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Conserved domains on  [gi|1712748710|gb|QDV59967|]
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adiponectin, partial [Martes americana]

Protein Classification

complement C1q domain-containing protein( domain architecture ID 10476615)

complement C1q domain-containing protein with an N-terminal collagen-like triple helix repeat domain similar to human C1q, which is a collagen-like hexameric glycoprotein, which associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 21-155 5.37e-56

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: 171.72  E-value: 5.37e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712748710   21 ESAYVHRSAFSVGLESRVTVPNVPIRFTKIFYNLQNHYDGTTGKFHCNIPGLYYFSYHITVYLKDVKVSLYKKDKAMLFT 100
Cdd:smart00110   1 NYKAQPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMST 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1712748710  101 YDQYQEKNVDQASGSVLLHLEVGDQVWLQVYGDGNsyGVYADNVHDSTFTGFLLY 155
Cdd:smart00110  81 YDEYQKGLYDVASGGALLQLRQGDQVWLELPDEKN--GLYAGEYVDSTFSGFLLF 133
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2-22 1.67e-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: 34.78  E-value: 1.67e-03
                          10        20
                  ....*....|....*....|.
gi 1712748710   2 GVEGPRGFPGTPGRKGEPGES 22
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPP 21
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 21-155 5.37e-56

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: 171.72  E-value: 5.37e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712748710   21 ESAYVHRSAFSVGLESRVTVPNVPIRFTKIFYNLQNHYDGTTGKFHCNIPGLYYFSYHITVYLKDVKVSLYKKDKAMLFT 100
Cdd:smart00110   1 NYKAQPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMST 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1712748710  101 YDQYQEKNVDQASGSVLLHLEVGDQVWLQVYGDGNsyGVYADNVHDSTFTGFLLY 155
Cdd:smart00110  81 YDEYQKGLYDVASGGALLQLRQGDQVWLELPDEKN--GLYAGEYVDSTFSGFLLF 133
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 29-154 3.70e-51

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: 3.70e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712748710  29 AFSVGLESRVTVPN-VPIRFTKIFYNLQNHYDGTTGKFHCNIPGLYYFSYHIT-VYLKDVKVSLYKKDKAMLFTYDQYQE 106
Cdd:pfam00386   1 AFSAGRTTGLTAPNeQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQPQK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1712748710 107 KNVDQASGSVLLHLEVGDQVWLQVYGDGNSYgvYADNVHDSTFTGFLL 154
Cdd:pfam00386  81 GSLDVASGSVVLELQRGDEVWLQLTGYNGLY--YDGSDTDSTFSGFLL 126
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2-22 1.67e-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: 34.78  E-value: 1.67e-03
                          10        20
                  ....*....|....*....|.
gi 1712748710   2 GVEGPRGFPGTPGRKGEPGES 22
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPP 21
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 21-155 5.37e-56

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: 171.72  E-value: 5.37e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712748710   21 ESAYVHRSAFSVGLESRVTVPNVPIRFTKIFYNLQNHYDGTTGKFHCNIPGLYYFSYHITVYLKDVKVSLYKKDKAMLFT 100
Cdd:smart00110   1 NYKAQPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMST 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1712748710  101 YDQYQEKNVDQASGSVLLHLEVGDQVWLQVYGDGNsyGVYADNVHDSTFTGFLLY 155
Cdd:smart00110  81 YDEYQKGLYDVASGGALLQLRQGDQVWLELPDEKN--GLYAGEYVDSTFSGFLLF 133
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 29-154 3.70e-51

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: 3.70e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712748710  29 AFSVGLESRVTVPN-VPIRFTKIFYNLQNHYDGTTGKFHCNIPGLYYFSYHIT-VYLKDVKVSLYKKDKAMLFTYDQYQE 106
Cdd:pfam00386   1 AFSAGRTTGLTAPNeQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQPQK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1712748710 107 KNVDQASGSVLLHLEVGDQVWLQVYGDGNSYgvYADNVHDSTFTGFLL 154
Cdd:pfam00386  81 GSLDVASGSVVLELQRGDEVWLQLTGYNGLY--YDGSDTDSTFSGFLL 126
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2-22 1.67e-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: 34.78  E-value: 1.67e-03
                          10        20
                  ....*....|....*....|.
gi 1712748710   2 GVEGPRGFPGTPGRKGEPGES 22
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPP 21
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2-21 3.53e-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: 34.01  E-value: 3.53e-03
                          10        20
                  ....*....|....*....|
gi 1712748710   2 GVEGPRGFPGTPGRKGEPGE 21
Cdd:pfam01391  37 GPPGPPGPPGPPGAPGAPGP 56
 
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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