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Conserved domains on  [gi|71989452|ref|NP_001024635|]
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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
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 149-327 1.28e-21

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: 94.97  E-value: 1.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989452  149 QQGPVGPAGPPGDDGLDGIDGKSGVDGPPGrdgillpplgqapepciicPPGQTGPPGFPGQKGPNGPRGSPGLQGQDGK 228
Cdd:NF038329 118 EKGEPGPAGPAGPAGEQGPRGDRGETGPAG-------------------PAGPPGPQGERGEKGPAGPQGEAGPQGPAGK 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989452  229 KGEQGMPGPQGPTGRPGRPGPKGPKGEDGRVIMVAGPAGPAGPPGLPGTPGK-RGARGMDGLPGPQGAPGQQGDSGLSGP 307
Cdd:NF038329 179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgDGQQGPDGDPGPTGEDGPQGPDGPAGK 258

                        170       180
                 ....*....|....*....|
gi 71989452  308 DGKEGARGERGPQGPQGLKG 327
Cdd:NF038329 259 DGPRGDRGEAGPDGPDGKDG 278
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 19-69 1.65e-18

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: 77.89  E-value: 1.65e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 71989452     19 AFLSVAISTFVVFCSVVMLPLIYNYVQTLQTHMLNEMDFCRTKSRDLWVEV 69
Cdd:smart01088   3 AYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 149-327 1.28e-21

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: 94.97  E-value: 1.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989452  149 QQGPVGPAGPPGDDGLDGIDGKSGVDGPPGrdgillpplgqapepciicPPGQTGPPGFPGQKGPNGPRGSPGLQGQDGK 228
Cdd:NF038329 118 EKGEPGPAGPAGPAGEQGPRGDRGETGPAG-------------------PAGPPGPQGERGEKGPAGPQGEAGPQGPAGK 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989452  229 KGEQGMPGPQGPTGRPGRPGPKGPKGEDGRVIMVAGPAGPAGPPGLPGTPGK-RGARGMDGLPGPQGAPGQQGDSGLSGP 307
Cdd:NF038329 179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgDGQQGPDGDPGPTGEDGPQGPDGPAGK 258

                        170       180
                 ....*....|....*....|
gi 71989452  308 DGKEGARGERGPQGPQGLKG 327
Cdd:NF038329 259 DGPRGDRGEAGPDGPDGKDG 278
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 170-327 1.74e-21

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: 94.59  E-value: 1.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989452  170 KSGVDGPPGRDGillpPLGQAPEPCIICPPGQTGPPGFPGQKGPNGPRGSPGL-----QGQDGKKGEQGMPGPQGPTGRP 244
Cdd:NF038329 181 EAGAKGPAGEKG----PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPTGEDGPQGPDGPA 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989452  245 GRPGPKGPKGEDGRvimvAGPAGPAGPPGLPGTPGKRGARGMDGLPGPQGAPGQQGDSGLSGPDGKEGARGERGPQGPQG 324
Cdd:NF038329 257 GKDGPRGDRGEAGP----DGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332


                 ...
gi 71989452  325 LKG 327
Cdd:NF038329 333 KDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 170-323 2.08e-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: 2.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989452  170 KSGVDGPPGRDGILLPPLGQAPE-PCIICPPGQTGPPGFPGQKGPNGPRGSPGLQGQDGKKGEQGMPGPQGPTGRPGRPG 248
Cdd:NF038329 205 EQGPAGPAGPDGEAGPAGEDGPAgPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVG 284

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71989452  249 PKGPKGEDGRVimvagpagpagppGLPGTPGKRGARGMDGLPGPQGAPGQQGDSGLSGPDGKEGARGERGPQGPQ 323
Cdd:NF038329 285 PAGKDGQNGKD-------------GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPE 346
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 19-69 1.65e-18

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: 77.89  E-value: 1.65e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 71989452     19 AFLSVAISTFVVFCSVVMLPLIYNYVQTLQTHMLNEMDFCRTKSRDLWVEV 69
Cdd:smart01088   3 AYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 20-69 1.08e-16

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: 72.88  E-value: 1.08e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 71989452    20 FLSVAISTFVVFCSVVMLPLIYNYVQTLQTHMLNEMDFCRTKSRDLWVEV 69
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 203-327 2.20e-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: 79.56  E-value: 2.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989452  203 GPPGFPGQKGPNGPRGSPGLQGQDGKKGEQGMPGPQGPTGRPGRPGPKGPKGEdgrvimvagpagpAGPPGLPGTPGKRG 282
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE-------------AGPQGPAGKDGEAG 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 71989452  283 ARGMDGLPGPQGAPGQQGDSGLSGPDGKEGARGERGPQGPQGLKG 327
Cdd:NF038329 184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG 228
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 226-327 2.97e-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: 70.32  E-value: 2.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989452  226 DGKKGEQGMPGPQGPTGRPGRPGPKGPKGEDGRVimvagpagpagppglpgtpGKRGARGMDGLPGPQGAPGQQGDSGLS 305
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPA-------------------GPPGPQGERGEKGPAGPQGEAGPQGPA 176

                         90       100
                 ....*....|....*....|..
gi 71989452  306 GPDGKEGARGERGPQGPQGLKG 327
Cdd:NF038329 177 GKDGEAGAKGPAGEKGPQGPRG 198
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 203-257 2.00e-08

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: 50.18  E-value: 2.00e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 71989452   203 GPPGFPGQKGPNGPRGSPGLQGQDGKKGEQGMPGPQGPTGRPGRPGPKGPKGEDG 257
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
172-322 7.96e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 41.17  E-value: 7.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989452 172 GVDGPPGRDGILLPPLGQAPEPCIICPPGQTGPPGFPGQKGPNGPRGSPGlQGQDGKKGEQGMPGPQGPTGRPGRPGPKG 251
Cdd:COG5164 132 GSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVK 210

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71989452 252 PKGEDGrvimvagpagpaGPPGLPGTPGKRGARGMDGLPGPQGAPGQQGDSGLSGPDGKEGARGERGPQGP 322
Cdd:COG5164 211 KDDKNG------------KGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTALEAENRAANP 269
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 149-327 1.28e-21

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: 94.97  E-value: 1.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989452  149 QQGPVGPAGPPGDDGLDGIDGKSGVDGPPGrdgillpplgqapepciicPPGQTGPPGFPGQKGPNGPRGSPGLQGQDGK 228
Cdd:NF038329 118 EKGEPGPAGPAGPAGEQGPRGDRGETGPAG-------------------PAGPPGPQGERGEKGPAGPQGEAGPQGPAGK 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989452  229 KGEQGMPGPQGPTGRPGRPGPKGPKGEDGRVIMVAGPAGPAGPPGLPGTPGK-RGARGMDGLPGPQGAPGQQGDSGLSGP 307
Cdd:NF038329 179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgDGQQGPDGDPGPTGEDGPQGPDGPAGK 258

                        170       180
                 ....*....|....*....|
gi 71989452  308 DGKEGARGERGPQGPQGLKG 327
Cdd:NF038329 259 DGPRGDRGEAGPDGPDGKDG 278
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 170-327 1.74e-21

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: 94.59  E-value: 1.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989452  170 KSGVDGPPGRDGillpPLGQAPEPCIICPPGQTGPPGFPGQKGPNGPRGSPGL-----QGQDGKKGEQGMPGPQGPTGRP 244
Cdd:NF038329 181 EAGAKGPAGEKG----PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPTGEDGPQGPDGPA 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989452  245 GRPGPKGPKGEDGRvimvAGPAGPAGPPGLPGTPGKRGARGMDGLPGPQGAPGQQGDSGLSGPDGKEGARGERGPQGPQG 324
Cdd:NF038329 257 GKDGPRGDRGEAGP----DGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332


                 ...
gi 71989452  325 LKG 327
Cdd:NF038329 333 KDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 170-323 2.08e-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: 2.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989452  170 KSGVDGPPGRDGILLPPLGQAPE-PCIICPPGQTGPPGFPGQKGPNGPRGSPGLQGQDGKKGEQGMPGPQGPTGRPGRPG 248
Cdd:NF038329 205 EQGPAGPAGPDGEAGPAGEDGPAgPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVG 284

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71989452  249 PKGPKGEDGRVimvagpagpagppGLPGTPGKRGARGMDGLPGPQGAPGQQGDSGLSGPDGKEGARGERGPQGPQ 323
Cdd:NF038329 285 PAGKDGQNGKD-------------GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPE 346
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 19-69 1.65e-18

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: 77.89  E-value: 1.65e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 71989452     19 AFLSVAISTFVVFCSVVMLPLIYNYVQTLQTHMLNEMDFCRTKSRDLWVEV 69
Cdd:smart01088   3 AYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 20-69 1.08e-16

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: 72.88  E-value: 1.08e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 71989452    20 FLSVAISTFVVFCSVVMLPLIYNYVQTLQTHMLNEMDFCRTKSRDLWVEV 69
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 203-327 2.20e-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: 79.56  E-value: 2.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989452  203 GPPGFPGQKGPNGPRGSPGLQGQDGKKGEQGMPGPQGPTGRPGRPGPKGPKGEdgrvimvagpagpAGPPGLPGTPGKRG 282
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE-------------AGPQGPAGKDGEAG 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 71989452  283 ARGMDGLPGPQGAPGQQGDSGLSGPDGKEGARGERGPQGPQGLKG 327
Cdd:NF038329 184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG 228
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 226-327 2.97e-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: 70.32  E-value: 2.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989452  226 DGKKGEQGMPGPQGPTGRPGRPGPKGPKGEDGRVimvagpagpagppglpgtpGKRGARGMDGLPGPQGAPGQQGDSGLS 305
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPA-------------------GPPGPQGERGEKGPAGPQGEAGPQGPA 176

                         90       100
                 ....*....|....*....|..
gi 71989452  306 GPDGKEGARGERGPQGPQGLKG 327
Cdd:NF038329 177 GKDGEAGAKGPAGEKGPQGPRG 198
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 203-257 2.00e-08

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: 50.18  E-value: 2.00e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 71989452   203 GPPGFPGQKGPNGPRGSPGLQGQDGKKGEQGMPGPQGPTGRPGRPGPKGPKGEDG 257
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 200-255 7.53e-08

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: 48.26  E-value: 7.53e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 71989452   200 GQTGPPGFPGQKGPNGPRGSPGLQGQDGKKGEQGMPGPQGPTGRPGRPGPKGPKGE 255
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 198-249 1.13e-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: 47.87  E-value: 1.13e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 71989452   198 PPGQTGPPGFPGQKGPNGPRGSPGLQGQDGKKGEQGMPGPQGPTGRPGRPGP 249
Cdd:pfam01391   5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 198-252 1.14e-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: 47.87  E-value: 1.14e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 71989452   198 PPGQTGPPGFPGQKGPNGPRGSPGLQGQDGKKGEQGMPGPQGPTGRPGRPGPKGP 252
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
172-322 7.96e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 41.17  E-value: 7.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989452 172 GVDGPPGRDGILLPPLGQAPEPCIICPPGQTGPPGFPGQKGPNGPRGSPGlQGQDGKKGEQGMPGPQGPTGRPGRPGPKG 251
Cdd:COG5164 132 GSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVK 210

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71989452 252 PKGEDGrvimvagpagpaGPPGLPGTPGKRGARGMDGLPGPQGAPGQQGDSGLSGPDGKEGARGERGPQGP 322
Cdd:COG5164 211 KDDKNG------------KGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTALEAENRAANP 269
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 281-327 1.16e-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: 1.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 71989452   281 RGARGMDGLPGPQGAPGQQGDSGLSGPDGKEGARGERGPQGPQGLKG 327
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
157-324 1.85e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 40.01  E-value: 1.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989452 157 GPPGDDGLDGIDGKSGVDGPPGRDGILLPPLGQAPEPciicPPGQTGPPGFPGQKGPNGPRGSPGLQGQDGKKGEQGMPG 236
Cdd:COG5164  37 RPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATG----PAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPD 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989452 237 PQGPTGRPGRPGPKGP--KGEDGRVIMVAGPAGPAGPPGLPGTPGKRGARGMDGLPGPQGAPGQQGDSGLSGP--DGKEG 312
Cdd:COG5164 113 DGGATGPPDDGGSTTPpsGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPpnKGETG 192

                       170
                ....*....|..
gi 71989452 313 ARGERGPQGPQG 324
Cdd:COG5164 193 TDIPTGGTPRQG 204
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 224-300 2.81e-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: 35.55  E-value: 2.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71989452   224 GQDGKKGEQGMPGPQGPTGRPGRPGPKGPKGEDGRvimvagpagpagppglpgtpgkRGARGMDGLPGPQGAPGQQG 300
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGP----------------------PGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 215-258 5.07e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 34.78  E-value: 5.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 71989452   215 GPRGSPGLQGQDGKKGEqgmPGPQGPTGRPGRPGPKGPKGEDGR 258
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGP---PGPPGPPGPPGPPGEPGPPGPPGP 41
 
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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