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Conserved domains on  [gi|17505428|ref|NP_492035|]
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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
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 150-279 4.38e-22

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: 95.74  E-value: 4.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505428  150 PVGLPGYPGRDGLPGEPGPNGKPGNPGYRGEDGKPGRPGEPGSSGLPGRPGSDGKPGLPGRDGKKGIGLPGRMGRPGFAG 229
Cdd:NF038329 172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG 251

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 17505428  230 KEGQPGINGKPGRMGLPGPAGPEGKPGYPGMLGRDGIPGEPGLAGGPGPD 279
Cdd:NF038329 252 PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD 301
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 7-58 7.54e-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: 56.71  E-value: 7.54e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 17505428      7 VAAVSTTCSLTAIVSCLVVLYGLFQEMDDIELQVNESIRVFQFETDPAWHDM 58
Cdd:smart01088   2 VAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 150-279 4.38e-22

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: 95.74  E-value: 4.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505428  150 PVGLPGYPGRDGLPGEPGPNGKPGNPGYRGEDGKPGRPGEPGSSGLPGRPGSDGKPGLPGRDGKKGIGLPGRMGRPGFAG 229
Cdd:NF038329 172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG 251

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 17505428  230 KEGQPGINGKPGRMGLPGPAGPEGKPGYPGMLGRDGIPGEPGLAGGPGPD 279
Cdd:NF038329 252 PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD 301
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 150-279 1.44e-19

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: 88.42  E-value: 1.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505428  150 PVGLPGYPGRDGLPGEPGPNGKPGNpGYRGEDGKPGRPGEPGSSGLPGRPGSDGKPGLPGRDGKKG-IGLPGRMGRPGFA 228
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGpDGKDGERGPVGPA 286

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17505428  229 GKEGQPGINGKPGRmglPGPAGPEGKPGYPGMLGRDGIPGEPGLAGGPGPD 279
Cdd:NF038329 287 GKDGQNGKDGLPGK---DGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD 334
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 150-235 4.55e-18

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: 83.80  E-value: 4.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505428  150 PVGLPGYPGRDGLPGEPGPNGKPGNPGYRGEDGKPGRPGEPGSSGLPGRPGSDG---KPGLPGRDGKKgiGLPGRMGRPG 226
Cdd:NF038329 252 PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGqngKDGLPGKDGKD--GQPGKDGLPG 329


                 ....*....
gi 17505428  227 FAGKEGQPG 235
Cdd:NF038329 330 KDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 150-271 1.19e-17

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: 82.65  E-value: 1.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505428  150 PVGLPGYPGRDGLPGEPG--PNGKPGNPGYRGEDGKPGRPGEPGSSGLPGRPGSDGKPGLPGRDGKKG-IGLPGRMGRPG 226
Cdd:NF038329 214 PDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGpVGPAGKDGQNG 293

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 17505428  227 FAGKEGQPGINGKPGRMGLPGPAGPEGKPGYPGMLGRDGIPGEPG 271
Cdd:NF038329 294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 7-58 7.54e-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: 56.71  E-value: 7.54e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 17505428      7 VAAVSTTCSLTAIVSCLVVLYGLFQEMDDIELQVNESIRVFQFETDPAWHDM 58
Cdd:smart01088   2 VAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 10-58 3.37e-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: 54.77  E-value: 3.37e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 17505428    10 VSTTCSLTAIVSCLVVLYGLFQEMDDIELQVNESIRVFQFETDPAWHDM 58
Cdd:pfam01484   2 VAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 155-209 2.23e-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: 47.10  E-value: 2.23e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17505428   155 GYPGRDGLPGEPGPNGKPGNPGYRGEDGKPGRPGEPGSSGLPGRPGSDGKPGLPG 209
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 155-281 4.63e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 38.41  E-value: 4.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505428  155 GYPGRDGLPGEPGPNGKPGNPGYRGEDGKPGRPGEPGSSGLPGRPGSDGKPGLPGRDGKKGiGLPGRMGRpGFAGKEGQP 234
Cdd:PHA03169  96 GSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHN-PSPNQQPS-SFLQPSHED 173

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 17505428  235 GINGKPGRMGLPGPAGPEGKPGYPGMLGRDGI--PGEPGLAGGPGPDAG 281
Cdd:PHA03169 174 SPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQspPDEPGEPQSPTPQQA 222
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 150-279 4.38e-22

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: 95.74  E-value: 4.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505428  150 PVGLPGYPGRDGLPGEPGPNGKPGNPGYRGEDGKPGRPGEPGSSGLPGRPGSDGKPGLPGRDGKKGIGLPGRMGRPGFAG 229
Cdd:NF038329 172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG 251

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 17505428  230 KEGQPGINGKPGRMGLPGPAGPEGKPGYPGMLGRDGIPGEPGLAGGPGPD 279
Cdd:NF038329 252 PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD 301
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 150-279 1.44e-19

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: 88.42  E-value: 1.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505428  150 PVGLPGYPGRDGLPGEPGPNGKPGNpGYRGEDGKPGRPGEPGSSGLPGRPGSDGKPGLPGRDGKKG-IGLPGRMGRPGFA 228
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGpDGKDGERGPVGPA 286

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17505428  229 GKEGQPGINGKPGRmglPGPAGPEGKPGYPGMLGRDGIPGEPGLAGGPGPD 279
Cdd:NF038329 287 GKDGQNGKDGLPGK---DGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD 334
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 150-235 4.55e-18

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: 83.80  E-value: 4.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505428  150 PVGLPGYPGRDGLPGEPGPNGKPGNPGYRGEDGKPGRPGEPGSSGLPGRPGSDG---KPGLPGRDGKKgiGLPGRMGRPG 226
Cdd:NF038329 252 PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGqngKDGLPGKDGKD--GQPGKDGLPG 329


                 ....*....
gi 17505428  227 FAGKEGQPG 235
Cdd:NF038329 330 KDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 150-271 1.19e-17

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: 82.65  E-value: 1.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505428  150 PVGLPGYPGRDGLPGEPG--PNGKPGNPGYRGEDGKPGRPGEPGSSGLPGRPGSDGKPGLPGRDGKKG-IGLPGRMGRPG 226
Cdd:NF038329 214 PDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGpVGPAGKDGQNG 293

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 17505428  227 FAGKEGQPGINGKPGRMGLPGPAGPEGKPGYPGMLGRDGIPGEPG 271
Cdd:NF038329 294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 7-58 7.54e-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: 56.71  E-value: 7.54e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 17505428      7 VAAVSTTCSLTAIVSCLVVLYGLFQEMDDIELQVNESIRVFQFETDPAWHDM 58
Cdd:smart01088   2 VAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 10-58 3.37e-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: 54.77  E-value: 3.37e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 17505428    10 VSTTCSLTAIVSCLVVLYGLFQEMDDIELQVNESIRVFQFETDPAWHDM 58
Cdd:pfam01484   2 VAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 155-209 2.23e-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: 47.10  E-value: 2.23e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17505428   155 GYPGRDGLPGEPGPNGKPGNPGYRGEDGKPGRPGEPGSSGLPGRPGSDGKPGLPG 209
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 150-205 2.54e-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: 46.72  E-value: 2.54e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17505428   150 PVGLPGYPGRDGLPGEPGPNGKPGNPGYRGEDGKPGRPGEPGSSGLPGRPGSDGKP 205
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 161-215 3.45e-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: 46.33  E-value: 3.45e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17505428   161 GLPGEPGPNGKPGNPGYRGEDGKPGRPGEPGSSGLPGRPGSDGKPGLPGRDGKKG 215
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 164-216 1.37e-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: 44.79  E-value: 1.37e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 17505428   164 GEPGPNGKPGNPGYRGEDGKPGRPGEPGSSGLPGRPGSDGKPGLPGRDGKKGI 216
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 158-213 3.65e-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: 3.65e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17505428   158 GRDGLPGEPGPNGKPGNPGYRGEDGKPGRPGEPGSSGLPGRPGSDGKPGLPGRDGK 213
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 217-271 5.63e-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: 5.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17505428   217 GLPGRMGRPGFAGKEGQPGINGKPGRMGLPGPAGPEGKPGYPGMLGRDGIPGEPG 271
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 229-279 3.03e-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: 38.24  E-value: 3.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 17505428   229 GKEGQPGINGKPGRMGLPGPAGPEGKPGYPGMLGRDGIPGEPGLAGGPGPD 279
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 223-278 3.27e-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: 3.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17505428   223 GRPGFAGKEGQPGINGKPGRMGLPGPAGPEGKPGYPGMLGRDGIPGEPGLAGGPGP 278
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Cytadhesin_P30 pfam07271
Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 ...
 154-267 4.86e-04

Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 and P30 proteins. P30 has been found to be membrane associated and localized on the tip organelle. It is thought that it is important in cytadherence and virulence. The N-terminus contains two predicted transmembrane helices followed by a long region of a short 6 residue proline rich repeat.


Pssm-ID: 429374 [Multi-domain]  Cd Length: 275  Bit Score: 41.11  E-value: 4.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505428   154 PGYPGRDGLPGEPGPNGKPGNPGYRGEDGKPGRPGEPGSSGLPGRPG-SDGKPGLPGRDGKKgiGLPGRMG-RPGFAgkE 231
Cdd:pfam07271 163 PNPQQRIGFPMQPNMGMRPGFNQMPGMPPNQMRPGFNQMPGMPPRPGfPNPMPNMQPRPGFR--PQPGPMGnRPGGG--F 238

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 17505428   232 GQPGINGKPGRMGLPGPAGPEG-KPGYPGMLGRDGIP 267
Cdd:pfam07271 239 PHPGTPMGPNRMPNPGMNQRPGmAPPRPGFPPQNGPR 275
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 182-255 1.76e-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: 1.76e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17505428   182 GKPGRPGEPGSSGLPGRPGSDGKPGLPGRdgkkgiglpgrmgrpgfAGKEGQPGINGKPGRMGLPGPAGPEGKP 255
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGP-----------------PGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 155-281 4.63e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 38.41  E-value: 4.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505428  155 GYPGRDGLPGEPGPNGKPGNPGYRGEDGKPGRPGEPGSSGLPGRPGSDGKPGLPGRDGKKGiGLPGRMGRpGFAGKEGQP 234
Cdd:PHA03169  96 GSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHN-PSPNQQPS-SFLQPSHED 173

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 17505428  235 GINGKPGRMGLPGPAGPEGKPGYPGMLGRDGI--PGEPGLAGGPGPDAG 281
Cdd:PHA03169 174 SPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQspPDEPGEPQSPTPQQA 222
 
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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