|
Name |
Accession |
Description |
Interval |
E-value |
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1593-1706 |
1.61e-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: 1.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1593 QAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTAAGaEGGGQSLVSPGSCLEDFRATPFIECSGArGTCHYFANKYSFWLT 1672
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78
|
90 100 110
....*....|....*....|....*....|....*
gi 578838289 1673 TVEErqQFGeLPVSETLKAG-QLHTRVSRCQVCMK 1706
Cdd:pfam01413 79 TVEE--QFR-KPMSQTPKAGnELRSYISRCVVCEA 110
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1485-1590 |
4.86e-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: 4.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1485 YTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYArRNDKSYWLST 1564
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYA-SNDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|.
gi 578838289 1565 TA-----PIPMMPVSQTQIPQYISRCSVCEA 1590
Cdd:pfam01413 80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
944-1182 |
1.35e-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: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 944 GSTGKMGPSGRAGTPGEKGDRGNPGPVGIPSPRRPMSNLWLKGDKGSQGSAGSNGFPGPRGDKGEAGRPGPPGLPGApgl 1023
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1024 pgiiKGVSGKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGsQGIRGSPGLPGASGLPGLKGDNGQTveisGSPGPKGQ 1103
Cdd:NF038329 194 ----QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA----GKDGPRGD 264
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578838289 1104 PGESGFKGTKGRDGLIGNIGFPGNKGEDGKVGVSGDVGLPGAPGFPGVAGMRGEPGLPGSSGHQGAIGPLGSPGLIGPK 1182
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
678-889 |
5.74e-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: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 678 GSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRGEKGLPGFPGLPGKDGLPGMIGS 757
Cdd:NF038329 138 GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 758 PGLPGSKGATGDIFGAENGAPGEQGLQGLTGHKGFLGDSGLPGLKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGP 837
Cdd:NF038329 218 AGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578838289 838 YGIKGKSGLPGAPGFPGISGHpgkkgtrgkKGPPGSIVKKGLPGLKGLPGNP 889
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 ... |
1240-1479 |
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 578838289 1240 GLRGQKGDRGFPGLQGPAGLPGAPGISLPSLIAGQPGDPGRPGLDGERGRPGPAGPPGPPGPSSNQGDTGDPGFPGIPGP 1319
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1320 KGPKGDQGIPGFSGLPGELGLKGMRGEPGFMGTPGkvgppgdpgfpgmKGKAGPRGSSGLQGDPGqtptaeavqvPPGPL 1399
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------------DGQQGPDGDPGPTGEDG----------PQGPD 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1400 GLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPGQ 1479
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
457-758 |
4.20e-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.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 89.19 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 457 FPGLRGEQGPKGNLGLKGIKGDSGfcacdggvpntgppgepgppgPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLVGPL 536
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRG---------------------DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 537 GPSGPKGKKGEPILSTIQGMPGDRGDSGSQGFRGVIGEPGKDGVPGLPGLPGLPGDGGQGFPGEKGLPGlpgekghpgpp 616
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG----------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 617 glpgnglpglpgPRGLPGDKGKDGLPGQQGLPGSKGDcccrevgkgdldtergitlpciiPGSYGPSGFPGTPGFPGPKG 696
Cdd:NF038329 243 ------------PTGEDGPQGPDGPAGKDGPRGDRGE-----------------------AGPDGPDGKDGERGPVGPAG 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578838289 697 SRGLPGTPGQPGSSGSKGEPGSPGLvhlpelpgfPGPRGEKGLPGFPGLPGKDGLPGMIGSP 758
Cdd:NF038329 288 KDGQNGKDGLPGKDGKDGQNGKDGL---------PGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
45-375 |
8.25e-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: 8.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 45 EKGARGRPGPIGIQGPTGPQGFTGSTGLSGLKGERGFPGLLGPYGPKGDKGPMGVPGFLGINGIPGHPGQPGPRGPPGLD 124
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 125 GCNGTQGAVGFPGPDGypgllgppglpgQKGSKGDPVLAPGSFKGMKGDPGLPGLDGITGPQGAPGFPGAVGpagppglq 204
Cdd:NF038329 201 GPAGEQGPAGPAGPDG------------EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG-------- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 205 gppgppgplgpdgnmglgfqgekgvkgdvglpgpagpppstgelefmgfPKGKKGSKGEPGPKGFPGISGPPGFPGLGTT 284
Cdd:NF038329 261 -------------------------------------------------PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 285 GEKGekgekgipGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDVFIDIDGAvisgnPGDP 364
Cdd:NF038329 292 NGKD--------GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTA-----PHTP 358
|
330
....*....|.
gi 578838289 365 GVPGLPGLKGD 375
Cdd:NF038329 359 KTPQIPGQSKD 369
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
909-964 |
5.86e-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: 36.70 E-value: 5.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 578838289 909 LSGPKGEKGSVGFVGFPGIPGLPGIPGTRGLKGIPGSTGKMGPSGRAGTPGEKGDR 964
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 ... |
1593-1706 |
1.61e-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: 1.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1593 QAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTAAGaEGGGQSLVSPGSCLEDFRATPFIECSGArGTCHYFANKYSFWLT 1672
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78
|
90 100 110
....*....|....*....|....*....|....*
gi 578838289 1673 TVEErqQFGeLPVSETLKAG-QLHTRVSRCQVCMK 1706
Cdd:pfam01413 79 TVEE--QFR-KPMSQTPKAGnELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1592-1706 |
2.53e-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: 2.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1592 SQAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTaAGAEGGGQSLVSPGSCLEDFRATPFIECSGaRGTCHYFANK-YSFW 1670
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASRNdYSFW 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 578838289 1671 LTTVEERQQFgELPVSETLKAGQLHTRVSRCQVCMK 1706
Cdd:smart00111 79 LSTIEPSDQF-TAPRPMTPKAGDLRPYISRCQVCEK 113
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1485-1590 |
4.86e-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: 4.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1485 YTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYArRNDKSYWLST 1564
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYA-SNDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|.
gi 578838289 1565 TA-----PIPMMPVSQTQIPQYISRCSVCEA 1590
Cdd:pfam01413 80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1484-1591 |
4.81e-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: 4.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1484 GYTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYARRNDKSYWLS 1563
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80
|
90 100 110
....*....|....*....|....*....|....*
gi 578838289 1564 T-------TAPIPMMPVSqTQIPQYISRCSVCEAP 1591
Cdd:smart00111 81 TiepsdqfTAPRPMTPKA-GDLRPYISRCQVCEKP 114
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
944-1182 |
1.35e-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: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 944 GSTGKMGPSGRAGTPGEKGDRGNPGPVGIPSPRRPMSNLWLKGDKGSQGSAGSNGFPGPRGDKGEAGRPGPPGLPGApgl 1023
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1024 pgiiKGVSGKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGsQGIRGSPGLPGASGLPGLKGDNGQTveisGSPGPKGQ 1103
Cdd:NF038329 194 ----QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA----GKDGPRGD 264
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578838289 1104 PGESGFKGTKGRDGLIGNIGFPGNKGEDGKVGVSGDVGLPGAPGFPGVAGMRGEPGLPGSSGHQGAIGPLGSPGLIGPK 1182
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
914-1188 |
7.20e-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: 103.83 E-value: 7.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 914 GEKGSVGFVGFPGIPGLPGIPGTRGLKGIPGSTGKMGPSGRAGTPGEKGDRGNPGPVGIPSPrrpmsnlwlKGDKGSQGS 993
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK---------DGEAGAKGP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 994 AGSNGFPGPRGdkgeagrpgppglpgapglpgiikgvsgKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGsQGIRGSP 1073
Cdd:NF038329 188 AGEKGPQGPRG----------------------------ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1074 GLPGASGLPGLKGDNGQTveisGSPGPKGQPGESGFKGTKGRDGLIGNIGFPGNKGEDGKVGvsgdvgLPGAPGFPGVAg 1153
Cdd:NF038329 239 GDPGPTGEDGPQGPDGPA----GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG------LPGKDGKDGQN- 307
|
250 260 270
....*....|....*....|....*....|....*
gi 578838289 1154 mrGEPGLPGSSGHQGAIGPLGSPGLIGPKGFPGFP 1188
Cdd:NF038329 308 --GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
801-1076 |
3.10e-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: 98.82 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 801 LKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAPGFPGISGhpgkkgtrgkkgPPGSIVKKGLP 880
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG------------PQGPAGKDGEA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 881 GLKGLPGNPGLVGLKGSPGSPGVAGLPALSGPKGEKGSVGFVGFPGIPGlPGIPGTRGLKGIPGSTGKMGPSGRAGTPGE 960
Cdd:NF038329 183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGP 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 961 KGDRGNPGPvgipsprrpmsnlwlkgdKGSQGSAGSNGFPGPRGDKGEagrpgppglpgapglpgiiKGVSGKPGPPGFM 1040
Cdd:NF038329 262 RGDRGEAGP------------------DGPDGKDGERGPVGPAGKDGQ-------------------NGKDGLPGKDGKD 304
|
250 260 270
....*....|....*....|....*....|....*.
gi 578838289 1041 GIRGLPGLKGSSGITGFPGMPGESGSQGIRGSPGLP 1076
Cdd:NF038329 305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
678-889 |
5.74e-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: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 678 GSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRGEKGLPGFPGLPGKDGLPGMIGS 757
Cdd:NF038329 138 GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 758 PGLPGSKGATGDIFGAENGAPGEQGLQGLTGHKGFLGDSGLPGLKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGP 837
Cdd:NF038329 218 AGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578838289 838 YGIKGKSGLPGAPGFPGISGHpgkkgtrgkKGPPGSIVKKGLPGLKGLPGNP 889
Cdd:NF038329 298 PGKDGKDGQNGKDGLPGKDGK---------DGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1240-1479 |
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 578838289 1240 GLRGQKGDRGFPGLQGPAGLPGAPGISLPSLIAGQPGDPGRPGLDGERGRPGPAGPPGPPGPSSNQGDTGDPGFPGIPGP 1319
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1320 KGPKGDQGIPGFSGLPGELGLKGMRGEPGFMGTPGkvgppgdpgfpgmKGKAGPRGSSGLQGDPGqtptaeavqvPPGPL 1399
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------------DGQQGPDGDPGPTGEDG----------PQGPD 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1400 GLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPGQ 1479
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1200-1470 |
7.38e-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: 94.59 E-value: 7.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1200 KGTHGTPGPSITGVPGPAGLPGPKGEKGypgigigAPGKPGLRGQKGDRGFPGLQGPAGLPGAPGISlpsliaGQPGDPG 1279
Cdd:NF038329 108 EGLQQLKGDGEKGEPGPAGPAGPAGEQG-------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ------GEAGPQG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1280 RPGLDGERGRPGPAGPPGPpgpssnQGDTGDPGFPGIPGPKGPKGDQGIPGFSGLPGELGLKGmRGEPGFMGTPGKVGPP 1359
Cdd:NF038329 175 PAGKDGEAGAKGPAGEKGP------QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGED 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1360 GDPGFPGMKGKAGPRGSSGLQGDPGQTPTAEavqvPPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDgpsg 1439
Cdd:NF038329 248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG----ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD---- 319
|
250 260 270
....*....|....*....|....*....|.
gi 578838289 1440 lpgppgalGDPGLPGLQGPPGFEGAPGQQGP 1470
Cdd:NF038329 320 --------GQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
457-758 |
4.20e-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: 89.19 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 457 FPGLRGEQGPKGNLGLKGIKGDSGfcacdggvpntgppgepgppgPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLVGPL 536
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRG---------------------DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 537 GPSGPKGKKGEPILSTIQGMPGDRGDSGSQGFRGVIGEPGKDGVPGLPGLPGLPGDGGQGFPGEKGLPGlpgekghpgpp 616
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG----------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 617 glpgnglpglpgPRGLPGDKGKDGLPGQQGLPGSKGDcccrevgkgdldtergitlpciiPGSYGPSGFPGTPGFPGPKG 696
Cdd:NF038329 243 ------------PTGEDGPQGPDGPAGKDGPRGDRGE-----------------------AGPDGPDGKDGERGPVGPAG 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578838289 697 SRGLPGTPGQPGSSGSKGEPGSPGLvhlpelpgfPGPRGEKGLPGFPGLPGKDGLPGMIGSP 758
Cdd:NF038329 288 KDGQNGKDGLPGKDGKDGQNGKDGL---------PGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
45-375 |
8.25e-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: 8.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 45 EKGARGRPGPIGIQGPTGPQGFTGSTGLSGLKGERGFPGLLGPYGPKGDKGPMGVPGFLGINGIPGHPGQPGPRGPPGLD 124
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 125 GCNGTQGAVGFPGPDGypgllgppglpgQKGSKGDPVLAPGSFKGMKGDPGLPGLDGITGPQGAPGFPGAVGpagppglq 204
Cdd:NF038329 201 GPAGEQGPAGPAGPDG------------EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG-------- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 205 gppgppgplgpdgnmglgfqgekgvkgdvglpgpagpppstgelefmgfPKGKKGSKGEPGPKGFPGISGPPGFPGLGTT 284
Cdd:NF038329 261 -------------------------------------------------PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 285 GEKGekgekgipGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDVFIDIDGAvisgnPGDP 364
Cdd:NF038329 292 NGKD--------GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTA-----PHTP 358
|
330
....*....|.
gi 578838289 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 ... |
456-719 |
2.66e-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: 80.33 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 456 GFPGLRGEQGPKGNLGLKGIKGDSGFCACDGGVPNTGPPGEPGPPGPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLVGP 535
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 536 LGPSGPKGKKGEPILSTIQGMPGDRGDsGSQGFRGVIGEPGKDgvpglpglpglpgdggqGFPGEKGLPGLPGEKghpgp 615
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGED-----------------GPQGPDGPAGKDGPR----- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 616 pglpgnglpglpGPRGLPGDKGKDGLPGQQGLPGskgdcccrEVGKGDLDTERGitlpciIPGSYGPSGFPGTPGFPGPK 695
Cdd:NF038329 263 ------------GDRGEAGPDGPDGKDGERGPVG--------PAGKDGQNGKDG------LPGKDGKDGQNGKDGLPGKD 316
|
250 260
....*....|....*....|....
gi 578838289 696 GSRGLPGTPGQPGSSGSKGEPGSP 719
Cdd:NF038329 317 GKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1283-1478 |
1.97e-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: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1283 LDGERGRPGPAGPPGPPGPSSNQGDTGDPGFPGIPGPKGPKGDQGIPGFSGLPGELGLKGMRGEPGFMGTPGKVGPPGDP 1362
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1363 GFPGMKGKAGPRGSSGLQGDPGQT-PTAEAVQVPPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLP 1441
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAgPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274
|
170 180 190
....*....|....*....|....*....|....*..
gi 578838289 1442 GPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPG 1478
Cdd:NF038329 275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
254-416 |
4.76e-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: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 254 PKGKKGSKGEPGPKGFPGISGPPGFPGlgTTGEKGEKGEKGIPGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQG 333
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAG--PPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 334 IEGQKGDIGLPGPDVFIDIDGAVISGNPGDPGVPGLPGLKGDEGIQGLRGPSGVPGLPALSGVPGALGPQGFPGLKGDQG 413
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
|
...
gi 578838289 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 ... |
297-548 |
7.28e-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: 7.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 297 GLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDvfidiDGAVISGNPGDPGVPGLPGLKGDE 376
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ-----GEAGPQGPAGKDGEAGAKGPAGEK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 377 GIQGLRGPSGVPGLPALSGVPGALGPQGFPGLKGDQGNPGRTTIGAAGlpgrdglpgppgppgppspefetetlhnkESG 456
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG-----------------------------DPG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 457 FPGLRGEQGPKGNLGLKGIKGDSGFCACDGGVPNTGPPGEPGPP---GPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLV 533
Cdd:NF038329 243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAgkdGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322
|
250
....*....|....*
gi 578838289 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 ... |
21-190 |
5.55e-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: 5.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 21 AAGEKSYGKPCGGQDCSGSCQCFPEKGARGRPGPIGIQGPTGPQGFTGSTGLSGLKGErgfPGLLGPYGPKGDKGPMGVP 100
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP---AGEKGPQGPRGETGPAGEQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 101 GFLGINGIPGHPGQPGPRGPPGLDGcNGTQGAVGFPGPDGYPGLLGPPGLPGQKGSKGDPVLA----PGSFKGMKGDPGL 176
Cdd:NF038329 207 GPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAgpdgPDGKDGERGPVGP 285
|
170
....*....|....
gi 578838289 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 ... |
1395-1505 |
1.47e-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: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1395 PPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDgpsGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMP 1474
Cdd:NF038329 127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ---GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203
|
90 100 110
....*....|....*....|....*....|.
gi 578838289 1475 GMPGQSMRVGYTLVKHSQSEQVPPCPIGMSQ 1505
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ 234
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1399-1502 |
2.85e-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: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1399 LGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPG 1478
Cdd:NF038329 113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192
|
90 100
....*....|....*....|....
gi 578838289 1479 QSMRVGYTLVKHSQSEQVPPCPIG 1502
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGPAGPDG 216
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1153-1208 |
5.00e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.78 E-value: 5.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 578838289 1153 GMRGEPGLPGSSGHQGAIGPLGSPGLIGPKGFPGFPGLHGLNGLPGTKGTHGTPGP 1208
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
684-740 |
5.86e-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: 5.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 578838289 684 GFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRGEKGLP 740
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
909-964 |
5.86e-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: 36.70 E-value: 5.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 578838289 909 LSGPKGEKGSVGFVGFPGIPGLPGIPGTRGLKGIPGSTGKMGPSGRAGTPGEKGDR 964
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 ... |
1593-1706 |
1.61e-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: 1.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1593 QAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTAAGaEGGGQSLVSPGSCLEDFRATPFIECSGArGTCHYFANKYSFWLT 1672
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78
|
90 100 110
....*....|....*....|....*....|....*
gi 578838289 1673 TVEErqQFGeLPVSETLKAG-QLHTRVSRCQVCMK 1706
Cdd:pfam01413 79 TVEE--QFR-KPMSQTPKAGnELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1592-1706 |
2.53e-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: 2.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1592 SQAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTaAGAEGGGQSLVSPGSCLEDFRATPFIECSGaRGTCHYFANK-YSFW 1670
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASRNdYSFW 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 578838289 1671 LTTVEERQQFgELPVSETLKAGQLHTRVSRCQVCMK 1706
Cdd:smart00111 79 LSTIEPSDQF-TAPRPMTPKAGDLRPYISRCQVCEK 113
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1485-1590 |
4.86e-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: 4.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1485 YTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYArRNDKSYWLST 1564
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYA-SNDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|.
gi 578838289 1565 TA-----PIPMMPVSQTQIPQYISRCSVCEA 1590
Cdd:pfam01413 80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1484-1591 |
4.81e-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: 4.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1484 GYTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYARRNDKSYWLS 1563
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80
|
90 100 110
....*....|....*....|....*....|....*
gi 578838289 1564 T-------TAPIPMMPVSqTQIPQYISRCSVCEAP 1591
Cdd:smart00111 81 TiepsdqfTAPRPMTPKA-GDLRPYISRCQVCEKP 114
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
944-1182 |
1.35e-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: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 944 GSTGKMGPSGRAGTPGEKGDRGNPGPVGIPSPRRPMSNLWLKGDKGSQGSAGSNGFPGPRGDKGEAGRPGPPGLPGApgl 1023
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1024 pgiiKGVSGKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGsQGIRGSPGLPGASGLPGLKGDNGQTveisGSPGPKGQ 1103
Cdd:NF038329 194 ----QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA----GKDGPRGD 264
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578838289 1104 PGESGFKGTKGRDGLIGNIGFPGNKGEDGKVGVSGDVGLPGAPGFPGVAGMRGEPGLPGSSGHQGAIGPLGSPGLIGPK 1182
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
914-1188 |
7.20e-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: 103.83 E-value: 7.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 914 GEKGSVGFVGFPGIPGLPGIPGTRGLKGIPGSTGKMGPSGRAGTPGEKGDRGNPGPVGIPSPrrpmsnlwlKGDKGSQGS 993
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK---------DGEAGAKGP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 994 AGSNGFPGPRGdkgeagrpgppglpgapglpgiikgvsgKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGsQGIRGSP 1073
Cdd:NF038329 188 AGEKGPQGPRG----------------------------ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1074 GLPGASGLPGLKGDNGQTveisGSPGPKGQPGESGFKGTKGRDGLIGNIGFPGNKGEDGKVGvsgdvgLPGAPGFPGVAg 1153
Cdd:NF038329 239 GDPGPTGEDGPQGPDGPA----GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG------LPGKDGKDGQN- 307
|
250 260 270
....*....|....*....|....*....|....*
gi 578838289 1154 mrGEPGLPGSSGHQGAIGPLGSPGLIGPKGFPGFP 1188
Cdd:NF038329 308 --GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
801-1076 |
3.10e-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: 98.82 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 801 LKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAPGFPGISGhpgkkgtrgkkgPPGSIVKKGLP 880
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG------------PQGPAGKDGEA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 881 GLKGLPGNPGLVGLKGSPGSPGVAGLPALSGPKGEKGSVGFVGFPGIPGlPGIPGTRGLKGIPGSTGKMGPSGRAGTPGE 960
Cdd:NF038329 183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGP 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 961 KGDRGNPGPvgipsprrpmsnlwlkgdKGSQGSAGSNGFPGPRGDKGEagrpgppglpgapglpgiiKGVSGKPGPPGFM 1040
Cdd:NF038329 262 RGDRGEAGP------------------DGPDGKDGERGPVGPAGKDGQ-------------------NGKDGLPGKDGKD 304
|
250 260 270
....*....|....*....|....*....|....*.
gi 578838289 1041 GIRGLPGLKGSSGITGFPGMPGESGSQGIRGSPGLP 1076
Cdd:NF038329 305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
678-889 |
5.74e-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: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 678 GSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRGEKGLPGFPGLPGKDGLPGMIGS 757
Cdd:NF038329 138 GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 758 PGLPGSKGATGDIFGAENGAPGEQGLQGLTGHKGFLGDSGLPGLKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGP 837
Cdd:NF038329 218 AGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578838289 838 YGIKGKSGLPGAPGFPGISGHpgkkgtrgkKGPPGSIVKKGLPGLKGLPGNP 889
Cdd:NF038329 298 PGKDGKDGQNGKDGLPGKDGK---------DGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1240-1479 |
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 578838289 1240 GLRGQKGDRGFPGLQGPAGLPGAPGISLPSLIAGQPGDPGRPGLDGERGRPGPAGPPGPPGPSSNQGDTGDPGFPGIPGP 1319
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1320 KGPKGDQGIPGFSGLPGELGLKGMRGEPGFMGTPGkvgppgdpgfpgmKGKAGPRGSSGLQGDPGqtptaeavqvPPGPL 1399
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------------DGQQGPDGDPGPTGEDG----------PQGPD 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1400 GLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPGQ 1479
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1200-1470 |
7.38e-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: 94.59 E-value: 7.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1200 KGTHGTPGPSITGVPGPAGLPGPKGEKGypgigigAPGKPGLRGQKGDRGFPGLQGPAGLPGAPGISlpsliaGQPGDPG 1279
Cdd:NF038329 108 EGLQQLKGDGEKGEPGPAGPAGPAGEQG-------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ------GEAGPQG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1280 RPGLDGERGRPGPAGPPGPpgpssnQGDTGDPGFPGIPGPKGPKGDQGIPGFSGLPGELGLKGmRGEPGFMGTPGKVGPP 1359
Cdd:NF038329 175 PAGKDGEAGAKGPAGEKGP------QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGED 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1360 GDPGFPGMKGKAGPRGSSGLQGDPGQTPTAEavqvPPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDgpsg 1439
Cdd:NF038329 248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG----ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD---- 319
|
250 260 270
....*....|....*....|....*....|.
gi 578838289 1440 lpgppgalGDPGLPGLQGPPGFEGAPGQQGP 1470
Cdd:NF038329 320 --------GQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
457-758 |
4.20e-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: 89.19 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 457 FPGLRGEQGPKGNLGLKGIKGDSGfcacdggvpntgppgepgppgPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLVGPL 536
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRG---------------------DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 537 GPSGPKGKKGEPILSTIQGMPGDRGDSGSQGFRGVIGEPGKDGVPGLPGLPGLPGDGGQGFPGEKGLPGlpgekghpgpp 616
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG----------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 617 glpgnglpglpgPRGLPGDKGKDGLPGQQGLPGSKGDcccrevgkgdldtergitlpciiPGSYGPSGFPGTPGFPGPKG 696
Cdd:NF038329 243 ------------PTGEDGPQGPDGPAGKDGPRGDRGE-----------------------AGPDGPDGKDGERGPVGPAG 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578838289 697 SRGLPGTPGQPGSSGSKGEPGSPGLvhlpelpgfPGPRGEKGLPGFPGLPGKDGLPGMIGSP 758
Cdd:NF038329 288 KDGQNGKDGLPGKDGKDGQNGKDGL---------PGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
45-375 |
8.25e-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: 8.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 45 EKGARGRPGPIGIQGPTGPQGFTGSTGLSGLKGERGFPGLLGPYGPKGDKGPMGVPGFLGINGIPGHPGQPGPRGPPGLD 124
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 125 GCNGTQGAVGFPGPDGypgllgppglpgQKGSKGDPVLAPGSFKGMKGDPGLPGLDGITGPQGAPGFPGAVGpagppglq 204
Cdd:NF038329 201 GPAGEQGPAGPAGPDG------------EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG-------- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 205 gppgppgplgpdgnmglgfqgekgvkgdvglpgpagpppstgelefmgfPKGKKGSKGEPGPKGFPGISGPPGFPGLGTT 284
Cdd:NF038329 261 -------------------------------------------------PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 285 GEKGekgekgipGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDVFIDIDGAvisgnPGDP 364
Cdd:NF038329 292 NGKD--------GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTA-----PHTP 358
|
330
....*....|.
gi 578838289 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 ... |
456-719 |
2.66e-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: 80.33 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 456 GFPGLRGEQGPKGNLGLKGIKGDSGFCACDGGVPNTGPPGEPGPPGPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLVGP 535
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 536 LGPSGPKGKKGEPILSTIQGMPGDRGDsGSQGFRGVIGEPGKDgvpglpglpglpgdggqGFPGEKGLPGLPGEKghpgp 615
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGED-----------------GPQGPDGPAGKDGPR----- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 616 pglpgnglpglpGPRGLPGDKGKDGLPGQQGLPGskgdcccrEVGKGDLDTERGitlpciIPGSYGPSGFPGTPGFPGPK 695
Cdd:NF038329 263 ------------GDRGEAGPDGPDGKDGERGPVG--------PAGKDGQNGKDG------LPGKDGKDGQNGKDGLPGKD 316
|
250 260
....*....|....*....|....
gi 578838289 696 GSRGLPGTPGQPGSSGSKGEPGSP 719
Cdd:NF038329 317 GKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1283-1478 |
1.97e-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: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1283 LDGERGRPGPAGPPGPPGPSSNQGDTGDPGFPGIPGPKGPKGDQGIPGFSGLPGELGLKGMRGEPGFMGTPGKVGPPGDP 1362
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1363 GFPGMKGKAGPRGSSGLQGDPGQT-PTAEAVQVPPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLP 1441
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAgPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274
|
170 180 190
....*....|....*....|....*....|....*..
gi 578838289 1442 GPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPG 1478
Cdd:NF038329 275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
254-416 |
4.76e-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: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 254 PKGKKGSKGEPGPKGFPGISGPPGFPGlgTTGEKGEKGEKGIPGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQG 333
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAG--PPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 334 IEGQKGDIGLPGPDVFIDIDGAVISGNPGDPGVPGLPGLKGDEGIQGLRGPSGVPGLPALSGVPGALGPQGFPGLKGDQG 413
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
|
...
gi 578838289 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 ... |
297-548 |
7.28e-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: 7.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 297 GLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDvfidiDGAVISGNPGDPGVPGLPGLKGDE 376
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ-----GEAGPQGPAGKDGEAGAKGPAGEK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 377 GIQGLRGPSGVPGLPALSGVPGALGPQGFPGLKGDQGNPGRTTIGAAGlpgrdglpgppgppgppspefetetlhnkESG 456
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG-----------------------------DPG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 457 FPGLRGEQGPKGNLGLKGIKGDSGFCACDGGVPNTGPPGEPGPP---GPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLV 533
Cdd:NF038329 243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAgkdGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322
|
250
....*....|....*
gi 578838289 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 ... |
21-190 |
5.55e-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: 5.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 21 AAGEKSYGKPCGGQDCSGSCQCFPEKGARGRPGPIGIQGPTGPQGFTGSTGLSGLKGErgfPGLLGPYGPKGDKGPMGVP 100
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP---AGEKGPQGPRGETGPAGEQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 101 GFLGINGIPGHPGQPGPRGPPGLDGcNGTQGAVGFPGPDGYPGLLGPPGLPGQKGSKGDPVLA----PGSFKGMKGDPGL 176
Cdd:NF038329 207 GPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAgpdgPDGKDGERGPVGP 285
|
170
....*....|....
gi 578838289 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 ... |
1395-1505 |
1.47e-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: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1395 PPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDgpsGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMP 1474
Cdd:NF038329 127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ---GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203
|
90 100 110
....*....|....*....|....*....|.
gi 578838289 1475 GMPGQSMRVGYTLVKHSQSEQVPPCPIGMSQ 1505
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ 234
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1399-1502 |
2.85e-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: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 1399 LGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPG 1478
Cdd:NF038329 113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192
|
90 100
....*....|....*....|....
gi 578838289 1479 QSMRVGYTLVKHSQSEQVPPCPIG 1502
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGPAGPDG 216
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1153-1208 |
5.00e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.78 E-value: 5.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 578838289 1153 GMRGEPGLPGSSGHQGAIGPLGSPGLIGPKGFPGFPGLHGLNGLPGTKGTHGTPGP 1208
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
684-740 |
5.86e-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: 5.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 578838289 684 GFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRGEKGLP 740
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
699-761 |
6.21e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.40 E-value: 6.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578838289 699 GLPGTPGQPGSSGSKGEPGSPGLvhlpelPGFPGPRGEKGLPGFPGLPGKDGLPGMIGSPGLP 761
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGP------PGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
690-752 |
7.42e-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: 7.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578838289 690 GFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLvhlpelPGFPGPRGEKGLPGFPGLPGKDGLP 752
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGE------PGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
677-720 |
1.46e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 38.24 E-value: 1.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 578838289 677 PGSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPG 720
Cdd:pfam01391 9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
681-741 |
1.78e-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: 38.24 E-value: 1.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578838289 681 GPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGlvhlpeLPGFPGPRGEKGLPG 741
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPG------PPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
803-859 |
2.06e-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: 2.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 578838289 803 GVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAPGFPGISGHP 859
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
677-736 |
2.46e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.86 E-value: 2.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838289 677 PGSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGlvhlpeLPGFPGPRGE 736
Cdd:pfam01391 3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG------PPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1032-1088 |
3.00e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.47 E-value: 3.00e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 578838289 1032 GKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGSQGIRGSPGLPGASGLPGLKGDN 1088
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
714-768 |
3.92e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.09 E-value: 3.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 578838289 714 GEPGSPGLVHLPELPGFPGPRGEKGLPGFPGLPGKDGLPGMIGSPGLPGSKGATG 768
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
794-850 |
5.31e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.70 E-value: 5.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 578838289 794 GDSGLPGLKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAP 850
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1132-1186 |
5.42e-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: 5.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 578838289 1132 GKVGVSGDVGLPGAPGFPGVAGMRGEPGLPGSSGHQGAIGPLGSPGLIGPKGFPG 1186
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
909-964 |
5.86e-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: 36.70 E-value: 5.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 578838289 909 LSGPKGEKGSVGFVGFPGIPGLPGIPGTRGLKGIPGSTGKMGPSGRAGTPGEKGDR 964
Cdd:pfam01391 2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1138-1192 |
9.05e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 35.93 E-value: 9.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 578838289 1138 GDVGLPGAPGFPGVAGMRGEPGLPGSSGHQGAIGPLGSPGLIGPKGFPGFPGLHG 1192
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| |
