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Conserved domains on  [gi|157082|gb|AAA28423|]
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type IV pro-collagen [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 ...
 1659-1773 3.63e-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: 207.63  E-value: 3.63e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082      1659 ANVIAVHSQTIEVPDCPNGWEGLWIGYSFLMHTAvGNGGGGQALQSPGSCLEDFRATPFIECNGaKGTCHFYE-TMTSFW 1737
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTG-NGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASrNDYSFW 78

                            90       100       110
                    ....*....|....*....|....*....|....*.
gi 157082      1738 MYNLESSQPFERPQQQTIKAGERQSHVSRCQVCMKN 1773
Cdd:smart00111   79 LSTIEPSDQFTAPRPMTPKAGDLRPYISRCQVCEKP 114
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1554-1658 3.22e-52

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: 179.12  E-value: 3.22e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082      1554 GILITRHSQSETVPACSAGHTELWTGYSLLYVDGNDYAHNQDL---GSCVPRFSTLPVLSCGQNNVCNYASRNDKTFWLT 1630
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLgspGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 157082      1631 TN-------AAIPMMPVENiEIRQYISRCVVCEAP 1658
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 5.41e-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: 131.57  E-value: 5.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     727 HGRDGAKGDKGSFGRSGEKGEPGscaldeikmpAKGNKGEPGQTGMPGPPGEDGSPGERGYTGLKGNTGPQGPPGVEGPR 806
Cdd:NF038329  113 LKGDGEKGEPGPAGPAGPAGEQG----------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     807 GLNGPRGEKGNQGAVGVPGNPGKDGLRGIPGRNGQPGPRGEPGisrpgPMGPPGlNGLQGEKGDRGPTGPIGFPGADGSV 886
Cdd:NF038329  183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDG-----PAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     887 GYPGDRGDAGLPGVSGRPGIVGEKGDVGPIGPAGVAGPPGVPGIDGVRGRDGAKGEPGSPGLVGMPGNKGDRGAPGNDGP 966
Cdd:NF038329  257 GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336


                  ..
gi 157082     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 ...
 1186-1448 4.97e-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: 122.32  E-value: 4.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1186 GLKGETGPVGLQGFTGAPGPKGERGIRGQpglpatvpdiRGDKGSQGERGYTGEKGEQGERGLTGPAGVAGAKGDRGLQG 1265
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGP----------AGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1266 PPGASGLNGIPGAKGDIGPRGEIGYPGVTikgekglpgrpgrngrqgliGAPGLIGERGLPGLPESRLVGLPGPIGPAGS 1345
Cdd:NF038329  187 PAGEKGPQGPRGETGPAGEQGPAGPAGPD--------------------GEAGPAGEDGPAGPAGDGQQGPDGDPGPTGE 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1346 KGERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQKgdkgdrglqGPSGLPGLVGQKGDTGYPGLNGNDG 1425
Cdd:NF038329  247 DGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN---------GKDGLPGKDGKDGQNGKDGLPGKDG 317

                         250       260
                  ....*....|....*....|...
gi 157082    1426 PVGAPGERGFTGPKGRDGRDGTP 1448
Cdd:NF038329  318 KDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 107-361 1.30e-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: 118.08  E-value: 1.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     107 GFPGMEGPSGDKGQKGDPGPYGQRGDKGERGSPGLHGQAGVPGVQGPAGNPGAPGINGKDGCDGQDGIPGLEGLSGMPGP 186
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     187 RGYAGQLGSKGEKGEPakengdyakGEKGEPGWRGTAGLAGPQGfPGEKGERGDSGPYGAKGPRGEHGLKGekgascygp 266
Cdd:NF038329  197 RGETGPAGEQGPAGPA---------GPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAG--------- 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     267 mKPGAPGIKGEKGEPassfpvkpthtvmGPRGDMGQKGEPGLVGRKGEPGPEGDTGLDGQKGEKGLPGGPGDRGRQGNFG 346
Cdd:NF038329  258 -KDGPRGDRGEAGPD-------------GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                         250
                  ....*....|....*
gi 157082     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 1.30e-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: 112.31  E-value: 1.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     543 GQKGDAGRPGTPGQKGDMGIKGDVGGKCSSCRAGPKGDKGTSGLPGIPGKDGARGPPGERGYPGERGHDGINGQTGPPGE 622
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     623 KGEDGRTGLPGATGEPGKpalcdlslieplKGDKGYPGAPGAKGVQGfKGAEGLPGIPGPKGEFGFKGEKGLSGAPGNDG 702
Cdd:NF038329  197 RGETGPAGEQGPAGPAGP------------DGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     703 TPGRAGRDGYPGIPGQsiKGEPGFHGRDGAKGDKGSFGRSGEKGEPGSCALDEikmpAKGNKGEPGQTGMPGPPGEDGSP 782
Cdd:NF038329  264 DRGEAGPDGPDGKDGE--RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG----KDGKDGQPGKDGLPGKDGKDGQP 337

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157082     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 ...
 1347-1554 2.27e-23

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 105.37  E-value: 2.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1347 GERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQKGDKGDRGLQGPSGLPGLVGQKGDTGYPGLNGNDGP 1426
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1427 VGAPGERGFTGPKGRDGRDGTPGLPGQKGEPGmlpppgpkgePGQPGRNGPKGEPGRPGERGLIGIQGELGEKGERGLIG 1506
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG----------PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 157082    1507 ETGNVGRPGPKGDRGEPGERGYEGAIGLIGQKGEPGAPAPAALDYLTG 1554
Cdd:NF038329  267 EAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG 314
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 355-642 4.77e-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: 101.52  E-value: 4.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     355 GDRGEPGLNGLPGNPGQKGEPGRAGATGEPGLlgppgppgggrgtpgppgpkgprgyVGAPGPQGLNGVDGLPGPQGYNG 434
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGP-------------------------AGPPGPQGERGEKGPAGPQGEAG 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     435 QKDGAGLPGRPGNEGPPGKKGEKGTAGLNGPkgsigpighpgppgpegqkgdaglpgygiqgsKGDAGIPGYPGLKGSKG 514
Cdd:NF038329  172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGP--------------------------------AGEQGPAGPAGPDGEAG 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     515 ERGFKGNAGAPGDSKLGRPGTPGAAGAPGQKGDAGRPGTPGQKGDMGIKGDVGgkcsscRAGPKGDKGTSGLPGIPGKDG 594
Cdd:NF038329  220 PAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG------PDGKDGERGPVGPAGKDGQNG 293

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 157082     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 2.09e-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: 2.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     969 FAGVTGAPGKRGPAGIPGVSGAKGDKGAsgltgndgpvggrgppgapglmgiKGDQGLAGAPGQQGLDGMPGEKGNQGFP 1048
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGE------------------------TGPAGPAGPPGPQGERGEKGPAGPQGEA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1049 GLDGPPGLPGDASEKGQKGEPGPSGLRGDTGPAGTPGWPGEKGLPGLAvhGRAGPPGEKGDQGRsGIDGRDGINGEKGEQ 1128
Cdd:NF038329  171 GPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEA--GPAGEDGPAGPAGD-GQQGPDGDPGPTGED 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1129 GLQGVWGQPGEKGSVGAPGIPGAPGMDGLPGAAGAPGAVGYPGDRGDKGEPGLSGLPGLKGETGPVGLQGFTGAPGPKGE 1208
Cdd:NF038329  248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327

                         250
                  ....*....|
gi 157082    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 ...
 1659-1773 3.63e-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: 207.63  E-value: 3.63e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082      1659 ANVIAVHSQTIEVPDCPNGWEGLWIGYSFLMHTAvGNGGGGQALQSPGSCLEDFRATPFIECNGaKGTCHFYE-TMTSFW 1737
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTG-NGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASrNDYSFW 78

                            90       100       110
                    ....*....|....*....|....*....|....*.
gi 157082      1738 MYNLESSQPFERPQQQTIKAGERQSHVSRCQVCMKN 1773
Cdd:smart00111   79 LSTIEPSDQFTAPRPMTPKAGDLRPYISRCQVCEKP 114
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1660-1772 3.07e-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: 3.07e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     1660 NVIAVHSQTIEVPDCPNGWEGLWIGYSFLMHTAVGnGGGGQALQSPGSCLEDFRATPFIECNGAkGTCHFYETMTSFWMY 1739
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78

                           90       100       110
                   ....*....|....*....|....*....|....
gi 157082     1740 NLEssQPFERPQQQTIKAGER-QSHVSRCQVCMK 1772
Cdd:pfam01413   79 TVE--EQFRKPMSQTPKAGNElRSYISRCVVCEA 110
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1554-1658 3.22e-52

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: 179.12  E-value: 3.22e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082      1554 GILITRHSQSETVPACSAGHTELWTGYSLLYVDGNDYAHNQDL---GSCVPRFSTLPVLSCGQNNVCNYASRNDKTFWLT 1630
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLgspGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 157082      1631 TN-------AAIPMMPVENiEIRQYISRCVVCEAP 1658
Cdd:smart00111   81 TIepsdqftAPRPMTPKAG-DLRPYISRCQVCEKP 114
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1555-1657 4.57e-51

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: 175.48  E-value: 4.57e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     1555 ILITRHSQSETVPACSAGHTELWTGYSLLYVDGNDYAHNQDL---GSCVPRFSTLPVLSCGQNNVCNYASrNDKTFWLTT 1631
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLgspGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 157082     1632 ---NAAIPMM--PVENIEIRQYISRCVVCEA 1657
Cdd:pfam01413   80 veeQFRKPMSqtPKAGNELRSYISRCVVCEA 110
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 727-968 5.41e-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: 131.57  E-value: 5.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     727 HGRDGAKGDKGSFGRSGEKGEPGscaldeikmpAKGNKGEPGQTGMPGPPGEDGSPGERGYTGLKGNTGPQGPPGVEGPR 806
Cdd:NF038329  113 LKGDGEKGEPGPAGPAGPAGEQG----------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     807 GLNGPRGEKGNQGAVGVPGNPGKDGLRGIPGRNGQPGPRGEPGisrpgPMGPPGlNGLQGEKGDRGPTGPIGFPGADGSV 886
Cdd:NF038329  183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDG-----PAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     887 GYPGDRGDAGLPGVSGRPGIVGEKGDVGPIGPAGVAGPPGVPGIDGVRGRDGAKGEPGSPGLVGMPGNKGDRGAPGNDGP 966
Cdd:NF038329  257 GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336


                  ..
gi 157082     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 ...
 853-1071 1.47e-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: 1.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     853 PGPMGPPGLNGLQGEKGDRGPTGPIGFPGADGSVGYPGDRGDAGLPGVSGRPGIVGEKGDVGPIGPAGVAGPPGVPGIDG 932
Cdd:NF038329  122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     933 VRGRDGAKGEPGSPGLVGMPGNKGDRGAPGN--DGPKGFAGVTGAPGKRGPAGIPGVSGAKGDKGASGLTGNDGPVGGRG 1010
Cdd:NF038329  202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157082    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 ...
 1186-1448 4.97e-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: 122.32  E-value: 4.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1186 GLKGETGPVGLQGFTGAPGPKGERGIRGQpglpatvpdiRGDKGSQGERGYTGEKGEQGERGLTGPAGVAGAKGDRGLQG 1265
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGP----------AGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1266 PPGASGLNGIPGAKGDIGPRGEIGYPGVTikgekglpgrpgrngrqgliGAPGLIGERGLPGLPESRLVGLPGPIGPAGS 1345
Cdd:NF038329  187 PAGEKGPQGPRGETGPAGEQGPAGPAGPD--------------------GEAGPAGEDGPAGPAGDGQQGPDGDPGPTGE 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1346 KGERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQKgdkgdrglqGPSGLPGLVGQKGDTGYPGLNGNDG 1425
Cdd:NF038329  247 DGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN---------GKDGLPGKDGKDGQNGKDGLPGKDG 317

                         250       260
                  ....*....|....*....|...
gi 157082    1426 PVGAPGERGFTGPKGRDGRDGTP 1448
Cdd:NF038329  318 KDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 107-361 1.30e-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: 118.08  E-value: 1.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     107 GFPGMEGPSGDKGQKGDPGPYGQRGDKGERGSPGLHGQAGVPGVQGPAGNPGAPGINGKDGCDGQDGIPGLEGLSGMPGP 186
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     187 RGYAGQLGSKGEKGEPakengdyakGEKGEPGWRGTAGLAGPQGfPGEKGERGDSGPYGAKGPRGEHGLKGekgascygp 266
Cdd:NF038329  197 RGETGPAGEQGPAGPA---------GPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAG--------- 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     267 mKPGAPGIKGEKGEPassfpvkpthtvmGPRGDMGQKGEPGLVGRKGEPGPEGDTGLDGQKGEKGLPGGPGDRGRQGNFG 346
Cdd:NF038329  258 -KDGPRGDRGEAGPD-------------GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                         250
                  ....*....|....*
gi 157082     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 ...
 1238-1484 1.79e-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: 1.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1238 GEKGEQGERGLTGPAGVAGAKGDRGLQGPPGASGLNGIPGAKGDIGPRGEIGYPGvtikgEKGLPGRPGRNGRQGLIGAP 1317
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG-----PQGPAGKDGEAGAKGPAGEK 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1318 GLIGERGLPGLPesrlvGLPGPIGPAGSKGERGLAGSPGQPGQDGfPGAPGLKGDTGPQGFKGERGLNGFEGQKGDKGDR 1397
Cdd:NF038329  192 GPQGPRGETGPA-----GEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1398 GLQGPSGLPGLVGQKGDTGYPGLNGNDGPVGAPgergftGPKGRDGRDGTPGLPGQKGEPGMlpppgpKGEPGQPGRNGP 1477
Cdd:NF038329  266 GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLP------GKDGKDGQNGKDGLPGKDGKDGQ------PGKDGLPGKDGK 333


                  ....*..
gi 157082    1478 KGEPGRP 1484
Cdd:NF038329  334 DGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 543-820 1.30e-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: 112.31  E-value: 1.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     543 GQKGDAGRPGTPGQKGDMGIKGDVGGKCSSCRAGPKGDKGTSGLPGIPGKDGARGPPGERGYPGERGHDGINGQTGPPGE 622
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     623 KGEDGRTGLPGATGEPGKpalcdlslieplKGDKGYPGAPGAKGVQGfKGAEGLPGIPGPKGEFGFKGEKGLSGAPGNDG 702
Cdd:NF038329  197 RGETGPAGEQGPAGPAGP------------DGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     703 TPGRAGRDGYPGIPGQsiKGEPGFHGRDGAKGDKGSFGRSGEKGEPGSCALDEikmpAKGNKGEPGQTGMPGPPGEDGSP 782
Cdd:NF038329  264 DRGEAGPDGPDGKDGE--RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG----KDGKDGQPGKDGLPGKDGKDGQP 337

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157082     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 1.21e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 109.22  E-value: 1.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     413 GAPGPQGLNGVDGLPGPQGYNGQKDGAGLPGRPGNEGPPGKKGEKGTAGLNGPKGSigpighpgppgpegqkgdaglpgy 492
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP------------------------ 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     493 giQGSKGDAGIPGYPGLKGSKGERGFKGNAGAPGdsKLGRPGTPGAAGAPGQKGDAGRPGtPGQKGDMGIKGDVGGKCSS 572
Cdd:NF038329  176 --AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG--PAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     573 CRAGPKGDKGTSGLPGIPGKDGARGPPGERGYPGERGHDGINGQTGPPGEKGEDGRTGLPGatgepgkpalcdlsliepL 652
Cdd:NF038329  251 GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG------------------L 312

                         250       260       270
                  ....*....|....*....|....*....|.
gi 157082     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 ...
 1335-1546 2.41e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 108.45  E-value: 2.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1335 GLPGPIGPA------GSKGERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQKGDKGDRGLQGPSGLPGL 1408
Cdd:NF038329  120 GEPGPAGPAgpageqGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1409 VGQKGDTGYPGLNGNDGPVGAPGERGFTGPKGR--DGRDGTPGLPGQKGEPGMLPPPGPKGEPGQPGRNGPKGEPGRPGE 1486
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGE 279

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157082    1487 RGLIGIQGELGEKGERGLI---GETGNVGRPGPKGDRGEPGERGYEGAIGLIGQKGEPGAPAP 1546
Cdd:NF038329  280 RGPVGPAGKDGQNGKDGLPgkdGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1347-1554 2.27e-23

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 105.37  E-value: 2.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1347 GERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQKGDKGDRGLQGPSGLPGLVGQKGDTGYPGLNGNDGP 1426
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1427 VGAPGERGFTGPKGRDGRDGTPGLPGQKGEPGmlpppgpkgePGQPGRNGPKGEPGRPGERGLIGIQGELGEKGERGLIG 1506
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG----------PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 157082    1507 ETGNVGRPGPKGDRGEPGERGYEGAIGLIGQKGEPGAPAPAALDYLTG 1554
Cdd:NF038329  267 EAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG 314
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 355-642 4.77e-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: 101.52  E-value: 4.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     355 GDRGEPGLNGLPGNPGQKGEPGRAGATGEPGLlgppgppgggrgtpgppgpkgprgyVGAPGPQGLNGVDGLPGPQGYNG 434
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGP-------------------------AGPPGPQGERGEKGPAGPQGEAG 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     435 QKDGAGLPGRPGNEGPPGKKGEKGTAGLNGPkgsigpighpgppgpegqkgdaglpgygiqgsKGDAGIPGYPGLKGSKG 514
Cdd:NF038329  172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGP--------------------------------AGEQGPAGPAGPDGEAG 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     515 ERGFKGNAGAPGDSKLGRPGTPGAAGAPGQKGDAGRPGTPGQKGDMGIKGDVGgkcsscRAGPKGDKGTSGLPGIPGKDG 594
Cdd:NF038329  220 PAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG------PDGKDGERGPVGPAGKDGQNG 293

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 157082     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 ...
 969-1218 2.09e-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: 2.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     969 FAGVTGAPGKRGPAGIPGVSGAKGDKGAsgltgndgpvggrgppgapglmgiKGDQGLAGAPGQQGLDGMPGEKGNQGFP 1048
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGE------------------------TGPAGPAGPPGPQGERGEKGPAGPQGEA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1049 GLDGPPGLPGDASEKGQKGEPGPSGLRGDTGPAGTPGWPGEKGLPGLAvhGRAGPPGEKGDQGRsGIDGRDGINGEKGEQ 1128
Cdd:NF038329  171 GPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEA--GPAGEDGPAGPAGD-GQQGPDGDPGPTGED 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1129 GLQGVWGQPGEKGSVGAPGIPGAPGMDGLPGAAGAPGAVGYPGDRGDKGEPGLSGLPGLKGETGPVGLQGFTGAPGPKGE 1208
Cdd:NF038329  248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327

                         250
                  ....*....|
gi 157082    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 1.06e-20

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: 97.28  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     276 GEKGEPASSFPVKPTHTVmGPRGDMGQKGEPGLVGRKGEPGPEGDTGLDGQKGEKGLPGGPGDRGRQGNFGPPGSTGQKG 355
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQ-GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     356 DRGEPGLNGLPGNPGQKGEPGRAGATGEPGLLGppgppgggrgtpgppgpkgprgyvgaPGPQGLNGVDGLPGPQGYNGQ 435
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG--------------------------PAGDGQQGPDGDPGPTGEDGP 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     436 KDGAGLPGRPGNEGPPGKKGEKGTAGLNGPKGSIgpighpgppgpegqkgdaglpgygiqGSKGDAGIPGYPGLKGSKGE 515
Cdd:NF038329  250 QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV--------------------------GPAGKDGQNGKDGLPGKDGK 303

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 157082     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 ...
 87-249 9.10e-17

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 84.96  E-value: 9.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082      87 EKGNRGLPGPLGPTGLKGEMGFPGMEGPSGDKGQKGDPGPYGQRGDKGERGSpGLHGQAGVPGVQGPAGNPGAPGINGKD 166
Cdd:NF038329  181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKD 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     167 GCDGQDGIPGLEGLSGMP---GPRGYAGQLGSKGEKGEPAKENGDYAKGEKGEPGWRGTAGLAGPQGFPGEKGERGDSGP 243
Cdd:NF038329  260 GPRGDRGEAGPDGPDGKDgerGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339


                  ....*.
gi 157082     244 YGAKGP 249
Cdd:NF038329  340 PAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1387-1544 1.94e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 84.19  E-value: 1.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1387 FEGQKGD------KGDRGLQGPSGLPGLVGQKGDTGYPGLNGNDGPVGAPGERGFTGPKGRDGRDGTPGL---PGQKGEP 1457
Cdd:NF038329  115 GDGEKGEpgpagpAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAkgpAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1458 GMLPPPGPKGEPGQPGRNGPKGEPGRPGERGLIGI-----QGELGEKGERGLIGETGNVGRPGPKGDRGEPGERGYEGAI 1532
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                         170
                  ....*....|..
gi 157082    1533 GLIGQKGEPGAP 1544
Cdd:NF038329  275 GKDGERGPVGPA 286
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 82-203 3.32e-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: 3.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082      82 PKCIAEKGNRGLPGPLGPTGLKGEMGFPGMEGPSGDKGQKGDPGPYGQRGDKGERGSPGLHGQAGvpgvqgpagNPGAPG 161
Cdd:NF038329  229 PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG---------KDGLPG 299

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 157082     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 ...
 1452-1575 2.78e-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: 51.83  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1452 GQKGEPGmlpppgPKGEPGQPGRNGPKGEPGRPGERGLIGIQGELGEKGERGLIGETGNVGRPGPKGDRGEPGERGYEGA 1531
Cdd:NF038329  117 GEKGEPG------PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 157082    1532 IGLIGQKGEPGAPAPAALDYLTGILITRHSQSETVPACSAGHTE 1575
Cdd:NF038329  191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ 234
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
849-1096 1.53e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 49.64  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    849 GISRPGPMGPPGLNGLQGEKGDRGPTGPigfPGADGSVGYPGDRGDAGLPGVSGRPGIVGEKGDVGPIGPAGVAGPPGVP 928
Cdd:COG5164    2 GLYGPGKTGPSDPGGVTTPAGSQGSTKP---AQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    929 GIDGVRGRDGAKGEPGSPGLVGMPGNKGDRGAPGNDGPKGFAGVTGA--PGKRGPAGIPGVSGAK-GDKGASGLTGNDGP 1005
Cdd:COG5164   79 GGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSttPPSGGSTTPPGDGGSTpPGPGSTGPGGSTTP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082   1006 VGGRGPPGAPGLMGIKG--DQGLAGAPGQQGLDGMPGEKGNQGFPGLDGPP----GLPGDASEKGQKGEPGPSGLRGDTG 1079
Cdd:COG5164  159 PGDGGSTTPPGPGGSTTppDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVkkddKNGKGNPPDDRGGKTGPKDQRPKTN 238

                        250
                 ....*....|....*..
gi 157082   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 1.75e-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: 1.75e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 157082      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 2.70e-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: 2.70e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157082      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 157082      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 2.08e-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: 2.08e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 157082     1017 LMGIKGDQGLAGAPGQQGLDGMPGEKGNQGFPGLDGPPGLPGDASEKGQKGEPGP 1071
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1341-1397 7.34e-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: 7.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157082     1341 GPAGSKGERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQKGDKGDR 1397
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1094-1366 9.05e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 43.87  E-value: 9.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082   1094 GLAVHGRAGPPGEKGDQGRSGIDGRDGINGEKGEQGLQGVWGQPGEKGSVGAPGIPGAPGMDGLPGAAGAPGAVGYPGDR 1173
Cdd:COG5164    2 GLYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082   1174 GDKGEPGLSGLPGLKGETGPVGLQGFTGAPGPKGERGIRGQPGlpATVPDIRGDKGSQGERGYTgekgeQGERGLTGPAG 1253
Cdd:COG5164   82 TPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGG--STTPPSGGSTTPPGDGGST-----PPGPGSTGPGG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082   1254 VAGAKGDRGLQGPPGASGLNGIPGAKGDIGPRGEIGYPGVTIKGEKGLPGRPGRNGRQGLIGAPGLIGERGLPGLPESRl 1333
Cdd:COG5164  155 STTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQ- 233

                        250       260       270
                 ....*....|....*....|....*....|...
gi 157082   1334 VGLPGPIGPAGSKGERGLAGSPGQPGQDGFPGA 1366
Cdd:COG5164  234 RPKTNPIERRGPERPEAAALPAELTALEAENRA 266
PHA03169 PHA03169
hypothetical protein; Provisional
 101-272 3.01e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.27  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     101 GLKGEMGFPGMEGPSGDKGQKGDPGPYGQRGDKGERGSPGLHGQAGVPGVQGPAGNPGAPGingkDGCDGQDGIPGLEGL 180
Cdd:PHA03169   82 GEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPS----HPGPHEPAPPESHNP 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     181 SGMPGPRGYAGqlGSKGEKGEPAKENGDYAKGEKGEPGWRGTAGLAGPQGFPGEKgERGDSGPYGAKGPRGEHGLKGEKG 260
Cdd:PHA03169  158 SPNQQPSSFLQ--PSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDE-PGEPQSPTPQQAPSPNTQQAVEHE 234

                         170
                  ....*....|..
gi 157082     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 ...
 1659-1773 3.63e-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: 207.63  E-value: 3.63e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082      1659 ANVIAVHSQTIEVPDCPNGWEGLWIGYSFLMHTAvGNGGGGQALQSPGSCLEDFRATPFIECNGaKGTCHFYE-TMTSFW 1737
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTG-NGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASrNDYSFW 78

                            90       100       110
                    ....*....|....*....|....*....|....*.
gi 157082      1738 MYNLESSQPFERPQQQTIKAGERQSHVSRCQVCMKN 1773
Cdd:smart00111   79 LSTIEPSDQFTAPRPMTPKAGDLRPYISRCQVCEKP 114
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1660-1772 3.07e-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: 3.07e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     1660 NVIAVHSQTIEVPDCPNGWEGLWIGYSFLMHTAVGnGGGGQALQSPGSCLEDFRATPFIECNGAkGTCHFYETMTSFWMY 1739
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78

                           90       100       110
                   ....*....|....*....|....*....|....
gi 157082     1740 NLEssQPFERPQQQTIKAGER-QSHVSRCQVCMK 1772
Cdd:pfam01413   79 TVE--EQFRKPMSQTPKAGNElRSYISRCVVCEA 110
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1554-1658 3.22e-52

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: 179.12  E-value: 3.22e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082      1554 GILITRHSQSETVPACSAGHTELWTGYSLLYVDGNDYAHNQDL---GSCVPRFSTLPVLSCGQNNVCNYASRNDKTFWLT 1630
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLgspGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 157082      1631 TN-------AAIPMMPVENiEIRQYISRCVVCEAP 1658
Cdd:smart00111   81 TIepsdqftAPRPMTPKAG-DLRPYISRCQVCEKP 114
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1555-1657 4.57e-51

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: 175.48  E-value: 4.57e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     1555 ILITRHSQSETVPACSAGHTELWTGYSLLYVDGNDYAHNQDL---GSCVPRFSTLPVLSCGQNNVCNYASrNDKTFWLTT 1631
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLgspGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 157082     1632 ---NAAIPMM--PVENIEIRQYISRCVVCEA 1657
Cdd:pfam01413   80 veeQFRKPMSqtPKAGNELRSYISRCVVCEA 110
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 727-968 5.41e-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: 131.57  E-value: 5.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     727 HGRDGAKGDKGSFGRSGEKGEPGscaldeikmpAKGNKGEPGQTGMPGPPGEDGSPGERGYTGLKGNTGPQGPPGVEGPR 806
Cdd:NF038329  113 LKGDGEKGEPGPAGPAGPAGEQG----------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     807 GLNGPRGEKGNQGAVGVPGNPGKDGLRGIPGRNGQPGPRGEPGisrpgPMGPPGlNGLQGEKGDRGPTGPIGFPGADGSV 886
Cdd:NF038329  183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDG-----PAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     887 GYPGDRGDAGLPGVSGRPGIVGEKGDVGPIGPAGVAGPPGVPGIDGVRGRDGAKGEPGSPGLVGMPGNKGDRGAPGNDGP 966
Cdd:NF038329  257 GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336


                  ..
gi 157082     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 ...
 853-1071 1.47e-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: 1.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     853 PGPMGPPGLNGLQGEKGDRGPTGPIGFPGADGSVGYPGDRGDAGLPGVSGRPGIVGEKGDVGPIGPAGVAGPPGVPGIDG 932
Cdd:NF038329  122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     933 VRGRDGAKGEPGSPGLVGMPGNKGDRGAPGN--DGPKGFAGVTGAPGKRGPAGIPGVSGAKGDKGASGLTGNDGPVGGRG 1010
Cdd:NF038329  202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157082    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 ...
 1186-1448 4.97e-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: 122.32  E-value: 4.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1186 GLKGETGPVGLQGFTGAPGPKGERGIRGQpglpatvpdiRGDKGSQGERGYTGEKGEQGERGLTGPAGVAGAKGDRGLQG 1265
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGP----------AGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1266 PPGASGLNGIPGAKGDIGPRGEIGYPGVTikgekglpgrpgrngrqgliGAPGLIGERGLPGLPESRLVGLPGPIGPAGS 1345
Cdd:NF038329  187 PAGEKGPQGPRGETGPAGEQGPAGPAGPD--------------------GEAGPAGEDGPAGPAGDGQQGPDGDPGPTGE 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1346 KGERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQKgdkgdrglqGPSGLPGLVGQKGDTGYPGLNGNDG 1425
Cdd:NF038329  247 DGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN---------GKDGLPGKDGKDGQNGKDGLPGKDG 317

                         250       260
                  ....*....|....*....|...
gi 157082    1426 PVGAPGERGFTGPKGRDGRDGTP 1448
Cdd:NF038329  318 KDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 107-361 1.30e-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: 118.08  E-value: 1.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     107 GFPGMEGPSGDKGQKGDPGPYGQRGDKGERGSPGLHGQAGVPGVQGPAGNPGAPGINGKDGCDGQDGIPGLEGLSGMPGP 186
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     187 RGYAGQLGSKGEKGEPakengdyakGEKGEPGWRGTAGLAGPQGfPGEKGERGDSGPYGAKGPRGEHGLKGekgascygp 266
Cdd:NF038329  197 RGETGPAGEQGPAGPA---------GPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAG--------- 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     267 mKPGAPGIKGEKGEPassfpvkpthtvmGPRGDMGQKGEPGLVGRKGEPGPEGDTGLDGQKGEKGLPGGPGDRGRQGNFG 346
Cdd:NF038329  258 -KDGPRGDRGEAGPD-------------GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                         250
                  ....*....|....*
gi 157082     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 ...
 1238-1484 1.79e-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: 1.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1238 GEKGEQGERGLTGPAGVAGAKGDRGLQGPPGASGLNGIPGAKGDIGPRGEIGYPGvtikgEKGLPGRPGRNGRQGLIGAP 1317
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG-----PQGPAGKDGEAGAKGPAGEK 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1318 GLIGERGLPGLPesrlvGLPGPIGPAGSKGERGLAGSPGQPGQDGfPGAPGLKGDTGPQGFKGERGLNGFEGQKGDKGDR 1397
Cdd:NF038329  192 GPQGPRGETGPA-----GEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1398 GLQGPSGLPGLVGQKGDTGYPGLNGNDGPVGAPgergftGPKGRDGRDGTPGLPGQKGEPGMlpppgpKGEPGQPGRNGP 1477
Cdd:NF038329  266 GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLP------GKDGKDGQNGKDGLPGKDGKDGQ------PGKDGLPGKDGK 333


                  ....*..
gi 157082    1478 KGEPGRP 1484
Cdd:NF038329  334 DGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 543-820 1.30e-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: 112.31  E-value: 1.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     543 GQKGDAGRPGTPGQKGDMGIKGDVGGKCSSCRAGPKGDKGTSGLPGIPGKDGARGPPGERGYPGERGHDGINGQTGPPGE 622
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     623 KGEDGRTGLPGATGEPGKpalcdlslieplKGDKGYPGAPGAKGVQGfKGAEGLPGIPGPKGEFGFKGEKGLSGAPGNDG 702
Cdd:NF038329  197 RGETGPAGEQGPAGPAGP------------DGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     703 TPGRAGRDGYPGIPGQsiKGEPGFHGRDGAKGDKGSFGRSGEKGEPGSCALDEikmpAKGNKGEPGQTGMPGPPGEDGSP 782
Cdd:NF038329  264 DRGEAGPDGPDGKDGE--RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG----KDGKDGQPGKDGLPGKDGKDGQP 337

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157082     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 1.21e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 109.22  E-value: 1.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     413 GAPGPQGLNGVDGLPGPQGYNGQKDGAGLPGRPGNEGPPGKKGEKGTAGLNGPKGSigpighpgppgpegqkgdaglpgy 492
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP------------------------ 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     493 giQGSKGDAGIPGYPGLKGSKGERGFKGNAGAPGdsKLGRPGTPGAAGAPGQKGDAGRPGtPGQKGDMGIKGDVGGKCSS 572
Cdd:NF038329  176 --AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG--PAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     573 CRAGPKGDKGTSGLPGIPGKDGARGPPGERGYPGERGHDGINGQTGPPGEKGEDGRTGLPGatgepgkpalcdlsliepL 652
Cdd:NF038329  251 GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG------------------L 312

                         250       260       270
                  ....*....|....*....|....*....|.
gi 157082     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 ...
 1335-1546 2.41e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 108.45  E-value: 2.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1335 GLPGPIGPA------GSKGERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQKGDKGDRGLQGPSGLPGL 1408
Cdd:NF038329  120 GEPGPAGPAgpageqGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1409 VGQKGDTGYPGLNGNDGPVGAPGERGFTGPKGR--DGRDGTPGLPGQKGEPGMLPPPGPKGEPGQPGRNGPKGEPGRPGE 1486
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGE 279

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157082    1487 RGLIGIQGELGEKGERGLI---GETGNVGRPGPKGDRGEPGERGYEGAIGLIGQKGEPGAPAP 1546
Cdd:NF038329  280 RGPVGPAGKDGQNGKDGLPgkdGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1347-1554 2.27e-23

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 105.37  E-value: 2.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1347 GERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQKGDKGDRGLQGPSGLPGLVGQKGDTGYPGLNGNDGP 1426
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1427 VGAPGERGFTGPKGRDGRDGTPGLPGQKGEPGmlpppgpkgePGQPGRNGPKGEPGRPGERGLIGIQGELGEKGERGLIG 1506
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG----------PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 157082    1507 ETGNVGRPGPKGDRGEPGERGYEGAIGLIGQKGEPGAPAPAALDYLTG 1554
Cdd:NF038329  267 EAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG 314
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 355-642 4.77e-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: 101.52  E-value: 4.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     355 GDRGEPGLNGLPGNPGQKGEPGRAGATGEPGLlgppgppgggrgtpgppgpkgprgyVGAPGPQGLNGVDGLPGPQGYNG 434
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGP-------------------------AGPPGPQGERGEKGPAGPQGEAG 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     435 QKDGAGLPGRPGNEGPPGKKGEKGTAGLNGPkgsigpighpgppgpegqkgdaglpgygiqgsKGDAGIPGYPGLKGSKG 514
Cdd:NF038329  172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGP--------------------------------AGEQGPAGPAGPDGEAG 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     515 ERGFKGNAGAPGDSKLGRPGTPGAAGAPGQKGDAGRPGTPGQKGDMGIKGDVGgkcsscRAGPKGDKGTSGLPGIPGKDG 594
Cdd:NF038329  220 PAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG------PDGKDGERGPVGPAGKDGQNG 293

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 157082     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 ...
 969-1218 2.09e-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: 2.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     969 FAGVTGAPGKRGPAGIPGVSGAKGDKGAsgltgndgpvggrgppgapglmgiKGDQGLAGAPGQQGLDGMPGEKGNQGFP 1048
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGE------------------------TGPAGPAGPPGPQGERGEKGPAGPQGEA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1049 GLDGPPGLPGDASEKGQKGEPGPSGLRGDTGPAGTPGWPGEKGLPGLAvhGRAGPPGEKGDQGRsGIDGRDGINGEKGEQ 1128
Cdd:NF038329  171 GPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEA--GPAGEDGPAGPAGD-GQQGPDGDPGPTGED 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1129 GLQGVWGQPGEKGSVGAPGIPGAPGMDGLPGAAGAPGAVGYPGDRGDKGEPGLSGLPGLKGETGPVGLQGFTGAPGPKGE 1208
Cdd:NF038329  248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327

                         250
                  ....*....|
gi 157082    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 1.06e-20

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: 97.28  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     276 GEKGEPASSFPVKPTHTVmGPRGDMGQKGEPGLVGRKGEPGPEGDTGLDGQKGEKGLPGGPGDRGRQGNFGPPGSTGQKG 355
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQ-GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     356 DRGEPGLNGLPGNPGQKGEPGRAGATGEPGLLGppgppgggrgtpgppgpkgprgyvgaPGPQGLNGVDGLPGPQGYNGQ 435
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG--------------------------PAGDGQQGPDGDPGPTGEDGP 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     436 KDGAGLPGRPGNEGPPGKKGEKGTAGLNGPKGSIgpighpgppgpegqkgdaglpgygiqGSKGDAGIPGYPGLKGSKGE 515
Cdd:NF038329  250 QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV--------------------------GPAGKDGQNGKDGLPGKDGK 303

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 157082     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 ...
 87-249 9.10e-17

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 84.96  E-value: 9.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082      87 EKGNRGLPGPLGPTGLKGEMGFPGMEGPSGDKGQKGDPGPYGQRGDKGERGSpGLHGQAGVPGVQGPAGNPGAPGINGKD 166
Cdd:NF038329  181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKD 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     167 GCDGQDGIPGLEGLSGMP---GPRGYAGQLGSKGEKGEPAKENGDYAKGEKGEPGWRGTAGLAGPQGFPGEKGERGDSGP 243
Cdd:NF038329  260 GPRGDRGEAGPDGPDGKDgerGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339


                  ....*.
gi 157082     244 YGAKGP 249
Cdd:NF038329  340 PAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1387-1544 1.94e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 84.19  E-value: 1.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1387 FEGQKGD------KGDRGLQGPSGLPGLVGQKGDTGYPGLNGNDGPVGAPGERGFTGPKGRDGRDGTPGL---PGQKGEP 1457
Cdd:NF038329  115 GDGEKGEpgpagpAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAkgpAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1458 GMLPPPGPKGEPGQPGRNGPKGEPGRPGERGLIGI-----QGELGEKGERGLIGETGNVGRPGPKGDRGEPGERGYEGAI 1532
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                         170
                  ....*....|..
gi 157082    1533 GLIGQKGEPGAP 1544
Cdd:NF038329  275 GKDGERGPVGPA 286
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 82-203 3.32e-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: 3.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082      82 PKCIAEKGNRGLPGPLGPTGLKGEMGFPGMEGPSGDKGQKGDPGPYGQRGDKGERGSPGLHGQAGvpgvqgpagNPGAPG 161
Cdd:NF038329  229 PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG---------KDGLPG 299

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 157082     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 ...
 1452-1575 2.78e-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: 51.83  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    1452 GQKGEPGmlpppgPKGEPGQPGRNGPKGEPGRPGERGLIGIQGELGEKGERGLIGETGNVGRPGPKGDRGEPGERGYEGA 1531
Cdd:NF038329  117 GEKGEPG------PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 157082    1532 IGLIGQKGEPGAPAPAALDYLTGILITRHSQSETVPACSAGHTE 1575
Cdd:NF038329  191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ 234
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
849-1096 1.53e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 49.64  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    849 GISRPGPMGPPGLNGLQGEKGDRGPTGPigfPGADGSVGYPGDRGDAGLPGVSGRPGIVGEKGDVGPIGPAGVAGPPGVP 928
Cdd:COG5164    2 GLYGPGKTGPSDPGGVTTPAGSQGSTKP---AQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082    929 GIDGVRGRDGAKGEPGSPGLVGMPGNKGDRGAPGNDGPKGFAGVTGA--PGKRGPAGIPGVSGAK-GDKGASGLTGNDGP 1005
Cdd:COG5164   79 GGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSttPPSGGSTTPPGDGGSTpPGPGSTGPGGSTTP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082   1006 VGGRGPPGAPGLMGIKG--DQGLAGAPGQQGLDGMPGEKGNQGFPGLDGPP----GLPGDASEKGQKGEPGPSGLRGDTG 1079
Cdd:COG5164  159 PGDGGSTTPPGPGGSTTppDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVkkddKNGKGNPPDDRGGKTGPKDQRPKTN 238

                        250
                 ....*....|....*..
gi 157082   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 1.75e-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: 1.75e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 157082      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 2.70e-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: 2.70e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157082      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 7.72e-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: 7.72e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 157082      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 1.21e-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: 1.21e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 157082      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 157082      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 2.08e-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: 2.08e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 157082     1017 LMGIKGDQGLAGAPGQQGLDGMPGEKGNQGFPGLDGPPGLPGDASEKGQKGEPGP 1071
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
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 157082      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 3.12e-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: 3.12e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 157082      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 3.15e-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: 3.15e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 157082      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 157082      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 4.53e-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: 4.53e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157082      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 4.62e-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: 4.62e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 157082      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 4.81e-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: 4.81e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157082     1037 GMPGEKGNQGFPGLDGPPGLPGDASEKGQKGEPGPSGLRGDTGPAGTPGWPGEKGLP 1093
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 774-829 5.30e-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: 39.78  E-value: 5.30e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 157082      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 5.74e-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: 5.74e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157082      792 GNTGPQGPPGVEGPRGLNGPRGEKGNQGAVGVPGNPGKDGLRGIPGRNGQPGPRGEP 848
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1341-1397 7.34e-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: 7.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157082     1341 GPAGSKGERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQKGDKGDR 1397
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1031-1085 7.49e-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: 7.49e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 157082     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 8.94e-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: 8.94e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082      840 GQPGPRGEPGisrpgPMGPPGLNGLQGEKGDRGPTGPIGFPGADGSVGYPGDRGDAGLPG 899
Cdd:pfam01391    1 GPPGPPGPPG-----PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1094-1366 9.05e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 43.87  E-value: 9.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082   1094 GLAVHGRAGPPGEKGDQGRSGIDGRDGINGEKGEQGLQGVWGQPGEKGSVGAPGIPGAPGMDGLPGAAGAPGAVGYPGDR 1173
Cdd:COG5164    2 GLYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082   1174 GDKGEPGLSGLPGLKGETGPVGLQGFTGAPGPKGERGIRGQPGlpATVPDIRGDKGSQGERGYTgekgeQGERGLTGPAG 1253
Cdd:COG5164   82 TPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGG--STTPPSGGSTTPPGDGGST-----PPGPGSTGPGG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082   1254 VAGAKGDRGLQGPPGASGLNGIPGAKGDIGPRGEIGYPGVTIKGEKGLPGRPGRNGRQGLIGAPGLIGERGLPGLPESRl 1333
Cdd:COG5164  155 STTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQ- 233

                        250       260       270
                 ....*....|....*....|....*....|...
gi 157082   1334 VGLPGPIGPAGSKGERGLAGSPGQPGQDGFPGA 1366
Cdd:COG5164  234 RPKTNPIERRGPERPEAAALPAELTALEAENRA 266
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 926-982 9.29e-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: 9.29e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157082      926 GVPGIDGVRGRDGAKGEPGSPGLVGMPGNKGDRGAPGNDGPKGFAGVTGAPGKRGPA 982
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 863-919 9.76e-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: 9.76e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157082      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 157082      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 1.15e-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: 38.63  E-value: 1.15e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 157082      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 1.22e-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: 38.63  E-value: 1.22e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 157082      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 157082     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 157082     1025 GLAGAPGQQGLDGMPGEKGNQGFPGLDGPPGLPGDASEKGQKGEPGPSGLRGDTGPA 1081
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1401-1457 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 157082     1401 GPSGLPGLVGQKGDTGYPGLNGNDGPVGAPGERGFTGPKGRDGRDGTPGLPGQKGEP 1457
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 834-892 2.02e-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: 37.86  E-value: 2.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 157082      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 ...
 1335-1390 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 157082     1335 GLPGPIGPAGSKGERGLAGSPGQPGQDGFPGAPGLKGDTGPQGFKGERGLNGFEGQ 1390
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
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 157082      579 GDKGTSGLPGIPGKDGARGPPGERGYPGERGHDGINGQTGPPGEKGEDGRTGLPGA 634
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03169 PHA03169
hypothetical protein; Provisional
 101-272 3.01e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.27  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     101 GLKGEMGFPGMEGPSGDKGQKGDPGPYGQRGDKGERGSPGLHGQAGVPGVQGPAGNPGAPGingkDGCDGQDGIPGLEGL 180
Cdd:PHA03169   82 GEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPS----HPGPHEPAPPESHNP 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157082     181 SGMPGPRGYAGqlGSKGEKGEPAKENGDYAKGEKGEPGWRGTAGLAGPQGFPGEKgERGDSGPYGAKGPRGEHGLKGEKG 260
Cdd:PHA03169  158 SPNQQPSSFLQ--PSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDE-PGEPQSPTPQQAPSPNTQQAVEHE 234

                         170
                  ....*....|..
gi 157082     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 3.18e-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: 3.18e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 157082      908 GEKGDVGPIGPAGVAGPPGVPGIDGVRGRDGAKGEPGSPGLVGMPGNKGDRGAPG 962
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 660-714 3.21e-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: 3.21e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 157082      660 GAPGAKGVQGFKGAEGLPGIPGPKGEFGFKGEKGLSGAPGNDGTPGRAGRDGYPG 714
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 585-641 3.31e-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: 3.31e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157082      585 GLPGIPGKDGARGPPGERGYPGERGHDGINGQTGPPGEKGEDGRTGLPGATGEPGKP 641
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 905-961 3.31e-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: 3.31e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157082      905 GIVGEKGDVGPIGPAGVAGPPGVPGIDGVRGRDGAKGEPGSPGLVGMPGNKGDRGAP 961
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1229-1285 3.58e-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: 3.58e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157082     1229 GSQGERGYTGEKGEQGERGLTGPAGVAGAKGDRGLQGPPGASGLNGIPGAKGDIGPR 1285
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1374-1430 3.95e-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: 3.95e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157082     1374 GPQGFKGERGLNGFEGQKGDKGDRGLQGPSGLPGLVGQKGDTGYPGLNGNDGPVGAP 1430
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 125-179 4.32e-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: 37.09  E-value: 4.32e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 157082      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 4.45e-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: 4.45e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 157082      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 4.63e-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: 37.09  E-value: 4.63e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 157082      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 4.91e-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: 4.91e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 157082     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 5.01e-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: 5.01e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 157082     1238 GEKGEQGERGLTGPAGVAGAKGDRGLQGPPGASGLNGIPGAKGDIGPRGEIGYPG 1292
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1350-1407 5.80e-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: 5.80e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 157082     1350 GLAGSPGQPGQDGFPGAPglkGDTGPQGFKGERGLNGFEGQKGDKGDRGLQGPSGLPG 1407
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPP---GPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 654-708 6.34e-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: 6.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 157082      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 6.73e-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: 6.73e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157082      319 GDTGLDGQKGEKGLPGGPGDRGRQGNFGPPGSTGQKGDRGEPGLNGLPGNPGQKGEP 375
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 131-187 9.31e-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: 9.31e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157082      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 9.31e-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: 9.31e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 157082      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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