|
Name |
Accession |
Description |
Interval |
E-value |
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1570-1683 |
1.52e-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: 1.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1570 QAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTAAGaEGGGQSLVSPGSCLEDFRATPFIECSGArGTCHYFANKYSFWLT 1649
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78
|
90 100 110
....*....|....*....|....*....|....*
gi 2462628177 1650 TVEErqQFGeLPVSETLKAG-QLHTRVSRCQVCMK 1683
Cdd:pfam01413 79 TVEE--QFR-KPMSQTPKAGnELRSYISRCVVCEA 110
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1462-1567 |
4.66e-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: 4.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1462 YTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYArRNDKSYWLST 1541
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYA-SNDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|.
gi 2462628177 1542 TA-----PIPMMPVSQTQIPQYISRCSVCEA 1567
Cdd:pfam01413 80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
945-1194 |
2.81e-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: 108.07 E-value: 2.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 945 GSTGKMGPSGRAGTPGEKGDRGNPGPVGIPSPRRPMSNLWLKGDKGSQGSAGSNGFPGPRGDKGEAGRPGPPGLPGApgl 1024
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1025 pgiiKGVSGKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGsQGIRGSPGLPGASGLPGLKGDNGQTveisGSPGPKGQ 1104
Cdd:NF038329 194 ----QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA----GKDGPRGD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1105 PGESGFKGTKGRDGLIGNIGFPGNKGEDGKVGVSGDVGLPGAPGFPGVAGMRGEPGLPGSSGHQGAIGPLGSPGLIGPKG 1184
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKT 344
|
250
....*....|
gi 2462628177 1185 PSITGVPGPA 1194
Cdd:NF038329 345 PEVPQKPDTA 354
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
679-890 |
5.60e-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: 98.05 E-value: 5.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 679 GSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRGEKGLPGFPGLPGKDGLPGMIGS 758
Cdd:NF038329 138 GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 759 PGLPGSKGATGDIFGAENGAPGEQGLQGLTGHKGFLGDSGLPGLKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGP 838
Cdd:NF038329 218 AGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462628177 839 YGIKGKSGLPGAPGFPGISGHpgkkgtrgkKGPPGSIVKKGLPGLKGLPGNP 890
Cdd:NF038329 298 PGKDGKDGQNGKDGLPGKDGK---------DGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1217-1456 |
6.52e-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: 97.67 E-value: 6.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1217 GLRGQKGDRGFPGLQGPAGLPGAPGISLPSLIAGQPGDPGRPGLDGERGRPGPAGPPGPPGPSSNQGDTGDPGFPGIPGP 1296
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1297 KGPKGDQGIPGFSGLPGELGLKGMRGEPGFMGTPGkvgppgdpgfpgmKGKAGPRGSSGLQGDPGqtptaeavqvPPGPL 1376
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------------DGQQGPDGDPGPTGEDG----------PQGPD 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1377 GLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPGQ 1456
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
457-720 |
3.47e-19 |
|
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: 92.66 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 457 FPGLRGEQGPKGNLGLKGIKGDSGfcacdggvpntgppgepgppgPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLVGPL 536
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRG---------------------DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 537 GPSGPKGKKGEPILSTIQGMPGDRGDSGSQGFRGVIGEPGKDGVPGLPGLPGLPGDGGQGFPGEKGLPGLPGEKghpgpp 616
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGED------ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 617 glpgnglpGLPGPRGLPGDKGKDGLPGQQGLPGSKGDCCCREKVGKGDLDTERGitlPCIIPGSYGPSGFPGTPGFPGPK 696
Cdd:NF038329 248 --------GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG---KDGLPGKDGKDGQNGKDGLPGKD 316
|
250 260
....*....|....*....|....
gi 2462628177 697 GSRGLPGTPGQPGSSGSKGEPGSP 720
Cdd:NF038329 317 GKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
45-375 |
8.19e-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.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 81.88 E-value: 8.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 45 EKGARGRPGPIGIQGPTGPQGFTGSTGLSGLKGERGFPGLLGPYGPKGDKGPMGVPGFLGINGIPGHPGQPGPRGPPGLD 124
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 125 GCNGTQGAVGFPGPDGypgllgppglpgQKGSKGDPVLAPGSFKGMKGDPGLPGLDGITGPQGAPGFPGAVGpagppglq 204
Cdd:NF038329 201 GPAGEQGPAGPAGPDG------------EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG-------- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 205 gppgppgplgpdgnmglgfqgekgvkgdvglpgpagpppstgelefmgfPKGKKGSKGEPGPKGFPGISGPPGFPGLGTT 284
Cdd:NF038329 261 -------------------------------------------------PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 285 GEKGekgekgipGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDVFIDIDGAvisgnPGDP 364
Cdd:NF038329 292 NGKD--------GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTA-----PHTP 358
|
330
....*....|.
gi 2462628177 365 GVPGLPGLKGD 375
Cdd:NF038329 359 KTPQIPGQSKD 369
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
910-965 |
5.78e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
:
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.70 E-value: 5.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462628177 910 LSGPKGEKGSVGFVGFPGIPGLPGIPGTRGLKGIPGSTGKMGPSGRAGTPGEKGDR 965
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 ... |
1570-1683 |
1.52e-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: 1.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1570 QAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTAAGaEGGGQSLVSPGSCLEDFRATPFIECSGArGTCHYFANKYSFWLT 1649
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78
|
90 100 110
....*....|....*....|....*....|....*
gi 2462628177 1650 TVEErqQFGeLPVSETLKAG-QLHTRVSRCQVCMK 1683
Cdd:pfam01413 79 TVEE--QFR-KPMSQTPKAGnELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1569-1683 |
2.20e-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: 191.06 E-value: 2.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1569 SQAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTaAGAEGGGQSLVSPGSCLEDFRATPFIECSGaRGTCHYFANK-YSFW 1647
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASRNdYSFW 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 2462628177 1648 LTTVEERQQFgELPVSETLKAGQLHTRVSRCQVCMK 1683
Cdd:smart00111 79 LSTIEPSDQF-TAPRPMTPKAGDLRPYISRCQVCEK 113
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1462-1567 |
4.66e-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: 4.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1462 YTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYArRNDKSYWLST 1541
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYA-SNDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|.
gi 2462628177 1542 TA-----PIPMMPVSQTQIPQYISRCSVCEA 1567
Cdd:pfam01413 80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1461-1568 |
4.27e-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: 4.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1461 GYTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYARRNDKSYWLS 1540
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80
|
90 100 110
....*....|....*....|....*....|....*
gi 2462628177 1541 T-------TAPIPMMPVSqTQIPQYISRCSVCEAP 1568
Cdd:smart00111 81 TiepsdqfTAPRPMTPKA-GDLRPYISRCQVCEKP 114
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
945-1194 |
2.81e-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: 108.07 E-value: 2.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 945 GSTGKMGPSGRAGTPGEKGDRGNPGPVGIPSPRRPMSNLWLKGDKGSQGSAGSNGFPGPRGDKGEAGRPGPPGLPGApgl 1024
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1025 pgiiKGVSGKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGsQGIRGSPGLPGASGLPGLKGDNGQTveisGSPGPKGQ 1104
Cdd:NF038329 194 ----QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA----GKDGPRGD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1105 PGESGFKGTKGRDGLIGNIGFPGNKGEDGKVGVSGDVGLPGAPGFPGVAGMRGEPGLPGSSGHQGAIGPLGSPGLIGPKG 1184
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKT 344
|
250
....*....|
gi 2462628177 1185 PSITGVPGPA 1194
Cdd:NF038329 345 PEVPQKPDTA 354
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
802-1077 |
3.22e-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: 98.82 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 802 LKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAPGFPGISGhpgkkgtrgkkgPPGSIVKKGLP 881
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG------------PQGPAGKDGEA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 882 GLKGLPGNPGLVGLKGSPGSPGVAGLPALSGPKGEKGSVGFVGFPGIPGlPGIPGTRGLKGIPGSTGKMGPSGRAGTPGE 961
Cdd:NF038329 183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGP 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 962 KGDRGNPGPvgipsprrpmsnlwlkgdKGSQGSAGSNGFPGPRGDKGEagrpgppglpgapglpgiiKGVSGKPGPPGFM 1041
Cdd:NF038329 262 RGDRGEAGP------------------DGPDGKDGERGPVGPAGKDGQ-------------------NGKDGLPGKDGKD 304
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462628177 1042 GIRGLPGLKGSSGITGFPGMPGESGSQGIRGSPGLP 1077
Cdd:NF038329 305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
679-890 |
5.60e-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: 5.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 679 GSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRGEKGLPGFPGLPGKDGLPGMIGS 758
Cdd:NF038329 138 GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 759 PGLPGSKGATGDIFGAENGAPGEQGLQGLTGHKGFLGDSGLPGLKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGP 838
Cdd:NF038329 218 AGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462628177 839 YGIKGKSGLPGAPGFPGISGHpgkkgtrgkKGPPGSIVKKGLPGLKGLPGNP 890
Cdd:NF038329 298 PGKDGKDGQNGKDGLPGKDGK---------DGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1217-1456 |
6.52e-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: 97.67 E-value: 6.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1217 GLRGQKGDRGFPGLQGPAGLPGAPGISLPSLIAGQPGDPGRPGLDGERGRPGPAGPPGPPGPSSNQGDTGDPGFPGIPGP 1296
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1297 KGPKGDQGIPGFSGLPGELGLKGMRGEPGFMGTPGkvgppgdpgfpgmKGKAGPRGSSGLQGDPGqtptaeavqvPPGPL 1376
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------------DGQQGPDGDPGPTGEDG----------PQGPD 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1377 GLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPGQ 1456
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1183-1447 |
9.34e-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: 94.20 E-value: 9.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1183 KGPSITGVPGPAGLPGPKGEKGypgigigAPGKPGLRGQKGDRGFPGLQGPAGLPGAPGISlpsliaGQPGDPGRPGLDG 1262
Cdd:NF038329 114 KGDGEKGEPGPAGPAGPAGEQG-------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ------GEAGPQGPAGKDG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1263 ERGRPGPAGPPGPpgpssnQGDTGDPGFPGIPGPKGPKGDQGIPGFSGLPGELGLKGmRGEPGFMGTPGKVGPPGDPGFP 1342
Cdd:NF038329 181 EAGAKGPAGEKGP------QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPD 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1343 GMKGKAGPRGSSGLQGDPGQTPTAEavqvPPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDgpsglpgppg 1422
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDG----ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD---------- 319
|
250 260
....*....|....*....|....*
gi 2462628177 1423 alGDPGLPGLQGPPGFEGAPGQQGP 1447
Cdd:NF038329 320 --GQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
457-720 |
3.47e-19 |
|
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: 92.66 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 457 FPGLRGEQGPKGNLGLKGIKGDSGfcacdggvpntgppgepgppgPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLVGPL 536
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRG---------------------DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 537 GPSGPKGKKGEPILSTIQGMPGDRGDSGSQGFRGVIGEPGKDGVPGLPGLPGLPGDGGQGFPGEKGLPGLPGEKghpgpp 616
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGED------ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 617 glpgnglpGLPGPRGLPGDKGKDGLPGQQGLPGSKGDCCCREKVGKGDLDTERGitlPCIIPGSYGPSGFPGTPGFPGPK 696
Cdd:NF038329 248 --------GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG---KDGLPGKDGKDGQNGKDGLPGKD 316
|
250 260
....*....|....*....|....
gi 2462628177 697 GSRGLPGTPGQPGSSGSKGEPGSP 720
Cdd:NF038329 317 GKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
509-769 |
2.00e-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: 89.96 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 509 PGLKGARGDRGSGGAQGPAGAPGLVGPLGPSGPKGKKGEPILSTIQGMPGDRGDSGSQGFRGVIGEPGKDGVPGLPGLPG 588
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 589 LPGDggQGFPGEKGLPGLPGEKGHPGPPGLPGNglpglpgprglpGDKGKDGLPGQQGLPGSKGdcccreKVGKgdldte 668
Cdd:NF038329 202 PAGE--QGPAGPAGPDGEAGPAGEDGPAGPAGD------------GQQGPDGDPGPTGEDGPQG------PDGP------ 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 669 rgitlpciiPGSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGspglvhlpeLPGFPGPRGEKGLPGFPGLPG 748
Cdd:NF038329 256 ---------AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG---------LPGKDGKDGQNGKDGLPGKDG 317
|
250 260
....*....|....*....|.
gi 2462628177 749 KDGLPGMIGSPGLPGSKGATG 769
Cdd:NF038329 318 KDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
45-375 |
8.19e-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: 81.88 E-value: 8.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 45 EKGARGRPGPIGIQGPTGPQGFTGSTGLSGLKGERGFPGLLGPYGPKGDKGPMGVPGFLGINGIPGHPGQPGPRGPPGLD 124
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 125 GCNGTQGAVGFPGPDGypgllgppglpgQKGSKGDPVLAPGSFKGMKGDPGLPGLDGITGPQGAPGFPGAVGpagppglq 204
Cdd:NF038329 201 GPAGEQGPAGPAGPDG------------EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG-------- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 205 gppgppgplgpdgnmglgfqgekgvkgdvglpgpagpppstgelefmgfPKGKKGSKGEPGPKGFPGISGPPGFPGLGTT 284
Cdd:NF038329 261 -------------------------------------------------PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 285 GEKGekgekgipGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDVFIDIDGAvisgnPGDP 364
Cdd:NF038329 292 NGKD--------GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTA-----PHTP 358
|
330
....*....|.
gi 2462628177 365 GVPGLPGLKGD 375
Cdd:NF038329 359 KTPQIPGQSKD 369
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1260-1455 |
1.99e-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: 77.64 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1260 LDGERGRPGPAGPPGPPGPSSNQGDTGDPGFPGIPGPKGPKGDQGIPGFSGLPGELGLKGMRGEPGFMGTPGKVGPPGDP 1339
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1340 GFPGMKGKAGPRGSSGLQGDPGQT-PTAEAVQVPPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLP 1418
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAgPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462628177 1419 GPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPG 1455
Cdd:NF038329 275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
297-548 |
2.19e-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: 77.64 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 297 GLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDvfidiDGAVISGNPGDPGVPGLPGLKGDE 376
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ-----GEAGPQGPAGKDGEAGAKGPAGEK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 377 GIQGLRGPSGVPGLPALSGVPGALGPQGFPGLKGDQGNPGRTTIGAAGlpgrdglpgppgppgppspefetetlhnkEPG 456
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG-----------------------------DPG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 457 FPGLRGEQGPKGNLGLKGIKGDSGFCACDGGVPNTGPPGEPGPP---GPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLV 533
Cdd:NF038329 243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAgkdGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322
|
250
....*....|....*
gi 2462628177 534 GPLGPSGPKGKKGEP 548
Cdd:NF038329 323 GKDGLPGKDGKDGQP 337
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
254-416 |
4.57e-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: 76.48 E-value: 4.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 254 PKGKKGSKGEPGPKGFPGISGPPGFPGlgTTGEKGEKGEKGIPGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQG 333
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAG--PPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 334 IEGQKGDIGLPGPDVFIDIDGAVISGNPGDPGVPGLPGLKGDEGIQGLRGPSGVPGLPALSGVPGALGPQGFPGLKGDQG 413
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
|
...
gi 2462628177 414 NPG 416
Cdd:NF038329 282 PVG 284
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
21-190 |
5.60e-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: 63.77 E-value: 5.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 21 AAGEKSYGKPCGGQDCSGSCQCFPEKGARGRPGPIGIQGPTGPQGFTGSTGLSGLKGErgfPGLLGPYGPKGDKGPMGVP 100
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP---AGEKGPQGPRGETGPAGEQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 101 GFLGINGIPGHPGQPGPRGPPGLDGcNGTQGAVGFPGPDGYPGLLGPPGLPGQKGSKGDPVLA----PGSFKGMKGDPGL 176
Cdd:NF038329 207 GPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAgpdgPDGKDGERGPVGP 285
|
170
....*....|....
gi 2462628177 177 PGLDGITGPQGAPG 190
Cdd:NF038329 286 AGKDGQNGKDGLPG 299
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1372-1482 |
1.45e-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: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1372 PPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDgpsGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMP 1451
Cdd:NF038329 127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ---GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203
|
90 100 110
....*....|....*....|....*....|.
gi 2462628177 1452 GMPGQSMRVGYTLVKHSQSEQVPPCPIGMSQ 1482
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ 234
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1376-1479 |
2.83e-04 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 45.28 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1376 LGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPG 1455
Cdd:NF038329 113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192
|
90 100
....*....|....*....|....
gi 2462628177 1456 QSMRVGYTLVKHSQSEQVPPCPIG 1479
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGPAGPDG 216
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
685-741 |
5.78e-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: 5.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462628177 685 GFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRGEKGLP 741
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1033-1089 |
2.96e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.47 E-value: 2.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462628177 1033 GKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGSQGIRGSPGLPGASGLPGLKGDN 1089
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
910-965 |
5.78e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.70 E-value: 5.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462628177 910 LSGPKGEKGSVGFVGFPGIPGLPGIPGTRGLKGIPGSTGKMGPSGRAGTPGEKGDR 965
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 ... |
1570-1683 |
1.52e-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: 1.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1570 QAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTAAGaEGGGQSLVSPGSCLEDFRATPFIECSGArGTCHYFANKYSFWLT 1649
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78
|
90 100 110
....*....|....*....|....*....|....*
gi 2462628177 1650 TVEErqQFGeLPVSETLKAG-QLHTRVSRCQVCMK 1683
Cdd:pfam01413 79 TVEE--QFR-KPMSQTPKAGnELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1569-1683 |
2.20e-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: 191.06 E-value: 2.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1569 SQAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTaAGAEGGGQSLVSPGSCLEDFRATPFIECSGaRGTCHYFANK-YSFW 1647
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASRNdYSFW 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 2462628177 1648 LTTVEERQQFgELPVSETLKAGQLHTRVSRCQVCMK 1683
Cdd:smart00111 79 LSTIEPSDQF-TAPRPMTPKAGDLRPYISRCQVCEK 113
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1462-1567 |
4.66e-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: 4.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1462 YTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYArRNDKSYWLST 1541
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYA-SNDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|.
gi 2462628177 1542 TA-----PIPMMPVSQTQIPQYISRCSVCEA 1567
Cdd:pfam01413 80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1461-1568 |
4.27e-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: 4.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1461 GYTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYARRNDKSYWLS 1540
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80
|
90 100 110
....*....|....*....|....*....|....*
gi 2462628177 1541 T-------TAPIPMMPVSqTQIPQYISRCSVCEAP 1568
Cdd:smart00111 81 TiepsdqfTAPRPMTPKA-GDLRPYISRCQVCEKP 114
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
945-1194 |
2.81e-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: 108.07 E-value: 2.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 945 GSTGKMGPSGRAGTPGEKGDRGNPGPVGIPSPRRPMSNLWLKGDKGSQGSAGSNGFPGPRGDKGEAGRPGPPGLPGApgl 1024
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1025 pgiiKGVSGKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGsQGIRGSPGLPGASGLPGLKGDNGQTveisGSPGPKGQ 1104
Cdd:NF038329 194 ----QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA----GKDGPRGD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1105 PGESGFKGTKGRDGLIGNIGFPGNKGEDGKVGVSGDVGLPGAPGFPGVAGMRGEPGLPGSSGHQGAIGPLGSPGLIGPKG 1184
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKT 344
|
250
....*....|
gi 2462628177 1185 PSITGVPGPA 1194
Cdd:NF038329 345 PEVPQKPDTA 354
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
802-1077 |
3.22e-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: 98.82 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 802 LKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAPGFPGISGhpgkkgtrgkkgPPGSIVKKGLP 881
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG------------PQGPAGKDGEA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 882 GLKGLPGNPGLVGLKGSPGSPGVAGLPALSGPKGEKGSVGFVGFPGIPGlPGIPGTRGLKGIPGSTGKMGPSGRAGTPGE 961
Cdd:NF038329 183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGP 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 962 KGDRGNPGPvgipsprrpmsnlwlkgdKGSQGSAGSNGFPGPRGDKGEagrpgppglpgapglpgiiKGVSGKPGPPGFM 1041
Cdd:NF038329 262 RGDRGEAGP------------------DGPDGKDGERGPVGPAGKDGQ-------------------NGKDGLPGKDGKD 304
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462628177 1042 GIRGLPGLKGSSGITGFPGMPGESGSQGIRGSPGLP 1077
Cdd:NF038329 305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
679-890 |
5.60e-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: 5.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 679 GSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRGEKGLPGFPGLPGKDGLPGMIGS 758
Cdd:NF038329 138 GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 759 PGLPGSKGATGDIFGAENGAPGEQGLQGLTGHKGFLGDSGLPGLKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGP 838
Cdd:NF038329 218 AGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462628177 839 YGIKGKSGLPGAPGFPGISGHpgkkgtrgkKGPPGSIVKKGLPGLKGLPGNP 890
Cdd:NF038329 298 PGKDGKDGQNGKDGLPGKDGK---------DGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1217-1456 |
6.52e-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: 97.67 E-value: 6.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1217 GLRGQKGDRGFPGLQGPAGLPGAPGISLPSLIAGQPGDPGRPGLDGERGRPGPAGPPGPPGPSSNQGDTGDPGFPGIPGP 1296
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1297 KGPKGDQGIPGFSGLPGELGLKGMRGEPGFMGTPGkvgppgdpgfpgmKGKAGPRGSSGLQGDPGqtptaeavqvPPGPL 1376
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------------DGQQGPDGDPGPTGEDG----------PQGPD 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1377 GLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPGQ 1456
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1183-1447 |
9.34e-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: 94.20 E-value: 9.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1183 KGPSITGVPGPAGLPGPKGEKGypgigigAPGKPGLRGQKGDRGFPGLQGPAGLPGAPGISlpsliaGQPGDPGRPGLDG 1262
Cdd:NF038329 114 KGDGEKGEPGPAGPAGPAGEQG-------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ------GEAGPQGPAGKDG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1263 ERGRPGPAGPPGPpgpssnQGDTGDPGFPGIPGPKGPKGDQGIPGFSGLPGELGLKGmRGEPGFMGTPGKVGPPGDPGFP 1342
Cdd:NF038329 181 EAGAKGPAGEKGP------QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPD 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1343 GMKGKAGPRGSSGLQGDPGQTPTAEavqvPPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDgpsglpgppg 1422
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDG----ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD---------- 319
|
250 260
....*....|....*....|....*
gi 2462628177 1423 alGDPGLPGLQGPPGFEGAPGQQGP 1447
Cdd:NF038329 320 --GQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
457-720 |
3.47e-19 |
|
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: 92.66 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 457 FPGLRGEQGPKGNLGLKGIKGDSGfcacdggvpntgppgepgppgPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLVGPL 536
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRG---------------------DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 537 GPSGPKGKKGEPILSTIQGMPGDRGDSGSQGFRGVIGEPGKDGVPGLPGLPGLPGDGGQGFPGEKGLPGLPGEKghpgpp 616
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGED------ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 617 glpgnglpGLPGPRGLPGDKGKDGLPGQQGLPGSKGDCCCREKVGKGDLDTERGitlPCIIPGSYGPSGFPGTPGFPGPK 696
Cdd:NF038329 248 --------GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG---KDGLPGKDGKDGQNGKDGLPGKD 316
|
250 260
....*....|....*....|....
gi 2462628177 697 GSRGLPGTPGQPGSSGSKGEPGSP 720
Cdd:NF038329 317 GKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
509-769 |
2.00e-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: 89.96 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 509 PGLKGARGDRGSGGAQGPAGAPGLVGPLGPSGPKGKKGEPILSTIQGMPGDRGDSGSQGFRGVIGEPGKDGVPGLPGLPG 588
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 589 LPGDggQGFPGEKGLPGLPGEKGHPGPPGLPGNglpglpgprglpGDKGKDGLPGQQGLPGSKGdcccreKVGKgdldte 668
Cdd:NF038329 202 PAGE--QGPAGPAGPDGEAGPAGEDGPAGPAGD------------GQQGPDGDPGPTGEDGPQG------PDGP------ 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 669 rgitlpciiPGSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGspglvhlpeLPGFPGPRGEKGLPGFPGLPG 748
Cdd:NF038329 256 ---------AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG---------LPGKDGKDGQNGKDGLPGKDG 317
|
250 260
....*....|....*....|.
gi 2462628177 749 KDGLPGMIGSPGLPGSKGATG 769
Cdd:NF038329 318 KDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
45-375 |
8.19e-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: 81.88 E-value: 8.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 45 EKGARGRPGPIGIQGPTGPQGFTGSTGLSGLKGERGFPGLLGPYGPKGDKGPMGVPGFLGINGIPGHPGQPGPRGPPGLD 124
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 125 GCNGTQGAVGFPGPDGypgllgppglpgQKGSKGDPVLAPGSFKGMKGDPGLPGLDGITGPQGAPGFPGAVGpagppglq 204
Cdd:NF038329 201 GPAGEQGPAGPAGPDG------------EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG-------- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 205 gppgppgplgpdgnmglgfqgekgvkgdvglpgpagpppstgelefmgfPKGKKGSKGEPGPKGFPGISGPPGFPGLGTT 284
Cdd:NF038329 261 -------------------------------------------------PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 285 GEKGekgekgipGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDVFIDIDGAvisgnPGDP 364
Cdd:NF038329 292 NGKD--------GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTA-----PHTP 358
|
330
....*....|.
gi 2462628177 365 GVPGLPGLKGD 375
Cdd:NF038329 359 KTPQIPGQSKD 369
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1260-1455 |
1.99e-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: 77.64 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1260 LDGERGRPGPAGPPGPPGPSSNQGDTGDPGFPGIPGPKGPKGDQGIPGFSGLPGELGLKGMRGEPGFMGTPGKVGPPGDP 1339
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1340 GFPGMKGKAGPRGSSGLQGDPGQT-PTAEAVQVPPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLP 1418
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAgPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462628177 1419 GPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPG 1455
Cdd:NF038329 275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
297-548 |
2.19e-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: 77.64 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 297 GLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDvfidiDGAVISGNPGDPGVPGLPGLKGDE 376
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ-----GEAGPQGPAGKDGEAGAKGPAGEK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 377 GIQGLRGPSGVPGLPALSGVPGALGPQGFPGLKGDQGNPGRTTIGAAGlpgrdglpgppgppgppspefetetlhnkEPG 456
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG-----------------------------DPG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 457 FPGLRGEQGPKGNLGLKGIKGDSGFCACDGGVPNTGPPGEPGPP---GPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLV 533
Cdd:NF038329 243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAgkdGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322
|
250
....*....|....*
gi 2462628177 534 GPLGPSGPKGKKGEP 548
Cdd:NF038329 323 GKDGLPGKDGKDGQP 337
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
254-416 |
4.57e-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: 76.48 E-value: 4.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 254 PKGKKGSKGEPGPKGFPGISGPPGFPGlgTTGEKGEKGEKGIPGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQG 333
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAG--PPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 334 IEGQKGDIGLPGPDVFIDIDGAVISGNPGDPGVPGLPGLKGDEGIQGLRGPSGVPGLPALSGVPGALGPQGFPGLKGDQG 413
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
|
...
gi 2462628177 414 NPG 416
Cdd:NF038329 282 PVG 284
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
21-190 |
5.60e-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: 63.77 E-value: 5.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 21 AAGEKSYGKPCGGQDCSGSCQCFPEKGARGRPGPIGIQGPTGPQGFTGSTGLSGLKGErgfPGLLGPYGPKGDKGPMGVP 100
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP---AGEKGPQGPRGETGPAGEQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 101 GFLGINGIPGHPGQPGPRGPPGLDGcNGTQGAVGFPGPDGYPGLLGPPGLPGQKGSKGDPVLA----PGSFKGMKGDPGL 176
Cdd:NF038329 207 GPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAgpdgPDGKDGERGPVGP 285
|
170
....*....|....
gi 2462628177 177 PGLDGITGPQGAPG 190
Cdd:NF038329 286 AGKDGQNGKDGLPG 299
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1372-1482 |
1.45e-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: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1372 PPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDgpsGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMP 1451
Cdd:NF038329 127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ---GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203
|
90 100 110
....*....|....*....|....*....|.
gi 2462628177 1452 GMPGQSMRVGYTLVKHSQSEQVPPCPIGMSQ 1482
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ 234
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1376-1479 |
2.83e-04 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 45.28 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 1376 LGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPG 1455
Cdd:NF038329 113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192
|
90 100
....*....|....*....|....
gi 2462628177 1456 QSMRVGYTLVKHSQSEQVPPCPIG 1479
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGPAGPDG 216
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
685-741 |
5.78e-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: 5.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462628177 685 GFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRGEKGLP 741
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
700-762 |
6.13e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.40 E-value: 6.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462628177 700 GLPGTPGQPGSSGSKGEPGSPGLvhlpelPGFPGPRGEKGLPGFPGLPGKDGLPGMIGSPGLP 762
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGP------PGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
691-753 |
7.32e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.01 E-value: 7.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462628177 691 GFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLvhlpelPGFPGPRGEKGLPGFPGLPGKDGLP 753
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGE------PGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1189-1242 |
1.33e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 38.24 E-value: 1.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462628177 1189 GVPGPAGLPGPKGEKGYPGIgIGAPGKPGLRGQKGDRGFPGLQGPAGLPGAPGI 1242
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGP-PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
678-721 |
1.44e-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: 1.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2462628177 678 PGSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPG 721
Cdd:pfam01391 9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
682-742 |
1.76e-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: 1.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462628177 682 GPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGlvhlpeLPGFPGPRGEKGLPG 742
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPG------PPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
804-860 |
2.04e-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: 2.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462628177 804 GVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAPGFPGISGHP 860
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
678-737 |
2.43e-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: 2.43e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628177 678 PGSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGlvhlpeLPGFPGPRGE 737
Cdd:pfam01391 3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG------PPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1033-1089 |
2.96e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.47 E-value: 2.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462628177 1033 GKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGSQGIRGSPGLPGASGLPGLKGDN 1089
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
715-769 |
3.86e-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: 3.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462628177 715 GEPGSPGLVHLPELPGFPGPRGEKGLPGFPGLPGKDGLPGMIGSPGLPGSKGATG 769
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
795-851 |
5.24e-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: 5.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462628177 795 GDSGLPGLKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAP 851
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
910-965 |
5.78e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.70 E-value: 5.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462628177 910 LSGPKGEKGSVGFVGFPGIPGLPGIPGTRGLKGIPGSTGKMGPSGRAGTPGEKGDR 965
Cdd:pfam01391 2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| |
