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Conserved domains on  [gi|34537067|gb|AAQ73993|]
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beta-fibrinogen, partial [Amazona auropalliata auropalliata]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FReD super family cl00085
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 1-40 2.01e-13

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.


The actual alignment was detected with superfamily member smart00186:

Pssm-ID: 412152 [Multi-domain]  Cd Length: 212  Bit Score: 59.98  E-value: 2.01e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 34537067      1 NGMFFSTFDRDNDGWLTTdprkqCSKEDGGGWWYNRCHSA 40
Cdd:smart00186 140 NGMQFSTYDRDNDKYSGN-----CAEEYGGGWWYNNCHAA 174
 
Name Accession Description Interval E-value
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 1-40 2.01e-13

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: 59.98  E-value: 2.01e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 34537067      1 NGMFFSTFDRDNDGWLTTdprkqCSKEDGGGWWYNRCHSA 40
Cdd:smart00186 140 NGMQFSTYDRDNDKYSGN-----CAEEYGGGWWYNNCHAA 174
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 1-40 2.05e-13

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: 59.95  E-value: 2.05e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 34537067   1 NGMFFSTFDRDNDGWLTTdprkqCSKEDGGGWWYNRCHSA 40
Cdd:cd00087 140 NGMKFSTFDRDNDGASGN-----CAESYSGGWWYNSCHAS 174
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
1-40 9.35e-13

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 58.30  E-value: 9.35e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 34537067     1 NGMFFSTFDRDNDgwlttDPRKQCSKEDGGGWWYNRCHSA 40
Cdd:pfam00147 147 NGMQFSTWDRDND-----SPDGNCALSYGGGWWYNNCHAA 181
 
Name Accession Description Interval E-value
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 1-40 2.01e-13

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: 59.98  E-value: 2.01e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 34537067      1 NGMFFSTFDRDNDGWLTTdprkqCSKEDGGGWWYNRCHSA 40
Cdd:smart00186 140 NGMQFSTYDRDNDKYSGN-----CAEEYGGGWWYNNCHAA 174
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 1-40 2.05e-13

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: 59.95  E-value: 2.05e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 34537067   1 NGMFFSTFDRDNDGWLTTdprkqCSKEDGGGWWYNRCHSA 40
Cdd:cd00087 140 NGMKFSTFDRDNDGASGN-----CAESYSGGWWYNSCHAS 174
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
1-40 9.35e-13

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 58.30  E-value: 9.35e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 34537067     1 NGMFFSTFDRDNDgwlttDPRKQCSKEDGGGWWYNRCHSA 40
Cdd:pfam00147 147 NGMQFSTWDRDND-----SPDGNCALSYGGGWWYNNCHAA 181
 
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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