NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|77917558|ref|NP_001030104|]
View 

complement C1q tumor necrosis factor-related protein 6 precursor [Rattus norvegicus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 130-258 1.07e-50

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: 162.07  E-value: 1.07e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917558   130 AFSVGRKTGLHSSENFLsLLFDRVFVNTDGHFDMATGRFVAPLRGLYFFSLNVHSWNYKETYVHIVHNEQAVVILYAQPS 209
Cdd:pfam00386   1 AFSAGRTTGLTAPNEQP-VRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDGKSLYVSLVKNGQEVVSFYDQPQ 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 77917558   210 ERS-IMQSQSVMLPLVPGDYVWVRLFKrerENGIYSDDMDTYITFSGHLI 258
Cdd:pfam00386  80 KGSlDVASGSVVLELQRGDEVWLQLTG---YNGLYYDGSDTDSTFSGFLL 126
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 82-121 5.56e-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: 5.56e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 77917558    82 GDKGDRGPSGTPGKPGKNGTRGDRGSQGIKGDKGQAGSPG 121
Cdd:pfam01391  10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
 
Name Accession Description Interval E-value
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 130-258 1.07e-50

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: 162.07  E-value: 1.07e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917558   130 AFSVGRKTGLHSSENFLsLLFDRVFVNTDGHFDMATGRFVAPLRGLYFFSLNVHSWNYKETYVHIVHNEQAVVILYAQPS 209
Cdd:pfam00386   1 AFSAGRTTGLTAPNEQP-VRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDGKSLYVSLVKNGQEVVSFYDQPQ 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 77917558   210 ERS-IMQSQSVMLPLVPGDYVWVRLFKrerENGIYSDDMDTYITFSGHLI 258
Cdd:pfam00386  80 KGSlDVASGSVVLELQRGDEVWLQLTG---YNGLYYDGSDTDSTFSGFLL 126
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 125-258 3.74e-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: 83.51  E-value: 3.74e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917558    125 QTHYSAFSVGRKTglHSSENFLSLLFDRVFVNTDGHFDMATGRFVAPLRGLYFFSLNVHSWnYKETYVHIVHNEQAVVIL 204
Cdd:smart00110   4 AQPRSAFSVIRSN--RPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESK-GRNVKVSLMKNGIQVMST 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 77917558    205 YAQPSERSIMQ-SQSVMLPLVPGDYVWVRLfKREReNGIYSDDmDTYITFSGHLI 258
Cdd:smart00110  81 YDEYQKGLYDVaSGGALLQLRQGDQVWLEL-PDEK-NGLYAGE-YVDSTFSGFLL 132
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 82-121 5.56e-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: 5.56e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 77917558    82 GDKGDRGPSGTPGKPGKNGTRGDRGSQGIKGDKGQAGSPG 121
Cdd:pfam01391  10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 82-121 1.15e-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: 49.13  E-value: 1.15e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 77917558   82 GDKGDRGPSGTPGKPGKNGTRGDRGSQGIKGDKGQAGSPG 121
Cdd:NF038329 245 GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVG 284
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 82-121 1.83e-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: 48.36  E-value: 1.83e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 77917558   82 GDKGDRGPSGTPGK---------PGKNGTRGDRGSQGIKGDKGQAGSPG 121
Cdd:NF038329 275 GKDGERGPVGPAGKdgqngkdglPGKDGKDGQNGKDGLPGKDGKDGQPG 323
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 80-121 3.92e-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: 47.59  E-value: 3.92e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 77917558   80 LKGDKGDRGPSGTPGKPGKNGTRGDRGSQGIKGDKGQAGSPG 121
Cdd:NF038329 240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
 
Name Accession Description Interval E-value
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 130-258 1.07e-50

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: 162.07  E-value: 1.07e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917558   130 AFSVGRKTGLHSSENFLsLLFDRVFVNTDGHFDMATGRFVAPLRGLYFFSLNVHSWNYKETYVHIVHNEQAVVILYAQPS 209
Cdd:pfam00386   1 AFSAGRTTGLTAPNEQP-VRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDGKSLYVSLVKNGQEVVSFYDQPQ 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 77917558   210 ERS-IMQSQSVMLPLVPGDYVWVRLFKrerENGIYSDDMDTYITFSGHLI 258
Cdd:pfam00386  80 KGSlDVASGSVVLELQRGDEVWLQLTG---YNGLYYDGSDTDSTFSGFLL 126
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 125-258 3.74e-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: 83.51  E-value: 3.74e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917558    125 QTHYSAFSVGRKTglHSSENFLSLLFDRVFVNTDGHFDMATGRFVAPLRGLYFFSLNVHSWnYKETYVHIVHNEQAVVIL 204
Cdd:smart00110   4 AQPRSAFSVIRSN--RPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESK-GRNVKVSLMKNGIQVMST 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 77917558    205 YAQPSERSIMQ-SQSVMLPLVPGDYVWVRLfKREReNGIYSDDmDTYITFSGHLI 258
Cdd:smart00110  81 YDEYQKGLYDVaSGGALLQLRQGDQVWLEL-PDEK-NGLYAGE-YVDSTFSGFLL 132
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 82-121 5.56e-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: 5.56e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 77917558    82 GDKGDRGPSGTPGKPGKNGTRGDRGSQGIKGDKGQAGSPG 121
Cdd:pfam01391  10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 82-122 8.48e-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: 8.48e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 77917558    82 GDKGDRGPSGTPGKPGKNGTRGDRGSQGIKGDKGQAGSPGS 122
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGP 44
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 85-122 1.42e-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: 47.10  E-value: 1.42e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 77917558    85 GDRGPSGTPGKPGKNGTRGDRGSQGIKGDKGQAGSPGS 122
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGP 38
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 82-121 2.97e-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: 46.33  E-value: 2.97e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 77917558    82 GDKGDRGPSGTPGKPGKNGTRGDRGSQGIKGDKGQAGSPG 121
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPG 40
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 82-121 1.15e-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: 49.13  E-value: 1.15e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 77917558   82 GDKGDRGPSGTPGKPGKNGTRGDRGSQGIKGDKGQAGSPG 121
Cdd:NF038329 245 GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVG 284
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 82-121 1.83e-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: 48.36  E-value: 1.83e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 77917558   82 GDKGDRGPSGTPGK---------PGKNGTRGDRGSQGIKGDKGQAGSPG 121
Cdd:NF038329 275 GKDGERGPVGPAGKdgqngkdglPGKDGKDGQNGKDGLPGKDGKDGQPG 323
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 80-121 3.92e-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: 47.59  E-value: 3.92e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 77917558   80 LKGDKGDRGPSGTPGKPGKNGTRGDRGSQGIKGDKGQAGSPG 121
Cdd:NF038329 240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 81-112 8.99e-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: 8.99e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 77917558    81 KGDKGDRGPSGTPGKPGKNGTRGDRGSQGIKG 112
Cdd:pfam01391  24 PGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 82-117 4.97e-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: 4.97e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 77917558    82 GDKGDRGPSGTPGKPGKNGTRGDRGSQGIKGDKGQA 117
Cdd:pfam01391  22 GPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH