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Conserved domains on  [gi|17553572|ref|NP_498086|]
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Cuticle collagen dpy-17 [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
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 154-331 3.14e-27

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: 111.15  E-value: 3.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  154 PAGPAGPKGTPGHDGPDGIPGVPGVDGEDADDAKAQTqqydgcfTCPAGPQGPPGSQGKPGARGMRGARGQaamPGRDGS 233
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE-------KGPAGPQGEAGPQGPAGKDGEAGAKGP---AGEKGP 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  234 PGMPGSLGPIGPPGAAGEEGPTGEPGADVEHQIGLPGAKGTPGAPGESGDQGEQGDRGATGIAGPPGERGPQGEKGDDGP 313
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                        170
                 ....*....|....*...
gi 17553572  314 NGAAGSPGEEGEPGQDAQ 331
Cdd:NF038329 274 DGKDGERGPVGPAGKDGQ 291
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 4-56 3.32e-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: 57.86  E-value: 3.32e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17553572      4 FAGYAACTLGAVSMLLCVSLVPQVYQQVSMLRDELTTEMEAWRLESDQIYMDM 56
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 154-331 3.14e-27

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: 111.15  E-value: 3.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  154 PAGPAGPKGTPGHDGPDGIPGVPGVDGEDADDAKAQTqqydgcfTCPAGPQGPPGSQGKPGARGMRGARGQaamPGRDGS 233
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE-------KGPAGPQGEAGPQGPAGKDGEAGAKGP---AGEKGP 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  234 PGMPGSLGPIGPPGAAGEEGPTGEPGADVEHQIGLPGAKGTPGAPGESGDQGEQGDRGATGIAGPPGERGPQGEKGDDGP 313
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                        170
                 ....*....|....*...
gi 17553572  314 NGAAGSPGEEGEPGQDAQ 331
Cdd:NF038329 274 DGKDGERGPVGPAGKDGQ 291
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 154-331 3.40e-24

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: 102.68  E-value: 3.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  154 PAGPAGPKGTPGHDGPDGIPGVPGVDGEDADDAKAQTQQYDGCfTCPAGPQGPPGSQGKPGARGMRGARGQaamPGRDGS 233
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGP-QGPAGKDGEAGAKGPAGEKGPQGPRGE---TGPAGE 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  234 PGMPGSLGPIGPPGAAGEEGPTGEPGADVEHQIGLPGAKGTPGAPGESGDQGEQGDRGATGIAGPPGERGPQGEKGDDGP 313
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285

                        170
                 ....*....|....*...
gi 17553572  314 NGAAGSPGEEGEPGQDAQ 331
Cdd:NF038329 286 AGKDGQNGKDGLPGKDGK 303
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 154-341 1.78e-16

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: 79.95  E-value: 1.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  154 PAGPAGPKGTPGHDGPDGIPGVPGvDGEDADDAKAQTQQYDGcftcPAGPQGPPGSQGKPGARGMRGARGQAAMPGRDGS 233
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDG----PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  234 PGMPGSLGPIGPPGAAGEEGPTGEPGADvehqiglpgakGTPGAPGESGDQGEQGDRGATGIAGPPGERGPQGEKGDDGP 313
Cdd:NF038329 283 VGPAGKDGQNGKDGLPGKDGKDGQNGKD-----------GLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKP 351

                        170       180
                 ....*....|....*....|....*...
gi 17553572  314 NGAAGSPGEEGEPGQDAQYCPCPQRNTN 341
Cdd:NF038329 352 DTAPHTPKTPQIPGQSKDVTPAPQNPSN 379
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 229-334 1.85e-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: 71.09  E-value: 1.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  229 GRDGSPGMPGSLGPIGPPGAAGEEGPTGEPGADVEH-QIGLPGAKGTPGAPGESGDQGEQGDRGATGIAGPPGERGPQGE 307
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPgPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100
                 ....*....|....*....|....*..
gi 17553572  308 KGDDGPNGAAGSPGEEGEPGQDAQYCP 334
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGE 223
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 235-338 4.57e-12

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: 66.85  E-value: 4.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  235 GMPGSLGPIGPPGAAGEEGPTGEPGAdvehqiglpgakgtPGAPGESGDQGEQGDRGATGIAGPPGERGPQGEKGDDGPN 314
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGE--------------TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                         90       100
                 ....*....|....*....|....
gi 17553572  315 GAAGSPGEEGEPGQDAQYCPCPQR 338
Cdd:NF038329 183 GAKGPAGEKGPQGPRGETGPAGEQ 206
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 4-56 3.32e-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: 57.86  E-value: 3.32e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17553572      4 FAGYAACTLGAVSMLLCVSLVPQVYQQVSMLRDELTTEMEAWRLESDQIYMDM 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 ...
 7-56 3.90e-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, 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: 57.47  E-value: 3.90e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 17553572     7 YAACTLGAVSMLLCVSLVPQVYQQVSMLRDELTTEMEAWRLESDQIYMDM 56
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 276-327 8.13e-07

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: 45.56  E-value: 8.13e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17553572   276 GAPGESGDQGEQGDRGATGIAGPPGERGPQGEKGDDGPNGAAGSPGEEGEPG 327
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
PHA03169 PHA03169
hypothetical protein; Provisional
 204-329 6.34e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.66  E-value: 6.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  204 QGPPGSQGKPGARGMRGARGQAAMPGRDGspGMPGSLGPIGPPGAAGEEGPTGEPGADVEHQIGLP-GAKGTPGAPGESG 282
Cdd:PHA03169  89 QGGPSGSGSESVGSPTPSPSGSAEELASG--LSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPeSHNPSPNQQPSSF 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17553572  283 DQGEQGD-----RGATGIAGPPGERGPQGEKGDDGPNGAAG--SPGEEGEPGQD 329
Cdd:PHA03169 167 LQPSHEDspeepEPPTSEPEPDSPGPPQSETPTSSPPPQSPpdEPGEPQSPTPQ 220
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 154-331 3.14e-27

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: 111.15  E-value: 3.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  154 PAGPAGPKGTPGHDGPDGIPGVPGVDGEDADDAKAQTqqydgcfTCPAGPQGPPGSQGKPGARGMRGARGQaamPGRDGS 233
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE-------KGPAGPQGEAGPQGPAGKDGEAGAKGP---AGEKGP 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  234 PGMPGSLGPIGPPGAAGEEGPTGEPGADVEHQIGLPGAKGTPGAPGESGDQGEQGDRGATGIAGPPGERGPQGEKGDDGP 313
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                        170
                 ....*....|....*...
gi 17553572  314 NGAAGSPGEEGEPGQDAQ 331
Cdd:NF038329 274 DGKDGERGPVGPAGKDGQ 291
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 154-331 3.40e-24

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: 102.68  E-value: 3.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  154 PAGPAGPKGTPGHDGPDGIPGVPGVDGEDADDAKAQTQQYDGCfTCPAGPQGPPGSQGKPGARGMRGARGQaamPGRDGS 233
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGP-QGPAGKDGEAGAKGPAGEKGPQGPRGE---TGPAGE 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  234 PGMPGSLGPIGPPGAAGEEGPTGEPGADVEHQIGLPGAKGTPGAPGESGDQGEQGDRGATGIAGPPGERGPQGEKGDDGP 313
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285

                        170
                 ....*....|....*...
gi 17553572  314 NGAAGSPGEEGEPGQDAQ 331
Cdd:NF038329 286 AGKDGQNGKDGLPGKDGK 303
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 154-341 1.78e-16

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: 79.95  E-value: 1.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  154 PAGPAGPKGTPGHDGPDGIPGVPGvDGEDADDAKAQTQQYDGcftcPAGPQGPPGSQGKPGARGMRGARGQAAMPGRDGS 233
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDG----PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  234 PGMPGSLGPIGPPGAAGEEGPTGEPGADvehqiglpgakGTPGAPGESGDQGEQGDRGATGIAGPPGERGPQGEKGDDGP 313
Cdd:NF038329 283 VGPAGKDGQNGKDGLPGKDGKDGQNGKD-----------GLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKP 351

                        170       180
                 ....*....|....*....|....*...
gi 17553572  314 NGAAGSPGEEGEPGQDAQYCPCPQRNTN 341
Cdd:NF038329 352 DTAPHTPKTPQIPGQSKDVTPAPQNPSN 379
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 229-334 1.85e-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: 71.09  E-value: 1.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  229 GRDGSPGMPGSLGPIGPPGAAGEEGPTGEPGADVEH-QIGLPGAKGTPGAPGESGDQGEQGDRGATGIAGPPGERGPQGE 307
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPgPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100
                 ....*....|....*....|....*..
gi 17553572  308 KGDDGPNGAAGSPGEEGEPGQDAQYCP 334
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGE 223
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 235-338 4.57e-12

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: 66.85  E-value: 4.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  235 GMPGSLGPIGPPGAAGEEGPTGEPGAdvehqiglpgakgtPGAPGESGDQGEQGDRGATGIAGPPGERGPQGEKGDDGPN 314
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGE--------------TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                         90       100
                 ....*....|....*....|....
gi 17553572  315 GAAGSPGEEGEPGQDAQYCPCPQR 338
Cdd:NF038329 183 GAKGPAGEKGPQGPRGETGPAGEQ 206
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 4-56 3.32e-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: 57.86  E-value: 3.32e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17553572      4 FAGYAACTLGAVSMLLCVSLVPQVYQQVSMLRDELTTEMEAWRLESDQIYMDM 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 ...
 7-56 3.90e-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, 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: 57.47  E-value: 3.90e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 17553572     7 YAACTLGAVSMLLCVSLVPQVYQQVSMLRDELTTEMEAWRLESDQIYMDM 56
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 276-327 8.13e-07

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: 45.56  E-value: 8.13e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17553572   276 GAPGESGDQGEQGDRGATGIAGPPGERGPQGEKGDDGPNGAAGSPGEEGEPG 327
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 270-326 2.54e-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: 44.02  E-value: 2.54e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17553572   270 GAKGTPGAPGESGDQGEQGDRGATGIAGPPGERGPQGEKGDDGPNGAAGSPGEEGEP 326
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 267-322 6.08e-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: 43.25  E-value: 6.08e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17553572   267 GLPGAKGTPGAPGESGDQGEQGDRGATGIAGPPGERGPQGEKGDDGPNGAAGSPGE 322
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03169 PHA03169
hypothetical protein; Provisional
 204-329 6.34e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.66  E-value: 6.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  204 QGPPGSQGKPGARGMRGARGQAAMPGRDGspGMPGSLGPIGPPGAAGEEGPTGEPGADVEHQIGLP-GAKGTPGAPGESG 282
Cdd:PHA03169  89 QGGPSGSGSESVGSPTPSPSGSAEELASG--LSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPeSHNPSPNQQPSSF 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17553572  283 DQGEQGD-----RGATGIAGPPGERGPQGEKGDDGPNGAAG--SPGEEGEPGQD 329
Cdd:PHA03169 167 LQPSHEDspeepEPPTSEPEPDSPGPPQSETPTSSPPPQSPpdEPGEPQSPTPQ 220
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 202-258 2.06e-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: 41.71  E-value: 2.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17553572   202 GPQGPPGSQGKPGARGMRGARGQAAMPGRDGSPGMPGSLGPIGPPGAAGEEGPTGEP 258
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 267-317 6.12e-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: 40.17  E-value: 6.12e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 17553572   267 GLPGAKGTPGAPGESGDQGEQGDRGATGIAGPPGERGPQGEKGDDGPNGAA 317
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 108-269 8.56e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 44.29  E-value: 8.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  108 NTPTLPGVIGVPPSVTGHPGGSPinPDGSPSAGPGDKCNCNTEnscPAGPAGPKGTPGHDGPDGIPGVPGVDGedADDAK 187
Cdd:PRK14959 358 NLAMLPRLMPVESLRPSGGGASA--PSGSAAEGPASGGAATIP---TPGTQGPQGTAPAAGMTPSSAAPATPA--PSAAP 430

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  188 AQTQQYDGCftcpagPQGPPGSQGKPgargmrgaRGQAAMPGRDGSPGMPGSLGpigppGAAGEEGPTGEPGADVEHQIG 267
Cdd:PRK14959 431 SPRVPWDDA------PPAPPRSGIPP--------RPAPRMPEASPVPGAPDSVA-----SASDAPPTLGDPSDTAEHTPS 491


                 ..
gi 17553572  268 LP 269
Cdd:PRK14959 492 GP 493
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 101-324 8.59e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 8.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  101 PGNTGSSNTPTLPGVIGVPPSVTGHPGGSPINPDGSPSAGPGDkcncNTENSCPAGPAGPKGTPGHDGPDGIPGVPGVDG 180
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGA----AAAPAEASAAPAPGVAAPEHHPKHVAVPDASDG 665

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  181 EDADDAKAQTQQydgcftcPAGPQGPPGSQGKPGARGMRGARGQAAMPGRDGSPGMPGSLGPigPPGAAGEEGPTGEPGA 260
Cdd:PRK07764 666 GDGWPAKAGGAA-------PAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQ--PPQAAQGASAPSPAAD 736

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17553572  261 DvehQIGLPGAKGTPGAPGESGDQGEQGDRGATgiAGPPGERGPQGEKGDDG--PNGAAGSPGEEG 324
Cdd:PRK07764 737 D---PVPLPPEPDDPPDPAGAPAQPPPPPAPAP--AAAPAAAPPPSPPSEEEemAEDDAPSMDDED 797
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 200-251 1.06e-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: 39.40  E-value: 1.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17553572   200 PAGPQGPPGSQGKPGARGMRGARGQAAMPGRDGSPGMPGSLGPIGPPGAAGE 251
Cdd:pfam01391   5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 177-352 1.25e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 43.74  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  177 GVDGEDADDAKAQTQQYDGCFTCPAGPQGPPGSQGKPGARGMRGARGQAAMPGRDGSPGMPGSLGPIGPP-GAAGEEGPT 255
Cdd:PRK12678  63 AAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRErGEAARRGAA 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  256 GEPGADVEHQ-IGLPGAKGTPGAPGESGDQGEQGDRGATGIAGPPGERGPQGEKGDDGPNGAAGSPGEEGEPGQDAQYCP 334
Cdd:PRK12678 143 RKAGEGGEQPaTEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRD 222

                        170
                 ....*....|....*...
gi 17553572  335 CPQRNTNAAVSGNQGYRN 352
Cdd:PRK12678 223 GGDRRGRRRRRDRRDARG 240
PHA03169 PHA03169
hypothetical protein; Provisional
 209-329 2.23e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.65  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  209 SQGKPGARGMRGARGQAAMPGRDGSPGMPGslgpiGPPGAAGEEGPTGEPGadvEHQIGLPGAKGTPGAPGESGDQGEQG 288
Cdd:PHA03169  88 GQGGPSGSGSESVGSPTPSPSGSAEELASG-----LSPENTSGSSPESPAS---HSPPPSPPSHPGPHEPAPPESHNPSP 159

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 17553572  289 DRGATGIAGPPGERGPQ------GEKGDDGPNGAAGSPGEEGEPGQD 329
Cdd:PHA03169 160 NQQPSSFLQPSHEDSPEepepptSEPEPDSPGPPQSETPTSSPPPQS 206
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 200-249 3.78e-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: 3.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 17553572   200 PAGPQGPPGSQGKPGARGMRGARGQAAMPGRDGSPGMPGSLGPIGPPGAA 249
Cdd:pfam01391   8 PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 197-346 4.55e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 4.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  197 FTCPAGPQGPPGSQGKPGARGMRGARGQAAMPGRDGSPGMPGSLGPIGPPGAAGEEGPTGEPGADVEHQIGLPGAKGTPG 276
Cdd:PRK07764 584 VEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAS 663

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17553572  277 APGeSGDQGEQGDRGATGIAGPPGERGPQGEKGDDGPNGAAGSPGEE-GEPGQDAQYCPCPQRNTNAAVSG 346
Cdd:PRK07764 664 DGG-DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPpAGQADDPAAQPPQAAQGASAPSP 733
PHA03169 PHA03169
hypothetical protein; Provisional
 165-337 6.89e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.11  E-value: 6.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  165 GHDGPDGIPGVPGVDGEDADDAKAQTQQYDGCFTCPAGPQGPPGSQGKPGArgmrGARGQAAMPGRDGSPGMPGSLGPIG 244
Cdd:PHA03169  90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSP----PSHPGPHEPAPPESHNPSPNQQPSS 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572  245 PPGAAGEEGPTGEPGADVEHQIGLPGAKGTPgAPGESGDQGEQGDRGATGiAGPPGERGPQGEKGDDGPNGAAGSPGEEG 324
Cdd:PHA03169 166 FLQPSHEDSPEEPEPPTSEPEPDSPGPPQSE-TPTSSPPPQSPPDEPGEP-QSPTPQQAPSPNTQQAVEHEDEPTEPERE 243

                        170
                 ....*....|...
gi 17553572  325 EPGQDAQYCPCPQ 337
Cdd:PHA03169 244 GPPFPGHRSHSYT 256
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 111-333 1.00e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 41.15  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572   111 TLPGVIGVPPSVTGHPGGsPINPDGSPSAGPGDKCNCNTENSCPAGPAGPKGTPGhdgPDGIPGVPGVDGEDADDAKAQT 190
Cdd:pfam09606  88 NLAGQGTRPQMMGPMGPG-PGGPMGQQMGGPGTASNLLASLGRPQMPMGGAGFPS---QMSRVGRMQPGGQAGGMMQPSS 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553572   191 QQYDGCFTCPAGPQGPPGSQGKPGARGMRGARGQAAMPGRDGSPGMPGSLGPIGPPGAA--GEEGPTGEPGADVEHQIGL 268
Cdd:pfam09606 164 GQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQaqANGGMNPQQMGGAPNQVAM 243

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17553572   269 PGAKGTP-------GAPGESGDQGEQGDRGATGIAGPPGERGPQGEK-GDDGPNGAAGSPGEEGEPGQDAQYC 333
Cdd:pfam09606 244 QQQQPQQqgqqsqlGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQpGAMPNVMSIGDQNNYQQQQTRQQQQ 316
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 241-302 1.04e-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: 36.70  E-value: 1.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17553572   241 GPIGPPGAAGEEGPTGEPGADvehqiGLPGAKGTPGAPGESGDQGEQGDRGATGIAGPPGER 302
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPP-----GPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 228-286 1.27e-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: 36.70  E-value: 1.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 17553572   228 PGRDGSPGMPGSLGPIGPPGAAGEEGPTGEPGADvehqiGLPGAKGTPGAPGESGDQGE 286
Cdd:pfam01391   3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPP-----GPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 285-328 2.01e-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: 35.93  E-value: 2.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 17553572   285 GEQGDRGATGIAGPPGERGPQGEKGDDGPNGAAGSPGEEGEPGQ 328
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGP 44
 
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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