fibrinogen-related domain-containing protein contains a C terminal globular domain similar to that of fibrinogen, and may be involved in one or more of a variety of binding interactions and functions including complement activation, signaling and regulation
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
292-507
1.44e-114
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: 337.29 E-value: 1.44e-114
HemX, putative uroporphyrinogen-III C-methyltransferase; This is a family of bacterial ...
140-242
1.48e-03
HemX, putative uroporphyrinogen-III C-methyltransferase; This is a family of bacterial putative uroporphyrinogen-III C-methyltransferase proteins. It forms one of the members of a complex of proteins involved in the biogenesis of the inner membrane in E.coli. Uroporphorphyrin-III C-methyltransferase (HemX) is a single spanning inner membrane protein that regulates the activity of NAD(P)H:glutamyl-tRNA reductase (HemA) in the tetrapyrrole biosynthesis pathway.
The actual alignment was detected with superfamily member PRK10920:
Pssm-ID: 452723 Cd Length: 390 Bit Score: 40.85 E-value: 1.48e-03
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
292-507
1.44e-114
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: 337.29 E-value: 1.44e-114
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
294-507
3.34e-98
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: 295.34 E-value: 3.34e-98
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
297-338
8.77e-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: 65.28 E-value: 8.77e-14
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
292-507
1.44e-114
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: 337.29 E-value: 1.44e-114
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
294-507
3.34e-98
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: 295.34 E-value: 3.34e-98
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
297-338
8.77e-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: 65.28 E-value: 8.77e-14
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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