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Conserved domains on  [gi|1207190552|ref|XP_021328284|]
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collagen alpha-1(XIII) chain isoform X6 [Danio rerio]

Protein Classification

collagen-like domain-containing protein( domain architecture ID 1903237)

collagen-like domain-containing protein such as collagens, which are extracellular structural proteins involved in formation of connective tissue structure

PubMed:  21421911|15837519

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 ...
 485-733 1.04e-24

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 107.68  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 485 KGDVGLPGPPGVDGEKGPRgkpgepgpigppgpegargegGVMGFPGPKGDKGDMGPSGSPGLDGPTGEKGVSGPPGHIG 564
Cdd:NF038329  119 KGEPGPAGPAGPAGEQGPR---------------------GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 565 LPGPMGQKGEPGEKGDKAElvygpagppgpagpvgpmgsPGLSGPKGEPG-IGLKGEKGSSGQKGDKGDRGHLGlPGAHG 643
Cdd:NF038329  178 KDGEAGAKGPAGEKGPQGP--------------------RGETGPAGEQGpAGPAGPDGEAGPAGEDGPAGPAG-DGQQG 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 644 LDGRPGPVGLIGPAGVPGPAGPKGEMGEKGDMGVAGPIGPQGIPGLVGPPGLKGIKGFRGL------KGEKGEPGLPGLD 717
Cdd:NF038329  237 PDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLpgkdgkDGQNGKDGLPGKD 316

                         250
                  ....*....|....*.
gi 1207190552 718 GLDAPcaVGDDGLPVP 733
Cdd:NF038329  317 GKDGQ--PGKDGLPGK 330
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 165-419 9.00e-23

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: 101.91  E-value: 9.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 165 RGFPGFPGPIGLDGKPGQNGPKGDMGPRGPKGVPGEPGPKGEKGACGEYTHRKRRIVNASAGGQATQMLPftvrkmpsis 244
Cdd:NF038329  119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA---------- 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 245 plilkhlkqgepgaqGPPGPPGPPGPPGPLGLTGAIGPPGKPGEPGKPGKDPKMLPGLKGEPGVPGQKGDRGEAGPSGPE 324
Cdd:NF038329  189 ---------------GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPD 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 325 GPMGIKGDEGQKGDQGTDGQRGEKGELGMPGMPGKQGVKGEPGFPGIPGRKGQTGLSGIPGKRGYKGEKGEpsaagTGIK 404
Cdd:NF038329  254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK-----DGLP 328

                         250
                  ....*....|....*
gi 1207190552 405 GEPGVAGQPGQAGPK 419
Cdd:NF038329  329 GKDGKDGQPGKPAPK 343
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 485-733 1.04e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 107.68  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 485 KGDVGLPGPPGVDGEKGPRgkpgepgpigppgpegargegGVMGFPGPKGDKGDMGPSGSPGLDGPTGEKGVSGPPGHIG 564
Cdd:NF038329  119 KGEPGPAGPAGPAGEQGPR---------------------GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 565 LPGPMGQKGEPGEKGDKAElvygpagppgpagpvgpmgsPGLSGPKGEPG-IGLKGEKGSSGQKGDKGDRGHLGlPGAHG 643
Cdd:NF038329  178 KDGEAGAKGPAGEKGPQGP--------------------RGETGPAGEQGpAGPAGPDGEAGPAGEDGPAGPAG-DGQQG 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 644 LDGRPGPVGLIGPAGVPGPAGPKGEMGEKGDMGVAGPIGPQGIPGLVGPPGLKGIKGFRGL------KGEKGEPGLPGLD 717
Cdd:NF038329  237 PDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLpgkdgkDGQNGKDGLPGKD 316

                         250
                  ....*....|....*.
gi 1207190552 718 GLDAPcaVGDDGLPVP 733
Cdd:NF038329  317 GKDGQ--PGKDGLPGK 330
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 485-731 3.64e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 106.14  E-value: 3.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 485 KGDVGLPGPPGVDGEKGPRGKPGEPGPIGPPGPEGARGEGGVMGFPGPKGDKGDMGPSGSPGLDGPTGEKGVSGPPGHIG 564
Cdd:NF038329  137 RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 565 LPGPMGQKGEPGEKGDkaelvygpagppgpagpvgpmgspglsgpkgepgiglkgekgssGQKGDKGDRGHLGLPGAHGL 644
Cdd:NF038329  217 EAGPAGEDGPAGPAGD--------------------------------------------GQQGPDGDPGPTGEDGPQGP 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 645 DGRPGPVGLIGPAGVPGPAGPKGEMGEKGDMGVAGPIGPQGIPGLVGPPGLKGIKGFRGLKGEKGEPGLPGLDGLDAPca 724
Cdd:NF038329  253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK-- 330


                  ....*..
gi 1207190552 725 VGDDGLP 731
Cdd:NF038329  331 DGKDGQP 337
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 165-419 9.00e-23

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: 101.91  E-value: 9.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 165 RGFPGFPGPIGLDGKPGQNGPKGDMGPRGPKGVPGEPGPKGEKGACGEYTHRKRRIVNASAGGQATQMLPftvrkmpsis 244
Cdd:NF038329  119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA---------- 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 245 plilkhlkqgepgaqGPPGPPGPPGPPGPLGLTGAIGPPGKPGEPGKPGKDPKMLPGLKGEPGVPGQKGDRGEAGPSGPE 324
Cdd:NF038329  189 ---------------GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPD 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 325 GPMGIKGDEGQKGDQGTDGQRGEKGELGMPGMPGKQGVKGEPGFPGIPGRKGQTGLSGIPGKRGYKGEKGEpsaagTGIK 404
Cdd:NF038329  254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK-----DGLP 328

                         250
                  ....*....|....*
gi 1207190552 405 GEPGVAGQPGQAGPK 419
Cdd:NF038329  329 GKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 296-505 2.42e-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: 85.34  E-value: 2.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 296 PKMLPGLKGEPGVPGQKGDRGEAGPSGPEGPMGIKGDEGQKGDQGTDGQRGEKGELGMPGMPGKQGVKGEPGFPGIPGRK 375
Cdd:NF038329  130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 376 GQTGLSGIPGKRGYKGEKGEPSAAGTGIKGEPGVAGQPGQAGPKGEKGDQGIKGDPGLEGPRGPPGPTGEPGKtlVNNNE 455
Cdd:NF038329  210 GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP--VGPAG 287

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207190552 456 NDIRNvhsmGAPGLPGPPGPPGLPGTPGLKGDVGLPGPPGVDGEKGPRGK 505
Cdd:NF038329  288 KDGQN----GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 570-731 5.04e-14

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: 74.94  E-value: 5.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 570 GQKGEPGEKGDKaelvygpagppGPAgpvgpmgspGLSGPKGEPgiglkGEKGSSGQKGDKGDRGHLGLPGAHGLDGRPG 649
Cdd:NF038329  117 GEKGEPGPAGPA-----------GPA---------GEQGPRGDR-----GETGPAGPAGPPGPQGERGEKGPAGPQGEAG 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 650 PVGLIGPAGVPGPAGPKGEMGEKGDMGVAGPIGPQGIPGLVGPPGLKGIKGFRGLKG-----EKGEPGLPGLDGLDAPca 724
Cdd:NF038329  172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPGPTGEDGP-- 249


                  ....*..
gi 1207190552 725 VGDDGLP 731
Cdd:NF038329  250 QGPDGPA 256
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 642-722 1.35e-10

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 64.16  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 642 HGLDGRPGPVGLIGPAGVPGPAGPKGEMGEKGDMGVAGPIGPQGIPGLVGPPGLKGIKGFRGLKGEKGEPGLPGLDGLDA 721
Cdd:NF038329  113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192


                  .
gi 1207190552 722 P 722
Cdd:NF038329  193 P 193
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 133-359 2.92e-05

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 47.21  E-value: 2.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 133 KGSLGIPGRMGAPGEPGLSIIGPRGPPGQPGTRGFPGFPGPIGLDGKPGQNGPKGDMGPRGPKGVPGEPGPKGEKGACGE 212
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGE 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 213 ythrkrrivnasaggqatqmlpftvrkmpsisplilkhlkqgepgaqgppgppgppgppgplgltgaigppgkpgepgkp 292
Cdd:NF038329      --------------------------------------------------------------------------------

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190552 293 gkdpkmlPGLKGEPGVPGQKGDRGEAGPSGPEGPMGIKGDEGQKGDQGTDGQRGEKGELGMPGMPGK 359
Cdd:NF038329  280 -------RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 655-711 1.48e-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: 40.17  E-value: 1.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190552 655 GPAGVPGPAGPKGEMGEKGDMGVAGPIGPQGIPGLVGPPGLKGIKGFRGLKGEKGEP 711
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 319-373 1.37e-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: 37.47  E-value: 1.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207190552 319 GPSGPEGPMGIKGDEGQKGDQGTDGQRGEKGELGMPGMPGKQGVKGEPGFPGIPG 373
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 485-733 1.04e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 107.68  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 485 KGDVGLPGPPGVDGEKGPRgkpgepgpigppgpegargegGVMGFPGPKGDKGDMGPSGSPGLDGPTGEKGVSGPPGHIG 564
Cdd:NF038329  119 KGEPGPAGPAGPAGEQGPR---------------------GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 565 LPGPMGQKGEPGEKGDKAElvygpagppgpagpvgpmgsPGLSGPKGEPG-IGLKGEKGSSGQKGDKGDRGHLGlPGAHG 643
Cdd:NF038329  178 KDGEAGAKGPAGEKGPQGP--------------------RGETGPAGEQGpAGPAGPDGEAGPAGEDGPAGPAG-DGQQG 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 644 LDGRPGPVGLIGPAGVPGPAGPKGEMGEKGDMGVAGPIGPQGIPGLVGPPGLKGIKGFRGL------KGEKGEPGLPGLD 717
Cdd:NF038329  237 PDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLpgkdgkDGQNGKDGLPGKD 316

                         250
                  ....*....|....*.
gi 1207190552 718 GLDAPcaVGDDGLPVP 733
Cdd:NF038329  317 GKDGQ--PGKDGLPGK 330
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 485-731 3.64e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 106.14  E-value: 3.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 485 KGDVGLPGPPGVDGEKGPRGKPGEPGPIGPPGPEGARGEGGVMGFPGPKGDKGDMGPSGSPGLDGPTGEKGVSGPPGHIG 564
Cdd:NF038329  137 RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 565 LPGPMGQKGEPGEKGDkaelvygpagppgpagpvgpmgspglsgpkgepgiglkgekgssGQKGDKGDRGHLGLPGAHGL 644
Cdd:NF038329  217 EAGPAGEDGPAGPAGD--------------------------------------------GQQGPDGDPGPTGEDGPQGP 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 645 DGRPGPVGLIGPAGVPGPAGPKGEMGEKGDMGVAGPIGPQGIPGLVGPPGLKGIKGFRGLKGEKGEPGLPGLDGLDAPca 724
Cdd:NF038329  253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK-- 330


                  ....*..
gi 1207190552 725 VGDDGLP 731
Cdd:NF038329  331 DGKDGQP 337
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 165-419 9.00e-23

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: 101.91  E-value: 9.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 165 RGFPGFPGPIGLDGKPGQNGPKGDMGPRGPKGVPGEPGPKGEKGACGEYTHRKRRIVNASAGGQATQMLPftvrkmpsis 244
Cdd:NF038329  119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA---------- 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 245 plilkhlkqgepgaqGPPGPPGPPGPPGPLGLTGAIGPPGKPGEPGKPGKDPKMLPGLKGEPGVPGQKGDRGEAGPSGPE 324
Cdd:NF038329  189 ---------------GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPD 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 325 GPMGIKGDEGQKGDQGTDGQRGEKGELGMPGMPGKQGVKGEPGFPGIPGRKGQTGLSGIPGKRGYKGEKGEpsaagTGIK 404
Cdd:NF038329  254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK-----DGLP 328

                         250
                  ....*....|....*
gi 1207190552 405 GEPGVAGQPGQAGPK 419
Cdd:NF038329  329 GKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 296-505 2.42e-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: 85.34  E-value: 2.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 296 PKMLPGLKGEPGVPGQKGDRGEAGPSGPEGPMGIKGDEGQKGDQGTDGQRGEKGELGMPGMPGKQGVKGEPGFPGIPGRK 375
Cdd:NF038329  130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 376 GQTGLSGIPGKRGYKGEKGEPSAAGTGIKGEPGVAGQPGQAGPKGEKGDQGIKGDPGLEGPRGPPGPTGEPGKtlVNNNE 455
Cdd:NF038329  210 GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP--VGPAG 287

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207190552 456 NDIRNvhsmGAPGLPGPPGPPGLPGTPGLKGDVGLPGPPGVDGEKGPRGK 505
Cdd:NF038329  288 KDGQN----GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 570-731 5.04e-14

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: 74.94  E-value: 5.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 570 GQKGEPGEKGDKaelvygpagppGPAgpvgpmgspGLSGPKGEPgiglkGEKGSSGQKGDKGDRGHLGLPGAHGLDGRPG 649
Cdd:NF038329  117 GEKGEPGPAGPA-----------GPA---------GEQGPRGDR-----GETGPAGPAGPPGPQGERGEKGPAGPQGEAG 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 650 PVGLIGPAGVPGPAGPKGEMGEKGDMGVAGPIGPQGIPGLVGPPGLKGIKGFRGLKG-----EKGEPGLPGLDGLDAPca 724
Cdd:NF038329  172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPGPTGEDGP-- 249


                  ....*..
gi 1207190552 725 VGDDGLP 731
Cdd:NF038329  250 QGPDGPA 256
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 642-722 1.35e-10

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 64.16  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 642 HGLDGRPGPVGLIGPAGVPGPAGPKGEMGEKGDMGVAGPIGPQGIPGLVGPPGLKGIKGFRGLKGEKGEPGLPGLDGLDA 721
Cdd:NF038329  113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192


                  .
gi 1207190552 722 P 722
Cdd:NF038329  193 P 193
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 133-359 2.92e-05

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 47.21  E-value: 2.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 133 KGSLGIPGRMGAPGEPGLSIIGPRGPPGQPGTRGFPGFPGPIGLDGKPGQNGPKGDMGPRGPKGVPGEPGPKGEKGACGE 212
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGE 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190552 213 ythrkrrivnasaggqatqmlpftvrkmpsisplilkhlkqgepgaqgppgppgppgppgplgltgaigppgkpgepgkp 292
Cdd:NF038329      --------------------------------------------------------------------------------

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190552 293 gkdpkmlPGLKGEPGVPGQKGDRGEAGPSGPEGPMGIKGDEGQKGDQGTDGQRGEKGELGMPGMPGK 359
Cdd:NF038329  280 -------RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 655-711 1.48e-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: 40.17  E-value: 1.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190552 655 GPAGVPGPAGPKGEMGEKGDMGVAGPIGPQGIPGLVGPPGLKGIKGFRGLKGEKGEP 711
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 649-703 4.77e-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: 38.63  E-value: 4.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207190552 649 GPVGLIGPAGVPGPAGPKGEMGEKGDMGVAGPIGPQGIPGLVGPPGLKGIKGFRG 703
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 643-697 5.26e-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: 38.63  E-value: 5.26e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207190552 643 GLDGRPGPVGLIGPAGVPGPAGPKGEMGEKGDMGVAGPIGPQGIPGLVGPPGLKG 697
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 658-714 5.80e-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: 38.63  E-value: 5.80e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190552 658 GVPGPAGPKGEMGEKGDMGVAGPIGPQGIPGLVGPPGLKGIKGFRGLKGEKGEPGLP 714
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 319-373 1.37e-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: 37.47  E-value: 1.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207190552 319 GPSGPEGPMGIKGDEGQKGDQGTDGQRGEKGELGMPGMPGKQGVKGEPGFPGIPG 373
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 346-400 3.55e-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: 36.32  E-value: 3.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207190552 346 GEKGELGMPGMPGKQGVKGEPGFPGIPGRKGQTGLSGIPGKRGYKGEKGEPSAAG 400
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 165-210 3.81e-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: 36.32  E-value: 3.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1207190552 165 RGFPGFPGPIGLDGKPGQNGPKGDMGPRGPKGVPGEPGPKGEKGAC 210
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 531-579 4.46e-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: 4.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1207190552 531 GPKGDKGDMGPSGSPGLDGPTGEKGVSGPPGHIGLPGPMGQKGEPGEKG 579
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 640-694 4.78e-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: 4.78e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207190552 640 GAHGLDGRPGPVGLIGPAGVPGPAGPKGEMGEKGDMGVAGPIGPQGIPGLVGPPG 694
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 325-379 7.52e-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: 35.16  E-value: 7.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207190552 325 GPMGIKGDEGQKGDQGTDGQRGEKGELGMPGMPGKQGVKGEPGFPGIPGRKGQTG 379
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 652-707 7.90e-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: 35.16  E-value: 7.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190552 652 GLIGPAGVPGPAGPKGEMGEKGDMGVAGPIGPQGIPGLVGPPGLKGIKGFRGLKGE 707
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 310-366 8.89e-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: 35.16  E-value: 8.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190552 310 GQKGDRGEAGPSGPEGPMGIKGDEGQKGDQGTDGQRGEKGELGMPGMPGKQGVKGEP 366
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
 
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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