|
Name |
Accession |
Description |
Interval |
E-value |
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1518-1631 |
1.54e-62 |
|
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: 208.22 E-value: 1.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1518 QAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTAAGaEGGGQSLVSPGSCLEDFRATPFIECSGArGTCHYFANKYSFWLT 1597
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78
|
90 100 110
....*....|....*....|....*....|....*
gi 567757604 1598 TVEErqQFGeLPVSETLKAG-QLHTRVSRCQVCMK 1631
Cdd:pfam01413 79 TVEE--QFR-KPMSQTPKAGnELRSYISRCVVCEA 110
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1410-1515 |
4.64e-56 |
|
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: 189.73 E-value: 4.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1410 YTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYArRNDKSYWLST 1489
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYA-SNDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|.
gi 567757604 1490 TA-----PIPMMPVSQTQIPQYISRCSVCEA 1515
Cdd:pfam01413 80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
926-1175 |
4.55e-24 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats. The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 107.30 E-value: 4.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 926 GSTGKMGPSGRAGTPGEKGDRGNPGPVGIPSPRRPMSNLWLKGDKGSQGSAGSNGFPGPRGDKGEAGRPGPPGLPGApgl 1005
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1006 pgiiKGVSGKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGsQGIRGSPGLPGASGLPGLKGDNGQTveisGSPGPKGQ 1085
Cdd:NF038329 194 ----QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA----GKDGPRGD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1086 PGESGFKGTKGRDGLIGNIGFPGNKGEDGKVGVSGDVGLPGAPGFPGVAGMRGEPGLPGSSGHQGAIGPLGSPGLIGPKG 1165
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKT 344
|
250
....*....|
gi 567757604 1166 PSITGVPGPA 1175
Cdd:NF038329 345 PEVPQKPDTA 354
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1117-1395 |
1.08e-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: 106.14 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1117 GVSGDVGLPGAPGFPGVAGMRGEPGLPGSSGHQGAIGPLGSPGLIGPKGPSitGVPGPAGLPGPKGEkgypgigigaPGK 1196
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ--GEAGPQGPAGKDGE----------AGA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1197 PGLRGQKGDRGFPGLQGPAGLPGAPGISLPSLIAGQPGDPGRPGLDGergrpgpagppgppgpssnQGDTGDPGFPGIPG 1276
Cdd:NF038329 185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------------------DGQQGPDGDPGPTG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1277 PKGPKGDQGIPGFSGLPGELGLKGSSGLQGDPGQTptaeavqvppGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGI 1356
Cdd:NF038329 246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER----------GPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK 315
|
250 260 270
....*....|....*....|....*....|....*....
gi 567757604 1357 PGKDgpsglpgppgalGDPGLPGLQGPPGFEGAPGQQGP 1395
Cdd:NF038329 316 DGKD------------GQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
515-750 |
1.29e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats. The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 103.06 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 515 GDRGSGGAQGPAGAPGLVGPLGPSGPKGKKGEPILSTIQGMPGDRGDSGSQGFRGVIGEPGKDGVPGLPGLPGLPGDggQ 594
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--Q 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 595 GFPGEKGLPGLPGEKGHPGPPGLPGNGLPGLPGPRGLPGDKGKDGLPGQQGLPGSKGitlPCIIPGSYGPSGFPGTPGFP 674
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG---PDGPAGKDGPRGDRGEAGPD 271
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 567757604 675 GPKGSRGLPGTPGQPGSSGSKGEPGspglvhlpeLPGFPGPRGEKGLPGFPGLPGKDGLPGMIGSPGLPGSKGATG 750
Cdd:NF038329 272 GPDGKDGERGPVGPAGKDGQNGKDG---------LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
638-871 |
1.83e-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: 102.68 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 638 DGLPGQQGLPGSKGITLPCIIPGSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRG 717
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 718 EKGLPGFPGLPGKDGLPGMIGSPGLPGSKGATGDIFGAENGAPGEQGLQGLTGHKGFLGDSGLPGLKGVHGKPGLLGPKG 797
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567757604 798 ERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAPGFPGISGHpgkkgtrgkKGPPGSIVKKGLPGLKGLPGNP 871
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGK---------DGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
44-374 |
1.30e-15 |
|
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: 81.49 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 44 EKGARGRPGPIGIQGPTGPQGFTGSTGLSGLKGERGFPGLLGPYGPKGDKGPMGVPGFLGINGIPGHPGQPGPRGPPGLD 123
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 124 GCNGTQGAVGFPGPDGypgllgppglpgQKGSKGDPVLAPGSFKGMKGDPGLPGLDGITGPQGAPGFPGAVGpagppglq 203
Cdd:NF038329 201 GPAGEQGPAGPAGPDG------------EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG-------- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 204 gppgppgplgpdgnmglgfqgekgvkgdvglpgpagpppstgelefmgfPKGKKGSKGEPGPKGFPGISGPPGFPGLGTT 283
Cdd:NF038329 261 -------------------------------------------------PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 284 GEKGekgekgipGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDVFIDIDGAvisgnPGDP 363
Cdd:NF038329 292 NGKD--------GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTA-----PHTP 358
|
330
....*....|.
gi 567757604 364 GVPGLPGLKGD 374
Cdd:NF038329 359 KTPQIPGQSKD 369
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
296-547 |
9.99e-14 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats. The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 75.33 E-value: 9.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 296 GLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDvfidiDGAVISGNPGDPGVPGLPGLKGDE 375
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ-----GEAGPQGPAGKDGEAGAKGPAGEK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 376 GIQGLRGPSGVPGLPALSGVPGALGPQGFPGLKGDQGNPGRTTIGAAGlpgrdglpgppgppgppspefetetlhnkESG 455
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG-----------------------------DPG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 456 FPGLRGEQGPKGNLGLKGIKGDSGFCACDGGVPNTGPPGEPGPP---GPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLV 532
Cdd:NF038329 243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAgkdGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322
|
250
....*....|....*
gi 567757604 533 GPLGPSGPKGKKGEP 547
Cdd:NF038329 323 GKDGLPGKDGKDGQP 337
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
891-946 |
5.60e-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: 5.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 567757604 891 LSGPKGEKGSVGFVGFPGIPGLPGIPGTRGLKGIPGSTGKMGPSGRAGTPGEKGDR 946
Cdd:pfam01391 2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1518-1631 |
1.54e-62 |
|
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: 208.22 E-value: 1.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1518 QAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTAAGaEGGGQSLVSPGSCLEDFRATPFIECSGArGTCHYFANKYSFWLT 1597
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78
|
90 100 110
....*....|....*....|....*....|....*
gi 567757604 1598 TVEErqQFGeLPVSETLKAG-QLHTRVSRCQVCMK 1631
Cdd:pfam01413 79 TVEE--QFR-KPMSQTPKAGnELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1517-1631 |
2.51e-56 |
|
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.
Pssm-ID: 128421 Cd Length: 114 Bit Score: 190.68 E-value: 2.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1517 SQAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTaAGAEGGGQSLVSPGSCLEDFRATPFIECSGaRGTCHYFANK-YSFW 1595
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASRNdYSFW 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 567757604 1596 LTTVEERQQFgELPVSETLKAGQLHTRVSRCQVCMK 1631
Cdd:smart00111 79 LSTIEPSDQF-TAPRPMTPKAGDLRPYISRCQVCEK 113
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1410-1515 |
4.64e-56 |
|
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: 189.73 E-value: 4.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1410 YTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYArRNDKSYWLST 1489
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYA-SNDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|.
gi 567757604 1490 TA-----PIPMMPVSQTQIPQYISRCSVCEA 1515
Cdd:pfam01413 80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1409-1516 |
4.97e-51 |
|
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: 175.66 E-value: 4.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1409 GYTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYARRNDKSYWLS 1488
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80
|
90 100 110
....*....|....*....|....*....|....*
gi 567757604 1489 T-------TAPIPMMPVSqTQIPQYISRCSVCEAP 1516
Cdd:smart00111 81 TiepsdqfTAPRPMTPKA-GDLRPYISRCQVCEKP 114
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
926-1175 |
4.55e-24 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 107.30 E-value: 4.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 926 GSTGKMGPSGRAGTPGEKGDRGNPGPVGIPSPRRPMSNLWLKGDKGSQGSAGSNGFPGPRGDKGEAGRPGPPGLPGApgl 1005
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1006 pgiiKGVSGKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGsQGIRGSPGLPGASGLPGLKGDNGQTveisGSPGPKGQ 1085
Cdd:NF038329 194 ----QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA----GKDGPRGD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1086 PGESGFKGTKGRDGLIGNIGFPGNKGEDGKVGVSGDVGLPGAPGFPGVAGMRGEPGLPGSSGHQGAIGPLGSPGLIGPKG 1165
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKT 344
|
250
....*....|
gi 567757604 1166 PSITGVPGPA 1175
Cdd:NF038329 345 PEVPQKPDTA 354
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1117-1395 |
1.08e-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: 106.14 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1117 GVSGDVGLPGAPGFPGVAGMRGEPGLPGSSGHQGAIGPLGSPGLIGPKGPSitGVPGPAGLPGPKGEkgypgigigaPGK 1196
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ--GEAGPQGPAGKDGE----------AGA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1197 PGLRGQKGDRGFPGLQGPAGLPGAPGISLPSLIAGQPGDPGRPGLDGergrpgpagppgppgpssnQGDTGDPGFPGIPG 1276
Cdd:NF038329 185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------------------DGQQGPDGDPGPTG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1277 PKGPKGDQGIPGFSGLPGELGLKGSSGLQGDPGQTptaeavqvppGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGI 1356
Cdd:NF038329 246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER----------GPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK 315
|
250 260 270
....*....|....*....|....*....|....*....
gi 567757604 1357 PGKDgpsglpgppgalGDPGLPGLQGPPGFEGAPGQQGP 1395
Cdd:NF038329 316 DGKD------------GQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
515-750 |
1.29e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 103.06 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 515 GDRGSGGAQGPAGAPGLVGPLGPSGPKGKKGEPILSTIQGMPGDRGDSGSQGFRGVIGEPGKDGVPGLPGLPGLPGDggQ 594
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--Q 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 595 GFPGEKGLPGLPGEKGHPGPPGLPGNGLPGLPGPRGLPGDKGKDGLPGQQGLPGSKGitlPCIIPGSYGPSGFPGTPGFP 674
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG---PDGPAGKDGPRGDRGEAGPD 271
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 567757604 675 GPKGSRGLPGTPGQPGSSGSKGEPGspglvhlpeLPGFPGPRGEKGLPGFPGLPGKDGLPGMIGSPGLPGSKGATG 750
Cdd:NF038329 272 GPDGKDGERGPVGPAGKDGQNGKDG---------LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
638-871 |
1.83e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 102.68 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 638 DGLPGQQGLPGSKGITLPCIIPGSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRG 717
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 718 EKGLPGFPGLPGKDGLPGMIGSPGLPGSKGATGDIFGAENGAPGEQGLQGLTGHKGFLGDSGLPGLKGVHGKPGLLGPKG 797
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567757604 798 ERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAPGFPGISGHpgkkgtrgkKGPPGSIVKKGLPGLKGLPGNP 871
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGK---------DGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1062-1344 |
1.08e-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: 99.98 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1062 GLPGLKGDNGQtveisGSPGPKGQPGESGFKGTKGRDGLIGNIGFPGNKGEDGKVGVSGDVGLPGAPGFPGVAGMRGEPG 1141
Cdd:NF038329 109 GLQQLKGDGEK-----GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1142 LPGSSGHQGAIGPLGSPGLIGPKGPSitGVPGPAGLPGPKGEKGYPGIGigAPGKPGLRGQKGDRGFPGLQGPAGLPGAp 1221
Cdd:NF038329 184 AKGPAGEKGPQGPRGETGPAGEQGPA--GPAGPDGEAGPAGEDGPAGPA--GDGQQGPDGDPGPTGEDGPQGPDGPAGK- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1222 gislpsliAGQPGDPGRPGLDGERGRPGPAGPPGPPGPSSNQGDTGDPGFPGIPGPKGPKGDQGIPGFSGLPGELGLKGS 1301
Cdd:NF038329 259 --------DGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 567757604 1302 SGLQGDPGQTP--TAEAVQVPPGPLGLPGIDGIPGLTGD--PGAQGP 1344
Cdd:NF038329 331 DGKDGQPGKPApkTPEVPQKPDTAPHTPKTPQIPGQSKDvtPAPQNP 377
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
783-1058 |
5.10e-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: 98.05 E-value: 5.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 783 LKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAPGFPGISGhpgkkgtrgkkgPPGSIVKKGLP 862
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG------------PQGPAGKDGEA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 863 GLKGLPGNPGLVGLKGSPGSPGVAGLPALSGPKGEKGSVGFVGFPGIPGlPGIPGTRGLKGIPGSTGKMGPSGRAGTPGE 942
Cdd:NF038329 183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGP 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 943 KGDRGNPGPvgipsprrpmsnlwlkgdKGSQGSAGSNGFPGPRGDKGEagrpgppglpgapglpgiiKGVSGKPGPPGFM 1022
Cdd:NF038329 262 RGDRGEAGP------------------DGPDGKDGERGPVGPAGKDGQ-------------------NGKDGLPGKDGKD 304
|
250 260 270
....*....|....*....|....*....|....*.
gi 567757604 1023 GIRGLPGLKGSSGITGFPGMPGESGSQGIRGSPGLP 1058
Cdd:NF038329 305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
456-725 |
2.14e-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: 96.13 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 456 FPGLRGEQGPKGNLGLKGIKGDSGfcacdggvpntgppgepgppgPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLVGPL 535
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRG---------------------DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 536 GPSGPKGKKGEPILSTIQGMPGDRGDSGSQGFRGVIGEPGKDGVPGLPGLPGLPGDGGQGFPGEKGLPGlpgekghpgpp 615
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG----------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 616 glpgnglpglpgPRGLPGDKGKDGLPGQQGLPGSKGITLPCIIPGSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSK 695
Cdd:NF038329 243 ------------PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD 310
|
250 260 270
....*....|....*....|....*....|
gi 567757604 696 GEPGSPGLVHLPELPGFPGPRGEKGLPGFP 725
Cdd:NF038329 311 GLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1159-1404 |
4.33e-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: 95.36 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1159 GLIGPKGPSITGVPGPAGLPGPKGEKGypgigigAPGKPGLRGQKGDRGFPGLQGPAGLPGAPGISlpsliaGQPGDPGR 1238
Cdd:NF038329 109 GLQQLKGDGEKGEPGPAGPAGPAGEQG-------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ------GEAGPQGP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1239 PGLDGERGRPGPAGPPGPPGPSSNQGDTGDPGFPGIPGPKGPKGDQGIPGFSGLPGelglKGSSGLQGDPGQTptaeAVQ 1318
Cdd:NF038329 176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPT----GED 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1319 VPPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGM 1398
Cdd:NF038329 248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327
|
....*.
gi 567757604 1399 PGMPGQ 1404
Cdd:NF038329 328 PGKDGK 333
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1190-1409 |
2.61e-18 |
|
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: 89.58 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1190 GIGAPGKPGLRGQKGDRGFPGLQGPAGLPGAPGISLPSLIAGQPGDPGRPGLDGERGRPGPAGPPGPPGPSSNQGDTGDP 1269
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1270 GFPGIPGPKGPKGDQGIPGFSGLPGELGLKGSSGLQGDPGQTPtaeavQVPPGPLGLPGIDGIPGLTGDPGAQGPVGLQG 1349
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGP-----DGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1350 SKGLPGIPGKDGPSGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPGQSMRVG 1409
Cdd:NF038329 270 PDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
44-374 |
1.30e-15 |
|
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: 81.49 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 44 EKGARGRPGPIGIQGPTGPQGFTGSTGLSGLKGERGFPGLLGPYGPKGDKGPMGVPGFLGINGIPGHPGQPGPRGPPGLD 123
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 124 GCNGTQGAVGFPGPDGypgllgppglpgQKGSKGDPVLAPGSFKGMKGDPGLPGLDGITGPQGAPGFPGAVGpagppglq 203
Cdd:NF038329 201 GPAGEQGPAGPAGPDG------------EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG-------- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 204 gppgppgplgpdgnmglgfqgekgvkgdvglpgpagpppstgelefmgfPKGKKGSKGEPGPKGFPGISGPPGFPGLGTT 283
Cdd:NF038329 261 -------------------------------------------------PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 284 GEKGekgekgipGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDVFIDIDGAvisgnPGDP 363
Cdd:NF038329 292 NGKD--------GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTA-----PHTP 358
|
330
....*....|.
gi 567757604 364 GVPGLPGLKGD 374
Cdd:NF038329 359 KTPQIPGQSKD 369
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
253-415 |
6.20e-14 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 76.10 E-value: 6.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 253 PKGKKGSKGEPGPKGFPGISGPPGFPGlgTTGEKGEKGEKGIPGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQG 332
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAG--PPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 333 IEGQKGDIGLPGPDVFIDIDGAVISGNPGDPGVPGLPGLKGDEGIQGLRGPSGVPGLPALSGVPGALGPQGFPGLKGDQG 412
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
|
...
gi 567757604 413 NPG 415
Cdd:NF038329 282 PVG 284
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
296-547 |
9.99e-14 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 75.33 E-value: 9.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 296 GLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDvfidiDGAVISGNPGDPGVPGLPGLKGDE 375
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ-----GEAGPQGPAGKDGEAGAKGPAGEK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 376 GIQGLRGPSGVPGLPALSGVPGALGPQGFPGLKGDQGNPGRTTIGAAGlpgrdglpgppgppgppspefetetlhnkESG 455
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG-----------------------------DPG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 456 FPGLRGEQGPKGNLGLKGIKGDSGFCACDGGVPNTGPPGEPGPP---GPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLV 532
Cdd:NF038329 243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAgkdGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322
|
250
....*....|....*
gi 567757604 533 GPLGPSGPKGKKGEP 547
Cdd:NF038329 323 GKDGLPGKDGKDGQP 337
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
20-189 |
6.96e-10 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 63.39 E-value: 6.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 20 AAGEKSYGKPCGGQDCSGSCQCFPEKGARGRPGPIGIQGPTGPQGFTGSTGLSGLKGErgfPGLLGPYGPKGDKGPMGVP 99
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP---AGEKGPQGPRGETGPAGEQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 100 GFLGINGIPGHPGQPGPRGPPGLDGcNGTQGAVGFPGPDGYPGLLGPPGLPGQKGSKGDPVLA----PGSFKGMKGDPGL 175
Cdd:NF038329 207 GPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAgpdgPDGKDGERGPVGP 285
|
170
....*....|....
gi 567757604 176 PGLDGITGPQGAPG 189
Cdd:NF038329 286 AGKDGQNGKDGLPG 299
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1298-1430 |
1.24e-05 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 49.52 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1298 LKGSSGLQGDPGQTPTAEAVqvPPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDgpsGLPGPPGALGDPGL 1377
Cdd:NF038329 107 DEGLQQLKGDGEKGEPGPAG--PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ---GEAGPQGPAGKDGE 181
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 567757604 1378 PGLQGPPGFEGAPGQQGPFGMPGMPGQSMRVGYTLVKHSQSEQVPPCPIGMSQ 1430
Cdd:NF038329 182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ 234
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
666-722 |
5.60e-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: 5.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 567757604 666 GFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRGEKGLP 722
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1170-1223 |
1.29e-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: 1.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 567757604 1170 GVPGPAGLPGPKGEKGYPGIgIGAPGKPGLRGQKGDRGFPGLQGPAGLPGAPGI 1223
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGP-PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
785-841 |
1.97e-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: 1.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 567757604 785 GVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAPGFPGISGHP 841
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1014-1070 |
2.87e-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: 2.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 567757604 1014 GKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGSQGIRGSPGLPGASGLPGLKGDN 1070
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
891-946 |
5.60e-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: 5.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 567757604 891 LSGPKGEKGSVGFVGFPGIPGLPGIPGTRGLKGIPGSTGKMGPSGRAGTPGEKGDR 946
Cdd:pfam01391 2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1518-1631 |
1.54e-62 |
|
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: 208.22 E-value: 1.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1518 QAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTAAGaEGGGQSLVSPGSCLEDFRATPFIECSGArGTCHYFANKYSFWLT 1597
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78
|
90 100 110
....*....|....*....|....*....|....*
gi 567757604 1598 TVEErqQFGeLPVSETLKAG-QLHTRVSRCQVCMK 1631
Cdd:pfam01413 79 TVEE--QFR-KPMSQTPKAGnELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1517-1631 |
2.51e-56 |
|
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.
Pssm-ID: 128421 Cd Length: 114 Bit Score: 190.68 E-value: 2.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1517 SQAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTaAGAEGGGQSLVSPGSCLEDFRATPFIECSGaRGTCHYFANK-YSFW 1595
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASRNdYSFW 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 567757604 1596 LTTVEERQQFgELPVSETLKAGQLHTRVSRCQVCMK 1631
Cdd:smart00111 79 LSTIEPSDQF-TAPRPMTPKAGDLRPYISRCQVCEK 113
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1410-1515 |
4.64e-56 |
|
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: 189.73 E-value: 4.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1410 YTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYArRNDKSYWLST 1489
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYA-SNDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|.
gi 567757604 1490 TA-----PIPMMPVSQTQIPQYISRCSVCEA 1515
Cdd:pfam01413 80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1409-1516 |
4.97e-51 |
|
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: 175.66 E-value: 4.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1409 GYTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYARRNDKSYWLS 1488
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80
|
90 100 110
....*....|....*....|....*....|....*
gi 567757604 1489 T-------TAPIPMMPVSqTQIPQYISRCSVCEAP 1516
Cdd:smart00111 81 TiepsdqfTAPRPMTPKA-GDLRPYISRCQVCEKP 114
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
926-1175 |
4.55e-24 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 107.30 E-value: 4.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 926 GSTGKMGPSGRAGTPGEKGDRGNPGPVGIPSPRRPMSNLWLKGDKGSQGSAGSNGFPGPRGDKGEAGRPGPPGLPGApgl 1005
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1006 pgiiKGVSGKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGsQGIRGSPGLPGASGLPGLKGDNGQTveisGSPGPKGQ 1085
Cdd:NF038329 194 ----QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA----GKDGPRGD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1086 PGESGFKGTKGRDGLIGNIGFPGNKGEDGKVGVSGDVGLPGAPGFPGVAGMRGEPGLPGSSGHQGAIGPLGSPGLIGPKG 1165
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKT 344
|
250
....*....|
gi 567757604 1166 PSITGVPGPA 1175
Cdd:NF038329 345 PEVPQKPDTA 354
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1117-1395 |
1.08e-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: 106.14 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1117 GVSGDVGLPGAPGFPGVAGMRGEPGLPGSSGHQGAIGPLGSPGLIGPKGPSitGVPGPAGLPGPKGEkgypgigigaPGK 1196
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ--GEAGPQGPAGKDGE----------AGA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1197 PGLRGQKGDRGFPGLQGPAGLPGAPGISLPSLIAGQPGDPGRPGLDGergrpgpagppgppgpssnQGDTGDPGFPGIPG 1276
Cdd:NF038329 185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------------------DGQQGPDGDPGPTG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1277 PKGPKGDQGIPGFSGLPGELGLKGSSGLQGDPGQTptaeavqvppGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGI 1356
Cdd:NF038329 246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER----------GPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK 315
|
250 260 270
....*....|....*....|....*....|....*....
gi 567757604 1357 PGKDgpsglpgppgalGDPGLPGLQGPPGFEGAPGQQGP 1395
Cdd:NF038329 316 DGKD------------GQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
515-750 |
1.29e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 103.06 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 515 GDRGSGGAQGPAGAPGLVGPLGPSGPKGKKGEPILSTIQGMPGDRGDSGSQGFRGVIGEPGKDGVPGLPGLPGLPGDggQ 594
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--Q 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 595 GFPGEKGLPGLPGEKGHPGPPGLPGNGLPGLPGPRGLPGDKGKDGLPGQQGLPGSKGitlPCIIPGSYGPSGFPGTPGFP 674
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG---PDGPAGKDGPRGDRGEAGPD 271
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 567757604 675 GPKGSRGLPGTPGQPGSSGSKGEPGspglvhlpeLPGFPGPRGEKGLPGFPGLPGKDGLPGMIGSPGLPGSKGATG 750
Cdd:NF038329 272 GPDGKDGERGPVGPAGKDGQNGKDG---------LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
638-871 |
1.83e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 102.68 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 638 DGLPGQQGLPGSKGITLPCIIPGSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRG 717
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 718 EKGLPGFPGLPGKDGLPGMIGSPGLPGSKGATGDIFGAENGAPGEQGLQGLTGHKGFLGDSGLPGLKGVHGKPGLLGPKG 797
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567757604 798 ERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAPGFPGISGHpgkkgtrgkKGPPGSIVKKGLPGLKGLPGNP 871
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGK---------DGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1062-1344 |
1.08e-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: 99.98 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1062 GLPGLKGDNGQtveisGSPGPKGQPGESGFKGTKGRDGLIGNIGFPGNKGEDGKVGVSGDVGLPGAPGFPGVAGMRGEPG 1141
Cdd:NF038329 109 GLQQLKGDGEK-----GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1142 LPGSSGHQGAIGPLGSPGLIGPKGPSitGVPGPAGLPGPKGEKGYPGIGigAPGKPGLRGQKGDRGFPGLQGPAGLPGAp 1221
Cdd:NF038329 184 AKGPAGEKGPQGPRGETGPAGEQGPA--GPAGPDGEAGPAGEDGPAGPA--GDGQQGPDGDPGPTGEDGPQGPDGPAGK- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1222 gislpsliAGQPGDPGRPGLDGERGRPGPAGPPGPPGPSSNQGDTGDPGFPGIPGPKGPKGDQGIPGFSGLPGELGLKGS 1301
Cdd:NF038329 259 --------DGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 567757604 1302 SGLQGDPGQTP--TAEAVQVPPGPLGLPGIDGIPGLTGD--PGAQGP 1344
Cdd:NF038329 331 DGKDGQPGKPApkTPEVPQKPDTAPHTPKTPQIPGQSKDvtPAPQNP 377
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
783-1058 |
5.10e-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: 98.05 E-value: 5.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 783 LKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAPGFPGISGhpgkkgtrgkkgPPGSIVKKGLP 862
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG------------PQGPAGKDGEA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 863 GLKGLPGNPGLVGLKGSPGSPGVAGLPALSGPKGEKGSVGFVGFPGIPGlPGIPGTRGLKGIPGSTGKMGPSGRAGTPGE 942
Cdd:NF038329 183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGP 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 943 KGDRGNPGPvgipsprrpmsnlwlkgdKGSQGSAGSNGFPGPRGDKGEagrpgppglpgapglpgiiKGVSGKPGPPGFM 1022
Cdd:NF038329 262 RGDRGEAGP------------------DGPDGKDGERGPVGPAGKDGQ-------------------NGKDGLPGKDGKD 304
|
250 260 270
....*....|....*....|....*....|....*.
gi 567757604 1023 GIRGLPGLKGSSGITGFPGMPGESGSQGIRGSPGLP 1058
Cdd:NF038329 305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
456-725 |
2.14e-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: 96.13 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 456 FPGLRGEQGPKGNLGLKGIKGDSGfcacdggvpntgppgepgppgPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLVGPL 535
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRG---------------------DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 536 GPSGPKGKKGEPILSTIQGMPGDRGDSGSQGFRGVIGEPGKDGVPGLPGLPGLPGDGGQGFPGEKGLPGlpgekghpgpp 615
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG----------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 616 glpgnglpglpgPRGLPGDKGKDGLPGQQGLPGSKGITLPCIIPGSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSK 695
Cdd:NF038329 243 ------------PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD 310
|
250 260 270
....*....|....*....|....*....|
gi 567757604 696 GEPGSPGLVHLPELPGFPGPRGEKGLPGFP 725
Cdd:NF038329 311 GLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1159-1404 |
4.33e-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: 95.36 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1159 GLIGPKGPSITGVPGPAGLPGPKGEKGypgigigAPGKPGLRGQKGDRGFPGLQGPAGLPGAPGISlpsliaGQPGDPGR 1238
Cdd:NF038329 109 GLQQLKGDGEKGEPGPAGPAGPAGEQG-------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ------GEAGPQGP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1239 PGLDGERGRPGPAGPPGPPGPSSNQGDTGDPGFPGIPGPKGPKGDQGIPGFSGLPGelglKGSSGLQGDPGQTptaeAVQ 1318
Cdd:NF038329 176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPT----GED 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1319 VPPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGM 1398
Cdd:NF038329 248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327
|
....*.
gi 567757604 1399 PGMPGQ 1404
Cdd:NF038329 328 PGKDGK 333
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1190-1409 |
2.61e-18 |
|
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: 89.58 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1190 GIGAPGKPGLRGQKGDRGFPGLQGPAGLPGAPGISLPSLIAGQPGDPGRPGLDGERGRPGPAGPPGPPGPSSNQGDTGDP 1269
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1270 GFPGIPGPKGPKGDQGIPGFSGLPGELGLKGSSGLQGDPGQTPtaeavQVPPGPLGLPGIDGIPGLTGDPGAQGPVGLQG 1349
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGP-----DGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1350 SKGLPGIPGKDGPSGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPGQSMRVG 1409
Cdd:NF038329 270 PDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
44-374 |
1.30e-15 |
|
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: 81.49 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 44 EKGARGRPGPIGIQGPTGPQGFTGSTGLSGLKGERGFPGLLGPYGPKGDKGPMGVPGFLGINGIPGHPGQPGPRGPPGLD 123
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 124 GCNGTQGAVGFPGPDGypgllgppglpgQKGSKGDPVLAPGSFKGMKGDPGLPGLDGITGPQGAPGFPGAVGpagppglq 203
Cdd:NF038329 201 GPAGEQGPAGPAGPDG------------EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG-------- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 204 gppgppgplgpdgnmglgfqgekgvkgdvglpgpagpppstgelefmgfPKGKKGSKGEPGPKGFPGISGPPGFPGLGTT 283
Cdd:NF038329 261 -------------------------------------------------PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 284 GEKGekgekgipGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDVFIDIDGAvisgnPGDP 363
Cdd:NF038329 292 NGKD--------GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTA-----PHTP 358
|
330
....*....|.
gi 567757604 364 GVPGLPGLKGD 374
Cdd:NF038329 359 KTPQIPGQSKD 369
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
253-415 |
6.20e-14 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 76.10 E-value: 6.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 253 PKGKKGSKGEPGPKGFPGISGPPGFPGlgTTGEKGEKGEKGIPGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQG 332
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAG--PPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 333 IEGQKGDIGLPGPDVFIDIDGAVISGNPGDPGVPGLPGLKGDEGIQGLRGPSGVPGLPALSGVPGALGPQGFPGLKGDQG 412
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
|
...
gi 567757604 413 NPG 415
Cdd:NF038329 282 PVG 284
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
296-547 |
9.99e-14 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 75.33 E-value: 9.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 296 GLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDvfidiDGAVISGNPGDPGVPGLPGLKGDE 375
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ-----GEAGPQGPAGKDGEAGAKGPAGEK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 376 GIQGLRGPSGVPGLPALSGVPGALGPQGFPGLKGDQGNPGRTTIGAAGlpgrdglpgppgppgppspefetetlhnkESG 455
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG-----------------------------DPG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 456 FPGLRGEQGPKGNLGLKGIKGDSGFCACDGGVPNTGPPGEPGPP---GPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLV 532
Cdd:NF038329 243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAgkdGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322
|
250
....*....|....*
gi 567757604 533 GPLGPSGPKGKKGEP 547
Cdd:NF038329 323 GKDGLPGKDGKDGQP 337
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
20-189 |
6.96e-10 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 63.39 E-value: 6.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 20 AAGEKSYGKPCGGQDCSGSCQCFPEKGARGRPGPIGIQGPTGPQGFTGSTGLSGLKGErgfPGLLGPYGPKGDKGPMGVP 99
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP---AGEKGPQGPRGETGPAGEQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 100 GFLGINGIPGHPGQPGPRGPPGLDGcNGTQGAVGFPGPDGYPGLLGPPGLPGQKGSKGDPVLA----PGSFKGMKGDPGL 175
Cdd:NF038329 207 GPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAgpdgPDGKDGERGPVGP 285
|
170
....*....|....
gi 567757604 176 PGLDGITGPQGAPG 189
Cdd:NF038329 286 AGKDGQNGKDGLPG 299
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1298-1430 |
1.24e-05 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 49.52 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 1298 LKGSSGLQGDPGQTPTAEAVqvPPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDgpsGLPGPPGALGDPGL 1377
Cdd:NF038329 107 DEGLQQLKGDGEKGEPGPAG--PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ---GEAGPQGPAGKDGE 181
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 567757604 1378 PGLQGPPGFEGAPGQQGPFGMPGMPGQSMRVGYTLVKHSQSEQVPPCPIGMSQ 1430
Cdd:NF038329 182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ 234
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
666-722 |
5.60e-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: 5.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 567757604 666 GFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRGEKGLP 722
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
681-743 |
5.94e-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: 39.40 E-value: 5.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 567757604 681 GLPGTPGQPGSSGSKGEPGSPGLvhlpelPGFPGPRGEKGLPGFPGLPGKDGLPGMIGSPGLP 743
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGP------PGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
672-734 |
7.09e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.01 E-value: 7.09e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 567757604 672 GFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLvhlpelPGFPGPRGEKGLPGFPGLPGKDGLP 734
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGE------PGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1170-1223 |
1.29e-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: 1.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 567757604 1170 GVPGPAGLPGPKGEKGYPGIgIGAPGKPGLRGQKGDRGFPGLQGPAGLPGAPGI 1223
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGP-PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
659-702 |
1.40e-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: 1.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 567757604 659 PGSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPG 702
Cdd:pfam01391 9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
663-723 |
1.70e-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: 1.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 567757604 663 GPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGlvhlpeLPGFPGPRGEKGLPG 723
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPG------PPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
785-841 |
1.97e-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: 1.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 567757604 785 GVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAPGFPGISGHP 841
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
659-718 |
2.36e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.86 E-value: 2.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 659 PGSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGlvhlpeLPGFPGPRGE 718
Cdd:pfam01391 3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG------PPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1014-1070 |
2.87e-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: 2.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 567757604 1014 GKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGSQGIRGSPGLPGASGLPGLKGDN 1070
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
696-750 |
3.74e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.09 E-value: 3.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 567757604 696 GEPGSPGLVHLPELPGFPGPRGEKGLPGFPGLPGKDGLPGMIGSPGLPGSKGATG 750
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
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| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
776-832 |
5.08e-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: 5.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 567757604 776 GDSGLPGLKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAP 832
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
891-946 |
5.60e-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: 5.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 567757604 891 LSGPKGEKGSVGFVGFPGIPGLPGIPGTRGLKGIPGSTGKMGPSGRAGTPGEKGDR 946
Cdd:pfam01391 2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
639-698 |
8.23e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.32 E-value: 8.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 567757604 639 GLPGQQGLPGSKGITLPciiPGSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEP 698
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGP---PGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
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