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Conserved domains on  [gi|24581824|ref|NP_723046|]
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collagen type IV alpha 1, isoform C [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1663-1777 4.33e-62

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


:

Pssm-ID: 128421  Cd Length: 114  Bit Score: 207.24  E-value: 4.33e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824    1663 ANVIAVHSQTIEVPDCPNGWEGLWIGYSFLMHTAvGNGGGGQALQSPGSCLEDFRATPFIECNGaKGTCHFYE-TMTSFW 1741
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTG-NGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASrNDYSFW 78

                            90       100       110
                    ....*....|....*....|....*....|....*.
gi 24581824    1742 MYNLESSQPFERPQQQTIKAGERQSHVSRCQVCMKN 1777
Cdd:smart00111   79 LSTIEPSDQFTAPRPMTPKAGDLRPYISRCQVCEKP 114
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1555-1662 3.11e-56

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


:

Pssm-ID: 128421  Cd Length: 114  Bit Score: 190.68  E-value: 3.11e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824    1555 GILITRHSQSETVPACSAGHTELWTGYSLLYVDGNDYAHNQDLGSPGSCVPRFSTLPVLSCGQNNVCNYASRNDKTFWLT 1634
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 24581824    1635 TN-------AAIPMMPVENiEIRQYISRCVVCEAP 1662
Cdd:smart00111   81 TIepsdqftAPRPMTPKAG-DLRPYISRCQVCEKP 114
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 727-968 8.17e-32

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: 130.80  E-value: 8.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   727 HGRDGAKGDKGSFGRSGEKGEPGscaldeikmpAKGNKGEPGQTGMPGPPGEDGSPGERGYTGLKGNTGPQGPPGVEGPR 806
Cdd:NF038329  113 LKGDGEKGEPGPAGPAGPAGEQG----------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   807 GLNGPRGEKGNQGAVGVPGNPGKDGLRGIPGRNGQPGPRGEPGisrpgPMGPPGlNGLQGEKGDRGPTGPIGFPGADGSV 886
Cdd:NF038329  183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDG-----PAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   887 GYPGDRGDAGLPGVSGRPGIVGEKGDVGPIGPAGVAGPPGVPGIDGVRGRDGAKGEPGSPGLVGMPGNKGDRGAPGNDGP 966
Cdd:NF038329  257 GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336


                  ..
gi 24581824   967 KG 968
Cdd:NF038329  337 PG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1186-1420 1.08e-29

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: 124.63  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1186 GLKGETGPVGLQGFTGAPGPKGERGIRGQpglpatvpdiRGDKGSQGERGYTGEKGEQGERGLTGPAGVAGAKGDRGLQG 1265
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGP----------AGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1266 PPGASGLNGIPGAKGDIGPRGEIGYPGVtiKGEKGLPGRPGRNGRQGLiGAPGLIGERGLPGLAGEPGLVGLPGPIGPAG 1345
Cdd:NF038329  187 PAGEKGPQGPRGETGPAGEQGPAGPAGP--DGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581824  1346 SKGERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQKGDKGDRGLQGPSGLPGLVGQKGDTGYPG 1420
Cdd:NF038329  264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1321-1547 4.89e-29

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: 122.71  E-value: 4.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1321 GERGLPGLAGEPGLVGLPGPIGPAGSKGERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQKGDKGDRGL 1400
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1401 QGPSGLPGLVGQKGDTGYPGLNGNDGPVGAPGERGfTGPKGRDGRDGTPGLPGQKGEPGMLPPPGPKGEPGQPGRNGPKG 1480
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824  1481 EPGRPGERGLIGIQGERGEKGERGLIGETGNVGRPGPKGDRGEPGERGYEGAIGLIGQKGEPGAPAP 1547
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 107-361 1.88e-27

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 117.70  E-value: 1.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   107 GFPGMEGPSGDKGQKGDPGPYGQRGDKGERGSPGLHGQAGVPGVQGPAGNPGAPGINGKDGCDGQDGIPGLEGLSGMPGP 186
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   187 RGYAGQLGSKGEKGEPakengdyakGEKGEPGWRGTAGLAGPQGfPGEKGERGDSGPYGAKGPRGEHGLKGekgascygp 266
Cdd:NF038329  197 RGETGPAGEQGPAGPA---------GPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAG--------- 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   267 mKPGAPGIKGEKGEPassfpvkpthtvmGPRGDMGQKGEPGLVGRKGEPGPEGDTGLDGQKGEKGLPGGPGDRGRQGNFG 346
Cdd:NF038329  258 -KDGPRGDRGEAGPD-------------GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                         250
                  ....*....|....*
gi 24581824   347 PPGSTGQKGDRGEPG 361
Cdd:NF038329  324 KDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 543-820 1.85e-25

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 111.92  E-value: 1.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   543 GQKGDAGRPGTPGQKGDMGIKGDVGGKCSSCRAGPKGDKGTSGLPGIPGKDGARGPPGERGYPGERGHDGINGQTGPPGE 622
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   623 KGEDGRTGLPGATGEPGKpalcdlslieplKGDKGYPGAPGAKGVQGfKGAEGLPGIPGPKGEFGFKGEKGLSGAPGNDG 702
Cdd:NF038329  197 RGETGPAGEQGPAGPAGP------------DGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   703 TPGRAGRDGYPGIPGQsiKGEPGFHGRDGAKGDKGSFGRSGEKGEPGSCALDEikmpAKGNKGEPGQTGMPGPPGEDGSP 782
Cdd:NF038329  264 DRGEAGPDGPDGKDGE--RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG----KDGKDGQPGKDGLPGKDGKDGQP 337

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824   783 GERG----YTGLKGNTGPQGPPGVEGP---------------RGLNGPRGEKGNQGA 820
Cdd:NF038329  338 GKPApktpEVPQKPDTAPHTPKTPQIPgqskdvtpapqnpsnRGLNKPQTQGGNQLA 394
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 355-642 1.26e-22

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 103.06  E-value: 1.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   355 GDRGEPGLNGLPGNPGQKGEPGRAGATGKPGLlgppgppgggrgtpgppgpkgprgyVGAPGPQGLNGVDGLPGPQGYNG 434
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGP-------------------------AGPPGPQGERGEKGPAGPQGEAG 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   435 QKGGAGLPGRPGNEGPPGKKGEKGTAGLNGPkgsigpighpgppgpegqkgdaglpgygiqgsKGDAGIPGYPGLKGSKG 514
Cdd:NF038329  172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGP--------------------------------AGEQGPAGPAGPDGEAG 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   515 ERGFKGNAGAPGDSKLGRPGTPGAAGAPGQKGDAGRPGTPGQKGDMGIKGDVGgkcsscRAGPKGDKGTSGLPGIPGKDG 594
Cdd:NF038329  220 PAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG------PDGKDGERGPVGPAGKDGQNG 293

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 24581824   595 ARGPPGERGYPGERGHDGINGQTGPPGEKGEDGRTGLPGATGEPGKPA 642
Cdd:NF038329  294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPA 341
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 969-1218 1.96e-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: 99.59  E-value: 1.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   969 FAGVTGAPGKRGPAGIPGVSGAKGDKGATGltgndgpvggrgppgapglmgikgDQGLAGAPGQQGLDGMPGEKGNQGFP 1048
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETG------------------------PAGPAGPPGPQGERGEKGPAGPQGEA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1049 GLDGPPGLPGDASEKGQKGEPGPSGLRGDTGPAGTPGWPGEKGLPGLAvhGRAGPPGEKGDQGRsGIDGRDGINGEKGEQ 1128
Cdd:NF038329  171 GPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEA--GPAGEDGPAGPAGD-GQQGPDGDPGPTGED 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1129 GLQGVWGQPGEKGSVGAPGIPGAPGMDGLPGAAGAPGAVGYPGDRGDKGEPGLSGLPGLKGETGPVGLQGFTGAPGPKGE 1208
Cdd:NF038329  248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327

                         250
                  ....*....|
gi 24581824  1209 RGIRGQPGLP 1218
Cdd:NF038329  328 PGKDGKDGQP 337
 
Name Accession Description Interval E-value
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1663-1777 4.33e-62

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 128421  Cd Length: 114  Bit Score: 207.24  E-value: 4.33e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824    1663 ANVIAVHSQTIEVPDCPNGWEGLWIGYSFLMHTAvGNGGGGQALQSPGSCLEDFRATPFIECNGaKGTCHFYE-TMTSFW 1741
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTG-NGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASrNDYSFW 78

                            90       100       110
                    ....*....|....*....|....*....|....*.
gi 24581824    1742 MYNLESSQPFERPQQQTIKAGERQSHVSRCQVCMKN 1777
Cdd:smart00111   79 LSTIEPSDQFTAPRPMTPKAGDLRPYISRCQVCEKP 114
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1664-1776 3.08e-59

C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 460201  Cd Length: 110  Bit Score: 198.97  E-value: 3.08e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   1664 NVIAVHSQTIEVPDCPNGWEGLWIGYSFLMHTAVGnGGGGQALQSPGSCLEDFRATPFIECNGAkGTCHFYETMTSFWMY 1743
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78

                           90       100       110
                   ....*....|....*....|....*....|....
gi 24581824   1744 NLEssQPFERPQQQTIKAGER-QSHVSRCQVCMK 1776
Cdd:pfam01413   79 TVE--EQFRKPMSQTPKAGNElRSYISRCVVCEA 110
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1555-1662 3.11e-56

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 128421  Cd Length: 114  Bit Score: 190.68  E-value: 3.11e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824    1555 GILITRHSQSETVPACSAGHTELWTGYSLLYVDGNDYAHNQDLGSPGSCVPRFSTLPVLSCGQNNVCNYASRNDKTFWLT 1634
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 24581824    1635 TN-------AAIPMMPVENiEIRQYISRCVVCEAP 1662
Cdd:smart00111   81 TIepsdqftAPRPMTPKAG-DLRPYISRCQVCEKP 114
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1556-1661 1.65e-55

C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 460201  Cd Length: 110  Bit Score: 188.19  E-value: 1.65e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   1556 ILITRHSQSETVPACSAGHTELWTGYSLLYVDGNDYAHNQDLGSPGSCVPRFSTLPVLSCGQNNVCNYASrNDKTFWLTT 1635
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 24581824   1636 ---NAAIPMM--PVENIEIRQYISRCVVCEA 1661
Cdd:pfam01413   80 veeQFRKPMSqtPKAGNELRSYISRCVVCEA 110
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 727-968 8.17e-32

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: 130.80  E-value: 8.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   727 HGRDGAKGDKGSFGRSGEKGEPGscaldeikmpAKGNKGEPGQTGMPGPPGEDGSPGERGYTGLKGNTGPQGPPGVEGPR 806
Cdd:NF038329  113 LKGDGEKGEPGPAGPAGPAGEQG----------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   807 GLNGPRGEKGNQGAVGVPGNPGKDGLRGIPGRNGQPGPRGEPGisrpgPMGPPGlNGLQGEKGDRGPTGPIGFPGADGSV 886
Cdd:NF038329  183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDG-----PAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   887 GYPGDRGDAGLPGVSGRPGIVGEKGDVGPIGPAGVAGPPGVPGIDGVRGRDGAKGEPGSPGLVGMPGNKGDRGAPGNDGP 966
Cdd:NF038329  257 GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336


                  ..
gi 24581824   967 KG 968
Cdd:NF038329  337 PG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1186-1420 1.08e-29

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: 124.63  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1186 GLKGETGPVGLQGFTGAPGPKGERGIRGQpglpatvpdiRGDKGSQGERGYTGEKGEQGERGLTGPAGVAGAKGDRGLQG 1265
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGP----------AGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1266 PPGASGLNGIPGAKGDIGPRGEIGYPGVtiKGEKGLPGRPGRNGRQGLiGAPGLIGERGLPGLAGEPGLVGLPGPIGPAG 1345
Cdd:NF038329  187 PAGEKGPQGPRGETGPAGEQGPAGPAGP--DGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581824  1346 SKGERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQKGDKGDRGLQGPSGLPGLVGQKGDTGYPG 1420
Cdd:NF038329  264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 853-1071 1.24e-29

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: 124.25  E-value: 1.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   853 PGPMGPPGLNGLQGEKGDRGPTGPIGFPGADGSVGYPGDRGDAGLPGVSGRPGIVGEKGDVGPIGPAGVAGPPGVPGIDG 932
Cdd:NF038329  122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   933 VRGRDGAKGEPGSPGLVGMPGNKGDRGAPGN--DGPKGFAGVTGAPGKRGPAGIPGVSGAKGDKGATGLTGNDGPVGGRG 1010
Cdd:NF038329  202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581824  1011 PPGAPGLMGIKGDQGLAGAPGQQGLDGMPGEKGNQGFPGLDGPPGLPGDASEKGQKGEPGP 1071
Cdd:NF038329  282 PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1321-1547 4.89e-29

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: 122.71  E-value: 4.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1321 GERGLPGLAGEPGLVGLPGPIGPAGSKGERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQKGDKGDRGL 1400
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1401 QGPSGLPGLVGQKGDTGYPGLNGNDGPVGAPGERGfTGPKGRDGRDGTPGLPGQKGEPGMLPPPGPKGEPGQPGRNGPKG 1480
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824  1481 EPGRPGERGLIGIQGERGEKGERGLIGETGNVGRPGPKGDRGEPGERGYEGAIGLIGQKGEPGAPAP 1547
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 107-361 1.88e-27

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 117.70  E-value: 1.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   107 GFPGMEGPSGDKGQKGDPGPYGQRGDKGERGSPGLHGQAGVPGVQGPAGNPGAPGINGKDGCDGQDGIPGLEGLSGMPGP 186
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   187 RGYAGQLGSKGEKGEPakengdyakGEKGEPGWRGTAGLAGPQGfPGEKGERGDSGPYGAKGPRGEHGLKGekgascygp 266
Cdd:NF038329  197 RGETGPAGEQGPAGPA---------GPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAG--------- 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   267 mKPGAPGIKGEKGEPassfpvkpthtvmGPRGDMGQKGEPGLVGRKGEPGPEGDTGLDGQKGEKGLPGGPGDRGRQGNFG 346
Cdd:NF038329  258 -KDGPRGDRGEAGPD-------------GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                         250
                  ....*....|....*
gi 24581824   347 PPGSTGQKGDRGEPG 361
Cdd:NF038329  324 KDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 543-820 1.85e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 111.92  E-value: 1.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   543 GQKGDAGRPGTPGQKGDMGIKGDVGGKCSSCRAGPKGDKGTSGLPGIPGKDGARGPPGERGYPGERGHDGINGQTGPPGE 622
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   623 KGEDGRTGLPGATGEPGKpalcdlslieplKGDKGYPGAPGAKGVQGfKGAEGLPGIPGPKGEFGFKGEKGLSGAPGNDG 702
Cdd:NF038329  197 RGETGPAGEQGPAGPAGP------------DGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   703 TPGRAGRDGYPGIPGQsiKGEPGFHGRDGAKGDKGSFGRSGEKGEPGSCALDEikmpAKGNKGEPGQTGMPGPPGEDGSP 782
Cdd:NF038329  264 DRGEAGPDGPDGKDGE--RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG----KDGKDGQPGKDGLPGKDGKDGQP 337

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824   783 GERG----YTGLKGNTGPQGPPGVEGP---------------RGLNGPRGEKGNQGA 820
Cdd:NF038329  338 GKPApktpEVPQKPDTAPHTPKTPQIPgqskdvtpapqnpsnRGLNKPQTQGGNQLA 394
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 413-683 3.42e-25

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: 110.77  E-value: 3.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   413 GAPGPQGLNGVDGLPGPQGYNGQKGGAGLPGRPGNEGPPGKKGEKGTAGLNGPKGSigpighpgppgpegqkgdaglpgy 492
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP------------------------ 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   493 giQGSKGDAGIPGYPGLKGSKGERGFKGNAGAPGdsKLGRPGTPGAAGAPGQKGDAGRPGtPGQKGDMGIKGDVGGKCSS 572
Cdd:NF038329  176 --AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG--PAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   573 CRAGPKGDKGTSGLPGIPGKDGARGPPGERGYPGERGHDGINGQTGPPGEKGEDGRTGLPGatgepgkpalcdlsliepL 652
Cdd:NF038329  251 GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG------------------L 312

                         250       260       270
                  ....*....|....*....|....*....|.
gi 24581824   653 KGDKGYPGAPGAKGVQGFKGAEGLPGIPGPK 683
Cdd:NF038329  313 PGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 355-642 1.26e-22

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 103.06  E-value: 1.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   355 GDRGEPGLNGLPGNPGQKGEPGRAGATGKPGLlgppgppgggrgtpgppgpkgprgyVGAPGPQGLNGVDGLPGPQGYNG 434
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGP-------------------------AGPPGPQGERGEKGPAGPQGEAG 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   435 QKGGAGLPGRPGNEGPPGKKGEKGTAGLNGPkgsigpighpgppgpegqkgdaglpgygiqgsKGDAGIPGYPGLKGSKG 514
Cdd:NF038329  172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGP--------------------------------AGEQGPAGPAGPDGEAG 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   515 ERGFKGNAGAPGDSKLGRPGTPGAAGAPGQKGDAGRPGTPGQKGDMGIKGDVGgkcsscRAGPKGDKGTSGLPGIPGKDG 594
Cdd:NF038329  220 PAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG------PDGKDGERGPVGPAGKDGQNG 293

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 24581824   595 ARGPPGERGYPGERGHDGINGQTGPPGEKGEDGRTGLPGATGEPGKPA 642
Cdd:NF038329  294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPA 341
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1348-1551 1.91e-22

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 102.68  E-value: 1.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1348 GERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQKGDKGDRGLQGPSGLPGLVGQKGDTGYPGLNGNDGP 1427
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1428 VGAPGERGFTGPKGRDGRDGTPGLPGQKGEPGmlpppgpkgePGQPGRNGPKGEPGRPGErgligiQGERGEKGERGLIG 1507
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG----------PAGDGQQGPDGDPGPTGE------DGPQGPDGPAGKDG 260

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 24581824  1508 ETGNVGRPGPKGDRGEPGERGYEGAIGLIGQKGEPGAPAPAALD 1551
Cdd:NF038329  261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKD 304
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 969-1218 1.96e-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: 99.59  E-value: 1.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   969 FAGVTGAPGKRGPAGIPGVSGAKGDKGATGltgndgpvggrgppgapglmgikgDQGLAGAPGQQGLDGMPGEKGNQGFP 1048
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETG------------------------PAGPAGPPGPQGERGEKGPAGPQGEA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1049 GLDGPPGLPGDASEKGQKGEPGPSGLRGDTGPAGTPGWPGEKGLPGLAvhGRAGPPGEKGDQGRsGIDGRDGINGEKGEQ 1128
Cdd:NF038329  171 GPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEA--GPAGEDGPAGPAGD-GQQGPDGDPGPTGED 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1129 GLQGVWGQPGEKGSVGAPGIPGAPGMDGLPGAAGAPGAVGYPGDRGDKGEPGLSGLPGLKGETGPVGLQGFTGAPGPKGE 1208
Cdd:NF038329  248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327

                         250
                  ....*....|
gi 24581824  1209 RGIRGQPGLP 1218
Cdd:NF038329  328 PGKDGKDGQP 337
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 276-557 2.55e-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: 99.21  E-value: 2.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   276 GEKGEPASSFPVKPTHTVmGPRGDMGQKGEPGLVGRKGEPGPEGDTGLDGQKGEKGLPGGPGDRGRQGNFGPPGSTGQKG 355
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQ-GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   356 DRGEPGLNGLPGNPGQKGEPGRAGATGKPGLLGppgppgggrgtpgppgpkgprgyvgaPGPQGLNGVDGLPGPQGYNGQ 435
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG--------------------------PAGDGQQGPDGDPGPTGEDGP 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   436 KGGAGLPGRPGNEGPPGKKGEKGTAGLNGPKGSIgpighpgppgpegqkgdaglpgygiqGSKGDAGIPGYPGLKGSKGE 515
Cdd:NF038329  250 QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV--------------------------GPAGKDGQNGKDGLPGKDGK 303

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 24581824   516 RGFKGNAGAPGDSklGRPGTPGAAGAPGQKGDAGRPGTPGQK 557
Cdd:NF038329  304 DGQNGKDGLPGKD--GKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 82-203 4.00e-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: 73.79  E-value: 4.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824    82 PKCIAEKGNRGLPGPLGPTGLKGEMGFPGMEGPSGDKGQKGDPGPYGQRGDKGERGSPGLHGQAGvpgvqgpagNPGAPG 161
Cdd:NF038329  229 PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG---------KDGLPG 299

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 24581824   162 INGKDGCDGQDGIPGLEGLSGMPGPRGYAGQLGSKGEKGEPA 203
Cdd:NF038329  300 KDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPA 341
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1411-1555 1.34e-11

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: 68.78  E-value: 1.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1411 GQKGDTGYPGLNGNDGPVGAPGERGFTGPKGRDGRDGTPGLPGQKGEPGMLPPPGPKGEPGQPGRNGPKGEPG---RPGE 1487
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGekgPQGP 196

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24581824  1488 RGLIGIQGERGEKGERGLIGETGNVGRPGPKG-----DRGEPGERGYEGAIGLIGQKGEPGAPAPAALDYLTG 1555
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1453-1576 1.63e-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: 52.60  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1453 GQKGEPGmlpppgPKGEPGQPGRNGPKGEPGRPGERGLIGIQGERGEKGERGLIGETGNVGRPGPKGDRGEPGERGYEGA 1532
Cdd:NF038329  117 GEKGEPG------PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 24581824  1533 IGLIGQKGEPGAPAPAALDYLTGILITRHSQSETVPACSAGHTE 1576
Cdd:NF038329  191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ 234
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1321-1376 1.01e-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: 44.41  E-value: 1.01e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24581824   1321 GERGLPGLAGEPGLVGLPGPIGPAGSKGERGLAGSPGQPGQDGFPGAPGLKGDTGP 1376
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
849-1096 1.22e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 50.03  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  849 GISRPGPMGPPGLNGLQGEKGDRGPTGPigfPGADGSVGYPGDRGDAGLPGVSGRPGIVGEKGDVGPIGPAGVAGPPGVP 928
Cdd:COG5164    2 GLYGPGKTGPSDPGGVTTPAGSQGSTKP---AQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  929 GIDGVRGRDGAKGEPGSPGLVGMPGNKGDRGAPGNDGPKGFAGVTGA--PGKRGPAGIPGVSGAK-GDKGATGLTGNDGP 1005
Cdd:COG5164   79 GGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSttPPSGGSTTPPGDGGSTpPGPGSTGPGGSTTP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824 1006 VGGRGPPGAPGLMGIKG--DQGLAGAPGQQGLDGMPGEKGNQGFPGLDGPP----GLPGDASEKGQKGEPGPSGLRGDTG 1079
Cdd:COG5164  159 PGDGGSTTPPGPGGSTTppDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVkkddKNGKGNPPDDRGGKTGPKDQRPKTN 238

                        250
                 ....*....|....*..
gi 24581824 1080 PAGTPGWPGEKGLPGLA 1096
Cdd:COG5164  239 PIERRGPERPEAAALPA 255
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 325-380 1.76e-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: 43.64  E-value: 1.76e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24581824    325 GQKGEKGLPGGPGDRGRQGNFGPPGSTGQKGDRGEPGLNGLPGNPGQKGEPGRAGA 380
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 768-824 2.71e-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: 43.25  E-value: 2.71e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824    768 GQTGMPGPPGEDGSPGERGYTGLKGNTGPQGPPGVEGPRGLNGPRGEKGNQGAVGVP 824
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 576-632 1.38e-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: 41.33  E-value: 1.38e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824    576 GPKGDKGTSGLPGIPGKDGARGPPGERGYPGERGHDGINGQTGPPGEKGEDGRTGLP 632
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1017-1071 2.09e-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: 40.94  E-value: 2.09e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24581824   1017 LMGIKGDQGLAGAPGQQGLDGMPGEKGNQGFPGLDGPPGLPGDASEKGQKGEPGP 1071
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1094-1367 6.12e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 44.64  E-value: 6.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824 1094 GLAVHGRAGPPGEKGDQGRSGIDGRDGINGEKGEQGLQGVWGQPGEKGSVGAPGIPGAPGMDGLPGAAGAPGAVGYPGDR 1173
Cdd:COG5164    2 GLYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824 1174 GDKGEPGLSGLPGLKGETGPVGLQGFTGAPGPKGERGIRGQPGlpATVPDIRGDKGSQGERGYTgekgeQGERGLTGPAG 1253
Cdd:COG5164   82 TPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGG--STTPPSGGSTTPPGDGGST-----PPGPGSTGPGG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824 1254 VAGAKGDRGLQGPPGASGLNGIPGAKGDIGPRGEIGYPGVTIKGEKGLPGRPGRNGRQGLIGAPGLIGERGlpGLAGEPG 1333
Cdd:COG5164  155 STTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGPKD 232

                        250       260       270
                 ....*....|....*....|....*....|....
gi 24581824 1334 LVGLPGPIGPAGSKGERGLAGSPGQPGQDGFPGA 1367
Cdd:COG5164  233 QRPKTNPIERRGPERPEAAALPAELTALEAENRA 266
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1402-1458 1.75e-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: 38.24  E-value: 1.75e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824   1402 GPSGLPGLVGQKGDTGYPGLNGNDGPVGAPGERGFTGPKGRDGRDGTPGLPGQKGEP 1458
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 101-272 3.04e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.27  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   101 GLKGEMGFPGMEGPSGDKGQKGDPGPYGQRGDKGERGSPGLHGQAGVPGVQGPAGNPGAPGingkDGCDGQDGIPGLEGL 180
Cdd:PHA03169   82 GEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPS----HPGPHEPAPPESHNP 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   181 SGMPGPRGYAGqlGSKGEKGEPAKENGDYAKGEKGEPGWRGTAGLAGPQGFPGEKgERGDSGPYGAKGPRGEHGLKGEKG 260
Cdd:PHA03169  158 SPNQQPSSFLQ--PSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDE-PGEPQSPTPQQAPSPNTQQAVEHE 234

                         170
                  ....*....|..
gi 24581824   261 ASCYGPMKPGAP 272
Cdd:PHA03169  235 DEPTEPEREGPP 246
 
Name Accession Description Interval E-value
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1663-1777 4.33e-62

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 128421  Cd Length: 114  Bit Score: 207.24  E-value: 4.33e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824    1663 ANVIAVHSQTIEVPDCPNGWEGLWIGYSFLMHTAvGNGGGGQALQSPGSCLEDFRATPFIECNGaKGTCHFYE-TMTSFW 1741
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTG-NGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASrNDYSFW 78

                            90       100       110
                    ....*....|....*....|....*....|....*.
gi 24581824    1742 MYNLESSQPFERPQQQTIKAGERQSHVSRCQVCMKN 1777
Cdd:smart00111   79 LSTIEPSDQFTAPRPMTPKAGDLRPYISRCQVCEKP 114
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1664-1776 3.08e-59

C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 460201  Cd Length: 110  Bit Score: 198.97  E-value: 3.08e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   1664 NVIAVHSQTIEVPDCPNGWEGLWIGYSFLMHTAVGnGGGGQALQSPGSCLEDFRATPFIECNGAkGTCHFYETMTSFWMY 1743
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78

                           90       100       110
                   ....*....|....*....|....*....|....
gi 24581824   1744 NLEssQPFERPQQQTIKAGER-QSHVSRCQVCMK 1776
Cdd:pfam01413   79 TVE--EQFRKPMSQTPKAGNElRSYISRCVVCEA 110
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1555-1662 3.11e-56

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 128421  Cd Length: 114  Bit Score: 190.68  E-value: 3.11e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824    1555 GILITRHSQSETVPACSAGHTELWTGYSLLYVDGNDYAHNQDLGSPGSCVPRFSTLPVLSCGQNNVCNYASRNDKTFWLT 1634
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 24581824    1635 TN-------AAIPMMPVENiEIRQYISRCVVCEAP 1662
Cdd:smart00111   81 TIepsdqftAPRPMTPKAG-DLRPYISRCQVCEKP 114
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1556-1661 1.65e-55

C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 460201  Cd Length: 110  Bit Score: 188.19  E-value: 1.65e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   1556 ILITRHSQSETVPACSAGHTELWTGYSLLYVDGNDYAHNQDLGSPGSCVPRFSTLPVLSCGQNNVCNYASrNDKTFWLTT 1635
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 24581824   1636 ---NAAIPMM--PVENIEIRQYISRCVVCEA 1661
Cdd:pfam01413   80 veeQFRKPMSqtPKAGNELRSYISRCVVCEA 110
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 727-968 8.17e-32

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: 130.80  E-value: 8.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   727 HGRDGAKGDKGSFGRSGEKGEPGscaldeikmpAKGNKGEPGQTGMPGPPGEDGSPGERGYTGLKGNTGPQGPPGVEGPR 806
Cdd:NF038329  113 LKGDGEKGEPGPAGPAGPAGEQG----------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   807 GLNGPRGEKGNQGAVGVPGNPGKDGLRGIPGRNGQPGPRGEPGisrpgPMGPPGlNGLQGEKGDRGPTGPIGFPGADGSV 886
Cdd:NF038329  183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDG-----PAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   887 GYPGDRGDAGLPGVSGRPGIVGEKGDVGPIGPAGVAGPPGVPGIDGVRGRDGAKGEPGSPGLVGMPGNKGDRGAPGNDGP 966
Cdd:NF038329  257 GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336


                  ..
gi 24581824   967 KG 968
Cdd:NF038329  337 PG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1186-1420 1.08e-29

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: 124.63  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1186 GLKGETGPVGLQGFTGAPGPKGERGIRGQpglpatvpdiRGDKGSQGERGYTGEKGEQGERGLTGPAGVAGAKGDRGLQG 1265
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGP----------AGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1266 PPGASGLNGIPGAKGDIGPRGEIGYPGVtiKGEKGLPGRPGRNGRQGLiGAPGLIGERGLPGLAGEPGLVGLPGPIGPAG 1345
Cdd:NF038329  187 PAGEKGPQGPRGETGPAGEQGPAGPAGP--DGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581824  1346 SKGERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQKGDKGDRGLQGPSGLPGLVGQKGDTGYPG 1420
Cdd:NF038329  264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 853-1071 1.24e-29

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: 124.25  E-value: 1.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   853 PGPMGPPGLNGLQGEKGDRGPTGPIGFPGADGSVGYPGDRGDAGLPGVSGRPGIVGEKGDVGPIGPAGVAGPPGVPGIDG 932
Cdd:NF038329  122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   933 VRGRDGAKGEPGSPGLVGMPGNKGDRGAPGN--DGPKGFAGVTGAPGKRGPAGIPGVSGAKGDKGATGLTGNDGPVGGRG 1010
Cdd:NF038329  202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581824  1011 PPGAPGLMGIKGDQGLAGAPGQQGLDGMPGEKGNQGFPGLDGPPGLPGDASEKGQKGEPGP 1071
Cdd:NF038329  282 PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1321-1547 4.89e-29

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: 122.71  E-value: 4.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1321 GERGLPGLAGEPGLVGLPGPIGPAGSKGERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQKGDKGDRGL 1400
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1401 QGPSGLPGLVGQKGDTGYPGLNGNDGPVGAPGERGfTGPKGRDGRDGTPGLPGQKGEPGMLPPPGPKGEPGQPGRNGPKG 1480
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824  1481 EPGRPGERGLIGIQGERGEKGERGLIGETGNVGRPGPKGDRGEPGERGYEGAIGLIGQKGEPGAPAP 1547
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 107-361 1.88e-27

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 117.70  E-value: 1.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   107 GFPGMEGPSGDKGQKGDPGPYGQRGDKGERGSPGLHGQAGVPGVQGPAGNPGAPGINGKDGCDGQDGIPGLEGLSGMPGP 186
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   187 RGYAGQLGSKGEKGEPakengdyakGEKGEPGWRGTAGLAGPQGfPGEKGERGDSGPYGAKGPRGEHGLKGekgascygp 266
Cdd:NF038329  197 RGETGPAGEQGPAGPA---------GPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAG--------- 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   267 mKPGAPGIKGEKGEPassfpvkpthtvmGPRGDMGQKGEPGLVGRKGEPGPEGDTGLDGQKGEKGLPGGPGDRGRQGNFG 346
Cdd:NF038329  258 -KDGPRGDRGEAGPD-------------GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                         250
                  ....*....|....*
gi 24581824   347 PPGSTGQKGDRGEPG 361
Cdd:NF038329  324 KDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 543-820 1.85e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 111.92  E-value: 1.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   543 GQKGDAGRPGTPGQKGDMGIKGDVGGKCSSCRAGPKGDKGTSGLPGIPGKDGARGPPGERGYPGERGHDGINGQTGPPGE 622
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   623 KGEDGRTGLPGATGEPGKpalcdlslieplKGDKGYPGAPGAKGVQGfKGAEGLPGIPGPKGEFGFKGEKGLSGAPGNDG 702
Cdd:NF038329  197 RGETGPAGEQGPAGPAGP------------DGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   703 TPGRAGRDGYPGIPGQsiKGEPGFHGRDGAKGDKGSFGRSGEKGEPGSCALDEikmpAKGNKGEPGQTGMPGPPGEDGSP 782
Cdd:NF038329  264 DRGEAGPDGPDGKDGE--RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG----KDGKDGQPGKDGLPGKDGKDGQP 337

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824   783 GERG----YTGLKGNTGPQGPPGVEGP---------------RGLNGPRGEKGNQGA 820
Cdd:NF038329  338 GKPApktpEVPQKPDTAPHTPKTPQIPgqskdvtpapqnpsnRGLNKPQTQGGNQLA 394
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 413-683 3.42e-25

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: 110.77  E-value: 3.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   413 GAPGPQGLNGVDGLPGPQGYNGQKGGAGLPGRPGNEGPPGKKGEKGTAGLNGPKGSigpighpgppgpegqkgdaglpgy 492
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP------------------------ 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   493 giQGSKGDAGIPGYPGLKGSKGERGFKGNAGAPGdsKLGRPGTPGAAGAPGQKGDAGRPGtPGQKGDMGIKGDVGGKCSS 572
Cdd:NF038329  176 --AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG--PAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   573 CRAGPKGDKGTSGLPGIPGKDGARGPPGERGYPGERGHDGINGQTGPPGEKGEDGRTGLPGatgepgkpalcdlsliepL 652
Cdd:NF038329  251 GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG------------------L 312

                         250       260       270
                  ....*....|....*....|....*....|.
gi 24581824   653 KGDKGYPGAPGAKGVQGFKGAEGLPGIPGPK 683
Cdd:NF038329  313 PGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 355-642 1.26e-22

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 103.06  E-value: 1.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   355 GDRGEPGLNGLPGNPGQKGEPGRAGATGKPGLlgppgppgggrgtpgppgpkgprgyVGAPGPQGLNGVDGLPGPQGYNG 434
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGP-------------------------AGPPGPQGERGEKGPAGPQGEAG 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   435 QKGGAGLPGRPGNEGPPGKKGEKGTAGLNGPkgsigpighpgppgpegqkgdaglpgygiqgsKGDAGIPGYPGLKGSKG 514
Cdd:NF038329  172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGP--------------------------------AGEQGPAGPAGPDGEAG 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   515 ERGFKGNAGAPGDSKLGRPGTPGAAGAPGQKGDAGRPGTPGQKGDMGIKGDVGgkcsscRAGPKGDKGTSGLPGIPGKDG 594
Cdd:NF038329  220 PAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG------PDGKDGERGPVGPAGKDGQNG 293

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 24581824   595 ARGPPGERGYPGERGHDGINGQTGPPGEKGEDGRTGLPGATGEPGKPA 642
Cdd:NF038329  294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPA 341
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1348-1551 1.91e-22

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 102.68  E-value: 1.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1348 GERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQKGDKGDRGLQGPSGLPGLVGQKGDTGYPGLNGNDGP 1427
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1428 VGAPGERGFTGPKGRDGRDGTPGLPGQKGEPGmlpppgpkgePGQPGRNGPKGEPGRPGErgligiQGERGEKGERGLIG 1507
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG----------PAGDGQQGPDGDPGPTGE------DGPQGPDGPAGKDG 260

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 24581824  1508 ETGNVGRPGPKGDRGEPGERGYEGAIGLIGQKGEPGAPAPAALD 1551
Cdd:NF038329  261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKD 304
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 969-1218 1.96e-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: 99.59  E-value: 1.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   969 FAGVTGAPGKRGPAGIPGVSGAKGDKGATGltgndgpvggrgppgapglmgikgDQGLAGAPGQQGLDGMPGEKGNQGFP 1048
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETG------------------------PAGPAGPPGPQGERGEKGPAGPQGEA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1049 GLDGPPGLPGDASEKGQKGEPGPSGLRGDTGPAGTPGWPGEKGLPGLAvhGRAGPPGEKGDQGRsGIDGRDGINGEKGEQ 1128
Cdd:NF038329  171 GPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEA--GPAGEDGPAGPAGD-GQQGPDGDPGPTGED 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1129 GLQGVWGQPGEKGSVGAPGIPGAPGMDGLPGAAGAPGAVGYPGDRGDKGEPGLSGLPGLKGETGPVGLQGFTGAPGPKGE 1208
Cdd:NF038329  248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327

                         250
                  ....*....|
gi 24581824  1209 RGIRGQPGLP 1218
Cdd:NF038329  328 PGKDGKDGQP 337
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 276-557 2.55e-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: 99.21  E-value: 2.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   276 GEKGEPASSFPVKPTHTVmGPRGDMGQKGEPGLVGRKGEPGPEGDTGLDGQKGEKGLPGGPGDRGRQGNFGPPGSTGQKG 355
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQ-GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   356 DRGEPGLNGLPGNPGQKGEPGRAGATGKPGLLGppgppgggrgtpgppgpkgprgyvgaPGPQGLNGVDGLPGPQGYNGQ 435
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG--------------------------PAGDGQQGPDGDPGPTGEDGP 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   436 KGGAGLPGRPGNEGPPGKKGEKGTAGLNGPKGSIgpighpgppgpegqkgdaglpgygiqGSKGDAGIPGYPGLKGSKGE 515
Cdd:NF038329  250 QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV--------------------------GPAGKDGQNGKDGLPGKDGK 303

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 24581824   516 RGFKGNAGAPGDSklGRPGTPGAAGAPGQKGDAGRPGTPGQK 557
Cdd:NF038329  304 DGQNGKDGLPGKD--GKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 82-203 4.00e-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: 73.79  E-value: 4.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824    82 PKCIAEKGNRGLPGPLGPTGLKGEMGFPGMEGPSGDKGQKGDPGPYGQRGDKGERGSPGLHGQAGvpgvqgpagNPGAPG 161
Cdd:NF038329  229 PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG---------KDGLPG 299

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 24581824   162 INGKDGCDGQDGIPGLEGLSGMPGPRGYAGQLGSKGEKGEPA 203
Cdd:NF038329  300 KDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPA 341
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1411-1555 1.34e-11

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: 68.78  E-value: 1.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1411 GQKGDTGYPGLNGNDGPVGAPGERGFTGPKGRDGRDGTPGLPGQKGEPGMLPPPGPKGEPGQPGRNGPKGEPG---RPGE 1487
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGekgPQGP 196

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24581824  1488 RGLIGIQGERGEKGERGLIGETGNVGRPGPKG-----DRGEPGERGYEGAIGLIGQKGEPGAPAPAALDYLTG 1555
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1453-1576 1.63e-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: 52.60  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  1453 GQKGEPGmlpppgPKGEPGQPGRNGPKGEPGRPGERGLIGIQGERGEKGERGLIGETGNVGRPGPKGDRGEPGERGYEGA 1532
Cdd:NF038329  117 GEKGEPG------PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 24581824  1533 IGLIGQKGEPGAPAPAALDYLTGILITRHSQSETVPACSAGHTE 1576
Cdd:NF038329  191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ 234
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1321-1376 1.01e-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: 44.41  E-value: 1.01e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24581824   1321 GERGLPGLAGEPGLVGLPGPIGPAGSKGERGLAGSPGQPGQDGFPGAPGLKGDTGP 1376
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
849-1096 1.22e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 50.03  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  849 GISRPGPMGPPGLNGLQGEKGDRGPTGPigfPGADGSVGYPGDRGDAGLPGVSGRPGIVGEKGDVGPIGPAGVAGPPGVP 928
Cdd:COG5164    2 GLYGPGKTGPSDPGGVTTPAGSQGSTKP---AQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824  929 GIDGVRGRDGAKGEPGSPGLVGMPGNKGDRGAPGNDGPKGFAGVTGA--PGKRGPAGIPGVSGAK-GDKGATGLTGNDGP 1005
Cdd:COG5164   79 GGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSttPPSGGSTTPPGDGGSTpPGPGSTGPGGSTTP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824 1006 VGGRGPPGAPGLMGIKG--DQGLAGAPGQQGLDGMPGEKGNQGFPGLDGPP----GLPGDASEKGQKGEPGPSGLRGDTG 1079
Cdd:COG5164  159 PGDGGSTTPPGPGGSTTppDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVkkddKNGKGNPPDDRGGKTGPKDQRPKTN 238

                        250
                 ....*....|....*..
gi 24581824 1080 PAGTPGWPGEKGLPGLA 1096
Cdd:COG5164  239 PIERRGPERPEAAALPA 255
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 325-380 1.76e-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: 43.64  E-value: 1.76e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24581824    325 GQKGEKGLPGGPGDRGRQGNFGPPGSTGQKGDRGEPGLNGLPGNPGQKGEPGRAGA 380
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 768-824 2.71e-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: 43.25  E-value: 2.71e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824    768 GQTGMPGPPGEDGSPGERGYTGLKGNTGPQGPPGVEGPRGLNGPRGEKGNQGAVGVP 824
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 798-850 7.74e-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: 42.10  E-value: 7.74e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 24581824    798 GPPGVEGPRGLNGPRGEKGNQGAVGVPGNPGKDGLRGIPGRNGQPGPRGEPGI 850
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 107-161 1.22e-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: 41.33  E-value: 1.22e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24581824    107 GFPGMEGPSGDKGQKGDPGPYGQRGDKGERGSPGLHGQAGVPGVQGPAGNPGAPG 161
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 576-632 1.38e-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: 41.33  E-value: 1.38e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824    576 GPKGDKGTSGLPGIPGKDGARGPPGERGYPGERGHDGINGQTGPPGEKGEDGRTGLP 632
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1312-1368 1.45e-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: 41.33  E-value: 1.45e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824   1312 GLIGAPGLIGERGLPGLAGEPGLVGLPGPIGPAGSKGERGLAGSPGQPGQDGFPGAP 1368
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1017-1071 2.09e-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: 40.94  E-value: 2.09e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24581824   1017 LMGIKGDQGLAGAPGQQGLDGMPGEKGNQGFPGLDGPPGLPGDASEKGQKGEPGP 1071
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1315-1369 2.30e-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: 40.55  E-value: 2.30e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24581824   1315 GAPGLIGERGLPGLAGEPGLVGLPGPIGPAGSKGERGLAGSPGQPGQDGFPGAPG 1369
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 762-814 2.30e-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: 40.55  E-value: 2.30e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 24581824    762 GNKGEPGQTGMPGPPGEDGSPGERGYTGLKGNTGPQGPPGVEGPRGLNGPRGE 814
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 110-165 3.13e-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: 3.13e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24581824    110 GMEGPSGDKGQKGDPGPYGQRGDKGERGSPGLHGQAGVPGVQGPAGNPGAPGINGK 165
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 938-992 3.16e-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: 3.16e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24581824    938 GAKGEPGSPGLVGMPGNKGDRGAPGNDGPKGFAGVTGAPGKRGPAGIPGVSGAKG 992
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 887-943 3.69e-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: 3.69e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824    887 GYPGDRGDAGLPGVSGRPGIVGEKGDVGPIGPAGVAGPPGVPGIDGVRGRDGAKGEP 943
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 582-638 4.54e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 4.54e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824    582 GTSGLPGIPGKDGARGPPGERGYPGERGHDGINGQTGPPGEKGEDGRTGLPGATGEP 638
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 591-641 4.63e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 4.63e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 24581824    591 GKDGARGPPGERGYPGERGHDGINGQTGPPGEKGEDGRTGLPGATGEPGKP 641
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1037-1093 4.82e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 4.82e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824   1037 GMPGEKGNQGFPGLDGPPGLPGDASEKGQKGEPGPSGLRGDTGPAGTPGWPGEKGLP 1093
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1303-1359 5.01e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 5.01e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824   1303 GRPGRNGRQGLIGAPGLIGERGLPGLAGEPGLVGLPGPIGPAGSKGERGLAGSPGQP 1359
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 774-829 5.32e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 5.32e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24581824    774 GPPGEDGSPGERGYTGLKGNTGPQGPPGVEGPRGLNGPRGEKGNQGAVGVPGNPGK 829
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 792-848 5.75e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 5.75e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824    792 GNTGPQGPPGVEGPRGLNGPRGEKGNQGAVGVPGNPGKDGLRGIPGRNGQPGPRGEP 848
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1094-1367 6.12e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 44.64  E-value: 6.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824 1094 GLAVHGRAGPPGEKGDQGRSGIDGRDGINGEKGEQGLQGVWGQPGEKGSVGAPGIPGAPGMDGLPGAAGAPGAVGYPGDR 1173
Cdd:COG5164    2 GLYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824 1174 GDKGEPGLSGLPGLKGETGPVGLQGFTGAPGPKGERGIRGQPGlpATVPDIRGDKGSQGERGYTgekgeQGERGLTGPAG 1253
Cdd:COG5164   82 TPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGG--STTPPSGGSTTPPGDGGST-----PPGPGSTGPGG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824 1254 VAGAKGDRGLQGPPGASGLNGIPGAKGDIGPRGEIGYPGVTIKGEKGLPGRPGRNGRQGLIGAPGLIGERGlpGLAGEPG 1333
Cdd:COG5164  155 STTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGPKD 232

                        250       260       270
                 ....*....|....*....|....*....|....
gi 24581824 1334 LVGLPGPIGPAGSKGERGLAGSPGQPGQDGFPGA 1367
Cdd:COG5164  233 QRPKTNPIERRGPERPEAAALPAELTALEAENRA 266
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1342-1398 7.36e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 7.36e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824   1342 GPAGSKGERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQKGDKGDR 1398
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1333-1387 7.50e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 7.50e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24581824   1333 GLVGLPGPIGPAGSKGERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNG 1387
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1031-1085 7.50e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 7.50e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24581824   1031 GQQGLDGMPGEKGNQGFPGLDGPPGLPGDASEKGQKGEPGPSGLRGDTGPAGTPG 1085
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 840-899 8.96e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 8.96e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824    840 GQPGPRGEPGisrpgPMGPPGLNGLQGEKGDRGPTGPIGFPGADGSVGYPGDRGDAGLPG 899
Cdd:pfam01391    1 GPPGPPGPPG-----PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 926-982 9.32e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 9.32e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824    926 GVPGIDGVRGRDGAKGEPGSPGLVGMPGNKGDRGAPGNDGPKGFAGVTGAPGKRGPA 982
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1330-1384 9.32e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 9.32e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24581824   1330 GEPGLVGLPGPIGPAGSKGERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERG 1384
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 863-919 9.79e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 9.79e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824    863 GLQGEKGDRGPTGPIGFPGADGSVGYPGDRGDAGLPGVSGRPGIVGEKGDVGPIGPA 919
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 914-968 1.11e-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: 38.63  E-value: 1.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24581824    914 GPIGPAGVAGPPGVPGIDGVRGRDGAKGEPGSPGLVGMPGNKGDRGAPGNDGPKG 968
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 588-641 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: 38.63  E-value: 1.16e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 24581824    588 GIPGKDGARGPPGERGYPGERGHDGINGQTGPPGEKGEDGRTGLPGATGEPGKP 641
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 574-625 1.23e-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: 38.63  E-value: 1.23e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 24581824    574 RAGPKGDKGTSGLPGIPGKDGARGPPGERGYPGERGHDGINGQTGPPGEKGE 625
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1232-1287 1.25e-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: 38.63  E-value: 1.25e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24581824   1232 GERGYTGEKGEQGERGLTGPAGVAGAKGDRGLQGPPGASGLNGIPGAKGDIGPRGE 1287
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1025-1081 1.35e-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: 38.63  E-value: 1.35e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824   1025 GLAGAPGQQGLDGMPGEKGNQGFPGLDGPPGLPGDASEKGQKGEPGPSGLRGDTGPA 1081
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1402-1458 1.75e-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: 38.24  E-value: 1.75e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824   1402 GPSGLPGLVGQKGDTGYPGLNGNDGPVGAPGERGFTGPKGRDGRDGTPGLPGQKGEP 1458
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 834-892 2.03e-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: 37.86  E-value: 2.03e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24581824    834 GIPGRNGQPGPRGEPGisRPGPMGPPGLNGLQGEKGDRGPTGPIGFPGADGSVGYPGDR 892
Cdd:pfam01391    1 GPPGPPGPPGPPGPPG--PPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1336-1391 2.15e-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: 37.86  E-value: 2.15e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24581824   1336 GLPGPIGPAGSKGERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQ 1391
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1492-1548 2.33e-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: 37.86  E-value: 2.33e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824   1492 GIQGERGEKGERGLIGETGNVGRPGPKGDRGEPGERGYEGAIGLIGQKGEPGAPAPA 1548
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 579-634 2.37e-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: 37.86  E-value: 2.37e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24581824    579 GDKGTSGLPGIPGKDGARGPPGERGYPGERGHDGINGQTGPPGEKGEDGRTGLPGA 634
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03169 PHA03169
hypothetical protein; Provisional
 101-272 3.04e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.27  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   101 GLKGEMGFPGMEGPSGDKGQKGDPGPYGQRGDKGERGSPGLHGQAGVPGVQGPAGNPGAPGingkDGCDGQDGIPGLEGL 180
Cdd:PHA03169   82 GEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPS----HPGPHEPAPPESHNP 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581824   181 SGMPGPRGYAGqlGSKGEKGEPAKENGDYAKGEKGEPGWRGTAGLAGPQGFPGEKgERGDSGPYGAKGPRGEHGLKGEKG 260
Cdd:PHA03169  158 SPNQQPSSFLQ--PSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDE-PGEPQSPTPQQAPSPNTQQAVEHE 234

                         170
                  ....*....|..
gi 24581824   261 ASCYGPMKPGAP 272
Cdd:PHA03169  235 DEPTEPEREGPP 246
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 908-962 3.19e-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: 3.19e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24581824    908 GEKGDVGPIGPAGVAGPPGVPGIDGVRGRDGAKGEPGSPGLVGMPGNKGDRGAPG 962
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1297-1350 3.19e-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: 3.19e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 24581824   1297 GEKGLPGRPGRNGRQGLIGAPGLIGERGLPGLAGEPGLVGLPGPIGPAGSKGER 1350
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 660-714 3.22e-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: 3.22e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24581824    660 GAPGAKGVQGFKGAEGLPGIPGPKGEFGFKGEKGLSGAPGNDGTPGRAGRDGYPG 714
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 905-961 3.32e-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: 3.32e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824    905 GIVGEKGDVGPIGPAGVAGPPGVPGIDGVRGRDGAKGEPGSPGLVGMPGNKGDRGAP 961
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 585-641 3.32e-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: 3.32e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824    585 GLPGIPGKDGARGPPGERGYPGERGHDGINGQTGPPGEKGEDGRTGLPGATGEPGKP 641
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1229-1285 3.59e-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: 3.59e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824   1229 GSQGERGYTGEKGEQGERGLTGPAGVAGAKGDRGLQGPPGASGLNGIPGAKGDIGPR 1285
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1375-1431 3.96e-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: 37.09  E-value: 3.96e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824   1375 GPQGFKGERGLNGFEGQKGDKGDRGLQGPSGLPGLVGQKGDTGYPGLNGNDGPVGAP 1431
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 125-179 4.33e-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: 37.09  E-value: 4.33e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24581824    125 GPYGQRGDKGERGSPGLHGQAGVPGVQGPAGNPGAPGINGKDGCDGQDGIPGLEG 179
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 122-176 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: 37.09  E-value: 4.46e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24581824    122 GDPGPYGQRGDKGERGSPGLHGQAGVPGVQGPAGNPGAPGINGKDGCDGQDGIPG 176
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 852-905 4.64e-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: 37.09  E-value: 4.64e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 24581824    852 RPGPMGPPGLNGLQGEKGDRGPTGPIGFPGADGSVGYPGDRGDAGLPGVSGRPG 905
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1226-1280 4.92e-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: 37.09  E-value: 4.92e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24581824   1226 GDKGSQGERGYTGEKGEQGERGLTGPAGVAGAKGDRGLQGPPGASGLNGIPGAKG 1280
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1238-1292 5.02e-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: 5.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24581824   1238 GEKGEQGERGLTGPAGVAGAKGDRGLQGPPGASGLNGIPGAKGDIGPRGEIGYPG 1292
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1351-1408 5.82e-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: 5.82e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24581824   1351 GLAGSPGQPGQDGFPGAPglkGDTGPQGFKGERGLNGFEGQKGDKGDRGLQGPSGLPG 1408
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPP---GPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 654-708 6.36e-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: 6.36e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24581824    654 GDKGYPGAPGAKGVQGFKGAEGLPGIPGPKGEFGFKGEKGLSGAPGNDGTPGRAG 708
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 319-375 6.74e-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: 6.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824    319 GDTGLDGQKGEKGLPGGPGDRGRQGNFGPPGSTGQKGDRGEPGLNGLPGNPGQKGEP 375
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1475-1527 8.63e-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: 8.63e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 24581824   1475 RNGPKGEPGRPGERGLIGIQGERGEKGERGLIGETGNVGRPGPKGDRGEPGER 1527
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 131-187 9.33e-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: 9.33e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24581824    131 GDKGERGSPGLHGQAGVPGVQGPAGNPGAPGINGKDGCDGQDGIPGLEGLSGMPGPR 187
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 866-920 9.33e-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: 9.33e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24581824    866 GEKGDRGPTGPIGFPGADGSVGYPGDRGDAGLPGVSGRPGIVGEKGDVGPIGPAG 920
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
 
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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