NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|77404440|ref|NP_034320|]
View 

ficolin-2 precursor [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 103-312 2.41e-115

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: 331.51  E-value: 2.41e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404440 103 PRTCKELLTQGHFLTGWYTIYLPDC-RPLTVLCDMDTDGGGWTVFQRRLDGSVDFFRDWTSYKRGFGSQLGEFWLGNDNI 181
Cdd:cd00087   3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404440 182 HALTTQGTSELRVDLSDFEGKHDFAKYSSFQIQGEAEKYKLILGNFlGGGAGDSLTPHNNRLFSTKDQDNDGSTSSCAMG 261
Cdd:cd00087  83 HLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGY-SGTAGDALSYHNGMKFSTFDRDNDGASGNCAES 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 77404440 262 YHGAWWYSQCHTSNLNGLYLRGPHK-SYANGVNWKSWRGYNYSCKVSEMKVR 312
Cdd:cd00087 162 YSGGWWYNSCHASNLNGRYYSGGHRnEYDNGINWATWKGSTYSLKFTEMKIR 213
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 40-95 2.11e-12

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: 60.97  E-value: 2.11e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 77404440    40 GCPGLPGAAGPKGEAGAKGDRGESGLPGIPGKEGPTGPKGNQGEKGIRGEKGDSGP 95
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 ...
 103-312 2.41e-115

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: 331.51  E-value: 2.41e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404440 103 PRTCKELLTQGHFLTGWYTIYLPDC-RPLTVLCDMDTDGGGWTVFQRRLDGSVDFFRDWTSYKRGFGSQLGEFWLGNDNI 181
Cdd:cd00087   3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404440 182 HALTTQGTSELRVDLSDFEGKHDFAKYSSFQIQGEAEKYKLILGNFlGGGAGDSLTPHNNRLFSTKDQDNDGSTSSCAMG 261
Cdd:cd00087  83 HLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGY-SGTAGDALSYHNGMKFSTFDRDNDGASGNCAES 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 77404440 262 YHGAWWYSQCHTSNLNGLYLRGPHK-SYANGVNWKSWRGYNYSCKVSEMKVR 312
Cdd:cd00087 162 YSGGWWYNSCHASNLNGRYYSGGHRnEYDNGINWATWKGSTYSLKFTEMKIR 213
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 103-312 3.31e-107

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: 311.13  E-value: 3.31e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404440    103 PRTCKELLTQGHFLTGWYTIYLPD-CRPLTVLCDMDTDGGGWTVFQRRLDGSVDFFRDWTSYKRGFGSQLGEFWLGNDNI 181
Cdd:smart00186   2 PRDCSDVLQNGGKTSGLYTIYPDGsSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404440    182 HALTTQGTSELRVDLSDFEGKHDFAKYSSFQIQGEAEKYKLILGNFLGGGAGDSLTPHNNRLFSTKDQDNDGSTSSCAMG 261
Cdd:smart00186  82 HLLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGYSGTAGDASLTYHNGMQFSTYDRDNDKYSGNCAEE 161

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 77404440    262 YHGAWWYSQCHTSNLNGLYlrGPHKSYANGVNWKSWRGYNYSCKVSEMKVR 312
Cdd:smart00186 162 YGGGWWYNNCHAANLNGRY--YPNNNYDNGINWATWKGSWYSLKFTEMKIR 210
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
103-312 1.48e-82

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 248.59  E-value: 1.48e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404440   103 PRTCKELLTQGHFLTGWYTIYL-PDCRPLTVLCDMDTDGGGWTVFQRRLDGSVDFFRDWTSYKRGFGS-QLGEFWLGNDN 180
Cdd:pfam00147   2 GRDCSDVYNKGAKTSGLYTIRPdGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNlSPGEFWLGNDK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404440   181 IHALTTQGTSELRVDLSDFEGKHDFAKYSSFQIQGEAEKYKLILGNFLGG------GAGDSLTPHNNRLFSTKDQDNDGS 254
Cdd:pfam00147  82 IHLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYIGDagdaldTAGRSMTYHNGMQFSTWDRDNDSP 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 77404440   255 TSSCAMGYHGAWWYSQCHTSNLNGLYLRGPHKSYANGVNWKSWRGYNYSCKVSEMKVR 312
Cdd:pfam00147 162 DGNCALSYGGGWWYNNCHAANLNGVYYYGGTYSKQNGIIWATWKGRWYSMKKAEMKIR 219
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 40-95 2.11e-12

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: 60.97  E-value: 2.11e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 77404440    40 GCPGLPGAAGPKGEAGAKGDRGESGLPGIPGKEGPTGPKGNQGEKGIRGEKGDSGP 95
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-104 7.25e-11

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: 62.62  E-value: 7.25e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 77404440   27 LDLEGYKQLTILQGCPGLPGAAGPKGEAGAKGDRGESGLPGIPGKEGPTGPKGNQGEKGIRGEKGDSGPSQscATGPR 104
Cdd:NF038329 113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG--AKGPA 188
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 105-146 1.35e-07

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: 47.17  E-value: 1.35e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 77404440  105 TCKELLTQGHFLT-GWYTIY---LPDCRPLTVLCDMDTDGGGWTVF 146
Cdd:NF040941   1 SCWEILQAGPSAPsGVYWIDpdgMGGLAPFQVYCDMTTDGGGWTLV 46
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 40-107 3.24e-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: 3.24e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 77404440   40 GCPGLPGAAGPKGEAGAKGDRGESGLPGIPGKEGPTGPKGNQGEKGIRGEKGDSGPsQSCATGPRTCK 107
Cdd:NF038329 293 GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVP-QKPDTAPHTPK 359
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 103-312 2.41e-115

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: 331.51  E-value: 2.41e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404440 103 PRTCKELLTQGHFLTGWYTIYLPDC-RPLTVLCDMDTDGGGWTVFQRRLDGSVDFFRDWTSYKRGFGSQLGEFWLGNDNI 181
Cdd:cd00087   3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404440 182 HALTTQGTSELRVDLSDFEGKHDFAKYSSFQIQGEAEKYKLILGNFlGGGAGDSLTPHNNRLFSTKDQDNDGSTSSCAMG 261
Cdd:cd00087  83 HLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGY-SGTAGDALSYHNGMKFSTFDRDNDGASGNCAES 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 77404440 262 YHGAWWYSQCHTSNLNGLYLRGPHK-SYANGVNWKSWRGYNYSCKVSEMKVR 312
Cdd:cd00087 162 YSGGWWYNSCHASNLNGRYYSGGHRnEYDNGINWATWKGSTYSLKFTEMKIR 213
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 103-312 3.31e-107

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: 311.13  E-value: 3.31e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404440    103 PRTCKELLTQGHFLTGWYTIYLPD-CRPLTVLCDMDTDGGGWTVFQRRLDGSVDFFRDWTSYKRGFGSQLGEFWLGNDNI 181
Cdd:smart00186   2 PRDCSDVLQNGGKTSGLYTIYPDGsSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404440    182 HALTTQGTSELRVDLSDFEGKHDFAKYSSFQIQGEAEKYKLILGNFLGGGAGDSLTPHNNRLFSTKDQDNDGSTSSCAMG 261
Cdd:smart00186  82 HLLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGYSGTAGDASLTYHNGMQFSTYDRDNDKYSGNCAEE 161

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 77404440    262 YHGAWWYSQCHTSNLNGLYlrGPHKSYANGVNWKSWRGYNYSCKVSEMKVR 312
Cdd:smart00186 162 YGGGWWYNNCHAANLNGRY--YPNNNYDNGINWATWKGSWYSLKFTEMKIR 210
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
103-312 1.48e-82

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 248.59  E-value: 1.48e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404440   103 PRTCKELLTQGHFLTGWYTIYL-PDCRPLTVLCDMDTDGGGWTVFQRRLDGSVDFFRDWTSYKRGFGS-QLGEFWLGNDN 180
Cdd:pfam00147   2 GRDCSDVYNKGAKTSGLYTIRPdGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNlSPGEFWLGNDK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404440   181 IHALTTQGTSELRVDLSDFEGKHDFAKYSSFQIQGEAEKYKLILGNFLGG------GAGDSLTPHNNRLFSTKDQDNDGS 254
Cdd:pfam00147  82 IHLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYIGDagdaldTAGRSMTYHNGMQFSTWDRDNDSP 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 77404440   255 TSSCAMGYHGAWWYSQCHTSNLNGLYLRGPHKSYANGVNWKSWRGYNYSCKVSEMKVR 312
Cdd:pfam00147 162 DGNCALSYGGGWWYNNCHAANLNGVYYYGGTYSKQNGIIWATWKGRWYSMKKAEMKIR 219
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 40-95 2.11e-12

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: 60.97  E-value: 2.11e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 77404440    40 GCPGLPGAAGPKGEAGAKGDRGESGLPGIPGKEGPTGPKGNQGEKGIRGEKGDSGP 95
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 38-91 2.46e-12

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: 60.97  E-value: 2.46e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 77404440    38 LQGCPGLPGAAGPKGEAGAKGDRGESGLPGIPGKEGPTGPKGNQGEKGIRGEKG 91
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-104 7.25e-11

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: 62.62  E-value: 7.25e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 77404440   27 LDLEGYKQLTILQGCPGLPGAAGPKGEAGAKGDRGESGLPGIPGKEGPTGPKGNQGEKGIRGEKGDSGPSQscATGPR 104
Cdd:NF038329 113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG--AKGPA 188
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 46-96 5.21e-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: 54.42  E-value: 5.21e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 77404440    46 GAAGPKGEAGAKGDRGESGLPGIPGKEGPTGPKGNQGEKGIRGEKGDSGPS 96
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 105-146 1.35e-07

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: 47.17  E-value: 1.35e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 77404440  105 TCKELLTQGHFLT-GWYTIY---LPDCRPLTVLCDMDTDGGGWTVF 146
Cdd:NF040941   1 SCWEILQAGPSAPsGVYWIDpdgMGGLAPFQVYCDMTTDGGGWTLV 46
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 39-77 6.91e-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: 6.91e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 77404440    39 QGCPGLPGAAGPKGEAGAKGDRGESGLPGIPGKEGPTGP 77
Cdd:pfam01391  18 PGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 40-107 3.24e-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: 3.24e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 77404440   40 GCPGLPGAAGPKGEAGAKGDRGESGLPGIPGKEGPTGPKGNQGEKGIRGEKGDSGPsQSCATGPRTCK 107
Cdd:NF038329 293 GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVP-QKPDTAPHTPK 359
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH