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Conserved domains on  [gi|148472646|emb|CAN86899|]
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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

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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 ...
 4-56 8.72e-12

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: 59.02  E-value: 8.72e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 148472646     4 LVVSGFAALSGFAILALTIFVPQIYWEMSDLQDQVVGVVESFKVETDSLWIDL 56
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 105-259 2.45e-09

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: 57.61  E-value: 2.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148472646 105 GAPGAPGTPGENGPRGMDNPHSLGSTSCDQQSIGcvqcprgppgPPGDVGSVGQRGPDGASGAPGAASQihgkpglPGPP 184
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG----------PQGEAGPQGPAGKDGEAGAKGPAGE-------KGPQ 194

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148472646 185 GDAGAPGAPGQDGAPGHPGADGQRQRGQPGPPGPPGRPGKVGINGEPGQKGIDGENGSEGIPGVPGPRGAPGQPG 259
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
 
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 ...
 4-56 8.72e-12

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: 59.02  E-value: 8.72e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 148472646     4 LVVSGFAALSGFAILALTIFVPQIYWEMSDLQDQVVGVVESFKVETDSLWIDL 56
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 10-56 4.74e-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: 54.00  E-value: 4.74e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 148472646   10 AALSGFAILALTIFVPQIYWEMSDLQDQVVGVVESFKVETDSLWIDL 56
Cdd:pfam01484   4 VAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 105-259 2.45e-09

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: 57.61  E-value: 2.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148472646 105 GAPGAPGTPGENGPRGMDNPHSLGSTSCDQQSIGcvqcprgppgPPGDVGSVGQRGPDGASGAPGAASQihgkpglPGPP 184
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG----------PQGEAGPQGPAGKDGEAGAKGPAGE-------KGPQ 194

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148472646 185 GDAGAPGAPGQDGAPGHPGADGQRQRGQPGPPGPPGRPGKVGINGEPGQKGIDGENGSEGIPGVPGPRGAPGQPG 259
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 114-275 2.98e-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: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 51.44  E-value: 2.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148472646 114 GENGPRGMDNPHslGSTSCDQQSIGCVQCPRGPPGPPGDVGSVGQRGPDGASGAPGaasqihgkpglpgppgDAGAPGAP 193
Cdd:NF038329 198 GETGPAGEQGPA--GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG----------------PDGPAGKD 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148472646 194 GQDGAPGHPGADGQRQRGQPGPPGppGRPGKVGINGEPGQKGIDGENGSEGIPGVPGPRGAPGQPGtigVPGGPGIPGRD 273
Cdd:NF038329 260 GPRGDRGEAGPDGPDGKDGERGPV--GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG---KDGLPGKDGKD 334


                 ..
gi 148472646 274 GQ 275
Cdd:NF038329 335 GQ 336
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 113-259 5.65e-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: 47.21  E-value: 5.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148472646 113 PGENGPRGMDNPHSLGSTSCDQQSIGCVQcPRGPPGPPGDVGSVGQRGPDGASGAPGAASQIHGKPGLPGPPGD-----A 187
Cdd:NF038329 134 QGPRGDRGETGPAGPAGPPGPQGERGEKG-PAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQgpagpA 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148472646 188 GAPGAPGQDGAPGHPGADGQRQ---------RGQPGPPGPPGRPGKVGINGEPGQKGIDGENGSEGIPGVPGPRGAPGQP 258
Cdd:NF038329 213 GPDGEAGPAGEDGPAGPAGDGQqgpdgdpgpTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN 292


                 .
gi 148472646 259 G 259
Cdd:NF038329 293 G 293
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 191-259 5.19e-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: 5.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148472646  191 GAPGQDGAPGHPGAdgqrqrgqpgppgpPGRPGKVGINGEPGQKGIDGENGSEGIPGVPGPRGAPGQPG 259
Cdd:pfam01391   1 GPPGPPGPPGPPGP--------------PGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
 
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 ...
 4-56 8.72e-12

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: 59.02  E-value: 8.72e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 148472646     4 LVVSGFAALSGFAILALTIFVPQIYWEMSDLQDQVVGVVESFKVETDSLWIDL 56
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 10-56 4.74e-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: 54.00  E-value: 4.74e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 148472646   10 AALSGFAILALTIFVPQIYWEMSDLQDQVVGVVESFKVETDSLWIDL 56
Cdd:pfam01484   4 VAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 105-259 2.45e-09

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: 57.61  E-value: 2.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148472646 105 GAPGAPGTPGENGPRGMDNPHSLGSTSCDQQSIGcvqcprgppgPPGDVGSVGQRGPDGASGAPGAASQihgkpglPGPP 184
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG----------PQGEAGPQGPAGKDGEAGAKGPAGE-------KGPQ 194

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148472646 185 GDAGAPGAPGQDGAPGHPGADGQRQRGQPGPPGPPGRPGKVGINGEPGQKGIDGENGSEGIPGVPGPRGAPGQPG 259
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 114-275 2.98e-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: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 51.44  E-value: 2.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148472646 114 GENGPRGMDNPHslGSTSCDQQSIGCVQCPRGPPGPPGDVGSVGQRGPDGASGAPGaasqihgkpglpgppgDAGAPGAP 193
Cdd:NF038329 198 GETGPAGEQGPA--GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG----------------PDGPAGKD 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148472646 194 GQDGAPGHPGADGQRQRGQPGPPGppGRPGKVGINGEPGQKGIDGENGSEGIPGVPGPRGAPGQPGtigVPGGPGIPGRD 273
Cdd:NF038329 260 GPRGDRGEAGPDGPDGKDGERGPV--GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG---KDGLPGKDGKD 334


                 ..
gi 148472646 274 GQ 275
Cdd:NF038329 335 GQ 336
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 113-259 5.65e-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: 47.21  E-value: 5.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148472646 113 PGENGPRGMDNPHSLGSTSCDQQSIGCVQcPRGPPGPPGDVGSVGQRGPDGASGAPGAASQIHGKPGLPGPPGD-----A 187
Cdd:NF038329 134 QGPRGDRGETGPAGPAGPPGPQGERGEKG-PAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQgpagpA 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148472646 188 GAPGAPGQDGAPGHPGADGQRQ---------RGQPGPPGPPGRPGKVGINGEPGQKGIDGENGSEGIPGVPGPRGAPGQP 258
Cdd:NF038329 213 GPDGEAGPAGEDGPAGPAGDGQqgpdgdpgpTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN 292


                 .
gi 148472646 259 G 259
Cdd:NF038329 293 G 293
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 191-259 5.19e-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: 5.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148472646  191 GAPGQDGAPGHPGAdgqrqrgqpgppgpPGRPGKVGINGEPGQKGIDGENGSEGIPGVPGPRGAPGQPG 259
Cdd:pfam01391   1 GPPGPPGPPGPPGP--------------PGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
 
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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