NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1677420989|emb|VIO99774|]
View 

Cuticle collagen 40, putative [Brugia malayi]

Protein Classification

cuticular collagen family protein( domain architecture ID 18387963)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 22-74 5.85e-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. 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: 70.57  E-value: 5.85e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1677420989   22 RIAFCGVTMSTVATLLCVISVPMFYNYLQQMQSVMIDQIEFCRSRSDHIWREI 74
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 235-285 6.76e-11

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: 56.73  E-value: 6.76e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1677420989 235 PRGPPGFVGQPGLPGRPGFRGFPGAPGRIGPPGQRGNAGKDGTPGKPGIPG 285
Cdd:pfam01391   5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 132-297 7.97e-09

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 56.45  E-value: 7.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677420989 132 DGRDGADGKRGEPGKDAPDAAIIEPhniplewcfdcedgppgaagkpgpkGPPGRPGQAGfPAEGGRRGPPGPPGLIGPP 211
Cdd:NF038329  176 AGKDGEAGAKGPAGEKGPQGPRGET-------------------------GPAGEQGPAG-PAGPDGEAGPAGEDGPAGP 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677420989 212 GTPGVPGIKGPPGIPGrvivKEQPRGPPGFVGQPGLPGRPGFRGFPGAPGRIGPPGQRGNAGKDGTPGKPGIPGSLGPAG 291
Cdd:NF038329  230 AGDGQQGPDGDPGPTG----EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDG 305


                  ....*.
gi 1677420989 292 TYGTTG 297
Cdd:NF038329  306 QNGKDG 311
 
Name Accession Description Interval E-value
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 22-74 5.85e-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. 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: 70.57  E-value: 5.85e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1677420989   22 RIAFCGVTMSTVATLLCVISVPMFYNYLQQMQSVMIDQIEFCRSRSDHIWREI 74
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 25-74 2.40e-15

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: 69.03  E-value: 2.40e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1677420989  25 FCGVTMSTVATLLCVISVPMFYNYLQQMQSVMIDQIEFCRSRSDHIWREI 74
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 235-285 6.76e-11

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: 56.73  E-value: 6.76e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1677420989 235 PRGPPGFVGQPGLPGRPGFRGFPGAPGRIGPPGQRGNAGKDGTPGKPGIPG 285
Cdd:pfam01391   5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 132-297 7.97e-09

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 56.45  E-value: 7.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677420989 132 DGRDGADGKRGEPGKDAPDAAIIEPhniplewcfdcedgppgaagkpgpkGPPGRPGQAGfPAEGGRRGPPGPPGLIGPP 211
Cdd:NF038329  176 AGKDGEAGAKGPAGEKGPQGPRGET-------------------------GPAGEQGPAG-PAGPDGEAGPAGEDGPAGP 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677420989 212 GTPGVPGIKGPPGIPGrvivKEQPRGPPGFVGQPGLPGRPGFRGFPGAPGRIGPPGQRGNAGKDGTPGKPGIPGSLGPAG 291
Cdd:NF038329  230 AGDGQQGPDGDPGPTG----EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDG 305


                  ....*.
gi 1677420989 292 TYGTTG 297
Cdd:NF038329  306 QNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 132-297 4.63e-08

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: 54.14  E-value: 4.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677420989 132 DGRDGADGKRGEPGKDAPDAAiiephniplewcfdcedgppgaagkpgpKGPPGRPGQAGFPAEGGRRGPPGPPGLIGPP 211
Cdd:NF038329  164 AGPQGEAGPQGPAGKDGEAGA----------------------------KGPAGEKGPQGPRGETGPAGEQGPAGPAGPD 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677420989 212 GTPGVPGIKGPPGIPGRVIVKEQ----PRGPPGFVGQPGLPGRPGFRGFPGAPGRIGPPGQRGNAGKDGTPGKPGIPGSL 287
Cdd:NF038329  216 GEAGPAGEDGPAGPAGDGQQGPDgdpgPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKD 295

                         170
                  ....*....|
gi 1677420989 288 GPAGTYGTTG 297
Cdd:NF038329  296 GLPGKDGKDG 305
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 138-297 6.34e-07

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: 50.29  E-value: 6.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677420989 138 DGKRGEPGKDAPDAAiiephniplewcfDCEDGPPGAAGKPGPKGPPGRPGQAGFPAEGGRRGPPGPPGLIGPPGTPGVP 217
Cdd:NF038329  116 DGEKGEPGPAGPAGP-------------AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677420989 218 GIKGPPGIPGrvivKEQPRGPPGFVGQPGLPGRPGFRGFPGAPGRIGPPGQ--RGNAGKDGTPGKPGIPGSLGPAGTYGT 295
Cdd:NF038329  183 GAKGPAGEKG----PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDGPQGPDGPAGK 258


                  ..
gi 1677420989 296 TG 297
Cdd:NF038329  259 DG 260
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 206-310 1.36e-06

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 49.52  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677420989 206 GLIGPPGTPGVPGIKGPPGIPGRVIVKEQ--------PRGPPGFVGQPGLPGRPGFRGFPGAPGRIGPPGQRGNAGKDGT 277
Cdd:NF038329  129 GPAGEQGPRGDRGETGPAGPAGPPGPQGErgekgpagPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGP 208

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1677420989 278 PGKPGIPGSLGPAGTYGTTGSCDHCPQ-PRTAPG 310
Cdd:NF038329  209 AGPAGPDGEAGPAGEDGPAGPAGDGQQgPDGDPG 242
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 132-281 2.57e-04

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 42.20  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677420989 132 DGRDGADGKRGEPGKDAPDAAIIEPhniplewcfdcedgppgaagkpgpkgppgrpGQAGFPAEGGRRGPPgppgligpp 211
Cdd:NF038329  244 TGEDGPQGPDGPAGKDGPRGDRGEA-------------------------------GPDGPDGKDGERGPV--------- 283

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677420989 212 gtpgvpgikGPPGIPGRViVKEQPRGPPGFVGQPGLPGRPGFRGFPGAPGRIGPPGQrgnAGKDGTPGKP 281
Cdd:NF038329  284 ---------GPAGKDGQN-GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK---DGKDGQPGKP 340
 
Name Accession Description Interval E-value
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 22-74 5.85e-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. 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: 70.57  E-value: 5.85e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1677420989   22 RIAFCGVTMSTVATLLCVISVPMFYNYLQQMQSVMIDQIEFCRSRSDHIWREI 74
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 25-74 2.40e-15

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: 69.03  E-value: 2.40e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1677420989  25 FCGVTMSTVATLLCVISVPMFYNYLQQMQSVMIDQIEFCRSRSDHIWREI 74
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 235-285 6.76e-11

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: 56.73  E-value: 6.76e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1677420989 235 PRGPPGFVGQPGLPGRPGFRGFPGAPGRIGPPGQRGNAGKDGTPGKPGIPG 285
Cdd:pfam01391   5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 235-290 1.77e-10

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: 55.58  E-value: 1.77e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1677420989 235 PRGPPGFVGQPGLPGRPGFRGFPGAPGRIGPPGQRGNAGKDGTPGKPGIPGSLGPA 290
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 243-297 1.56e-09

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: 52.88  E-value: 1.56e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1677420989 243 GQPGLPGRPGFRGFPGAPGRIGPPGQRGNAGKDGTPGKPGIPGSLGPAGTYGTTG 297
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 240-294 4.57e-09

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: 51.73  E-value: 4.57e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1677420989 240 GFVGQPGLPGRPGFRGFPGAPGRIGPPGQRGNAGKDGTPGKPGIPGSLGPAGTYG 294
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 132-297 7.97e-09

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 56.45  E-value: 7.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677420989 132 DGRDGADGKRGEPGKDAPDAAIIEPhniplewcfdcedgppgaagkpgpkGPPGRPGQAGfPAEGGRRGPPGPPGLIGPP 211
Cdd:NF038329  176 AGKDGEAGAKGPAGEKGPQGPRGET-------------------------GPAGEQGPAG-PAGPDGEAGPAGEDGPAGP 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677420989 212 GTPGVPGIKGPPGIPGrvivKEQPRGPPGFVGQPGLPGRPGFRGFPGAPGRIGPPGQRGNAGKDGTPGKPGIPGSLGPAG 291
Cdd:NF038329  230 AGDGQQGPDGDPGPTG----EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDG 305


                  ....*.
gi 1677420989 292 TYGTTG 297
Cdd:NF038329  306 QNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 132-297 4.63e-08

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: 54.14  E-value: 4.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677420989 132 DGRDGADGKRGEPGKDAPDAAiiephniplewcfdcedgppgaagkpgpKGPPGRPGQAGFPAEGGRRGPPGPPGLIGPP 211
Cdd:NF038329  164 AGPQGEAGPQGPAGKDGEAGA----------------------------KGPAGEKGPQGPRGETGPAGEQGPAGPAGPD 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677420989 212 GTPGVPGIKGPPGIPGRVIVKEQ----PRGPPGFVGQPGLPGRPGFRGFPGAPGRIGPPGQRGNAGKDGTPGKPGIPGSL 287
Cdd:NF038329  216 GEAGPAGEDGPAGPAGDGQQGPDgdpgPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKD 295

                         170
                  ....*....|
gi 1677420989 288 GPAGTYGTTG 297
Cdd:NF038329  296 GLPGKDGKDG 305
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 138-297 6.34e-07

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: 50.29  E-value: 6.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677420989 138 DGKRGEPGKDAPDAAiiephniplewcfDCEDGPPGAAGKPGPKGPPGRPGQAGFPAEGGRRGPPGPPGLIGPPGTPGVP 217
Cdd:NF038329  116 DGEKGEPGPAGPAGP-------------AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677420989 218 GIKGPPGIPGrvivKEQPRGPPGFVGQPGLPGRPGFRGFPGAPGRIGPPGQ--RGNAGKDGTPGKPGIPGSLGPAGTYGT 295
Cdd:NF038329  183 GAKGPAGEKG----PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDGPQGPDGPAGK 258


                  ..
gi 1677420989 296 TG 297
Cdd:NF038329  259 DG 260
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 206-310 1.36e-06

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 49.52  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677420989 206 GLIGPPGTPGVPGIKGPPGIPGRVIVKEQ--------PRGPPGFVGQPGLPGRPGFRGFPGAPGRIGPPGQRGNAGKDGT 277
Cdd:NF038329  129 GPAGEQGPRGDRGETGPAGPAGPPGPQGErgekgpagPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGP 208

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1677420989 278 PGKPGIPGSLGPAGTYGTTGSCDHCPQ-PRTAPG 310
Cdd:NF038329  209 AGPAGPDGEAGPAGEDGPAGPAGDGQQgPDGDPG 242
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 220-261 9.51e-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: 39.40  E-value: 9.51e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1677420989 220 KGPPGIPGrvivkeqPRGPPGFVGQPGLPGRPGFRGFPGAPG 261
Cdd:pfam01391  21 PGPPGPPG-------PPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 132-281 2.57e-04

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 42.20  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677420989 132 DGRDGADGKRGEPGKDAPDAAIIEPhniplewcfdcedgppgaagkpgpkgppgrpGQAGFPAEGGRRGPPgppgligpp 211
Cdd:NF038329  244 TGEDGPQGPDGPAGKDGPRGDRGEA-------------------------------GPDGPDGKDGERGPV--------- 283

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677420989 212 gtpgvpgikGPPGIPGRViVKEQPRGPPGFVGQPGLPGRPGFRGFPGAPGRIGPPGQrgnAGKDGTPGKP 281
Cdd:NF038329  284 ---------GPAGKDGQN-GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK---DGKDGQPGKP 340
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 255-298 2.57e-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: 2.57e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1677420989 255 GFPGAPGRIGPPGQRGNAGKDGTPGKPGIPGSLGPAGTYGTTGS 298
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH