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Conserved domains on  [gi|392889069|ref|NP_493913|]
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Cuticle collagen 40 [Caenorhabditis elegans]

Protein Classification

cuticular collagen family protein( domain architecture ID 18387963)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 15-66 2.09e-21

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: 85.21  E-value: 2.09e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 392889069    15 KLAFFGISVSTIATLTAIIAVPMLYNYMQHVQSSLQNEVEFCKHRTDGLWDE 66
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNE 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 253-285 1.08e-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: 42.10  E-value: 1.08e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 392889069  253 EPGPAGPAGDAGPDGAPGNAGAPGAPGEAGAPG 285
Cdd:pfam01391  23 PPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 126-288 1.38e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 39.89  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889069 126 GAPGEDGKAGNPGTAGSDAEAAAAPTASDFCFDCPPGPAGPAGGPGPAGPPGPAGADGNTPSGGGEGPAGPPGPPGPAGN 205
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889069 206 PGTDGAPGNPGAPGQVTETPGTPGPAGAAGPPgppgpagnpgsagASEPGPAGPAGDAGPDGAPGNAGAPGAPGEAGAPG 285
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGP-------------DGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272


                 ...
gi 392889069 286 SGG 288
Cdd:NF038329 273 PDG 275
 
Name Accession Description Interval E-value
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 15-66 2.09e-21

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: 85.21  E-value: 2.09e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 392889069    15 KLAFFGISVSTIATLTAIIAVPMLYNYMQHVQSSLQNEVEFCKHRTDGLWDE 66
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNE 52
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 18-66 4.95e-18

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: 75.96  E-value: 4.95e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 392889069   18 FFGISVSTIATLTAIIAVPMLYNYMQHVQSSLQNEVEFCKHRTDGLWDE 66
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNE 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 253-285 1.08e-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: 42.10  E-value: 1.08e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 392889069  253 EPGPAGPAGDAGPDGAPGNAGAPGAPGEAGAPG 285
Cdd:pfam01391  23 PPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 126-288 1.38e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 39.89  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889069 126 GAPGEDGKAGNPGTAGSDAEAAAAPTASDFCFDCPPGPAGPAGGPGPAGPPGPAGADGNTPSGGGEGPAGPPGPPGPAGN 205
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889069 206 PGTDGAPGNPGAPGQVTETPGTPGPAGAAGPPgppgpagnpgsagASEPGPAGPAGDAGPDGAPGNAGAPGAPGEAGAPG 285
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGP-------------DGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272


                 ...
gi 392889069 286 SGG 288
Cdd:NF038329 273 PDG 275
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 126-298 1.55e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 39.89  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889069 126 GAPGEDGKAGNPGTAGSDAEAAAAPTASDFCFDCPPGPAGPAGGPGPAGPPGPAGADGNtpsgGGEGPAGPPGPPGPAGN 205
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGP 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889069 206 PGTDGAPGNPGAPGQVTETPGTPGPAGAAGPPGPPGPAGNPGSAGASEPGPAGPAGDAGPDGAPGNAGAPGAPGEAGAPG 285
Cdd:NF038329 250 QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329

                        170
                 ....*....|....*
gi 392889069 286 SGG--GCDHCPPPRT 298
Cdd:NF038329 330 KDGkdGQPGKPAPKT 344
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 249-288 3.02e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 39.12  E-value: 3.02e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 392889069 249 AGASEPGPAGPAGDAGPDGAPGNAGAPGAPGEAGAPGSGG 288
Cdd:NF038329 114 KGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPG 153
 
Name Accession Description Interval E-value
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 15-66 2.09e-21

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: 85.21  E-value: 2.09e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 392889069    15 KLAFFGISVSTIATLTAIIAVPMLYNYMQHVQSSLQNEVEFCKHRTDGLWDE 66
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNE 52
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 18-66 4.95e-18

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: 75.96  E-value: 4.95e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 392889069   18 FFGISVSTIATLTAIIAVPMLYNYMQHVQSSLQNEVEFCKHRTDGLWDE 66
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNE 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 253-285 1.08e-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: 42.10  E-value: 1.08e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 392889069  253 EPGPAGPAGDAGPDGAPGNAGAPGAPGEAGAPG 285
Cdd:pfam01391  23 PPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 253-288 2.24e-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: 41.33  E-value: 2.24e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 392889069  253 EPGPAGPAGDAGPDGAPGNAGAPGAPGEAGAPGSGG 288
Cdd:pfam01391  20 PPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 253-284 4.82e-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: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.47  E-value: 4.82e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 392889069  253 EPGPAGPAGDAGPDGAPGNAGAPGAPGEAGAP 284
Cdd:pfam01391  26 PPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 126-288 1.38e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 39.89  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889069 126 GAPGEDGKAGNPGTAGSDAEAAAAPTASDFCFDCPPGPAGPAGGPGPAGPPGPAGADGNTPSGGGEGPAGPPGPPGPAGN 205
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889069 206 PGTDGAPGNPGAPGQVTETPGTPGPAGAAGPPgppgpagnpgsagASEPGPAGPAGDAGPDGAPGNAGAPGAPGEAGAPG 285
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGP-------------DGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272


                 ...
gi 392889069 286 SGG 288
Cdd:NF038329 273 PDG 275
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 126-298 1.55e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 39.89  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889069 126 GAPGEDGKAGNPGTAGSDAEAAAAPTASDFCFDCPPGPAGPAGGPGPAGPPGPAGADGNtpsgGGEGPAGPPGPPGPAGN 205
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGP 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889069 206 PGTDGAPGNPGAPGQVTETPGTPGPAGAAGPPGPPGPAGNPGSAGASEPGPAGPAGDAGPDGAPGNAGAPGAPGEAGAPG 285
Cdd:NF038329 250 QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329

                        170
                 ....*....|....*
gi 392889069 286 SGG--GCDHCPPPRT 298
Cdd:NF038329 330 KDGkdGQPGKPAPKT 344
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 249-288 3.02e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 39.12  E-value: 3.02e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 392889069 249 AGASEPGPAGPAGDAGPDGAPGNAGAPGAPGEAGAPGSGG 288
Cdd:NF038329 114 KGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPG 153
 
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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