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Conserved domains on  [gi|71994252|ref|NP_499889|]
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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
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 9-61 3.14e-14

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: 65.95  E-value: 3.14e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 71994252      9 TSTIVGSVVSTFAVLTVIIGLPLMHNHVQKVTTLMLTEVELCKTESQDIWKQM 61
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 93-287 2.60e-13

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: 69.93  E-value: 2.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994252   93 QGSPGPRGQPGDDGEPGRDGFPGREGDNGIAGKYLPAPPPGTNACQ-KCPTGAPGPPGLPGPKGPRGPAGIEGKPGRLGE 171
Cdd:NF038329 167 QGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAgPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGE 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994252  172 DNRPGPPGPPGVRGEPGSPGEKGPTGDRGKVLNGAPPGPTGPPGKVGPRGLSGGKGHDGKPGLGGQPGVRgavGARGDAG 251
Cdd:NF038329 247 DGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKD---GKDGQPG 323

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 71994252  252 NPGLPGPQGPKGEPGNPgtchhcqnrAPAPSEAPGK 287
Cdd:NF038329 324 KDGLPGKDGKDGQPGKP---------APKTPEVPQK 350
 
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 ...
 9-61 3.14e-14

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: 65.95  E-value: 3.14e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 71994252      9 TSTIVGSVVSTFAVLTVIIGLPLMHNHVQKVTTLMLTEVELCKTESQDIWKQM 61
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 12-61 3.71e-14

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: 65.56  E-value: 3.71e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 71994252    12 IVGSVVSTFAVLTVIIGLPLMHNHVQKVTTLMLTEVELCKTESQDIWKQM 61
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 93-287 2.60e-13

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: 69.93  E-value: 2.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994252   93 QGSPGPRGQPGDDGEPGRDGFPGREGDNGIAGKYLPAPPPGTNACQ-KCPTGAPGPPGLPGPKGPRGPAGIEGKPGRLGE 171
Cdd:NF038329 167 QGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAgPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGE 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994252  172 DNRPGPPGPPGVRGEPGSPGEKGPTGDRGKVLNGAPPGPTGPPGKVGPRGLSGGKGHDGKPGLGGQPGVRgavGARGDAG 251
Cdd:NF038329 247 DGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKD---GKDGQPG 323

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 71994252  252 NPGLPGPQGPKGEPGNPgtchhcqnrAPAPSEAPGK 287
Cdd:NF038329 324 KDGLPGKDGKDGQPGKP---------APKTPEVPQK 350
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 97-269 4.93e-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: 56.84  E-value: 4.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994252   97 GPRGQPGDDGEPGRDGFPGREGDNGIAGKYLPAPPPGTNACQkcptgapgppglpgpkgprgpagieGKPGRLGEDNRPG 176
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGER-------------------------GEKGPAGPQGEAG 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994252  177 PPGPPGVRGEPGSPGEKGPTGDRGKVLNGAPPGPTGPPGKVGPRGLSGGKGHDGKPGLGGQ--------PGVRGAVGARG 248
Cdd:NF038329 172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpdgdPGPTGEDGPQG 251

                        170       180
                 ....*....|....*....|.
gi 71994252  249 DAGNPGLPGPQGPKGEPGNPG 269
Cdd:NF038329 252 PDGPAGKDGPRGDRGEAGPDG 272
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 157-290 1.23e-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: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 43.36  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994252  157 RGPAGIEGKPGRLGEDNRPGPPGPPGVRGEPGSPGEKGPTGDRGkvlngappgptgPPGKVGPRGLSGGKGHDGKPGLGG 236
Cdd:NF038329 131 AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG------------PAGKDGEAGAKGPAGEKGPQGPRG 198

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 71994252  237 QPGVRGAVGARGDAGNPGLPGPQGPKGEPGNPGTCHHCQNRAPAPSEAPGKAPP 290
Cdd:NF038329 199 ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGP 252
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 220-265 7.18e-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: 37.09  E-value: 7.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 71994252   220 RGLSGGKGHDGKPGLGGQPGVRGAVGARGDAGNPGLPGPQGPKGEP 265
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 222-309 7.45e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 41.20  E-value: 7.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994252  222 LSGGKGHDGKPGLGGQPGvrgavGARGDAGNPGLPGPQGPKG-EPGNPGTCHHCQNRAPAPSEAPgkAPPPPQDYTRPAP 300
Cdd:PRK14959 371 LRPSGGGASAPSGSAAEG-----PASGGAATIPTPGTQGPQGtAPAAGMTPSSAAPATPAPSAAP--SPRVPWDDAPPAP 443


                 ....*....
gi 71994252  301 ESYPSAPNG 309
Cdd:PRK14959 444 PRSGIPPRP 452
 
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 ...
 9-61 3.14e-14

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: 65.95  E-value: 3.14e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 71994252      9 TSTIVGSVVSTFAVLTVIIGLPLMHNHVQKVTTLMLTEVELCKTESQDIWKQM 61
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 12-61 3.71e-14

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: 65.56  E-value: 3.71e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 71994252    12 IVGSVVSTFAVLTVIIGLPLMHNHVQKVTTLMLTEVELCKTESQDIWKQM 61
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 93-287 2.60e-13

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: 69.93  E-value: 2.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994252   93 QGSPGPRGQPGDDGEPGRDGFPGREGDNGIAGKYLPAPPPGTNACQ-KCPTGAPGPPGLPGPKGPRGPAGIEGKPGRLGE 171
Cdd:NF038329 167 QGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAgPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGE 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994252  172 DNRPGPPGPPGVRGEPGSPGEKGPTGDRGKVLNGAPPGPTGPPGKVGPRGLSGGKGHDGKPGLGGQPGVRgavGARGDAG 251
Cdd:NF038329 247 DGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKD---GKDGQPG 323

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 71994252  252 NPGLPGPQGPKGEPGNPgtchhcqnrAPAPSEAPGK 287
Cdd:NF038329 324 KDGLPGKDGKDGQPGKP---------APKTPEVPQK 350
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 97-269 4.93e-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: 56.84  E-value: 4.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994252   97 GPRGQPGDDGEPGRDGFPGREGDNGIAGKYLPAPPPGTNACQkcptgapgppglpgpkgprgpagieGKPGRLGEDNRPG 176
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGER-------------------------GEKGPAGPQGEAG 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994252  177 PPGPPGVRGEPGSPGEKGPTGDRGKVLNGAPPGPTGPPGKVGPRGLSGGKGHDGKPGLGGQ--------PGVRGAVGARG 248
Cdd:NF038329 172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpdgdPGPTGEDGPQG 251

                        170       180
                 ....*....|....*....|.
gi 71994252  249 DAGNPGLPGPQGPKGEPGNPG 269
Cdd:NF038329 252 PDGPAGKDGPRGDRGEAGPDG 272
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 157-290 1.23e-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: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 43.36  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994252  157 RGPAGIEGKPGRLGEDNRPGPPGPPGVRGEPGSPGEKGPTGDRGkvlngappgptgPPGKVGPRGLSGGKGHDGKPGLGG 236
Cdd:NF038329 131 AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG------------PAGKDGEAGAKGPAGEKGPQGPRG 198

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 71994252  237 QPGVRGAVGARGDAGNPGLPGPQGPKGEPGNPGTCHHCQNRAPAPSEAPGKAPP 290
Cdd:NF038329 199 ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGP 252
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 220-265 7.18e-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: 37.09  E-value: 7.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 71994252   220 RGLSGGKGHDGKPGLGGQPGVRGAVGARGDAGNPGLPGPQGPKGEP 265
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 222-309 7.45e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 41.20  E-value: 7.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994252  222 LSGGKGHDGKPGLGGQPGvrgavGARGDAGNPGLPGPQGPKG-EPGNPGTCHHCQNRAPAPSEAPgkAPPPPQDYTRPAP 300
Cdd:PRK14959 371 LRPSGGGASAPSGSAAEG-----PASGGAATIPTPGTQGPQGtAPAAGMTPSSAAPATPAPSAAP--SPRVPWDDAPPAP 443


                 ....*....
gi 71994252  301 ESYPSAPNG 309
Cdd:PRK14959 444 PRSGIPPRP 452
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 230-269 6.65e-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: 6.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 71994252   230 GKPGLGGQPGVRGAVGARGDAGNPGLPGPQGPKGEPGNPG 269
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPG 40
 
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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