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Conserved domains on  [gi|8051584|ref|NP_001994|]
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ficolin-1 precursor [Homo sapiens]

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 ...
 115-325 5.99e-124

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: 353.85  E-value: 5.99e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8051584  115 PRNCKDLLDRGYFLSGWHTIYLPDC-RPLTVLCDMDTDGGGWTVFQRRMDGSVDFYRDWAAYKQGFGSQLGEFWLGNDNI 193
Cdd:cd00087   3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8051584  194 HALTAQGSSELRVDLVDFEGNHQFAKYKSFKVADEAEKYKLVLGAFvGGSAGNSLTGHNNNFFSTKDQDNDVSSSNCAEK 273
Cdd:cd00087  83 HLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGY-SGTAGDALSYHNGMKFSTFDRDNDGASGNCAES 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 8051584  274 FQGAWWYADCHASNLNGLYLMGPHE-SYANGINWSAAKGYKYSYKVSEMKVRP 325
Cdd:cd00087 162 YSGGWWYNSCHASNLNGRYYSGGHRnEYDNGINWATWKGSTYSLKFTEMKIRP 214
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 52-107 1.84e-13

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: 64.05  E-value: 1.84e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 8051584     52 GCPGLPGAPGPKGEAGVIGERGERGLPGAPGKAGPVGPKGDRGEKGMRGEKGDAGQ 107
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 115-325 5.99e-124

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: 353.85  E-value: 5.99e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8051584  115 PRNCKDLLDRGYFLSGWHTIYLPDC-RPLTVLCDMDTDGGGWTVFQRRMDGSVDFYRDWAAYKQGFGSQLGEFWLGNDNI 193
Cdd:cd00087   3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8051584  194 HALTAQGSSELRVDLVDFEGNHQFAKYKSFKVADEAEKYKLVLGAFvGGSAGNSLTGHNNNFFSTKDQDNDVSSSNCAEK 273
Cdd:cd00087  83 HLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGY-SGTAGDALSYHNGMKFSTFDRDNDGASGNCAES 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 8051584  274 FQGAWWYADCHASNLNGLYLMGPHE-SYANGINWSAAKGYKYSYKVSEMKVRP 325
Cdd:cd00087 162 YSGGWWYNSCHASNLNGRYYSGGHRnEYDNGINWATWKGSTYSLKFTEMKIRP 214
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 115-326 2.79e-122

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: 349.65  E-value: 2.79e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8051584     115 PRNCKDLLDRGYFLSGWHTIYLPD-CRPLTVLCDMDTDGGGWTVFQRRMDGSVDFYRDWAAYKQGFGSQLGEFWLGNDNI 193
Cdd:smart00186   2 PRDCSDVLQNGGKTSGLYTIYPDGsSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8051584     194 HALTAQGSSELRVDLVDFEGNHQFAKYKSFKVADEAEKYKLVLGAFVGGSAGNSLTGHNNNFFSTKDQDNDVSSSNCAEK 273
Cdd:smart00186  82 HLLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGYSGTAGDASLTYHNGMQFSTYDRDNDKYSGNCAEE 161

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 8051584     274 FQGAWWYADCHASNLNGLYlmGPHESYANGINWSAAKGYKYSYKVSEMKVRPA 326
Cdd:smart00186 162 YGGGWWYNNCHAANLNGRY--YPNNNYDNGINWATWKGSWYSLKFTEMKIRPL 212
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
115-325 2.59e-85

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 256.30  E-value: 2.59e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8051584    115 PRNCKDLLDRGYFLSGWHTIYL-PDCRPLTVLCDMDTDGGGWTVFQRRMDGSVDFYRDWAAYKQGFGS-QLGEFWLGNDN 192
Cdd:pfam00147   2 GRDCSDVYNKGAKTSGLYTIRPdGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNlSPGEFWLGNDK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8051584    193 IHALTAQGSSELRVDLVDFEGNHQFAKYKSFKVADEAEKYKLVLGAFVGG------SAGNSLTGHNNNFFSTKDQDNDVS 266
Cdd:pfam00147  82 IHLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYIGDagdaldTAGRSMTYHNGMQFSTWDRDNDSP 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 8051584    267 SSNCAEKFQGAWWYADCHASNLNGLYLMGPHESYANGINWSAAKGYKYSYKVSEMKVRP 325
Cdd:pfam00147 162 DGNCALSYGGGWWYNNCHAANLNGVYYYGGTYSKQNGIIWATWKGRWYSMKKAEMKIRP 220
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 52-107 1.84e-13

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: 64.05  E-value: 1.84e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 8051584     52 GCPGLPGAPGPKGEAGVIGERGERGLPGAPGKAGPVGPKGDRGEKGMRGEKGDAGQ 107
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 35-116 1.04e-12

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: 68.39  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8051584    35 EVKVVGLEGSDKLTILRGCPGLPGAPGPKGEAGVIGERGERGLPGAPGKAGPVGPKGDRGEKGMRGEKGDAG-QSQSCAT 113
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGpQGPRGET 200


                 ...
gi 8051584   114 GPR 116
Cdd:NF038329 201 GPA 203
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 70-115 1.24e-08

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: 56.07  E-value: 1.24e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 8051584    70 GERGERGLPGAPGKAGPVGPKGDRGEKGMRGEKGDAG-QSQSCATGP 115
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGpQGERGEKGP 163
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 39-107 2.74e-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: 51.83  E-value: 2.74e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8051584    39 VGLEGSDkltilrGCPGLPGAPGPKGEAGVIGERGERGLPG---APGKAGPVGPKGDRGEKGMRGEKGDAGQ 107
Cdd:NF038329 253 DGPAGKD------GPRGDRGEAGPDGPDGKDGERGPVGPAGkdgQNGKDGLPGKDGKDGQNGKDGLPGKDGK 318
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 40-106 5.97e-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: 50.67  E-value: 5.97e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8051584    40 GLEGSDKLTILRGCPGLPGAPGPKG------EAGVIGERGERGLPGAPGKAGPVGPKGDRGEKGMRGEKGDAG 106
Cdd:NF038329 239 GDPGPTGEDGPQGPDGPAGKDGPRGdrgeagPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 117-158 3.28e-06

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: 43.32  E-value: 3.28e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 8051584   117 NCKDLLDRGYFL-SGWHTIY---LPDCRPLTVLCDMDTDGGGWTVF 158
Cdd:NF040941   1 SCWEILQAGPSApSGVYWIDpdgMGGLAPFQVYCDMTTDGGGWTLV 46
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 39-97 1.71e-04

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: 42.97  E-value: 1.71e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 8051584    39 VGLEGSDKLtilRGCPGLPGAPGPKGEAGVIGERGERGLPGAPGKAGPVGPKGDRGEKG 97
Cdd:NF038329 283 VGPAGKDGQ---NGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 115-325 5.99e-124

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: 353.85  E-value: 5.99e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8051584  115 PRNCKDLLDRGYFLSGWHTIYLPDC-RPLTVLCDMDTDGGGWTVFQRRMDGSVDFYRDWAAYKQGFGSQLGEFWLGNDNI 193
Cdd:cd00087   3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8051584  194 HALTAQGSSELRVDLVDFEGNHQFAKYKSFKVADEAEKYKLVLGAFvGGSAGNSLTGHNNNFFSTKDQDNDVSSSNCAEK 273
Cdd:cd00087  83 HLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGY-SGTAGDALSYHNGMKFSTFDRDNDGASGNCAES 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 8051584  274 FQGAWWYADCHASNLNGLYLMGPHE-SYANGINWSAAKGYKYSYKVSEMKVRP 325
Cdd:cd00087 162 YSGGWWYNSCHASNLNGRYYSGGHRnEYDNGINWATWKGSTYSLKFTEMKIRP 214
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 115-326 2.79e-122

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: 349.65  E-value: 2.79e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8051584     115 PRNCKDLLDRGYFLSGWHTIYLPD-CRPLTVLCDMDTDGGGWTVFQRRMDGSVDFYRDWAAYKQGFGSQLGEFWLGNDNI 193
Cdd:smart00186   2 PRDCSDVLQNGGKTSGLYTIYPDGsSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8051584     194 HALTAQGSSELRVDLVDFEGNHQFAKYKSFKVADEAEKYKLVLGAFVGGSAGNSLTGHNNNFFSTKDQDNDVSSSNCAEK 273
Cdd:smart00186  82 HLLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGYSGTAGDASLTYHNGMQFSTYDRDNDKYSGNCAEE 161

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 8051584     274 FQGAWWYADCHASNLNGLYlmGPHESYANGINWSAAKGYKYSYKVSEMKVRPA 326
Cdd:smart00186 162 YGGGWWYNNCHAANLNGRY--YPNNNYDNGINWATWKGSWYSLKFTEMKIRPL 212
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
115-325 2.59e-85

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 256.30  E-value: 2.59e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8051584    115 PRNCKDLLDRGYFLSGWHTIYL-PDCRPLTVLCDMDTDGGGWTVFQRRMDGSVDFYRDWAAYKQGFGS-QLGEFWLGNDN 192
Cdd:pfam00147   2 GRDCSDVYNKGAKTSGLYTIRPdGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNlSPGEFWLGNDK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8051584    193 IHALTAQGSSELRVDLVDFEGNHQFAKYKSFKVADEAEKYKLVLGAFVGG------SAGNSLTGHNNNFFSTKDQDNDVS 266
Cdd:pfam00147  82 IHLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYIGDagdaldTAGRSMTYHNGMQFSTWDRDNDSP 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 8051584    267 SSNCAEKFQGAWWYADCHASNLNGLYLMGPHESYANGINWSAAKGYKYSYKVSEMKVRP 325
Cdd:pfam00147 162 DGNCALSYGGGWWYNNCHAANLNGVYYYGGTYSKQNGIIWATWKGRWYSMKKAEMKIRP 220
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 52-107 1.84e-13

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: 64.05  E-value: 1.84e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 8051584     52 GCPGLPGAPGPKGEAGVIGERGERGLPGAPGKAGPVGPKGDRGEKGMRGEKGDAGQ 107
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 50-105 3.16e-13

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: 63.28  E-value: 3.16e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 8051584     50 LRGCPGLPGAPGPKGEAGVIGERGERGLPGAPGKAGPVGPKGDRGEKGMRGEKGDA 105
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 35-116 1.04e-12

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: 68.39  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8051584    35 EVKVVGLEGSDKLTILRGCPGLPGAPGPKGEAGVIGERGERGLPGAPGKAGPVGPKGDRGEKGMRGEKGDAG-QSQSCAT 113
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGpQGPRGET 200


                 ...
gi 8051584   114 GPR 116
Cdd:NF038329 201 GPA 203
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 40-97 3.14e-10

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: 55.19  E-value: 3.14e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 8051584     40 GLEGSDKLTILRGCPGLPGAPGPKGEAgviGERGERGLPGAPGKAGPVGPKGDRGEKG 97
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPP---GPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 58-108 8.42e-10

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: 54.04  E-value: 8.42e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 8051584     58 GAPGPKGEAGVIGERGERGLPGAPGKAGPVGPKGDRGEKGMRGEKGDAGQS 108
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 70-115 1.24e-08

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: 56.07  E-value: 1.24e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 8051584    70 GERGERGLPGAPGKAGPVGPKGDRGEKGMRGEKGDAG-QSQSCATGP 115
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGpQGERGEKGP 163
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 39-107 2.74e-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: 51.83  E-value: 2.74e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8051584    39 VGLEGSDkltilrGCPGLPGAPGPKGEAGVIGERGERGLPG---APGKAGPVGPKGDRGEKGMRGEKGDAGQ 107
Cdd:NF038329 253 DGPAGKD------GPRGDRGEAGPDGPDGKDGERGPVGPAGkdgQNGKDGLPGKDGKDGQNGKDGLPGKDGK 318
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 40-106 5.97e-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: 50.67  E-value: 5.97e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8051584    40 GLEGSDKLTILRGCPGLPGAPGPKG------EAGVIGERGERGLPGAPGKAGPVGPKGDRGEKGMRGEKGDAG 106
Cdd:NF038329 239 GDPGPTGEDGPQGPDGPAGKDGPRGdrgeagPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 117-158 3.28e-06

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: 43.32  E-value: 3.28e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 8051584   117 NCKDLLDRGYFL-SGWHTIY---LPDCRPLTVLCDMDTDGGGWTVF 158
Cdd:NF040941   1 SCWEILQAGPSApSGVYWIDpdgMGGLAPFQVYCDMTTDGGGWTLV 46
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 39-97 1.71e-04

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: 42.97  E-value: 1.71e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 8051584    39 VGLEGSDKLtilRGCPGLPGAPGPKGEAGVIGERGERGLPGAPGKAGPVGPKGDRGEKG 97
Cdd:NF038329 283 VGPAGKDGQ---NGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
 
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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