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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672044741 123 PRSCKDLLTRGIFLTGWYTIYLPDC-RPLTVLCDMDVDGGGWTVFQRRVDGSINFYRDWDSYKRGFGNLGTEFWLGNDYL 201
Cdd:cd00087    3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 672044741 202 HLLTANGNQELRVDLREFQGQTSFAKYSSFQVSGEQEKYKLTLGQFlEGTAG 253
Cdd:cd00087   83 HLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGY-SGTAG 133

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672044741 123 PRSCKDLLTRGIFLTGWYTIYLPDC-RPLTVLCDMDVDGGGWTVFQRRVDGSINFYRDWDSYKRGFGNLGTEFWLGNDYL 201
Cdd:cd00087    3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 672044741 202 HLLTANGNQELRVDLREFQGQTSFAKYSSFQVSGEQEKYKLTLGQFlEGTAG 253
Cdd:cd00087   83 HLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGY-SGTAG 133

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672044741  123 PRSCKDLLTRGIFLTGWYTIYL-PDCRPLTVLCDMDVDGGGWTVFQRRVDGSINFYRDWDSYKRGFGNL-GTEFWLGNDY 200
Cdd:pfam00147   2 GRDCSDVYNKGAKTSGLYTIRPdGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLsPGEFWLGNDK 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 672044741  201 LHLLTANGNQELRVDLREFQGQTSFAKYSSFQVSGEQEKYKLTLGQFlEGTAG 253
Cdd:pfam00147  82 IHLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENY-IGDAG 133

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 672044741  68 GERGLQGSPGKMGPAGSKGEPGTMGPPGVKGEKGERGTASPLGQKELG--DALCRRGPR 124
Cdd:NF038329 180 GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAgpAGDGQQGPD 238

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 672044741 125 SCKDLLTRGIFLT-GWYTIY---LPDCRPLTVLCDMDVDGGGWTVF 166
Cdd:NF040941   1 SCWEILQAGPSAPsGVYWIDpdgMGGLAPFQVYCDMTTDGGGWTLV 46

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 672044741  70 RGLQGSPGKMGPAGSKGEPGTMGPPGVKGEKGERGTASPLGQ 111
Cdd:NF038329 262 RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGK 303

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672044741 123 PRSCKDLLTRGIFLTGWYTIYLPDC-RPLTVLCDMDVDGGGWTVFQRRVDGSINFYRDWDSYKRGFGNLGTEFWLGNDYL 201
Cdd:cd00087    3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 672044741 202 HLLTANGNQELRVDLREFQGQTSFAKYSSFQVSGEQEKYKLTLGQFlEGTAG 253
Cdd:cd00087   83 HLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGY-SGTAG 133

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672044741  123 PRSCKDLLTRGIFLTGWYTIYL-PDCRPLTVLCDMDVDGGGWTVFQRRVDGSINFYRDWDSYKRGFGNL-GTEFWLGNDY 200
Cdd:pfam00147   2 GRDCSDVYNKGAKTSGLYTIRPdGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLsPGEFWLGNDK 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 672044741  201 LHLLTANGNQELRVDLREFQGQTSFAKYSSFQVSGEQEKYKLTLGQFlEGTAG 253
Cdd:pfam00147  82 IHLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENY-IGDAG 133

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 672044741  68 GERGLQGSPGKMGPAGSKGEPGTMGPPGVKGEKGERGTASPLGQKELG--DALCRRGPR 124
Cdd:NF038329 180 GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAgpAGDGQQGPD 238

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 672044741   67 RGERGLQGSPGKMGPAGSKGEPGTMGPPGVKGEKGERGTASPLGQK 112
Cdd:pfam01391   3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 672044741  58 KGEPGSPAGRGERGLQGSPGKMGPAGSKGEPGTMGPPGVKGEKGERGTASPLGQ 111
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGE 181

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.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 672044741   58 KGEPGSPAGRGERGLQGSPGKMGPAGSKGEPGTMGPP 94
Cdd:pfam01391  21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57