|
Name |
Accession |
Description |
Interval |
E-value |
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1565-1678 |
1.23e-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: 208.60 E-value: 1.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1565 QAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTAAGaEGGGQSLVSPGSCLEDFRATPFIECSGArGTCHYFANKYSFWLT 1644
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78
|
90 100 110
....*....|....*....|....*....|....*
gi 768037311 1645 TVEErqQFGeLPVSETLKAG-QLHTRVSRCQVCMK 1678
Cdd:pfam01413 79 TVEE--QFR-KPMSQTPKAGnELRSYISRCVVCEA 110
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1457-1562 |
3.83e-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: 190.11 E-value: 3.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1457 YTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYArRNDKSYWLST 1536
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYA-SNDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|.
gi 768037311 1537 TA-----PIPMMPVSQTQIPQYISRCSVCEA 1562
Cdd:pfam01413 80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
916-1154 |
1.33e-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: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 916 GSTGKMGPSGRAGTPGEKGDRGNPGPVGIPSPRRPMSNLWLKGDKGSQGSAGSNGFPGPRGDKGEAGRPGPPGLPGApgl 995
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 996 pgiiKGVSGKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGsQGIRGSPGLPGASGLPGLKGDNGQTveisGSPGPKGQ 1075
Cdd:NF038329 194 ----QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA----GKDGPRGD 264
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768037311 1076 PGESGFKGTKGRDGLIGNIGFPGNKGEDGKVGVSGDVGLPGAPGFPGVAGMRGEPGLPGSSGHQGAIGPLGSPGLIGPK 1154
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
650-861 |
5.68e-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: 5.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 650 GSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRGEKGLPGFPGLPGKDGLPGMIGS 729
Cdd:NF038329 138 GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 730 PGLPGSKGATGDIFGAENGAPGEQGLQGLTGHKGFLGDSGLPGLKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGP 809
Cdd:NF038329 218 AGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 768037311 810 YGIKGKSGLPGAPGFPGISGHpgkkgtrgkKGPPGSIVKKGLPGLKGLPGNP 861
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 ... |
1212-1451 |
6.38e-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: 6.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1212 GLRGQKGDRGFPGLQGPAGLPGAPGISLPSLIAGQPGDPGRPGLDGERGRPGPAGPPGPPGPSSNQGDTGDPGFPGIPGP 1291
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1292 KGPKGDQGIPGFSGLPGELGLKGMRGEPGFMGTPGkvgppgdpgfpgmKGKAGPRGSSGLQGDPGqtptaeavqvPPGPL 1371
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------------DGQQGPDGDPGPTGEDG----------PQGPD 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1372 GLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPGQ 1451
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
429-730 |
4.23e-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: 4.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 429 FPGLRGEQGPKGNLGLKGIKGDSGfcacdggvpntgppgepgppgPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLVGPL 508
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRG---------------------DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 509 GPSGPKGKKGEPILSTIQGMPGDRGDSGSQGFRGVIGEPGKDGVPGLPGLPGLPGDGGQGFPGEKGLPGlpgekghpgpp 588
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG----------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 589 glpgnglpglpgPRGLPGDKGKDGLPGQQGLPGSKGDcccrevgkgdldtergitlpciiPGSYGPSGFPGTPGFPGPKG 668
Cdd:NF038329 243 ------------PTGEDGPQGPDGPAGKDGPRGDRGE-----------------------AGPDGPDGKDGERGPVGPAG 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768037311 669 SRGLPGTPGQPGSSGSKGEPGSPGLvhlpelpgfPGPRGEKGLPGFPGLPGKDGLPGMIGSP 730
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 ... |
21-347 |
6.01e-15 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 79.18 E-value: 6.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 21 QGRPGPIGIQGPTGPQGFTGSTGLSGLKGERGFPGLLGPYGPKGDKGPMGVPGFLGINGIPGHPGQPGPRGPPGLDGCNG 100
Cdd:NF038329 125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 101 TQGAVGFPGPDGypgllgppglpgQKGSKGDPVLAPGSFKGMKGDPGLPGLDGITGPQGAPGFPGAVGpagppglqgppg 180
Cdd:NF038329 205 EQGPAGPAGPDG------------EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG------------ 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 181 ppgplgpdgnmglgfqgekgvkgdvglpgpagpppstgelefmgfPKGKKGSKGEPGPKGFPGISGPPGFPGLGTTGEKG 260
Cdd:NF038329 261 ---------------------------------------------PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKD 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 261 ekgekgipGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDVFIDIDGAvisgnPGDPGVPG 340
Cdd:NF038329 296 --------GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTA-----PHTPKTPQ 362
|
....*..
gi 768037311 341 LPGLKGD 347
Cdd:NF038329 363 IPGQSKD 369
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
881-936 |
5.77e-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: 5.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 768037311 881 LSGPKGEKGSVGFVGFPGIPGLPGIPGTRGLKGIPGSTGKMGPSGRAGTPGEKGDR 936
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 ... |
1565-1678 |
1.23e-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: 208.60 E-value: 1.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1565 QAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTAAGaEGGGQSLVSPGSCLEDFRATPFIECSGArGTCHYFANKYSFWLT 1644
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78
|
90 100 110
....*....|....*....|....*....|....*
gi 768037311 1645 TVEErqQFGeLPVSETLKAG-QLHTRVSRCQVCMK 1678
Cdd:pfam01413 79 TVEE--QFR-KPMSQTPKAGnELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1564-1678 |
2.11e-56 |
|
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.
Pssm-ID: 128421 Cd Length: 114 Bit Score: 191.06 E-value: 2.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1564 SQAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTaAGAEGGGQSLVSPGSCLEDFRATPFIECSGaRGTCHYFANK-YSFW 1642
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASRNdYSFW 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 768037311 1643 LTTVEERQQFgELPVSETLKAGQLHTRVSRCQVCMK 1678
Cdd:smart00111 79 LSTIEPSDQF-TAPRPMTPKAGDLRPYISRCQVCEK 113
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1457-1562 |
3.83e-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: 190.11 E-value: 3.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1457 YTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYArRNDKSYWLST 1536
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYA-SNDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|.
gi 768037311 1537 TA-----PIPMMPVSQTQIPQYISRCSVCEA 1562
Cdd:pfam01413 80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1456-1563 |
4.05e-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: 176.04 E-value: 4.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1456 GYTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYARRNDKSYWLS 1535
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80
|
90 100 110
....*....|....*....|....*....|....*
gi 768037311 1536 T-------TAPIPMMPVSqTQIPQYISRCSVCEAP 1563
Cdd:smart00111 81 TiepsdqfTAPRPMTPKA-GDLRPYISRCQVCEKP 114
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
916-1154 |
1.33e-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: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 916 GSTGKMGPSGRAGTPGEKGDRGNPGPVGIPSPRRPMSNLWLKGDKGSQGSAGSNGFPGPRGDKGEAGRPGPPGLPGApgl 995
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 996 pgiiKGVSGKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGsQGIRGSPGLPGASGLPGLKGDNGQTveisGSPGPKGQ 1075
Cdd:NF038329 194 ----QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA----GKDGPRGD 264
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768037311 1076 PGESGFKGTKGRDGLIGNIGFPGNKGEDGKVGVSGDVGLPGAPGFPGVAGMRGEPGLPGSSGHQGAIGPLGSPGLIGPK 1154
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
886-1160 |
7.18e-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: 7.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 886 GEKGSVGFVGFPGIPGLPGIPGTRGLKGIPGSTGKMGPSGRAGTPGEKGDRGNPGPVGIPSPrrpmsnlwlKGDKGSQGS 965
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK---------DGEAGAKGP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 966 AGSNGFPGPRGdkgeagrpgppglpgapglpgiikgvsgKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGsQGIRGSP 1045
Cdd:NF038329 188 AGEKGPQGPRG----------------------------ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1046 GLPGASGLPGLKGDNGQTveisGSPGPKGQPGESGFKGTKGRDGLIGNIGFPGNKGEDGKVGvsgdvgLPGAPGFPGVAg 1125
Cdd:NF038329 239 GDPGPTGEDGPQGPDGPA----GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG------LPGKDGKDGQN- 307
|
250 260 270
....*....|....*....|....*....|....*
gi 768037311 1126 mrGEPGLPGSSGHQGAIGPLGSPGLIGPKGFPGFP 1160
Cdd:NF038329 308 --GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
773-1048 |
3.12e-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: 3.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 773 LKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAPGFPGISGhpgkkgtrgkkgPPGSIVKKGLP 852
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG------------PQGPAGKDGEA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 853 GLKGLPGNPGLVGLKGSPGSPGVAGLPALSGPKGEKGSVGFVGFPGIPGlPGIPGTRGLKGIPGSTGKMGPSGRAGTPGE 932
Cdd:NF038329 183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGP 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 933 KGDRGNPGPvgipsprrpmsnlwlkgdKGSQGSAGSNGFPGPRGDKGEagrpgppglpgapglpgiiKGVSGKPGPPGFM 1012
Cdd:NF038329 262 RGDRGEAGP------------------DGPDGKDGERGPVGPAGKDGQ-------------------NGKDGLPGKDGKD 304
|
250 260 270
....*....|....*....|....*....|....*.
gi 768037311 1013 GIRGLPGLKGSSGITGFPGMPGESGSQGIRGSPGLP 1048
Cdd:NF038329 305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
650-861 |
5.68e-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: 5.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 650 GSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRGEKGLPGFPGLPGKDGLPGMIGS 729
Cdd:NF038329 138 GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 730 PGLPGSKGATGDIFGAENGAPGEQGLQGLTGHKGFLGDSGLPGLKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGP 809
Cdd:NF038329 218 AGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 768037311 810 YGIKGKSGLPGAPGFPGISGHpgkkgtrgkKGPPGSIVKKGLPGLKGLPGNP 861
Cdd:NF038329 298 PGKDGKDGQNGKDGLPGKDGK---------DGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1212-1451 |
6.38e-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: 6.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1212 GLRGQKGDRGFPGLQGPAGLPGAPGISLPSLIAGQPGDPGRPGLDGERGRPGPAGPPGPPGPSSNQGDTGDPGFPGIPGP 1291
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1292 KGPKGDQGIPGFSGLPGELGLKGMRGEPGFMGTPGkvgppgdpgfpgmKGKAGPRGSSGLQGDPGqtptaeavqvPPGPL 1371
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------------DGQQGPDGDPGPTGEDG----------PQGPD 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1372 GLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPGQ 1451
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1172-1442 |
7.43e-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: 7.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1172 KGTHGTPGPSITGVPGPAGLPGPKGEKGypgigigAPGKPGLRGQKGDRGFPGLQGPAGLPGAPGISlpsliaGQPGDPG 1251
Cdd:NF038329 108 EGLQQLKGDGEKGEPGPAGPAGPAGEQG-------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ------GEAGPQG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1252 RPGLDGERGRPGPAGPPGPpgpssnQGDTGDPGFPGIPGPKGPKGDQGIPGFSGLPGELGLKGmRGEPGFMGTPGKVGPP 1331
Cdd:NF038329 175 PAGKDGEAGAKGPAGEKGP------QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGED 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1332 GDPGFPGMKGKAGPRGSSGLQGDPGQTPTAEavqvPPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDgpsg 1411
Cdd:NF038329 248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG----ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD---- 319
|
250 260 270
....*....|....*....|....*....|.
gi 768037311 1412 lpgppgalGDPGLPGLQGPPGFEGAPGQQGP 1442
Cdd:NF038329 320 --------GQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
429-730 |
4.23e-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: 4.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 429 FPGLRGEQGPKGNLGLKGIKGDSGfcacdggvpntgppgepgppgPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLVGPL 508
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRG---------------------DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 509 GPSGPKGKKGEPILSTIQGMPGDRGDSGSQGFRGVIGEPGKDGVPGLPGLPGLPGDGGQGFPGEKGLPGlpgekghpgpp 588
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG----------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 589 glpgnglpglpgPRGLPGDKGKDGLPGQQGLPGSKGDcccrevgkgdldtergitlpciiPGSYGPSGFPGTPGFPGPKG 668
Cdd:NF038329 243 ------------PTGEDGPQGPDGPAGKDGPRGDRGE-----------------------AGPDGPDGKDGERGPVGPAG 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768037311 669 SRGLPGTPGQPGSSGSKGEPGSPGLvhlpelpgfPGPRGEKGLPGFPGLPGKDGLPGMIGSP 730
Cdd:NF038329 288 KDGQNGKDGLPGKDGKDGQNGKDGL---------PGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
428-691 |
2.61e-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: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 428 GFPGLRGEQGPKGNLGLKGIKGDSGFCACDGGVPNTGPPGEPGPPGPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLVGP 507
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 508 LGPSGPKGKKGEPILSTIQGMPGDRGDsGSQGFRGVIGEPGKDgvpglpglpglpgdggqGFPGEKGLPGLPGEKghpgp 587
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGED-----------------GPQGPDGPAGKDGPR----- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 588 pglpgnglpglpGPRGLPGDKGKDGLPGQQGLPGskgdcccrEVGKGDLDTERGitlpciIPGSYGPSGFPGTPGFPGPK 667
Cdd:NF038329 263 ------------GDRGEAGPDGPDGKDGERGPVG--------PAGKDGQNGKDG------LPGKDGKDGQNGKDGLPGKD 316
|
250 260
....*....|....*....|....
gi 768037311 668 GSRGLPGTPGQPGSSGSKGEPGSP 691
Cdd:NF038329 317 GKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
21-347 |
6.01e-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: 79.18 E-value: 6.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 21 QGRPGPIGIQGPTGPQGFTGSTGLSGLKGERGFPGLLGPYGPKGDKGPMGVPGFLGINGIPGHPGQPGPRGPPGLDGCNG 100
Cdd:NF038329 125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 101 TQGAVGFPGPDGypgllgppglpgQKGSKGDPVLAPGSFKGMKGDPGLPGLDGITGPQGAPGFPGAVGpagppglqgppg 180
Cdd:NF038329 205 EQGPAGPAGPDG------------EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG------------ 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 181 ppgplgpdgnmglgfqgekgvkgdvglpgpagpppstgelefmgfPKGKKGSKGEPGPKGFPGISGPPGFPGLGTTGEKG 260
Cdd:NF038329 261 ---------------------------------------------PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKD 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 261 ekgekgipGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDVFIDIDGAvisgnPGDPGVPG 340
Cdd:NF038329 296 --------GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTA-----PHTPKTPQ 362
|
....*..
gi 768037311 341 LPGLKGD 347
Cdd:NF038329 363 IPGQSKD 369
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1255-1450 |
1.98e-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: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1255 LDGERGRPGPAGPPGPPGPSSNQGDTGDPGFPGIPGPKGPKGDQGIPGFSGLPGELGLKGMRGEPGFMGTPGKVGPPGDP 1334
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1335 GFPGMKGKAGPRGSSGLQGDPGQT-PTAEAVQVPPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLP 1413
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAgPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274
|
170 180 190
....*....|....*....|....*....|....*..
gi 768037311 1414 GPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPG 1450
Cdd:NF038329 275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
226-388 |
4.71e-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: 4.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 226 PKGKKGSKGEPGPKGFPGISGPPGFPGlgTTGEKGEKGEKGIPGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQG 305
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAG--PPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 306 IEGQKGDIGLPGPDVFIDIDGAVISGNPGDPGVPGLPGLKGDEGIQGLRGPSGVPGLPALSGVPGALGPQGFPGLKGDQG 385
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
|
...
gi 768037311 386 NPG 388
Cdd:NF038329 282 PVG 284
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
269-520 |
7.20e-14 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 76.10 E-value: 7.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 269 GLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDvfidiDGAVISGNPGDPGVPGLPGLKGDE 348
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ-----GEAGPQGPAGKDGEAGAKGPAGEK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 349 GIQGLRGPSGVPGLPALSGVPGALGPQGFPGLKGDQGNPGRTTIGAAGlpgrdglpgppgppgppspefetetlhnkESG 428
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG-----------------------------DPG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 429 FPGLRGEQGPKGNLGLKGIKGDSGFCACDGGVPNTGPPGEPGPP---GPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLV 505
Cdd:NF038329 243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAgkdGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322
|
250
....*....|....*
gi 768037311 506 GPLGPSGPKGKKGEP 520
Cdd:NF038329 323 GKDGLPGKDGKDGQP 337
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1367-1477 |
1.46e-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: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1367 PPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDgpsGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMP 1446
Cdd:NF038329 127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ---GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203
|
90 100 110
....*....|....*....|....*....|.
gi 768037311 1447 GMPGQSMRVGYTLVKHSQSEQVPPCPIGMSQ 1477
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ 234
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1371-1474 |
2.84e-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: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1371 LGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPG 1450
Cdd:NF038329 113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192
|
90 100
....*....|....*....|....
gi 768037311 1451 QSMRVGYTLVKHSQSEQVPPCPIG 1474
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGPAGPDG 216
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1125-1180 |
4.92e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.78 E-value: 4.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 768037311 1125 GMRGEPGLPGSSGHQGAIGPLGSPGLIGPKGFPGFPGLHGLNGLPGTKGTHGTPGP 1180
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
656-712 |
5.76e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.40 E-value: 5.76e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 768037311 656 GFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRGEKGLP 712
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
881-936 |
5.77e-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: 5.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 768037311 881 LSGPKGEKGSVGFVGFPGIPGLPGIPGTRGLKGIPGSTGKMGPSGRAGTPGEKGDR 936
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 ... |
1565-1678 |
1.23e-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: 208.60 E-value: 1.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1565 QAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTAAGaEGGGQSLVSPGSCLEDFRATPFIECSGArGTCHYFANKYSFWLT 1644
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78
|
90 100 110
....*....|....*....|....*....|....*
gi 768037311 1645 TVEErqQFGeLPVSETLKAG-QLHTRVSRCQVCMK 1678
Cdd:pfam01413 79 TVEE--QFR-KPMSQTPKAGnELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1564-1678 |
2.11e-56 |
|
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.
Pssm-ID: 128421 Cd Length: 114 Bit Score: 191.06 E-value: 2.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1564 SQAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTaAGAEGGGQSLVSPGSCLEDFRATPFIECSGaRGTCHYFANK-YSFW 1642
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASRNdYSFW 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 768037311 1643 LTTVEERQQFgELPVSETLKAGQLHTRVSRCQVCMK 1678
Cdd:smart00111 79 LSTIEPSDQF-TAPRPMTPKAGDLRPYISRCQVCEK 113
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1457-1562 |
3.83e-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: 190.11 E-value: 3.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1457 YTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYArRNDKSYWLST 1536
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYA-SNDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|.
gi 768037311 1537 TA-----PIPMMPVSQTQIPQYISRCSVCEA 1562
Cdd:pfam01413 80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1456-1563 |
4.05e-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: 176.04 E-value: 4.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1456 GYTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYARRNDKSYWLS 1535
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80
|
90 100 110
....*....|....*....|....*....|....*
gi 768037311 1536 T-------TAPIPMMPVSqTQIPQYISRCSVCEAP 1563
Cdd:smart00111 81 TiepsdqfTAPRPMTPKA-GDLRPYISRCQVCEKP 114
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
916-1154 |
1.33e-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: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 916 GSTGKMGPSGRAGTPGEKGDRGNPGPVGIPSPRRPMSNLWLKGDKGSQGSAGSNGFPGPRGDKGEAGRPGPPGLPGApgl 995
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 996 pgiiKGVSGKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGsQGIRGSPGLPGASGLPGLKGDNGQTveisGSPGPKGQ 1075
Cdd:NF038329 194 ----QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPA----GKDGPRGD 264
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768037311 1076 PGESGFKGTKGRDGLIGNIGFPGNKGEDGKVGVSGDVGLPGAPGFPGVAGMRGEPGLPGSSGHQGAIGPLGSPGLIGPK 1154
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
886-1160 |
7.18e-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: 7.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 886 GEKGSVGFVGFPGIPGLPGIPGTRGLKGIPGSTGKMGPSGRAGTPGEKGDRGNPGPVGIPSPrrpmsnlwlKGDKGSQGS 965
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK---------DGEAGAKGP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 966 AGSNGFPGPRGdkgeagrpgppglpgapglpgiikgvsgKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGsQGIRGSP 1045
Cdd:NF038329 188 AGEKGPQGPRG----------------------------ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1046 GLPGASGLPGLKGDNGQTveisGSPGPKGQPGESGFKGTKGRDGLIGNIGFPGNKGEDGKVGvsgdvgLPGAPGFPGVAg 1125
Cdd:NF038329 239 GDPGPTGEDGPQGPDGPA----GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG------LPGKDGKDGQN- 307
|
250 260 270
....*....|....*....|....*....|....*
gi 768037311 1126 mrGEPGLPGSSGHQGAIGPLGSPGLIGPKGFPGFP 1160
Cdd:NF038329 308 --GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
773-1048 |
3.12e-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: 3.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 773 LKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAPGFPGISGhpgkkgtrgkkgPPGSIVKKGLP 852
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG------------PQGPAGKDGEA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 853 GLKGLPGNPGLVGLKGSPGSPGVAGLPALSGPKGEKGSVGFVGFPGIPGlPGIPGTRGLKGIPGSTGKMGPSGRAGTPGE 932
Cdd:NF038329 183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGP 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 933 KGDRGNPGPvgipsprrpmsnlwlkgdKGSQGSAGSNGFPGPRGDKGEagrpgppglpgapglpgiiKGVSGKPGPPGFM 1012
Cdd:NF038329 262 RGDRGEAGP------------------DGPDGKDGERGPVGPAGKDGQ-------------------NGKDGLPGKDGKD 304
|
250 260 270
....*....|....*....|....*....|....*.
gi 768037311 1013 GIRGLPGLKGSSGITGFPGMPGESGSQGIRGSPGLP 1048
Cdd:NF038329 305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
650-861 |
5.68e-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: 5.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 650 GSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRGEKGLPGFPGLPGKDGLPGMIGS 729
Cdd:NF038329 138 GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 730 PGLPGSKGATGDIFGAENGAPGEQGLQGLTGHKGFLGDSGLPGLKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGP 809
Cdd:NF038329 218 AGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 768037311 810 YGIKGKSGLPGAPGFPGISGHpgkkgtrgkKGPPGSIVKKGLPGLKGLPGNP 861
Cdd:NF038329 298 PGKDGKDGQNGKDGLPGKDGK---------DGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1212-1451 |
6.38e-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: 6.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1212 GLRGQKGDRGFPGLQGPAGLPGAPGISLPSLIAGQPGDPGRPGLDGERGRPGPAGPPGPPGPSSNQGDTGDPGFPGIPGP 1291
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1292 KGPKGDQGIPGFSGLPGELGLKGMRGEPGFMGTPGkvgppgdpgfpgmKGKAGPRGSSGLQGDPGqtptaeavqvPPGPL 1371
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------------DGQQGPDGDPGPTGEDG----------PQGPD 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1372 GLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPGQ 1451
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1172-1442 |
7.43e-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: 7.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1172 KGTHGTPGPSITGVPGPAGLPGPKGEKGypgigigAPGKPGLRGQKGDRGFPGLQGPAGLPGAPGISlpsliaGQPGDPG 1251
Cdd:NF038329 108 EGLQQLKGDGEKGEPGPAGPAGPAGEQG-------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ------GEAGPQG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1252 RPGLDGERGRPGPAGPPGPpgpssnQGDTGDPGFPGIPGPKGPKGDQGIPGFSGLPGELGLKGmRGEPGFMGTPGKVGPP 1331
Cdd:NF038329 175 PAGKDGEAGAKGPAGEKGP------QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGED 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1332 GDPGFPGMKGKAGPRGSSGLQGDPGQTPTAEavqvPPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDgpsg 1411
Cdd:NF038329 248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG----ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD---- 319
|
250 260 270
....*....|....*....|....*....|.
gi 768037311 1412 lpgppgalGDPGLPGLQGPPGFEGAPGQQGP 1442
Cdd:NF038329 320 --------GQPGKDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
429-730 |
4.23e-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: 4.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 429 FPGLRGEQGPKGNLGLKGIKGDSGfcacdggvpntgppgepgppgPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLVGPL 508
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRG---------------------DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 509 GPSGPKGKKGEPILSTIQGMPGDRGDSGSQGFRGVIGEPGKDGVPGLPGLPGLPGDGGQGFPGEKGLPGlpgekghpgpp 588
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG----------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 589 glpgnglpglpgPRGLPGDKGKDGLPGQQGLPGSKGDcccrevgkgdldtergitlpciiPGSYGPSGFPGTPGFPGPKG 668
Cdd:NF038329 243 ------------PTGEDGPQGPDGPAGKDGPRGDRGE-----------------------AGPDGPDGKDGERGPVGPAG 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768037311 669 SRGLPGTPGQPGSSGSKGEPGSPGLvhlpelpgfPGPRGEKGLPGFPGLPGKDGLPGMIGSP 730
Cdd:NF038329 288 KDGQNGKDGLPGKDGKDGQNGKDGL---------PGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
428-691 |
2.61e-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: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 428 GFPGLRGEQGPKGNLGLKGIKGDSGFCACDGGVPNTGPPGEPGPPGPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLVGP 507
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 508 LGPSGPKGKKGEPILSTIQGMPGDRGDsGSQGFRGVIGEPGKDgvpglpglpglpgdggqGFPGEKGLPGLPGEKghpgp 587
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGED-----------------GPQGPDGPAGKDGPR----- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 588 pglpgnglpglpGPRGLPGDKGKDGLPGQQGLPGskgdcccrEVGKGDLDTERGitlpciIPGSYGPSGFPGTPGFPGPK 667
Cdd:NF038329 263 ------------GDRGEAGPDGPDGKDGERGPVG--------PAGKDGQNGKDG------LPGKDGKDGQNGKDGLPGKD 316
|
250 260
....*....|....*....|....
gi 768037311 668 GSRGLPGTPGQPGSSGSKGEPGSP 691
Cdd:NF038329 317 GKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
21-347 |
6.01e-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: 79.18 E-value: 6.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 21 QGRPGPIGIQGPTGPQGFTGSTGLSGLKGERGFPGLLGPYGPKGDKGPMGVPGFLGINGIPGHPGQPGPRGPPGLDGCNG 100
Cdd:NF038329 125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 101 TQGAVGFPGPDGypgllgppglpgQKGSKGDPVLAPGSFKGMKGDPGLPGLDGITGPQGAPGFPGAVGpagppglqgppg 180
Cdd:NF038329 205 EQGPAGPAGPDG------------EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG------------ 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 181 ppgplgpdgnmglgfqgekgvkgdvglpgpagpppstgelefmgfPKGKKGSKGEPGPKGFPGISGPPGFPGLGTTGEKG 260
Cdd:NF038329 261 ---------------------------------------------PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKD 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 261 ekgekgipGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDVFIDIDGAvisgnPGDPGVPG 340
Cdd:NF038329 296 --------GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTA-----PHTPKTPQ 362
|
....*..
gi 768037311 341 LPGLKGD 347
Cdd:NF038329 363 IPGQSKD 369
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1255-1450 |
1.98e-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: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1255 LDGERGRPGPAGPPGPPGPSSNQGDTGDPGFPGIPGPKGPKGDQGIPGFSGLPGELGLKGMRGEPGFMGTPGKVGPPGDP 1334
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1335 GFPGMKGKAGPRGSSGLQGDPGQT-PTAEAVQVPPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLP 1413
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAgPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274
|
170 180 190
....*....|....*....|....*....|....*..
gi 768037311 1414 GPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPG 1450
Cdd:NF038329 275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
226-388 |
4.71e-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: 4.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 226 PKGKKGSKGEPGPKGFPGISGPPGFPGlgTTGEKGEKGEKGIPGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQG 305
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAG--PPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 306 IEGQKGDIGLPGPDVFIDIDGAVISGNPGDPGVPGLPGLKGDEGIQGLRGPSGVPGLPALSGVPGALGPQGFPGLKGDQG 385
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
|
...
gi 768037311 386 NPG 388
Cdd:NF038329 282 PVG 284
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
269-520 |
7.20e-14 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 76.10 E-value: 7.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 269 GLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDvfidiDGAVISGNPGDPGVPGLPGLKGDE 348
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ-----GEAGPQGPAGKDGEAGAKGPAGEK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 349 GIQGLRGPSGVPGLPALSGVPGALGPQGFPGLKGDQGNPGRTTIGAAGlpgrdglpgppgppgppspefetetlhnkESG 428
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG-----------------------------DPG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 429 FPGLRGEQGPKGNLGLKGIKGDSGFCACDGGVPNTGPPGEPGPP---GPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLV 505
Cdd:NF038329 243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAgkdGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322
|
250
....*....|....*
gi 768037311 506 GPLGPSGPKGKKGEP 520
Cdd:NF038329 323 GKDGLPGKDGKDGQP 337
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1367-1477 |
1.46e-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: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1367 PPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDgpsGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMP 1446
Cdd:NF038329 127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ---GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203
|
90 100 110
....*....|....*....|....*....|.
gi 768037311 1447 GMPGQSMRVGYTLVKHSQSEQVPPCPIGMSQ 1477
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ 234
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1371-1474 |
2.84e-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: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 1371 LGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPG 1450
Cdd:NF038329 113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192
|
90 100
....*....|....*....|....
gi 768037311 1451 QSMRVGYTLVKHSQSEQVPPCPIG 1474
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGPAGPDG 216
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1125-1180 |
4.92e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.78 E-value: 4.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 768037311 1125 GMRGEPGLPGSSGHQGAIGPLGSPGLIGPKGFPGFPGLHGLNGLPGTKGTHGTPGP 1180
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
656-712 |
5.76e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.40 E-value: 5.76e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 768037311 656 GFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRGEKGLP 712
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
671-733 |
6.11e-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: 6.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768037311 671 GLPGTPGQPGSSGSKGEPGSPGLvhlpelPGFPGPRGEKGLPGFPGLPGKDGLPGMIGSPGLP 733
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGP------PGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
662-724 |
7.29e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.01 E-value: 7.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768037311 662 GFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLvhlpelPGFPGPRGEKGLPGFPGLPGKDGLP 724
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGE------PGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
649-692 |
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 768037311 649 PGSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPG 692
Cdd:pfam01391 9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
653-713 |
1.75e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 38.24 E-value: 1.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768037311 653 GPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGlvhlpeLPGFPGPRGEKGLPG 713
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPG------PPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
775-831 |
2.03e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.86 E-value: 2.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 768037311 775 GVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAPGFPGISGHP 831
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
649-708 |
2.42e-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: 37.86 E-value: 2.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768037311 649 PGSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGlvhlpeLPGFPGPRGE 708
Cdd:pfam01391 3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG------PPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1004-1060 |
2.95e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.47 E-value: 2.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 768037311 1004 GKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGSQGIRGSPGLPGASGLPGLKGDN 1060
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
686-740 |
3.85e-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: 3.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 768037311 686 GEPGSPGLVHLPELPGFPGPRGEKGLPGFPGLPGKDGLPGMIGSPGLPGSKGATG 740
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
766-822 |
5.23e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.70 E-value: 5.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 768037311 766 GDSGLPGLKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAP 822
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1104-1158 |
5.33e-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: 36.70 E-value: 5.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 768037311 1104 GKVGVSGDVGLPGAPGFPGVAGMRGEPGLPGSSGHQGAIGPLGSPGLIGPKGFPG 1158
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
881-936 |
5.77e-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: 5.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 768037311 881 LSGPKGEKGSVGFVGFPGIPGLPGIPGTRGLKGIPGSTGKMGPSGRAGTPGEKGDR 936
Cdd:pfam01391 2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1110-1164 |
8.90e-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: 8.90e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 768037311 1110 GDVGLPGAPGFPGVAGMRGEPGLPGSSGHQGAIGPLGSPGLIGPKGFPGFPGLHG 1164
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| |
