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Conserved domains on  [gi|13124116|sp|Q9WTS8|]
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RecName: Full=Ficolin-1; AltName: Full=Collagen/fibrinogen domain-containing protein 1; AltName: Full=Ficolin-A; AltName: Full=Ficolin-alpha; AltName: Full=M-ficolin; Flags: Precursor

Protein Classification

ficolin family protein( domain architecture ID 10476102)

ficolin family protein belongs to a group of proteins characterized by the presence of collagen-like and fibrinogen-like domains.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 123-333 5.16e-117

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: 336.91  E-value: 5.16e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124116 123 PRSCKDLLTRGIFLTGWYTIYLPDC-RPLTVLCDMDVDGGGWTVFQRRVDGSINFYRDWDSYKRGFGNLGTEFWLGNDYL 201
Cdd:cd00087   3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124116 202 HLLTANGNQELRVDLREFQGQTSFAKYSSFQVSGEQEKYKLTLGQFlEGTAGDSLTKHNNMAFSTHDQDNDTNGGkNCAA 281
Cdd:cd00087  83 HLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGY-SGTAGDALSYHNGMKFSTFDRDNDGASG-NCAE 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 13124116 282 LFHGAWWYHDCHQSNLNGRYLPGSHE-SYADGINWLSGRGHRYSYKVAEMKIR 333
Cdd:cd00087 161 SYSGGWWYNSCHASNLNGRYYSGGHRnEYDNGINWATWKGSTYSLKFTEMKIR 213
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 64-108 1.52e-08

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: 50.18  E-value: 1.52e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 13124116    64 PAGRGERGLQGSPGKMGPPGSKGEPGTMGPPGVKGEKGERGTASP 108
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 123-333 5.16e-117

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: 336.91  E-value: 5.16e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124116 123 PRSCKDLLTRGIFLTGWYTIYLPDC-RPLTVLCDMDVDGGGWTVFQRRVDGSINFYRDWDSYKRGFGNLGTEFWLGNDYL 201
Cdd:cd00087   3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124116 202 HLLTANGNQELRVDLREFQGQTSFAKYSSFQVSGEQEKYKLTLGQFlEGTAGDSLTKHNNMAFSTHDQDNDTNGGkNCAA 281
Cdd:cd00087  83 HLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGY-SGTAGDALSYHNGMKFSTFDRDNDGASG-NCAE 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 13124116 282 LFHGAWWYHDCHQSNLNGRYLPGSHE-SYADGINWLSGRGHRYSYKVAEMKIR 333
Cdd:cd00087 161 SYSGGWWYNSCHASNLNGRYYSGGHRnEYDNGINWATWKGSTYSLKFTEMKIR 213
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 123-333 5.18e-100

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: 293.41  E-value: 5.18e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124116    123 PRSCKDLLTRGIFLTGWYTIYLPD-CRPLTVLCDMDVDGGGWTVFQRRVDGSINFYRDWDSYKRGFGNLGTEFWLGNDYL 201
Cdd:smart00186   2 PRDCSDVLQNGGKTSGLYTIYPDGsSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124116    202 HLLTANGNQELRVDLREFQGQTSFAKYSSFQVSGEQEKYKLTLGQFlEGTAGD-SLTKHNNMAFSTHDQDNDTNGGkNCA 280
Cdd:smart00186  82 HLLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGY-SGTAGDaSLTYHNGMQFSTYDRDNDKYSG-NCA 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 13124116    281 ALFHGAWWYHDCHQSNLNGRYlpGSHESYADGINWLSGRGHRYSYKVAEMKIR 333
Cdd:smart00186 160 EEYGGGWWYNNCHAANLNGRY--YPNNNYDNGINWATWKGSWYSLKFTEMKIR 210
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
123-333 2.29e-81

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 246.67  E-value: 2.29e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124116   123 PRSCKDLLTRGIFLTGWYTIYL-PDCRPLTVLCDMDVDGGGWTVFQRRVDGSINFYRDWDSYKRGFGNL-GTEFWLGNDY 200
Cdd:pfam00147   2 GRDCSDVYNKGAKTSGLYTIRPdGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLsPGEFWLGNDK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124116   201 LHLLTANGNQELRVDLREFQGQTSFAKYSSFQVSGEQEKYKLTLGQF------LEGTAGDSLTKHNNMAFSTHDQDNDTN 274
Cdd:pfam00147  82 IHLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYigdagdALDTAGRSMTYHNGMQFSTWDRDNDSP 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 13124116   275 GGkNCAALFHGAWWYHDCHQSNLNGRYLPGSHESYADGINWLSGRGHRYSYKVAEMKIR 333
Cdd:pfam00147 162 DG-NCALSYGGGWWYNNCHAANLNGVYYYGGTYSKQNGIIWATWKGRWYSMKKAEMKIR 219
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 64-108 1.52e-08

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: 50.18  E-value: 1.52e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 13124116    64 PAGRGERGLQGSPGKMGPPGSKGEPGTMGPPGVKGEKGERGTASP 108
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 68-111 1.22e-07

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: 52.99  E-value: 1.22e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 13124116   68 GERGLQGSPGKMGPPGSKGEPGTMGPPGVKGEKGERGTASPLGQ 111
Cdd:NF038329 162 GPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 58-111 8.23e-06

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: 47.21  E-value: 8.23e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 13124116   58 KGEPGSPAGRGERGLQGSPGKMGPPGSKGEPGTMGPPGVKGEKGERGTASPLGQ 111
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGE 181
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 125-166 1.56e-05

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: 41.39  E-value: 1.56e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 13124116  125 SCKDLLTRGIFLT-GWYTIY---LPDCRPLTVLCDMDVDGGGWTVF 166
Cdd:NF040941   1 SCWEILQAGPSAPsGVYWIDpdgMGGLAPFQVYCDMTTDGGGWTLV 46
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 67-124 3.85e-05

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: 45.28  E-value: 3.85e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 13124116   67 RGERGLQGSPGKMGPPGSKGEPGTMGPPGVKGEKGeRGTASPLGQKELGDALCRRGPR 124
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPD 253
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 68-111 4.17e-05

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: 44.90  E-value: 4.17e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 13124116   68 GERGLQGSPGKMGPPGSKGEPGTMGPPGVKGEKGERGTASPLGQ 111
Cdd:NF038329 260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGK 303
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 83-124 6.58e-03

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: 37.96  E-value: 6.58e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 13124116   83 GSKGEPGTMGPPGVKGEKGERGTASPLGQKELGDALCRRGPR 124
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGER 158
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 123-333 5.16e-117

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: 336.91  E-value: 5.16e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124116 123 PRSCKDLLTRGIFLTGWYTIYLPDC-RPLTVLCDMDVDGGGWTVFQRRVDGSINFYRDWDSYKRGFGNLGTEFWLGNDYL 201
Cdd:cd00087   3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124116 202 HLLTANGNQELRVDLREFQGQTSFAKYSSFQVSGEQEKYKLTLGQFlEGTAGDSLTKHNNMAFSTHDQDNDTNGGkNCAA 281
Cdd:cd00087  83 HLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGY-SGTAGDALSYHNGMKFSTFDRDNDGASG-NCAE 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 13124116 282 LFHGAWWYHDCHQSNLNGRYLPGSHE-SYADGINWLSGRGHRYSYKVAEMKIR 333
Cdd:cd00087 161 SYSGGWWYNSCHASNLNGRYYSGGHRnEYDNGINWATWKGSTYSLKFTEMKIR 213
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 123-333 5.18e-100

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: 293.41  E-value: 5.18e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124116    123 PRSCKDLLTRGIFLTGWYTIYLPD-CRPLTVLCDMDVDGGGWTVFQRRVDGSINFYRDWDSYKRGFGNLGTEFWLGNDYL 201
Cdd:smart00186   2 PRDCSDVLQNGGKTSGLYTIYPDGsSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124116    202 HLLTANGNQELRVDLREFQGQTSFAKYSSFQVSGEQEKYKLTLGQFlEGTAGD-SLTKHNNMAFSTHDQDNDTNGGkNCA 280
Cdd:smart00186  82 HLLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGY-SGTAGDaSLTYHNGMQFSTYDRDNDKYSG-NCA 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 13124116    281 ALFHGAWWYHDCHQSNLNGRYlpGSHESYADGINWLSGRGHRYSYKVAEMKIR 333
Cdd:smart00186 160 EEYGGGWWYNNCHAANLNGRY--YPNNNYDNGINWATWKGSWYSLKFTEMKIR 210
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
123-333 2.29e-81

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 246.67  E-value: 2.29e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124116   123 PRSCKDLLTRGIFLTGWYTIYL-PDCRPLTVLCDMDVDGGGWTVFQRRVDGSINFYRDWDSYKRGFGNL-GTEFWLGNDY 200
Cdd:pfam00147   2 GRDCSDVYNKGAKTSGLYTIRPdGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLsPGEFWLGNDK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124116   201 LHLLTANGNQELRVDLREFQGQTSFAKYSSFQVSGEQEKYKLTLGQF------LEGTAGDSLTKHNNMAFSTHDQDNDTN 274
Cdd:pfam00147  82 IHLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYigdagdALDTAGRSMTYHNGMQFSTWDRDNDSP 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 13124116   275 GGkNCAALFHGAWWYHDCHQSNLNGRYLPGSHESYADGINWLSGRGHRYSYKVAEMKIR 333
Cdd:pfam00147 162 DG-NCALSYGGGWWYNNCHAANLNGVYYYGGTYSKQNGIIWATWKGRWYSMKKAEMKIR 219
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 64-108 1.52e-08

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: 50.18  E-value: 1.52e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 13124116    64 PAGRGERGLQGSPGKMGPPGSKGEPGTMGPPGVKGEKGERGTASP 108
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 67-112 6.37e-08

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: 48.64  E-value: 6.37e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 13124116    67 RGERGLQGSPGKMGPPGSKGEPGTMGPPGVKGEKGERGTASPLGQK 112
Cdd:pfam01391   3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 68-111 1.22e-07

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: 52.99  E-value: 1.22e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 13124116   68 GERGLQGSPGKMGPPGSKGEPGTMGPPGVKGEKGERGTASPLGQ 111
Cdd:NF038329 162 GPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 67-103 6.86e-07

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: 45.56  E-value: 6.86e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 13124116    67 RGERGLQGSPGKMGPPGSKGEPGTMGPPGVKGEKGER 103
Cdd:pfam01391  21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 58-111 8.23e-06

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: 47.21  E-value: 8.23e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 13124116   58 KGEPGSPAGRGERGLQGSPGKMGPPGSKGEPGTMGPPGVKGEKGERGTASPLGQ 111
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGE 181
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 125-166 1.56e-05

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: 41.39  E-value: 1.56e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 13124116  125 SCKDLLTRGIFLT-GWYTIY---LPDCRPLTVLCDMDVDGGGWTVF 166
Cdd:NF040941   1 SCWEILQAGPSAPsGVYWIDpdgMGGLAPFQVYCDMTTDGGGWTLV 46
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 67-124 3.85e-05

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: 45.28  E-value: 3.85e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 13124116   67 RGERGLQGSPGKMGPPGSKGEPGTMGPPGVKGEKGeRGTASPLGQKELGDALCRRGPR 124
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPD 253
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 68-111 4.17e-05

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: 44.90  E-value: 4.17e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 13124116   68 GERGLQGSPGKMGPPGSKGEPGTMGPPGVKGEKGERGTASPLGQ 111
Cdd:NF038329 260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGK 303
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 83-124 6.58e-03

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: 37.96  E-value: 6.58e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 13124116   83 GSKGEPGTMGPPGVKGEKGERGTASPLGQKELGDALCRRGPR 124
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGER 158
 
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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