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Conserved domains on  [gi|3357909|dbj|BAA31992|]
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intelectin [Mus musculus]

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
GGGWT_bact super family cl49103
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 40-82 7.11e-14

fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.


The actual alignment was detected with superfamily member NF040941:

Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 64.89  E-value: 7.11e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 3357909    40 SCKEIKQEHTKAQDGLYFLRT-KNGVI--YQTFCDMTTAGGGWTLV 82
Cdd:NF040941   1 SCWEILQAGPSAPSGVYWIDPdGMGGLapFQVYCDMTTDGGGWTLV 46
 
Name Accession Description Interval E-value
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 40-82 7.11e-14

fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.


Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 64.89  E-value: 7.11e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 3357909    40 SCKEIKQEHTKAQDGLYFLRT-KNGVI--YQTFCDMTTAGGGWTLV 82
Cdd:NF040941   1 SCWEILQAGPSAPSGVYWIDPdGMGGLapFQVYCDMTTDGGGWTLV 46
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 37-82 6.08e-06

Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation.


Pssm-ID: 238040 [Multi-domain]  Cd Length: 215  Bit Score: 46.46  E-value: 6.08e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 3357909   37 LPRSCKEIKQEHTKAqDGLYFLR-TKNGVIYQTFCDMTTAGGGWTLV 82
Cdd:cd00087   2 LPRDCSEVLQRGGRT-SGVYTIQpPGSNEPFQVYCDMDTDGGGWTVI 47
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 37-82 2.20e-04

Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and gamma chains, and a variety of fibrinogen-related proteins, including tenascin and Drosophila scabrous.


Pssm-ID: 214548 [Multi-domain]  Cd Length: 212  Bit Score: 41.49  E-value: 2.20e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 3357909      37 LPRSCKEIKQEHTKAqDGLYFLRTKNG-VIYQTFCDMTTAGGGWTLV 82
Cdd:smart00186   1 LPRDCSDVLQNGGKT-SGLYTIYPDGSsRPLKVYCDMETDGGGWTVI 46
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
38-116 9.42e-04

Fibrinogen beta and gamma chains, C-terminal globular domain;


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 39.81  E-value: 9.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3357909     38 PRSCKEIKQEHTKAQdGLYFLR-TKNGVIYQTFCDMTTAGGGWTlvasVHENNMRGKCTVGDRWSsqqgnraDYPEGDGN 116
Cdd:pfam00147   2 GRDCSDVYNKGAKTS-GLYTIRpDGATKPFEVYCDMETDGGGWT----VFQRRLDGSTNFKRNWK-------DYKAGFGN 69
 
Name Accession Description Interval E-value
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 40-82 7.11e-14

fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.


Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 64.89  E-value: 7.11e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 3357909    40 SCKEIKQEHTKAQDGLYFLRT-KNGVI--YQTFCDMTTAGGGWTLV 82
Cdd:NF040941   1 SCWEILQAGPSAPSGVYWIDPdGMGGLapFQVYCDMTTDGGGWTLV 46
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 37-82 6.08e-06

Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation.


Pssm-ID: 238040 [Multi-domain]  Cd Length: 215  Bit Score: 46.46  E-value: 6.08e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 3357909   37 LPRSCKEIKQEHTKAqDGLYFLR-TKNGVIYQTFCDMTTAGGGWTLV 82
Cdd:cd00087   2 LPRDCSEVLQRGGRT-SGVYTIQpPGSNEPFQVYCDMDTDGGGWTVI 47
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 37-82 2.20e-04

Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and gamma chains, and a variety of fibrinogen-related proteins, including tenascin and Drosophila scabrous.


Pssm-ID: 214548 [Multi-domain]  Cd Length: 212  Bit Score: 41.49  E-value: 2.20e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 3357909      37 LPRSCKEIKQEHTKAqDGLYFLRTKNG-VIYQTFCDMTTAGGGWTLV 82
Cdd:smart00186   1 LPRDCSDVLQNGGKT-SGLYTIYPDGSsRPLKVYCDMETDGGGWTVI 46
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
38-116 9.42e-04

Fibrinogen beta and gamma chains, C-terminal globular domain;


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 39.81  E-value: 9.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3357909     38 PRSCKEIKQEHTKAQdGLYFLR-TKNGVIYQTFCDMTTAGGGWTlvasVHENNMRGKCTVGDRWSsqqgnraDYPEGDGN 116
Cdd:pfam00147   2 GRDCSDVYNKGAKTS-GLYTIRpDGATKPFEVYCDMETDGGGWT----VFQRRLDGSTNFKRNWK-------DYKAGFGN 69
 
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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