLdVASGSVVLELQRGDEVWLQLT---GYNGLYYDGSDTDSTFSGFLL 126
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 69-111 2.11e-07

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


:

Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.72  E-value: 2.11e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 116686136   69 KGEKGEAGVRGRAGRSGKEGPPGARGLQGRRGQKGQVGPPGAA 111
Cdd:pfam01391  15 PGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
 
Name Accession Description Interval E-value
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 118-246 1.04e-49

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: 159.37  E-value: 1.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686136  118 AFSVGRREGLHSSDHfQAVPFDTELVNLDGAFDLAAGRFLCTVPGVYFLSLNVHTWNYKETYLHIMLNRRPAAVLYAQPS 197
Cdd:pfam00386   1 AFSAGRTTGLTAPNE-QPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDGKSLYVSLVKNGQEVVSFYDQPQ 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 116686136  198 ERSV-MQAQSLMLLLAAGDAVWVRMFqrdRDNAIYGEHGDLYITFSGHLV 246
Cdd:pfam00386  80 KGSLdVASGSVVLELQRGDEVWLQLT---GYNGLYYDGSDTDSTFSGFLL 126
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 118-248 3.82e-16

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: 72.72  E-value: 3.82e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686136   118 AFSVGRREGLHSSdhFQAVPFDTELVNLDGAFDLAAGRFLCTVPGVYFLSLNVHTWnYKETYLHIMLNRRPAAVLYAQPS 197
Cdd:smart00110   9 AFSVIRSNRPPPP--GQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESK-GRNVKVSLMKNGIQVMSTYDEYQ 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 116686136   198 ERSVMQAQSLMLL-LAAGDAVWVRMfqRDRDNAIYGEHGDlYITFSGHLVKP 248
Cdd:smart00110  86 KGLYDVASGGALLqLRQGDQVWLEL--PDEKNGLYAGEYV-DSTFSGFLLFP 134
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 69-111 2.11e-07

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.72  E-value: 2.11e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 116686136   69 KGEKGEAGVRGRAGRSGKEGPPGARGLQGRRGQKGQVGPPGAA 111
Cdd:pfam01391  15 PGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 68-109 2.16e-06

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: 47.98  E-value: 2.16e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 116686136  68 LKGEKGEAGVRGRAGRSGKEGPPGARGLQGRRGQKGQVGPPG 109
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG 156
 
Name Accession Description Interval E-value
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 118-246 1.04e-49

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: 159.37  E-value: 1.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686136  118 AFSVGRREGLHSSDHfQAVPFDTELVNLDGAFDLAAGRFLCTVPGVYFLSLNVHTWNYKETYLHIMLNRRPAAVLYAQPS 197
Cdd:pfam00386   1 AFSAGRTTGLTAPNE-QPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDGKSLYVSLVKNGQEVVSFYDQPQ 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 116686136  198 ERSV-MQAQSLMLLLAAGDAVWVRMFqrdRDNAIYGEHGDLYITFSGHLV 246
Cdd:pfam00386  80 KGSLdVASGSVVLELQRGDEVWLQLT---GYNGLYYDGSDTDSTFSGFLL 126
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 118-248 3.82e-16

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: 72.72  E-value: 3.82e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686136   118 AFSVGRREGLHSSdhFQAVPFDTELVNLDGAFDLAAGRFLCTVPGVYFLSLNVHTWnYKETYLHIMLNRRPAAVLYAQPS 197
Cdd:smart00110   9 AFSVIRSNRPPPP--GQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESK-GRNVKVSLMKNGIQVMSTYDEYQ 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 116686136   198 ERSVMQAQSLMLL-LAAGDAVWVRMfqRDRDNAIYGEHGDlYITFSGHLVKP 248
Cdd:smart00110  86 KGLYDVASGGALLqLRQGDQVWLEL--PDEKNGLYAGEYV-DSTFSGFLLFP 134
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 69-111 2.11e-07

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.72  E-value: 2.11e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 116686136   69 KGEKGEAGVRGRAGRSGKEGPPGARGLQGRRGQKGQVGPPGAA 111
Cdd:pfam01391  15 PGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 70-111 5.97e-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: 45.56  E-value: 5.97e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 116686136   70 GEKGEAGVRGRAGRSGKEGPPGARGLQGRRGQKGQVGPPGAA 111
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPP 45
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 69-109 1.84e-06

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.02  E-value: 1.84e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 116686136   69 KGEKGEAGVRGRAGRSGKEGPPGARGLQGRRGQKGQVGPPG 109
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 68-109 2.16e-06

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: 47.98  E-value: 2.16e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 116686136  68 LKGEKGEAGVRGRAGRSGKEGPPGARGLQGRRGQKGQVGPPG 109
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG 156
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 69-111 3.96e-06

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 3.96e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 116686136   69 KGEKGEAGVRGRAGRSGKEGPPGARGLQGRRGQKGQVGPPGAA 111
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 70-111 7.93e-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: 42.10  E-value: 7.93e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 116686136   70 GEKGEAGVRGRAGRSGKEGPPGARGLQGRRGQKGQVGPPGAA 111
Cdd:pfam01391  10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 70-111 1.08e-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: 1.08e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 116686136   70 GEKGEAGVRGRAGRSGKEGPPGARGLQGRRGQKGQVGPPGAA 111
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPP 42
 
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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