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Conserved domains on  [gi|1726075686|ref|XP_030317700|]
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complement C1q tumor necrosis factor-related protein 1 [Calypte anna]

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 ...
 268-396 4.87e-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: 175.17  E-value: 4.87e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726075686 268 AFSVGRKKPLHSNDYyQTLIFDTEFVNLYDHFNMFTGKFYCYVPGIYYFSLNVHTWNQKETYLHIMHNGAEVVILYAQVS 347
Cdd:pfam00386   1 AFSAGRTTGLTAPNE-QPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDGKSLYVSLVKNGQEVVSFYDQPQ 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1726075686 348 DRS-IMQSQSVMLELQEQDEVWVRLYKgerENAVFSDEYDTYITFSGHLI 396
Cdd:pfam00386  80 KGSlDVASGSVVLELQRGDEVWLQLTG---YNGLYYDGSDTDSTFSGFLL 126
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 219-261 8.09e-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: 42.87  E-value: 8.09e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1726075686 219 KGEKGDRGERGMQGKFGKTGMAGSRGHTGPKGQKGSVGAPGER 261
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 ...
 268-396 4.87e-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: 175.17  E-value: 4.87e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726075686 268 AFSVGRKKPLHSNDYyQTLIFDTEFVNLYDHFNMFTGKFYCYVPGIYYFSLNVHTWNQKETYLHIMHNGAEVVILYAQVS 347
Cdd:pfam00386   1 AFSAGRTTGLTAPNE-QPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDGKSLYVSLVKNGQEVVSFYDQPQ 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1726075686 348 DRS-IMQSQSVMLELQEQDEVWVRLYKgerENAVFSDEYDTYITFSGHLI 396
Cdd:pfam00386  80 KGSlDVASGSVVLELQRGDEVWLQLTG---YNGLYYDGSDTDSTFSGFLL 126
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 261-396 2.03e-20

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: 86.59  E-value: 2.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726075686  261 RCKSHY-AAFSVGRKKPLHSNDyyQTLIFDTEFVNLYDHFNMFTGKFYCYVPGIYYFSLNVHTWnQKETYLHIMHNGAEV 339
Cdd:smart00110   1 NYKAQPrSAFSVIRSNRPPPPG--QPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESK-GRNVKVSLMKNGIQV 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1726075686  340 VILYAQVSDRSIMQ-SQSVMLELQEQDEVWVRLYKgeRENAVFSDEYdTYITFSGHLI 396
Cdd:smart00110  78 MSTYDEYQKGLYDVaSGGALLQLRQGDQVWLELPD--EKNGLYAGEY-VDSTFSGFLL 132
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 219-261 8.09e-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: 42.87  E-value: 8.09e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1726075686 219 KGEKGDRGERGMQGKFGKTGMAGSRGHTGPKGQKGSVGAPGER 261
Cdd:pfam01391  15 PGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 218-261 2.34e-05

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 46.44  E-value: 2.34e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1726075686 218 LKGEKGDRGERGMQGKFGKTGMAGSRGHTGPKGQKGSVGAPGER 261
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGER 158
 
Name Accession Description Interval E-value
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 268-396 4.87e-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: 175.17  E-value: 4.87e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726075686 268 AFSVGRKKPLHSNDYyQTLIFDTEFVNLYDHFNMFTGKFYCYVPGIYYFSLNVHTWNQKETYLHIMHNGAEVVILYAQVS 347
Cdd:pfam00386   1 AFSAGRTTGLTAPNE-QPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDGKSLYVSLVKNGQEVVSFYDQPQ 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1726075686 348 DRS-IMQSQSVMLELQEQDEVWVRLYKgerENAVFSDEYDTYITFSGHLI 396
Cdd:pfam00386  80 KGSlDVASGSVVLELQRGDEVWLQLTG---YNGLYYDGSDTDSTFSGFLL 126
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 261-396 2.03e-20

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: 86.59  E-value: 2.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1726075686  261 RCKSHY-AAFSVGRKKPLHSNDyyQTLIFDTEFVNLYDHFNMFTGKFYCYVPGIYYFSLNVHTWnQKETYLHIMHNGAEV 339
Cdd:smart00110   1 NYKAQPrSAFSVIRSNRPPPPG--QPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESK-GRNVKVSLMKNGIQV 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1726075686  340 VILYAQVSDRSIMQ-SQSVMLELQEQDEVWVRLYKgeRENAVFSDEYdTYITFSGHLI 396
Cdd:smart00110  78 MSTYDEYQKGLYDVaSGGALLQLRQGDQVWLELPD--EKNGLYAGEY-VDSTFSGFLL 132
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 219-261 8.09e-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: 42.87  E-value: 8.09e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1726075686 219 KGEKGDRGERGMQGKFGKTGMAGSRGHTGPKGQKGSVGAPGER 261
Cdd:pfam01391  15 PGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 220-260 1.22e-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: 1.22e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1726075686 220 GEKGDRGERGMQGKFGKTGMAGSRGHTGPKGQKGSVGAPGE 260
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGP 41
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 218-261 2.34e-05

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 46.44  E-value: 2.34e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1726075686 218 LKGEKGDRGERGMQGKFGKTGMAGSRGHTGPKGQKGSVGAPGER 261
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGER 158
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 219-261 6.24e-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: 40.55  E-value: 6.24e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1726075686 219 KGEKGDRGERGMQGKFGKTGMAGSRGHTGPKGQKGSVGAPGER 261
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 220-260 8.47e-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: 40.17  E-value: 8.47e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1726075686 220 GEKGDRGERGMQGKFGKTGMAGSRGHTGPKGQKGSVGAPGE 260
Cdd:pfam01391  10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 220-259 3.29e-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: 38.24  E-value: 3.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1726075686 220 GEKGDRGERGMQGKFGKTGMAGSRGHTGPKGQKGSVGAPG 259
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPG 43
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 229-261 8.08e-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: 34.39  E-value: 8.08e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1726075686 229 GMQGKFGKTGMAGSRGHTGPKGQKGSVGAPGER 261
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEP 33
 
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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