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Conserved domains on  [gi|6679763|ref|NP_032021|]
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ficolin-1 isoform 1 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

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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 ...
123-332 2.01e-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  Cd Length: 215  Bit Score: 337.68  E-value: 2.01e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679763  123 PRSCKDLLTRGIFLTGWYTIHLPDC-RPLTVLCDMDVDGGGWTVFQRRVDGSIDFFRDWDSYKRGFGNLGTEFWLGNDYL 201
Cdd:cd00087   3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679763  202 HLLTANGNQELRVDLQDFQGKGSYAKYSSFQVSEEQEKYKLTLGQFlEGTAGDSLTKHNNMSFTTHDQDNDANSMNCAAL 281
Cdd:cd00087  83 HLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGY-SGTAGDALSYHNGMKFSTFDRDNDGASGNCAES 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 6679763  282 FHGAWWYHNCHQSNLNGRYLSGSHE-SYADGINWGTGQGHHYSYKVAEMKIR 332
Cdd:cd00087 162 YSGGWWYNSCHASNLNGRYYSGGHRnEYDNGINWATWKGSTYSLKFTEMKIR 213
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
67-106 1.04e-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: 396114 [Multi-domain]  Cd Length: 57  Bit Score: 47.87  E-value: 1.04e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 6679763     67 RGERGF---QGSPGKMGPAGSKGEPGTMGPPGVKGEKGDTGAA 106
Cdd:pfam01391  12 PGPPGPpgpPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
123-332 2.01e-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  Cd Length: 215  Bit Score: 337.68  E-value: 2.01e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679763  123 PRSCKDLLTRGIFLTGWYTIHLPDC-RPLTVLCDMDVDGGGWTVFQRRVDGSIDFFRDWDSYKRGFGNLGTEFWLGNDYL 201
Cdd:cd00087   3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679763  202 HLLTANGNQELRVDLQDFQGKGSYAKYSSFQVSEEQEKYKLTLGQFlEGTAGDSLTKHNNMSFTTHDQDNDANSMNCAAL 281
Cdd:cd00087  83 HLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGY-SGTAGDALSYHNGMKFSTFDRDNDGASGNCAES 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 6679763  282 FHGAWWYHNCHQSNLNGRYLSGSHE-SYADGINWGTGQGHHYSYKVAEMKIR 332
Cdd:cd00087 162 YSGGWWYNSCHASNLNGRYYSGGHRnEYDNGINWATWKGSTYSLKFTEMKIR 213
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
123-332 3.10e-101

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: 296.50  E-value: 3.10e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679763     123 PRSCKDLLTRGIFLTGWYTIHLPD-CRPLTVLCDMDVDGGGWTVFQRRVDGSIDFFRDWDSYKRGFGNLGTEFWLGNDYL 201
Cdd:smart00186   2 PRDCSDVLQNGGKTSGLYTIYPDGsSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679763     202 HLLTANGNQELRVDLQDFQGKGSYAKYSSFQVSEEQEKYKLTLGQFlEGTAGD-SLTKHNNMSFTTHDQDNDANSMNCAA 280
Cdd:smart00186  82 HLLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGY-SGTAGDaSLTYHNGMQFSTYDRDNDKYSGNCAE 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 6679763     281 LFHGAWWYHNCHQSNLNGRYlsGSHESYADGINWGTGQGHHYSYKVAEMKIR 332
Cdd:smart00186 161 EYGGGWWYNNCHAANLNGRY--YPNNNYDNGINWATWKGSWYSLKFTEMKIR 210
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
123-332 5.32e-82

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 248.21  E-value: 5.32e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679763    123 PRSCKDLLTRGIFLTGWYTIHL-PDCRPLTVLCDMDVDGGGWTVFQRRVDGSIDFFRDWDSYKRGFGNL-GTEFWLGNDY 200
Cdd:pfam00147   2 GRDCSDVYNKGAKTSGLYTIRPdGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLsPGEFWLGNDK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679763    201 LHLLTANGNQELRVDLQDFQGKGSYAKYSSFQVSEEQEKYKLTLGQF------LEGTAGDSLTKHNNMSFTTHDQDNDAN 274
Cdd:pfam00147  82 IHLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYigdagdALDTAGRSMTYHNGMQFSTWDRDNDSP 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6679763    275 SMNCAALFHGAWWYHNCHQSNLNGRYLSGSHESYADGINWGTGQGHHYSYKVAEMKIR 332
Cdd:pfam00147 162 DGNCALSYGGGWWYNNCHAANLNGVYYYGGTYSKQNGIIWATWKGRWYSMKKAEMKIR 219
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
67-106 1.04e-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: 396114 [Multi-domain]  Cd Length: 57  Bit Score: 47.87  E-value: 1.04e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 6679763     67 RGERGF---QGSPGKMGPAGSKGEPGTMGPPGVKGEKGDTGAA 106
Cdd:pfam01391  12 PGPPGPpgpPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
67-123 6.57e-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: 439624 [Multi-domain]  Cd Length: 440  Bit Score: 50.66  E-value: 6.57e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6679763    67 RGERGFQGSPGKMGPAGSKGEPGTMGPPGVKGEKGDTGAAPSLGEKELGDTLCQRGP 123
Cdd:NF038329 155 QGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
68-124 1.07e-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: 439624 [Multi-domain]  Cd Length: 440  Bit Score: 49.89  E-value: 1.07e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6679763    68 GERGFQGSPGKMGPAGSKGEPGTMGPPGVKGEKGDTGAAPSLGEKELG--DTLCQRGPR 124
Cdd:NF038329 180 GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAgpAGDGQQGPD 238
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
68-111 1.15e-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: 439624 [Multi-domain]  Cd Length: 440  Bit Score: 49.89  E-value: 1.15e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 6679763    68 GERGFQGSPGKMGPAGSKGEPGTMGPPGVKGEKGDTGAAPSLGE 111
Cdd:NF038329 150 GPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
58-124 1.74e-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: 439624 [Multi-domain]  Cd Length: 440  Bit Score: 42.95  E-value: 1.74e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679763    58 KGEPGSPAGRGERGFQGSPGKMGPAGSKGEPGTMGPPGVKGEKGDTGAAPSLGEKELGDTLCQRGPR 124
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
65-124 2.31e-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: 439624 [Multi-domain]  Cd Length: 440  Bit Score: 39.49  E-value: 2.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6679763    65 AGRGERGFQGSPGkmgPAGSKGEPGTMGPPGVKGEKGDTGAAPSLGEK-ELGdtlcQRGPR 124
Cdd:NF038329 230 AGDGQQGPDGDPG---PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDgKDG----ERGPV 283
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
123-332 2.01e-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  Cd Length: 215  Bit Score: 337.68  E-value: 2.01e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679763  123 PRSCKDLLTRGIFLTGWYTIHLPDC-RPLTVLCDMDVDGGGWTVFQRRVDGSIDFFRDWDSYKRGFGNLGTEFWLGNDYL 201
Cdd:cd00087   3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679763  202 HLLTANGNQELRVDLQDFQGKGSYAKYSSFQVSEEQEKYKLTLGQFlEGTAGDSLTKHNNMSFTTHDQDNDANSMNCAAL 281
Cdd:cd00087  83 HLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGY-SGTAGDALSYHNGMKFSTFDRDNDGASGNCAES 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 6679763  282 FHGAWWYHNCHQSNLNGRYLSGSHE-SYADGINWGTGQGHHYSYKVAEMKIR 332
Cdd:cd00087 162 YSGGWWYNSCHASNLNGRYYSGGHRnEYDNGINWATWKGSTYSLKFTEMKIR 213
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
123-332 3.10e-101

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: 296.50  E-value: 3.10e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679763     123 PRSCKDLLTRGIFLTGWYTIHLPD-CRPLTVLCDMDVDGGGWTVFQRRVDGSIDFFRDWDSYKRGFGNLGTEFWLGNDYL 201
Cdd:smart00186   2 PRDCSDVLQNGGKTSGLYTIYPDGsSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679763     202 HLLTANGNQELRVDLQDFQGKGSYAKYSSFQVSEEQEKYKLTLGQFlEGTAGD-SLTKHNNMSFTTHDQDNDANSMNCAA 280
Cdd:smart00186  82 HLLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGY-SGTAGDaSLTYHNGMQFSTYDRDNDKYSGNCAE 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 6679763     281 LFHGAWWYHNCHQSNLNGRYlsGSHESYADGINWGTGQGHHYSYKVAEMKIR 332
Cdd:smart00186 161 EYGGGWWYNNCHAANLNGRY--YPNNNYDNGINWATWKGSWYSLKFTEMKIR 210
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
123-332 5.32e-82

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


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 248.21  E-value: 5.32e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679763    123 PRSCKDLLTRGIFLTGWYTIHL-PDCRPLTVLCDMDVDGGGWTVFQRRVDGSIDFFRDWDSYKRGFGNL-GTEFWLGNDY 200
Cdd:pfam00147   2 GRDCSDVYNKGAKTSGLYTIRPdGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLsPGEFWLGNDK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679763    201 LHLLTANGNQELRVDLQDFQGKGSYAKYSSFQVSEEQEKYKLTLGQF------LEGTAGDSLTKHNNMSFTTHDQDNDAN 274
Cdd:pfam00147  82 IHLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYigdagdALDTAGRSMTYHNGMQFSTWDRDNDSP 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6679763    275 SMNCAALFHGAWWYHNCHQSNLNGRYLSGSHESYADGINWGTGQGHHYSYKVAEMKIR 332
Cdd:pfam00147 162 DGNCALSYGGGWWYNNCHAANLNGVYYYGGTYSKQNGIIWATWKGRWYSMKKAEMKIR 219
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
67-106 1.04e-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: 396114 [Multi-domain]  Cd Length: 57  Bit Score: 47.87  E-value: 1.04e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 6679763     67 RGERGF---QGSPGKMGPAGSKGEPGTMGPPGVKGEKGDTGAA 106
Cdd:pfam01391  12 PGPPGPpgpPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
67-106 1.30e-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: 396114 [Multi-domain]  Cd Length: 57  Bit Score: 47.49  E-value: 1.30e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 6679763     67 RGERGFQGSPGKMGPAGSKGEPGTMGPPGVKGEKGDTGAA 106
Cdd:pfam01391  18 PGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
67-123 6.57e-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: 439624 [Multi-domain]  Cd Length: 440  Bit Score: 50.66  E-value: 6.57e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6679763    67 RGERGFQGSPGKMGPAGSKGEPGTMGPPGVKGEKGDTGAAPSLGEKELGDTLCQRGP 123
Cdd:NF038329 155 QGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
68-124 1.07e-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: 439624 [Multi-domain]  Cd Length: 440  Bit Score: 49.89  E-value: 1.07e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6679763    68 GERGFQGSPGKMGPAGSKGEPGTMGPPGVKGEKGDTGAAPSLGEKELG--DTLCQRGPR 124
Cdd:NF038329 180 GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAgpAGDGQQGPD 238
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
68-111 1.15e-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: 439624 [Multi-domain]  Cd Length: 440  Bit Score: 49.89  E-value: 1.15e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 6679763    68 GERGFQGSPGKMGPAGSKGEPGTMGPPGVKGEKGDTGAAPSLGE 111
Cdd:NF038329 150 GPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
58-124 1.74e-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: 439624 [Multi-domain]  Cd Length: 440  Bit Score: 42.95  E-value: 1.74e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679763    58 KGEPGSPAGRGERGFQGSPGKMGPAGSKGEPGTMGPPGVKGEKGDTGAAPSLGEKELGDTLCQRGPR 124
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
58-94 3.78e-04

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: 396114 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 3.78e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 6679763     58 KGEPGSPAGRGERGFQGSPGKMGPAGSKGEPGTMGPP 94
Cdd:pfam01391  21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
65-124 2.31e-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: 439624 [Multi-domain]  Cd Length: 440  Bit Score: 39.49  E-value: 2.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6679763    65 AGRGERGFQGSPGkmgPAGSKGEPGTMGPPGVKGEKGDTGAAPSLGEK-ELGdtlcQRGPR 124
Cdd:NF038329 230 AGDGQQGPDGDPG---PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDgKDG----ERGPV 283
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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