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Conserved domains on  [gi|17567621|ref|NP_509162|]
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Nematode cuticle collagen N-terminal domain-containing protein [Caenorhabditis elegans]

Protein Classification

cuticular collagen family protein( domain architecture ID 10661019)

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

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 ...
 22-72 2.27e-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: 58.25  E-value: 2.27e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 17567621     22 AVIGVALSIGAAIVCVMTVPFVYNYVQRVETVLQNEADFCRAKRDSVLKEL 72
Cdd:smart01088   3 AYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 135-163 4.46e-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: 34.78  E-value: 4.46e-03
                          10        20
                  ....*....|....*....|....*....
gi 17567621   135 GSPGEPGSPGQDGHDGVDGRPGSDGNPGA 163
Cdd:pfam01391  16 GPPGPPGPPGPPGPPGEPGPPGPPGPPGP 44
 
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 ...
 22-72 2.27e-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: 58.25  E-value: 2.27e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 17567621     22 AVIGVALSIGAAIVCVMTVPFVYNYVQRVETVLQNEADFCRAKRDSVLKEL 72
Cdd:smart01088   3 AYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 23-72 2.16e-08

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: 49.77  E-value: 2.16e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 17567621    23 VIGVALSIGAAIVCVMTVPFVYNYVQRVETVLQNEADFCRAKRDSVLKEL 72
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 135-163 4.46e-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: 34.78  E-value: 4.46e-03
                          10        20
                  ....*....|....*....|....*....
gi 17567621   135 GSPGEPGSPGQDGHDGVDGRPGSDGNPGA 163
Cdd:pfam01391  16 GPPGPPGPPGPPGPPGEPGPPGPPGPPGP 44
 
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 ...
 22-72 2.27e-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: 58.25  E-value: 2.27e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 17567621     22 AVIGVALSIGAAIVCVMTVPFVYNYVQRVETVLQNEADFCRAKRDSVLKEL 72
Cdd:smart01088   3 AYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 23-72 2.16e-08

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: 49.77  E-value: 2.16e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 17567621    23 VIGVALSIGAAIVCVMTVPFVYNYVQRVETVLQNEADFCRAKRDSVLKEL 72
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 135-163 4.46e-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: 34.78  E-value: 4.46e-03
                          10        20
                  ....*....|....*....|....*....
gi 17567621   135 GSPGEPGSPGQDGHDGVDGRPGSDGNPGA 163
Cdd:pfam01391  16 GPPGPPGPPGPPGPPGEPGPPGPPGPPGP 44
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 135-163 5.53e-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: 34.78  E-value: 5.53e-03
                          10        20
                  ....*....|....*....|....*....
gi 17567621   135 GSPGEPGSPGQDGHDGVDGRPGSDGNPGA 163
Cdd:pfam01391  28 GPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
 
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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