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Conserved domains on  [gi|17534799|ref|NP_493702|]
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Nematode cuticle collagen N-terminal domain-containing protein [Caenorhabditis elegans]

Protein Classification

cuticular collagen family protein( domain architecture ID 18387949)

cuticular collagen family protein is a structural macromolecule of the extracellular matrix containing triple helix domains that form tight interactions and stabilize supramolecular aggregates

Gene Ontology:  GO:0042302|GO:0005581
PubMed:  1916105|21421911

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 139-314 1.49e-16

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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 80.72  E-value: 1.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534799  139 PPGPQGPTGYPGAPGEPGSRGLDGRPGANGVTLIAYDQEIPGciqcPQGPQGPPGAVGPCGPSGIPGLPGNPGYTSPPGL 218
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKG----PAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534799  219 PGPPGPCGEAGREGP---------NGTPGLKGEPGNNSIRQISLPGRKGPPGLPGQCGPPGPPGYTPPPGPPGTPGVQGE 289
Cdd:NF038329 197 RGETGPAGEQGPAGPagpdgeagpAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                        170       180
                 ....*....|....*....|....*
gi 17534799  290 AGQDGEPGVPGVTGYPGVRGPPGQD 314
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKD 301
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 16-68 4.30e-11

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


:

Pssm-ID: 198156  Cd Length: 53  Bit Score: 57.48  E-value: 4.30e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17534799     16 TVIRVSFIASSLLISLCLFLIMMTSREISEFREQTLDDLKEWKYFSDAAWNEM 68
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 139-314 1.49e-16

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: 80.72  E-value: 1.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534799  139 PPGPQGPTGYPGAPGEPGSRGLDGRPGANGVTLIAYDQEIPGciqcPQGPQGPPGAVGPCGPSGIPGLPGNPGYTSPPGL 218
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKG----PAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534799  219 PGPPGPCGEAGREGP---------NGTPGLKGEPGNNSIRQISLPGRKGPPGLPGQCGPPGPPGYTPPPGPPGTPGVQGE 289
Cdd:NF038329 197 RGETGPAGEQGPAGPagpdgeagpAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                        170       180
                 ....*....|....*....|....*
gi 17534799  290 AGQDGEPGVPGVTGYPGVRGPPGQD 314
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKD 301
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 139-314 4.59e-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: 67.24  E-value: 4.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534799  139 PPGPQGPTGYPGAPGEPGSRGLDGRPGANGVTLIAYDQEIPGciqcPQGPQGPPGAVGPCGPSGIPGLPGNPGytspPGL 218
Cdd:NF038329 163 PAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG----EQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQ 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534799  219 PGPPGPCGEAGREGPNGTPGLKGEPGNNSIRqiSLPGRKGPPGLPGQCGPPGPPGYTPPPGPPGTPGVQGEAGQDGEPGV 298
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR--GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL 312

                        170
                 ....*....|....*....
gi 17534799  299 P---GVTGYPGVRGPPGQD 314
Cdd:NF038329 313 PgkdGKDGQPGKDGLPGKD 331
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 139-341 8.53e-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: 66.47  E-value: 8.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534799  139 PPGPQGPTGYPGAPGEPGSRGLDGRPGANGVTLIAYDQEIPGCI-QCPQGPQGPPGAVGPCGPSGIPGLPGNPGYTSPPG 217
Cdd:NF038329 187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534799  218 LPGPPGPCGEAGREGPNGTPGLKGEPGNNSirqisLPGRKGPPGLPGQCGPPGPpgytpppgppgtpgvQGEAGQDGEPG 297
Cdd:NF038329 267 EAGPDGPDGKDGERGPVGPAGKDGQNGKDG-----LPGKDGKDGQNGKDGLPGK---------------DGKDGQPGKDG 326

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17534799  298 VPGVTGYPGVRGPPG-------QDAEYCPCPPKNAGVNRNSY-VQPAPVSTS 341
Cdd:NF038329 327 LPGKDGKDGQPGKPApktpevpQKPDTAPHTPKTPQIPGQSKdVTPAPQNPS 378
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 16-68 4.30e-11

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 198156  Cd Length: 53  Bit Score: 57.48  E-value: 4.30e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17534799     16 TVIRVSFIASSLLISLCLFLIMMTSREISEFREQTLDDLKEWKYFSDAAWNEM 68
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 20-68 9.54e-10

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens, see pfam01391. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 460226  Cd Length: 50  Bit Score: 53.62  E-value: 9.54e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 17534799    20 VSFIASSLLISLCLFLIMMTSREISEFREQTLDDLKEWKYFSDAAWNEM 68
Cdd:pfam01484   2 VAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 147-211 2.61e-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: 49.80  E-value: 2.61e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17534799   147 GYPGAPGEPGSRGLDGRPGANGvtliaydqeIPGciqcPQGPQGPPGAVGPCGPSGIPGLPGNPG 211
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPG---------PPG----PPGPPGEPGPPGPPGPPGPPGPPGAPG 52
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 187-328 5.29e-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: 48.36  E-value: 5.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534799  187 GPQGPPGAVGPCGPSGIPGLPGNPGytsppglpgppgpcgEAGREGPNGTPGLKGEPGnnsirqisLPGRKGPPGLPGQC 266
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRG---------------ETGPAGPAGPPGPQGERG--------EKGPAGPQGEAGPQ 173

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17534799  267 GPPGPPGYTPPPGPPGTPGVQGEAGQDGEPGVPGVTGYPGVRGPPGQDAEYCPCPPKNAGVN 328
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQ 235
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 139-314 1.49e-16

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: 80.72  E-value: 1.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534799  139 PPGPQGPTGYPGAPGEPGSRGLDGRPGANGVTLIAYDQEIPGciqcPQGPQGPPGAVGPCGPSGIPGLPGNPGYTSPPGL 218
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKG----PAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534799  219 PGPPGPCGEAGREGP---------NGTPGLKGEPGNNSIRQISLPGRKGPPGLPGQCGPPGPPGYTPPPGPPGTPGVQGE 289
Cdd:NF038329 197 RGETGPAGEQGPAGPagpdgeagpAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                        170       180
                 ....*....|....*....|....*
gi 17534799  290 AGQDGEPGVPGVTGYPGVRGPPGQD 314
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKD 301
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 139-314 4.59e-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: 67.24  E-value: 4.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534799  139 PPGPQGPTGYPGAPGEPGSRGLDGRPGANGVTLIAYDQEIPGciqcPQGPQGPPGAVGPCGPSGIPGLPGNPGytspPGL 218
Cdd:NF038329 163 PAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG----EQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQ 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534799  219 PGPPGPCGEAGREGPNGTPGLKGEPGNNSIRqiSLPGRKGPPGLPGQCGPPGPPGYTPPPGPPGTPGVQGEAGQDGEPGV 298
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR--GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL 312

                        170
                 ....*....|....*....
gi 17534799  299 P---GVTGYPGVRGPPGQD 314
Cdd:NF038329 313 PgkdGKDGQPGKDGLPGKD 331
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 139-341 8.53e-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: 66.47  E-value: 8.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534799  139 PPGPQGPTGYPGAPGEPGSRGLDGRPGANGVTLIAYDQEIPGCI-QCPQGPQGPPGAVGPCGPSGIPGLPGNPGYTSPPG 217
Cdd:NF038329 187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534799  218 LPGPPGPCGEAGREGPNGTPGLKGEPGNNSirqisLPGRKGPPGLPGQCGPPGPpgytpppgppgtpgvQGEAGQDGEPG 297
Cdd:NF038329 267 EAGPDGPDGKDGERGPVGPAGKDGQNGKDG-----LPGKDGKDGQNGKDGLPGK---------------DGKDGQPGKDG 326

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17534799  298 VPGVTGYPGVRGPPG-------QDAEYCPCPPKNAGVNRNSY-VQPAPVSTS 341
Cdd:NF038329 327 LPGKDGKDGQPGKPApktpevpQKPDTAPHTPKTPQIPGQSKdVTPAPQNPS 378
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 16-68 4.30e-11

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 198156  Cd Length: 53  Bit Score: 57.48  E-value: 4.30e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17534799     16 TVIRVSFIASSLLISLCLFLIMMTSREISEFREQTLDDLKEWKYFSDAAWNEM 68
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 20-68 9.54e-10

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens, see pfam01391. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 460226  Cd Length: 50  Bit Score: 53.62  E-value: 9.54e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 17534799    20 VSFIASSLLISLCLFLIMMTSREISEFREQTLDDLKEWKYFSDAAWNEM 68
Cdd:pfam01484   2 VAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 147-211 2.61e-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: 49.80  E-value: 2.61e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17534799   147 GYPGAPGEPGSRGLDGRPGANGvtliaydqeIPGciqcPQGPQGPPGAVGPCGPSGIPGLPGNPG 211
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPG---------PPG----PPGPPGEPGPPGPPGPPGPPGPPGAPG 52
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 187-328 5.29e-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: 48.36  E-value: 5.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534799  187 GPQGPPGAVGPCGPSGIPGLPGNPGytsppglpgppgpcgEAGREGPNGTPGLKGEPGnnsirqisLPGRKGPPGLPGQC 266
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRG---------------ETGPAGPAGPPGPQGERG--------EKGPAGPQGEAGPQ 173

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17534799  267 GPPGPPGYTPPPGPPGTPGVQGEAGQDGEPGVPGVTGYPGVRGPPGQDAEYCPCPPKNAGVN 328
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQ 235
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 185-245 4.38e-05

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: 40.94  E-value: 4.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17534799   185 PQGPQGPPGAVGPCGPSGIPGLPGNPGYtsppglpgppgpCGEAGREGPNGTPGLKGEPGN 245
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGP------------PGEPGPPGPPGPPGPPGPPGA 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 150-243 7.84e-03

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: 34.39  E-value: 7.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17534799   150 GAPGEPGSRGLDGRPGangvtliaydqeipgciqcPQGPQGPPGAVGPCGPSGIPGLPGNPgytsppglpgppgpcgeaG 229
Cdd:pfam01391   1 GPPGPPGPPGPPGPPG-------------------PPGPPGPPGPPGPPGEPGPPGPPGPP------------------G 43

                          90
                  ....*....|....
gi 17534799   230 REGPNGTPGLKGEP 243
Cdd:pfam01391  44 PPGPPGAPGAPGPP 57
 
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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