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Conserved domains on  [gi|17550712|ref|NP_510630|]
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Col_cuticle_N domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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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 ...
 168-285 5.58e-10

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: 59.92  E-value: 5.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550712  168 GDDGEPGAPGRRGLSGTfltgikklrgppgepgepgrpgtPGTPGNDGKDGRNGyrlrpdkiTRGPPGPMGARGEPGHRG 247
Cdd:NF038329 263 GDRGEAGPDGPDGKDGE-----------------------RGPVGPAGKDGQNG--------KDGLPGKDGKDGQNGKDG 311

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 17550712  248 LPGDNGMPgpmgppgyrGDNGRRGAPGLPGRTGRHGKP 285
Cdd:NF038329 312 LPGKDGKD---------GQPGKDGLPGKDGKDGQPGKP 340
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 168-285 5.58e-10

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: 59.92  E-value: 5.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550712  168 GDDGEPGAPGRRGLSGTfltgikklrgppgepgepgrpgtPGTPGNDGKDGRNGyrlrpdkiTRGPPGPMGARGEPGHRG 247
Cdd:NF038329 263 GDRGEAGPDGPDGKDGE-----------------------RGPVGPAGKDGQNG--------KDGLPGKDGKDGQNGKDG 311

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 17550712  248 LPGDNGMPgpmgppgyrGDNGRRGAPGLPGRTGRHGKP 285
Cdd:NF038329 312 LPGKDGKD---------GQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 168-288 1.63e-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: 58.38  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550712  168 GDDGEPGAPGRRGLSGTFLTGIKKLRGPPGEPGEPGRPGTPGTPGNDGKDGRNGYRLRPDKI----TRGPPGPMGARGEP 243
Cdd:NF038329 213 GPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDgkdgERGPVGPAGKDGQN 292

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 17550712  244 GHRGLPGDNgmpgpmgppgyrGDNGRRGAPGLPGRTGRHGKPGGD 288
Cdd:NF038329 293 GKDGLPGKD------------GKDGQNGKDGLPGKDGKDGQPGKD 325
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 121-286 1.20e-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: 49.52  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550712  121 GEPGPSGLPGRRGINNYETLPLKKCIWRERLAciMCPRGPPGRRGRMGDDGEPGAPGRRGLSGTflTGIKKLRGPPGEPG 200
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGP--AGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--QGPRGETGPAGEQG 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550712  201 EPGRPGTPGTPGNDGKDGRNGYRLRPDKITRGPPGPMGARGEPGHRGLPGD---NGMPGPMGPPGYRGDNGRRGAPGLPG 277
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKdgpRGDRGEAGPDGPDGKDGERGPVGPAG 287


                 ....*....
gi 17550712  278 RTGRHGKPG 286
Cdd:NF038329 288 KDGQNGKDG 296
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 231-286 3.38e-06

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: 43.64  E-value: 3.38e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17550712   231 RGPPGPMGARGEPGHRGLPGDNgmpgpmgppGYRGDNGRRGAPGLPGRTGRHGKPG 286
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPP---------GPPGEPGPPGPPGPPGPPGPPGAPG 52
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 208-296 4.30e-05

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: 44.90  E-value: 4.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550712  208 PGTPGNDGKDGRNGYR-LRPDKITRGPPGPMGARGEPGHRGLPGDNGMPGPMGPPGYRGDNGRRGAPGLPGRTGRHGKPG 286
Cdd:NF038329 122 PGPAGPAGPAGEQGPRgDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                         90
                 ....*....|
gi 17550712  287 GDSSYCPCPP 296
Cdd:NF038329 202 PAGEQGPAGP 211
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 168-285 5.58e-10

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: 59.92  E-value: 5.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550712  168 GDDGEPGAPGRRGLSGTfltgikklrgppgepgepgrpgtPGTPGNDGKDGRNGyrlrpdkiTRGPPGPMGARGEPGHRG 247
Cdd:NF038329 263 GDRGEAGPDGPDGKDGE-----------------------RGPVGPAGKDGQNG--------KDGLPGKDGKDGQNGKDG 311

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 17550712  248 LPGDNGMPgpmgppgyrGDNGRRGAPGLPGRTGRHGKP 285
Cdd:NF038329 312 LPGKDGKD---------GQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 168-288 1.63e-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: 58.38  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550712  168 GDDGEPGAPGRRGLSGTFLTGIKKLRGPPGEPGEPGRPGTPGTPGNDGKDGRNGYRLRPDKI----TRGPPGPMGARGEP 243
Cdd:NF038329 213 GPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDgkdgERGPVGPAGKDGQN 292

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 17550712  244 GHRGLPGDNgmpgpmgppgyrGDNGRRGAPGLPGRTGRHGKPGGD 288
Cdd:NF038329 293 GKDGLPGKD------------GKDGQNGKDGLPGKDGKDGQPGKD 325
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 121-286 1.20e-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: 49.52  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550712  121 GEPGPSGLPGRRGINNYETLPLKKCIWRERLAciMCPRGPPGRRGRMGDDGEPGAPGRRGLSGTflTGIKKLRGPPGEPG 200
Cdd:NF038329 132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGP--AGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--QGPRGETGPAGEQG 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550712  201 EPGRPGTPGTPGNDGKDGRNGYRLRPDKITRGPPGPMGARGEPGHRGLPGD---NGMPGPMGPPGYRGDNGRRGAPGLPG 277
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKdgpRGDRGEAGPDGPDGKDGERGPVGPAG 287


                 ....*....
gi 17550712  278 RTGRHGKPG 286
Cdd:NF038329 288 KDGQNGKDG 296
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 231-286 3.38e-06

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: 43.64  E-value: 3.38e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17550712   231 RGPPGPMGARGEPGHRGLPGDNgmpgpmgppGYRGDNGRRGAPGLPGRTGRHGKPG 286
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPP---------GPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 232-286 2.85e-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: 2.85e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17550712   232 GPPGPMGARGEPGHRGLPGDNGMPGPMGPPGYRGDNGRRGAPGLPGRTGRHGKPG 286
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 208-296 4.30e-05

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: 44.90  E-value: 4.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550712  208 PGTPGNDGKDGRNGYR-LRPDKITRGPPGPMGARGEPGHRGLPGDNGMPGPMGPPGYRGDNGRRGAPGLPGRTGRHGKPG 286
Cdd:NF038329 122 PGPAGPAGPAGEQGPRgDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                         90
                 ....*....|
gi 17550712  287 GDSSYCPCPP 296
Cdd:NF038329 202 PAGEQGPAGP 211
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 231-286 3.76e-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: 37.86  E-value: 3.76e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17550712   231 RGPPGPMGARGEPGHRGLPGDngmpgpmgppgyRGDNGRRGAPGLPGRTGRHGKPG 286
Cdd:pfam01391   3 PGPPGPPGPPGPPGPPGPPGP------------PGPPGPPGEPGPPGPPGPPGPPG 46
 
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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