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Conserved domains on  [gi|87252711|ref|NP_033735|]
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adiponectin precursor [Mus musculus]

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 ...
 112-245 2.38e-61

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: 189.05  E-value: 2.38e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87252711    112 YVYRSAFSVGLETRVTVPNVPIRFTKIFYNQQNHYDGSTGKFYCNIPGLYYFSYHITVYMKDVKVSLFKKDKAVLFTYDQ 191
Cdd:smart00110   4 AQPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMSTYDE 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 87252711    192 YQEKNVDQASGSVLLHLEVGDQVWLQVYGDGdhNGLYADNVNDSTFTGFLLYHD 245
Cdd:smart00110  84 YQKGLYDVASGGALLQLRQGDQVWLELPDEK--NGLYAGEYVDSTFSGFLLFPD 135
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 54-110 2.06e-10

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: 54.81  E-value: 2.06e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 87252711    54 GTPGRDGRDGTPGEKGEKGDAGLLGPKGETGDVGMTGAEGPRGFPGTPGRKGEPGEA 110
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 112-245 2.38e-61

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: 189.05  E-value: 2.38e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87252711    112 YVYRSAFSVGLETRVTVPNVPIRFTKIFYNQQNHYDGSTGKFYCNIPGLYYFSYHITVYMKDVKVSLFKKDKAVLFTYDQ 191
Cdd:smart00110   4 AQPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMSTYDE 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 87252711    192 YQEKNVDQASGSVLLHLEVGDQVWLQVYGDGdhNGLYADNVNDSTFTGFLLYHD 245
Cdd:smart00110  84 YQKGLYDVASGGALLQLRQGDQVWLELPDEK--NGLYAGEYVDSTFSGFLLFPD 135
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 117-242 4.48e-56

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: 4.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87252711   117 AFSVGLETRVTVPN-VPIRFTKIFYNQQNHYDGSTGKFYCNIPGLYYFSYHIT-VYMKDVKVSLFKKDKAVLFTYDQYQE 194
Cdd:pfam00386   1 AFSAGRTTGLTAPNeQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQPQK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 87252711   195 KNVDQASGSVLLHLEVGDQVWLQVYGdgdHNGLYADNV-NDSTFTGFLL 242
Cdd:pfam00386  81 GSLDVASGSVVLELQRGDEVWLQLTG---YNGLYYDGSdTDSTFSGFLL 126
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 54-110 2.06e-10

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: 54.81  E-value: 2.06e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 87252711    54 GTPGRDGRDGTPGEKGEKGDAGLLGPKGETGDVGMTGAEGPRGFPGTPGRKGEPGEA 110
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 69-110 1.73e-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: 42.20  E-value: 1.73e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 87252711   69 GEKGDAGLLGPKGETGDVGMTG---AEGPRGFPGTPGRKGEPGEA 110
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGdrgETGPAGPAGPPGPQGERGEK 161
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 112-245 2.38e-61

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: 189.05  E-value: 2.38e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87252711    112 YVYRSAFSVGLETRVTVPNVPIRFTKIFYNQQNHYDGSTGKFYCNIPGLYYFSYHITVYMKDVKVSLFKKDKAVLFTYDQ 191
Cdd:smart00110   4 AQPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMSTYDE 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 87252711    192 YQEKNVDQASGSVLLHLEVGDQVWLQVYGDGdhNGLYADNVNDSTFTGFLLYHD 245
Cdd:smart00110  84 YQKGLYDVASGGALLQLRQGDQVWLELPDEK--NGLYAGEYVDSTFSGFLLFPD 135
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 117-242 4.48e-56

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: 4.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87252711   117 AFSVGLETRVTVPN-VPIRFTKIFYNQQNHYDGSTGKFYCNIPGLYYFSYHIT-VYMKDVKVSLFKKDKAVLFTYDQYQE 194
Cdd:pfam00386   1 AFSAGRTTGLTAPNeQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQPQK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 87252711   195 KNVDQASGSVLLHLEVGDQVWLQVYGdgdHNGLYADNV-NDSTFTGFLL 242
Cdd:pfam00386  81 GSLDVASGSVVLELQRGDEVWLQLTG---YNGLYYDGSdTDSTFSGFLL 126
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 54-110 2.06e-10

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: 54.81  E-value: 2.06e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 87252711    54 GTPGRDGRDGTPGEKGEKGDAGLLGPKGETGDVGMTGAEGPRGFPGTPGRKGEPGEA 110
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 48-107 2.30e-10

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: 54.81  E-value: 2.30e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 87252711    48 GHPGHNGTPGRDGRDGTPGEKGEKGDAgllGPKGETGDVGMTGAEGPRGFPGTPGRKGEP 107
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPP---GPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 44-75 1.70e-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: 38.63  E-value: 1.70e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 87252711    44 AGIPGHPGHNGTPGRDGRDGTPGEKGEKGDAG 75
Cdd:pfam01391  24 PGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 69-110 1.73e-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: 42.20  E-value: 1.73e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 87252711   69 GEKGDAGLLGPKGETGDVGMTG---AEGPRGFPGTPGRKGEPGEA 110
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGdrgETGPAGPAGPPGPQGERGEK 161
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 44-79 2.47e-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: 35.16  E-value: 2.47e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 87252711    44 AGIPGHPGHNGTPGRDGRDGTPGEKGEKGDAGLLGP 79
Cdd:pfam01391  21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 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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