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Conserved domains on  [gi|1046900127|ref|XP_017451111|]
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complement C1q tumor necrosis factor-related protein 5 isoform X2 [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

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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 ...
 105-232 3.74e-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: 167.85  E-value: 3.74e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900127 105 AFSAKRSESRvPPPADTPLPFDRVLLNEQGHYDATTGKFTCQVPGVYYFAVHAT-VYRASLQFDLVKNGQSIASFFQFFG 183
Cdd:pfam00386   1 AFSAGRTTGL-TAPNEQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQPQ 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1046900127 184 GWpKPASLSGGAMVRLEPEDQVWVQvgVGDYIGIYAS-IKTDSTFSGFLV 232
Cdd:pfam00386  80 KG-SLDVASGSVVLELQRGDEVWLQ--LTGYNGLYYDgSDTDSTFSGFLL 126
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 29-95 1.56e-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: 1.56e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046900127  29 PGQPGLPGTPGHHGSQGlpgrdgrdgrdgAPGAPGEKGEGGRPGLPGPRGEPGPRGEAGPVGAIGPA 95
Cdd:pfam01391   3 PGPPGPPGPPGPPGPPG------------PPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 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 ...
 105-232 3.74e-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: 167.85  E-value: 3.74e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900127 105 AFSAKRSESRvPPPADTPLPFDRVLLNEQGHYDATTGKFTCQVPGVYYFAVHAT-VYRASLQFDLVKNGQSIASFFQFFG 183
Cdd:pfam00386   1 AFSAGRTTGL-TAPNEQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQPQ 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1046900127 184 GWpKPASLSGGAMVRLEPEDQVWVQvgVGDYIGIYAS-IKTDSTFSGFLV 232
Cdd:pfam00386  80 KG-SLDVASGSVVLELQRGDEVWLQ--LTGYNGLYYDgSDTDSTFSGFLL 126
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 97-235 2.28e-43

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: 143.21  E-value: 2.28e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900127   97 ECSVPPRSAFSAKRSesRVPPPADTPLPFDRVLLNEQGHYDATTGKFTCQVPGVYYFAVHATVYRASLQFDLVKNGQSIA 176
Cdd:smart00110   1 NYKAQPRSAFSVIRS--NRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVM 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900127  177 SFF-QFFGGWPKPAslSGGAMVRLEPEDQVWVQVGVGDYiGIYASIKTDSTFSGFLVYSD 235
Cdd:smart00110  79 STYdEYQKGLYDVA--SGGALLQLRQGDQVWLELPDEKN-GLYAGEYVDSTFSGFLLFPD 135
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 29-95 1.56e-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: 1.56e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046900127  29 PGQPGLPGTPGHHGSQGlpgrdgrdgrdgAPGAPGEKGEGGRPGLPGPRGEPGPRGEAGPVGAIGPA 95
Cdd:pfam01391   3 PGPPGPPGPPGPPGPPG------------PPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 30-97 3.93e-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: 47.21  E-value: 3.93e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046900127  30 GQPGLPGTPGHHGSQGlpgrdgrdgrdgAPGAPGEKGEGGRPGLPGPRGEPGPRGEAGPVGAIGPAGE 97
Cdd:NF038329  120 GEPGPAGPAGPAGEQG------------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP 175
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 30-97 1.50e-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: 45.28  E-value: 1.50e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900127  30 GQPGLPGTPGH--HGSQGLPGRDGRDGRDGAPGAPGEKGEGGRPGLPGPRGEPGPRGEAGPVGAIGPAGE 97
Cdd:NF038329  222 GEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 30-94 9.60e-04

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: 39.89  E-value: 9.60e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046900127  30 GQPGLPGTPGHHGSQGLPGRDGRDGRDGAPGAPGEKGEGgrpGLPGPRGEPGPRGEAGPVGAIGP 94
Cdd:NF038329  281 GPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD---GQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 30-96 2.26e-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: 38.73  E-value: 2.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046900127  30 GQPGLPGTPGHHGSQGLPGRDGRDGRDGAPGAPGEKGEGGRPGLPGPRGEPGPRGEAGPVGAIGPAG 96
Cdd:NF038329  233 GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPG 299
PHA03201 PHA03201
uracil DNA glycosylase; Provisional
 47-130 7.54e-03

uracil DNA glycosylase; Provisional


Pssm-ID: 165468  Cd Length: 318  Bit Score: 36.79  E-value: 7.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900127  47 PGRDGRDGRDGAPGAPGEKGEGGRPGLPGPRGEPGPRGEAGPVGAI-----GPAG---ECSVPPRSAFSAKRSESRVPPP 118
Cdd:PHA03201   11 PPRRPSPPRPTPPRSPDASPEETPPSPPGPGAEPPPGRAAGPAAPRrrprgCPAGvtfSSSAPPRPPLGLDDAPAATPPP 90

                          90
                  ....*....|..
gi 1046900127 119 ADTPlPFDRVLL 130
Cdd:PHA03201   91 LDWT-EFRRRFL 101
 
Name Accession Description Interval E-value
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 105-232 3.74e-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: 167.85  E-value: 3.74e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900127 105 AFSAKRSESRvPPPADTPLPFDRVLLNEQGHYDATTGKFTCQVPGVYYFAVHAT-VYRASLQFDLVKNGQSIASFFQFFG 183
Cdd:pfam00386   1 AFSAGRTTGL-TAPNEQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQPQ 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1046900127 184 GWpKPASLSGGAMVRLEPEDQVWVQvgVGDYIGIYAS-IKTDSTFSGFLV 232
Cdd:pfam00386  80 KG-SLDVASGSVVLELQRGDEVWLQ--LTGYNGLYYDgSDTDSTFSGFLL 126
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 97-235 2.28e-43

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: 143.21  E-value: 2.28e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900127   97 ECSVPPRSAFSAKRSesRVPPPADTPLPFDRVLLNEQGHYDATTGKFTCQVPGVYYFAVHATVYRASLQFDLVKNGQSIA 176
Cdd:smart00110   1 NYKAQPRSAFSVIRS--NRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVM 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900127  177 SFF-QFFGGWPKPAslSGGAMVRLEPEDQVWVQVGVGDYiGIYASIKTDSTFSGFLVYSD 235
Cdd:smart00110  79 STYdEYQKGLYDVA--SGGALLQLRQGDQVWLELPDEKN-GLYAGEYVDSTFSGFLLFPD 135
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 29-95 1.56e-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: 1.56e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046900127  29 PGQPGLPGTPGHHGSQGlpgrdgrdgrdgAPGAPGEKGEGGRPGLPGPRGEPGPRGEAGPVGAIGPA 95
Cdd:pfam01391   3 PGPPGPPGPPGPPGPPG------------PPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 30-97 3.93e-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: 47.21  E-value: 3.93e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046900127  30 GQPGLPGTPGHHGSQGlpgrdgrdgrdgAPGAPGEKGEGGRPGLPGPRGEPGPRGEAGPVGAIGPAGE 97
Cdd:NF038329  120 GEPGPAGPAGPAGEQG------------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP 175
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 30-97 1.50e-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: 45.28  E-value: 1.50e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900127  30 GQPGLPGTPGH--HGSQGLPGRDGRDGRDGAPGAPGEKGEGGRPGLPGPRGEPGPRGEAGPVGAIGPAGE 97
Cdd:NF038329  222 GEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 30-94 9.60e-04

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: 39.89  E-value: 9.60e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046900127  30 GQPGLPGTPGHHGSQGLPGRDGRDGRDGAPGAPGEKGEGgrpGLPGPRGEPGPRGEAGPVGAIGP 94
Cdd:NF038329  281 GPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD---GQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 30-96 2.26e-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: 38.73  E-value: 2.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046900127  30 GQPGLPGTPGHHGSQGLPGRDGRDGRDGAPGAPGEKGEGGRPGLPGPRGEPGPRGEAGPVGAIGPAG 96
Cdd:NF038329  233 GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPG 299
PHA03201 PHA03201
uracil DNA glycosylase; Provisional
 47-130 7.54e-03

uracil DNA glycosylase; Provisional


Pssm-ID: 165468  Cd Length: 318  Bit Score: 36.79  E-value: 7.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900127  47 PGRDGRDGRDGAPGAPGEKGEGGRPGLPGPRGEPGPRGEAGPVGAI-----GPAG---ECSVPPRSAFSAKRSESRVPPP 118
Cdd:PHA03201   11 PPRRPSPPRPTPPRSPDASPEETPPSPPGPGAEPPPGRAAGPAAPRrrprgCPAGvtfSSSAPPRPPLGLDDAPAATPPP 90

                          90
                  ....*....|..
gi 1046900127 119 ADTPlPFDRVLL 130
Cdd:PHA03201   91 LDWT-EFRRRFL 101
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 31-126 7.62e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 37.27  E-value: 7.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900127  31 QPGLPGTPGHHGSQGLPGRDGRDGRDGAPGAPGEKGEGGRPGLPGPRGEPGPRGEAGPVGAIGPAGECSVPPRSAFSAKR 110
Cdd:PRK07764  654 PKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSP 733

                          90
                  ....*....|....*.
gi 1046900127 111 SESRVPPPADTPLPFD 126
Cdd:PRK07764  734 AADDPVPLPPEPDDPP 749
 
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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