|
Name |
Accession |
Description |
Interval |
E-value |
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1123-1236 |
3.21e-61 |
|
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: 203.98 E-value: 3.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 1123 QAIAVHSQDIIVPQCPLGWHSLWIGYSFLMHTAAGaEGGGQSLVSPGSCLEDFRATPFIECSGArGTCHYFANKYSFWLT 1202
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78
|
90 100 110
....*....|....*....|....*....|....*
gi 148682815 1203 TVEErgQFReEPVSETLKTG-QLHTRVSRCQVCMK 1236
Cdd:pfam01413 79 TVEE--QFR-KPMSQTPKAGnELRSYISRCVVCEA 110
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1015-1120 |
3.63e-55 |
|
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: 187.03 E-value: 3.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 1015 YTLVKHSQSEQVPLCPTGMSRLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYArRNDKSYWLST 1094
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYA-SNDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|.
gi 148682815 1095 TA-----PIPMMPVGQTQIPQYISRCSVCEA 1120
Cdd:pfam01413 80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
42-284 |
1.36e-25 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 111.54 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 42 GEPGLPGIQGPIGLQGFKGTKGDPGSRGASGPAGTPGLFGPRGQTGLKGKKGEPtvsrgskmsGDKGDPGPQGTPGLAGT 121
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA---------GPQGPAGKDGEAGAKGP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 122 PGKDGRPGLPGLPGIQG-DGGSGFPGERGLPGLPGEKGHDGPIGPPGIGLPGPPGPRGLPGDKGVDGLPGQQGLRGAQGV 200
Cdd:NF038329 188 AGEKGPQGPRGETGPAGeQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 201 TLPCIIPGSYGPSGFPGAPGFPGSKGARGLPGIPGKPGTHGskggpgspglmhLPGLPGFPGVRGEKGLPGFPGLPGKDG 280
Cdd:NF038329 268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG------------KDGLPGKDGKDGQPGKDGLPGKDGKDG 335
|
....
gi 148682815 281 YPGK 284
Cdd:NF038329 336 QPGK 339
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
610-892 |
9.67e-24 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 105.76 E-value: 9.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 610 GIPGLKGDqgqtlGISGSPGPKGQPGELGFKGVKGKDGLVGDRGYPGNKGDGGKVGITGDPGFPGSPGLQGISGMNGDPG 689
Cdd:NF038329 109 GLQQLKGD-----GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 690 LPGSSGhlgSIGRPGPSGLIGPKGFPGAPGLHGLNGLPGTKGTHGTPGASITGVPGPAGLPGPKGERGVPGIVigdpGKQ 769
Cdd:NF038329 184 AKGPAG---EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPD----GPA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 770 GSKGQKGDQGSPGLQGPAGTpgapgislpsviAGQPGDPGRPGLDGERGRPgppgppgppgpssdqgdpgdsgfpGIPGL 849
Cdd:NF038329 257 GKDGPRGDRGEAGPDGPDGK------------DGERGPVGPAGKDGQNGKD------------------------GLPGK 300
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 148682815 850 QGFKGNQGLPGFSGLSGELGLKGMRGEPglmGTPGKIGQPGDP 892
Cdd:NF038329 301 DGKDGQNGKDGLPGKDGKDGQPGKDGLP---GKDGKDGQPGKP 340
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
186-428 |
4.33e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 100.75 E-value: 4.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 186 DGLPGQQGLRGAQGVTLPCIIPGSYGPSGFPGAPGFPGSKGARGLPGIPGKPGTHGSKGGPGSPGLMHLPGLPGFPGVRG 265
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 266 EKGLPGFPGLPGKDGYPGKAGSPGLPGFKGAAGDIFGAENGASGEQGLQGLPGDKGFPGDSGLPGPKGLNGKPGMLGPKG 345
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 346 ERGnpgtsgppgqpgpsgstdPFGIKGTSGFPGAPGLPGISGHPGKKGQRGDIGQPGSTGKRGLPGIKGLPGPQGSPGFL 425
Cdd:NF038329 276 KDG------------------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
|
...
gi 148682815 426 GSP 428
Cdd:NF038329 338 GKP 340
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
311-593 |
7.63e-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: 96.90 E-value: 7.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 311 QGLQGLPGDkgfpGDSGLPGPKGLNGKPGMLGPKGERGnpgtsgppgqpgpsgstdPFGIKGTSGFPGAPGLPGISGHPG 390
Cdd:NF038329 108 EGLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRG------------------ETGPAGPAGPPGPQGERGEKGPAG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 391 KKGQRGDIGQPGSTGKRGLPGIKGLPGPQGSPGFLGSPGLSGVTGLPGIEGQKGEKGSSGPVGfpglPGLPGLPGADGLK 470
Cdd:NF038329 166 PQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG----PAGDGQQGPDGDP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 471 GFSGSFGKVGQPGQTGTSGEKGDRGDPGPVGISSPRppmlnlwfkGEKGSRGSAGSDGFPGPRGDKGEPGIpglpgppga 550
Cdd:NF038329 242 GPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD---------GERGPVGPAGKDGQNGKDGLPGKDGK--------- 303
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 148682815 551 tgqtntiKGLNGRPGSPGSMGRRGLPGLKGSLGIAGFPGMPGK 593
Cdd:NF038329 304 -------DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
803-1014 |
1.52e-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.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 96.13 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 803 GQPGDPGRPGLDGERGRPGPPGPPGPPGPSSDQGDPGDSGFPGIPGLQGFKGNQGLPGFSGLSGELGLKGMRGEPGLMGT 882
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 883 PGKIGQPGDPGFPGMKGKAGPRGFSGPQGAPGHTPiaeamQVPPGPLGLPGIDGIPGLIGDPGSQGSVGLQGSKGLPGIP 962
Cdd:NF038329 200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ-----QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 148682815 963 GKDGPSGLPGPSGILGDPGLPGLQGPPG------FEGAPGNQGPIGQPGMPGHGVRVG 1014
Cdd:NF038329 275 GKDGERGPVGPAGKDGQNGKDGLPGKDGkdgqngKDGLPGKDGKDGQPGKDGLPGKDG 332
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1123-1236 |
3.21e-61 |
|
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: 203.98 E-value: 3.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 1123 QAIAVHSQDIIVPQCPLGWHSLWIGYSFLMHTAAGaEGGGQSLVSPGSCLEDFRATPFIECSGArGTCHYFANKYSFWLT 1202
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78
|
90 100 110
....*....|....*....|....*....|....*
gi 148682815 1203 TVEErgQFReEPVSETLKTG-QLHTRVSRCQVCMK 1236
Cdd:pfam01413 79 TVEE--QFR-KPMSQTPKAGnELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1122-1237 |
3.51e-55 |
|
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: 187.21 E-value: 3.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 1122 SQAIAVHSQDIIVPQCPLGWHSLWIGYSFLMHTaAGAEGGGQSLVSPGSCLEDFRATPFIECSGaRGTCHYFANK-YSFW 1200
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASRNdYSFW 78
|
90 100 110
....*....|....*....|....*....|....*..
gi 148682815 1201 LTTVEERGQFReEPVSETLKTGQLHTRVSRCQVCMKT 1237
Cdd:smart00111 79 LSTIEPSDQFT-APRPMTPKAGDLRPYISRCQVCEKP 114
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1015-1120 |
3.63e-55 |
|
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: 187.03 E-value: 3.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 1015 YTLVKHSQSEQVPLCPTGMSRLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYArRNDKSYWLST 1094
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYA-SNDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|.
gi 148682815 1095 TA-----PIPMMPVGQTQIPQYISRCSVCEA 1120
Cdd:pfam01413 80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1014-1121 |
1.69e-50 |
|
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: 173.73 E-value: 1.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 1014 GYTLVKHSQSEQVPLCPTGMSRLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYARRNDKSYWLS 1093
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80
|
90 100 110
....*....|....*....|....*....|....*
gi 148682815 1094 T-------TAPIPMMPVgQTQIPQYISRCSVCEAP 1121
Cdd:smart00111 81 TiepsdqfTAPRPMTPK-AGDLRPYISRCQVCEKP 114
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
42-284 |
1.36e-25 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 111.54 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 42 GEPGLPGIQGPIGLQGFKGTKGDPGSRGASGPAGTPGLFGPRGQTGLKGKKGEPtvsrgskmsGDKGDPGPQGTPGLAGT 121
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA---------GPQGPAGKDGEAGAKGP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 122 PGKDGRPGLPGLPGIQG-DGGSGFPGERGLPGLPGEKGHDGPIGPPGIGLPGPPGPRGLPGDKGVDGLPGQQGLRGAQGV 200
Cdd:NF038329 188 AGEKGPQGPRGETGPAGeQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 201 TLPCIIPGSYGPSGFPGAPGFPGSKGARGLPGIPGKPGTHGskggpgspglmhLPGLPGFPGVRGEKGLPGFPGLPGKDG 280
Cdd:NF038329 268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG------------KDGLPGKDGKDGQPGKDGLPGKDGKDG 335
|
....
gi 148682815 281 YPGK 284
Cdd:NF038329 336 QPGK 339
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
39-288 |
2.98e-25 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 110.38 E-value: 2.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 39 GPHGEPGLPGIQGPIGLQgfkGTKGDPGSRGASGPAGTPGLFGPRGQTGLKGKKGEPtvsrgskmsGDKGDPGPQGTPGL 118
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQ---GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA---------GPQGPAGKDGEAGA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 119 AGTPGKDGRPGLPGLPGIQG-DGGSGFPGERGLPGLPGEKGHDGPIGPPGIGLPGPPGPRGLPGDKGVDGLPGQQGLRGA 197
Cdd:NF038329 185 KGPAGEKGPQGPRGETGPAGeQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 198 QGVTLPCIIPGSYGPSGFPGAPGFPGSKGARGLPGIPGKPGTHgskggpgspglmhlpGLPGFPGVRGEKGLPGFPGLPG 277
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN---------------GKDGLPGKDGKDGQPGKDGLPG 329
|
250
....*....|.
gi 148682815 278 KDGYPGKAGSP 288
Cdd:NF038329 330 KDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
610-892 |
9.67e-24 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 105.76 E-value: 9.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 610 GIPGLKGDqgqtlGISGSPGPKGQPGELGFKGVKGKDGLVGDRGYPGNKGDGGKVGITGDPGFPGSPGLQGISGMNGDPG 689
Cdd:NF038329 109 GLQQLKGD-----GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 690 LPGSSGhlgSIGRPGPSGLIGPKGFPGAPGLHGLNGLPGTKGTHGTPGASITGVPGPAGLPGPKGERGVPGIVigdpGKQ 769
Cdd:NF038329 184 AKGPAG---EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPD----GPA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 770 GSKGQKGDQGSPGLQGPAGTpgapgislpsviAGQPGDPGRPGLDGERGRPgppgppgppgpssdqgdpgdsgfpGIPGL 849
Cdd:NF038329 257 GKDGPRGDRGEAGPDGPDGK------------DGERGPVGPAGKDGQNGKD------------------------GLPGK 300
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 148682815 850 QGFKGNQGLPGFSGLSGELGLKGMRGEPglmGTPGKIGQPGDP 892
Cdd:NF038329 301 DGKDGQNGKDGLPGKDGKDGQPGKDGLP---GKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
767-1007 |
1.44e-23 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 105.37 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 767 GKQGSKGQKGDQGSPGLQGPAGTPGAPGISLPSVIAGQPGDPGRPGLDGERGRPGPPGPPGPPGPSSDQGDPGDSGFPGI 846
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 847 PGLQGFKGNQGLPGFSGLSGELGLKGMRGEPGLMGtPGKIGQPGDPGFPGMKGKAGPRGFSGPQGapghtpiaeamqvPP 926
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDG-------------PR 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 927 GPLGLPGIDGIPGLIGDPGSQGSVGLQGSKGLPGIPGKDGPSGLPGPSGIlgdPGLPGLQGPPGFEGAPGNQGPIGQPGM 1006
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL---PGKDGKDGQPGKDGLPGKDGKDGQPGK 339
|
.
gi 148682815 1007 P 1007
Cdd:NF038329 340 P 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
186-428 |
4.33e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 100.75 E-value: 4.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 186 DGLPGQQGLRGAQGVTLPCIIPGSYGPSGFPGAPGFPGSKGARGLPGIPGKPGTHGSKGGPGSPGLMHLPGLPGFPGVRG 265
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 266 EKGLPGFPGLPGKDGYPGKAGSPGLPGFKGAAGDIFGAENGASGEQGLQGLPGDKGFPGDSGLPGPKGLNGKPGMLGPKG 345
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 346 ERGnpgtsgppgqpgpsgstdPFGIKGTSGFPGAPGLPGISGHPGKKGQRGDIGQPGSTGKRGLPGIKGLPGPQGSPGFL 425
Cdd:NF038329 276 KDG------------------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
|
...
gi 148682815 426 GSP 428
Cdd:NF038329 338 GKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
265-508 |
4.37e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 100.75 E-value: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 265 GEKGLPGFPGLPGKDGYPGKAGSPGLPGFKGAAGdifgaENGASGEQGLQGLPGDKGFPGDSGLPGPKGLNGKPGMLGPK 344
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAG-----PPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 345 GERGNPGTSGPPGQPGPSGSTDPFGIKGTSGFPGAPGLPGiSGHPGKKGQRGDIGQPGSTGKRGLPGIKGLPGPQGSPGF 424
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 425 LGSPGLSGVTGLPGIEGQKGEKGSSGPVGfpglpgLPGLPGADGLKGFSGSFGKVGQPGQTGTSGEKGDRGDPGPVGISS 504
Cdd:NF038329 271 DGPDGKDGERGPVGPAGKDGQNGKDGLPG------KDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKT 344
|
....
gi 148682815 505 PRPP 508
Cdd:NF038329 345 PEVP 348
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
730-988 |
6.69e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 100.36 E-value: 6.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 730 KGTHGTPGASITGVPGPAGLPGPKGERGVPGivigDPGKQGSKGQKGDQGSPGLQGPAGTPGApgislpsviAGQPGDPG 809
Cdd:NF038329 108 EGLQQLKGDGEKGEPGPAGPAGPAGEQGPRG----DRGETGPAGPAGPPGPQGERGEKGPAGP---------QGEAGPQG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 810 RPGLDGERGRPGPPGPPGPPGPSSDQGDPGDSGFPGIPGLQGFKGNQGLPGFSGLSGelglKGMRGEPGLMGTPGKIGQP 889
Cdd:NF038329 175 PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQ 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 890 GDPGFPGMKGKAGPRGFSGPQGAPGHTPiaeamqvPPGPLGLPGIDGIPGLIGDPGSQGSVGLQGSKGLPGIPGKDGPSG 969
Cdd:NF038329 251 GPDGPAGKDGPRGDRGEAGPDGPDGKDG-------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323
|
250
....*....|....*....
gi 148682815 970 LPGPSGILGDPGLPGLQGP 988
Cdd:NF038329 324 KDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
55-344 |
7.87e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 99.98 E-value: 7.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 55 LQGFKGTKGDpGSRGASGPAGTPGLFGPRGQTGLKGKKGEPtvsrgskmsGDKGDPGPQGTPGLAGTPGKDGRPGLPGLP 134
Cdd:NF038329 107 DEGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPA---------GPAGPPGPQGERGEKGPAGPQGEAGPQGPA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 135 GIQG-DGGSGFPGERGLPGLPGEKGHDGPIGPPGIGlpgppgprglpgdkGVDGLPGQQGLRGAQGVTLpciiPGSYGPS 213
Cdd:NF038329 177 GKDGeAGAKGPAGEKGPQGPRGETGPAGEQGPAGPA--------------GPDGEAGPAGEDGPAGPAG----DGQQGPD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 214 GFPGAPGFPGSKGARGLPGIPGKPGthgskggpgspglmhLPGLPGFPGVRGEKGLPGFPGLPGKDGYPGKAGSPGLPGf 293
Cdd:NF038329 239 GDPGPTGEDGPQGPDGPAGKDGPRG---------------DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG- 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 148682815 294 kgaagdifgaENGASGEQGLQGLPGDKGFPGDSGLPGPKGLNGKPGMLGPK 344
Cdd:NF038329 303 ----------KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
492-730 |
2.53e-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: 98.44 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 492 GDRGDPGPVGISSPRppmlnlwfkGEKGSRGSAGSDGFPGPRGDKGEPGIPGLPGPPGATGQTntikGLNGRPGSPGSMG 571
Cdd:NF038329 117 GEKGEPGPAGPAGPA---------GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA----GPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 572 RRGLPGLKGSLGIAGFPGMPGKSGSQGLTGTSGLLGATGIPGLKGDQGQ-TLGISGSPGPKGQPGELGFKGVKGKDGLVG 650
Cdd:NF038329 184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 651 DRGYPGNKGDGGKVGITGDPGFPGSPGLQGISGMNGDPGLPGSSGHLGSIGRPGPSGLIGPKGFPGAPGLHGLNGLPGTK 730
Cdd:NF038329 264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
577-820 |
2.93e-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: 98.44 E-value: 2.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 577 GLKGSLGIAGFPGMPGKSGSQGLTGTSGLLGATGIPGLKGDQGQTlgisGSPGPKGQPGELGFKGVKGKDGLVGDRGYPG 656
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEK----GPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 657 NKGDGGKVGITGDPGFPGSPGLQGISGMNGDPGLPGSSGHlgsiGRPGPSGLIGPKGFPGAPGLHGLNGLPGTKGTHGTP 736
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 737 GasitgvpgPAGLPGPKGERGvpgivigDPGKQGSKGQKGDQGSPGLQGPAGTPGAPGISLPSVIAGQPGDPGRPGLDGE 816
Cdd:NF038329 269 G--------PDGPDGKDGERG-------PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333
|
....
gi 148682815 817 RGRP 820
Cdd:NF038329 334 DGQP 337
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
311-593 |
7.63e-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: 96.90 E-value: 7.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 311 QGLQGLPGDkgfpGDSGLPGPKGLNGKPGMLGPKGERGnpgtsgppgqpgpsgstdPFGIKGTSGFPGAPGLPGISGHPG 390
Cdd:NF038329 108 EGLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRG------------------ETGPAGPAGPPGPQGERGEKGPAG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 391 KKGQRGDIGQPGSTGKRGLPGIKGLPGPQGSPGFLGSPGLSGVTGLPGIEGQKGEKGSSGPVGfpglPGLPGLPGADGLK 470
Cdd:NF038329 166 PQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG----PAGDGQQGPDGDP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 471 GFSGSFGKVGQPGQTGTSGEKGDRGDPGPVGISSPRppmlnlwfkGEKGSRGSAGSDGFPGPRGDKGEPGIpglpgppga 550
Cdd:NF038329 242 GPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD---------GERGPVGPAGKDGQNGKDGLPGKDGK--------- 303
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 148682815 551 tgqtntiKGLNGRPGSPGSMGRRGLPGLKGSLGIAGFPGMPGK 593
Cdd:NF038329 304 -------DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
803-1014 |
1.52e-20 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 96.13 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 803 GQPGDPGRPGLDGERGRPGPPGPPGPPGPSSDQGDPGDSGFPGIPGLQGFKGNQGLPGFSGLSGELGLKGMRGEPGLMGT 882
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 883 PGKIGQPGDPGFPGMKGKAGPRGFSGPQGAPGHTPiaeamQVPPGPLGLPGIDGIPGLIGDPGSQGSVGLQGSKGLPGIP 962
Cdd:NF038329 200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ-----QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 148682815 963 GKDGPSGLPGPSGILGDPGLPGLQGPPG------FEGAPGNQGPIGQPGMPGHGVRVG 1014
Cdd:NF038329 275 GKDGERGPVGPAGKDGQNGKDGLPGKDGkdgqngKDGLPGKDGKDGQPGKDGLPGKDG 332
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
813-1008 |
6.43e-19 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 91.12 E-value: 6.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 813 LDGERGRPGPPGPPGPPGPSSDQGDPGDSGFPGIPGLQGFKGNQGLPGFSGLSGELGLKGMRGEPGLMGTPGKIGQPGDP 892
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 893 GFPGMKGKAGPRGFSGPQGAPGHT-PIAEAMQVPPGPLGLPGIDGIPGLIGDPGSQGSVGLQGSKGLPGIPGKDGPSGLP 971
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAgPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274
|
170 180 190
....*....|....*....|....*....|....*..
gi 148682815 972 GPSGILGDPGLPGLQGPPGFEGAPGNQGPIGQPGMPG 1008
Cdd:NF038329 275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
345-616 |
8.57e-19 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 90.73 E-value: 8.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 345 GERGNPgtsgppgqpgpsGSTDPFGIKGTSGFPGAPGLPGISGHPGKKGQRGDIGQPGSTGKRGLPGIKGLPGPQGSPGF 424
Cdd:NF038329 117 GEKGEP------------GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 425 LGSPGLSGVTGLPGIEGQKGEKGSSGPVGfpglpglpglpgADGLKGFSGSFGKVGQPGQtgtsGEKGDRGDPGPVGISS 504
Cdd:NF038329 185 KGPAGEKGPQGPRGETGPAGEQGPAGPAG------------PDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 505 PRPPMLNLWFKGEKGSRGSAGSDGFPGPRGDkgepgipglpgppgatgqtntiKGLNGRPGSPGSMGRRGLPGLKGSLGI 584
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGE----------------------RGPVGPAGKDGQNGKDGLPGKDGKDGQ 306
|
250 260 270
....*....|....*....|....*....|..
gi 148682815 585 AGFPGMPGKSGSQGLTGTSGLLGATGIPGLKG 616
Cdd:NF038329 307 NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
925-1032 |
1.79e-07 |
|
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: 55.30 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 925 PPGPLGLPGIDGIPGLIGDPGS---QGSVGLQGSKGLPGIPGKDGPSGLPGPSGILGDPGLPGLQGPPGFEGAPGNQGPI 1001
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGEtgpAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200
|
90 100 110
....*....|....*....|....*....|.
gi 148682815 1002 GQPGMPGHGVRVGYTLVKHSQSEQVPLCPTG 1032
Cdd:NF038329 201 GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG 231
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
951-1007 |
1.03e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 41.33 E-value: 1.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 148682815 951 GLQGSKGLPGIPGKDGPSGLPGPSGILGDPGLPGLQGPPGFEGAPGNQGPIGQPGMP 1007
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
393-447 |
1.61e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.86 E-value: 1.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 148682815 393 GQRGDIGQPGSTGKRGLPGIKGLPGPQGSPGFLGSPGLSGVTGLPGIEGQKGEKG 447
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
860-914 |
4.68e-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: 4.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 148682815 860 GFSGLSGELGLKGMRGEPGLMGTPGKIGQPGDPGFPGMKGKAGPRGFSGPQGAPG 914
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
39-95 |
5.81e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.32 E-value: 5.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 148682815 39 GPHGEPGLPGIQGPIGLQGFKGTKGDPGSRGASGPAGTPGLFGPRGQTGLKGKKGEP 95
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK14959 |
PRK14959 |
DNA polymerase III subunits gamma and tau; Provisional |
925-1040 |
7.59e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 40.43 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 925 PPGPLGLPG-IDGIPGLIGDPGSQGSVGLQGSKGLP---GIPGKDGPSGLPGPSGILGD-PGLPGLQGPPGFeGAPGNQG 999
Cdd:PRK14959 380 APSGSAAEGpASGGAATIPTPGTQGPQGTAPAAGMTpssAAPATPAPSAAPSPRVPWDDaPPAPPRSGIPPR-PAPRMPE 458
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 148682815 1000 PIGQPGMPGHGVRVGYTLVKHSQSEQVPLCPTGMSRLWVGY 1040
Cdd:PRK14959 459 ASPVPGAPDSVASASDAPPTLGDPSDTAEHTPSGPRTWDGF 499
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1123-1236 |
3.21e-61 |
|
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: 203.98 E-value: 3.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 1123 QAIAVHSQDIIVPQCPLGWHSLWIGYSFLMHTAAGaEGGGQSLVSPGSCLEDFRATPFIECSGArGTCHYFANKYSFWLT 1202
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78
|
90 100 110
....*....|....*....|....*....|....*
gi 148682815 1203 TVEErgQFReEPVSETLKTG-QLHTRVSRCQVCMK 1236
Cdd:pfam01413 79 TVEE--QFR-KPMSQTPKAGnELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1122-1237 |
3.51e-55 |
|
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: 187.21 E-value: 3.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 1122 SQAIAVHSQDIIVPQCPLGWHSLWIGYSFLMHTaAGAEGGGQSLVSPGSCLEDFRATPFIECSGaRGTCHYFANK-YSFW 1200
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASRNdYSFW 78
|
90 100 110
....*....|....*....|....*....|....*..
gi 148682815 1201 LTTVEERGQFReEPVSETLKTGQLHTRVSRCQVCMKT 1237
Cdd:smart00111 79 LSTIEPSDQFT-APRPMTPKAGDLRPYISRCQVCEKP 114
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1015-1120 |
3.63e-55 |
|
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: 187.03 E-value: 3.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 1015 YTLVKHSQSEQVPLCPTGMSRLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYArRNDKSYWLST 1094
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYA-SNDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|.
gi 148682815 1095 TA-----PIPMMPVGQTQIPQYISRCSVCEA 1120
Cdd:pfam01413 80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1014-1121 |
1.69e-50 |
|
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: 173.73 E-value: 1.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 1014 GYTLVKHSQSEQVPLCPTGMSRLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYARRNDKSYWLS 1093
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80
|
90 100 110
....*....|....*....|....*....|....*
gi 148682815 1094 T-------TAPIPMMPVgQTQIPQYISRCSVCEAP 1121
Cdd:smart00111 81 TiepsdqfTAPRPMTPK-AGDLRPYISRCQVCEKP 114
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
42-284 |
1.36e-25 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 111.54 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 42 GEPGLPGIQGPIGLQGFKGTKGDPGSRGASGPAGTPGLFGPRGQTGLKGKKGEPtvsrgskmsGDKGDPGPQGTPGLAGT 121
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA---------GPQGPAGKDGEAGAKGP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 122 PGKDGRPGLPGLPGIQG-DGGSGFPGERGLPGLPGEKGHDGPIGPPGIGLPGPPGPRGLPGDKGVDGLPGQQGLRGAQGV 200
Cdd:NF038329 188 AGEKGPQGPRGETGPAGeQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 201 TLPCIIPGSYGPSGFPGAPGFPGSKGARGLPGIPGKPGTHGskggpgspglmhLPGLPGFPGVRGEKGLPGFPGLPGKDG 280
Cdd:NF038329 268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG------------KDGLPGKDGKDGQPGKDGLPGKDGKDG 335
|
....
gi 148682815 281 YPGK 284
Cdd:NF038329 336 QPGK 339
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
39-288 |
2.98e-25 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 110.38 E-value: 2.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 39 GPHGEPGLPGIQGPIGLQgfkGTKGDPGSRGASGPAGTPGLFGPRGQTGLKGKKGEPtvsrgskmsGDKGDPGPQGTPGL 118
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQ---GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA---------GPQGPAGKDGEAGA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 119 AGTPGKDGRPGLPGLPGIQG-DGGSGFPGERGLPGLPGEKGHDGPIGPPGIGLPGPPGPRGLPGDKGVDGLPGQQGLRGA 197
Cdd:NF038329 185 KGPAGEKGPQGPRGETGPAGeQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 198 QGVTLPCIIPGSYGPSGFPGAPGFPGSKGARGLPGIPGKPGTHgskggpgspglmhlpGLPGFPGVRGEKGLPGFPGLPG 277
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN---------------GKDGLPGKDGKDGQPGKDGLPG 329
|
250
....*....|.
gi 148682815 278 KDGYPGKAGSP 288
Cdd:NF038329 330 KDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
610-892 |
9.67e-24 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 105.76 E-value: 9.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 610 GIPGLKGDqgqtlGISGSPGPKGQPGELGFKGVKGKDGLVGDRGYPGNKGDGGKVGITGDPGFPGSPGLQGISGMNGDPG 689
Cdd:NF038329 109 GLQQLKGD-----GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 690 LPGSSGhlgSIGRPGPSGLIGPKGFPGAPGLHGLNGLPGTKGTHGTPGASITGVPGPAGLPGPKGERGVPGIVigdpGKQ 769
Cdd:NF038329 184 AKGPAG---EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPD----GPA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 770 GSKGQKGDQGSPGLQGPAGTpgapgislpsviAGQPGDPGRPGLDGERGRPgppgppgppgpssdqgdpgdsgfpGIPGL 849
Cdd:NF038329 257 GKDGPRGDRGEAGPDGPDGK------------DGERGPVGPAGKDGQNGKD------------------------GLPGK 300
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 148682815 850 QGFKGNQGLPGFSGLSGELGLKGMRGEPglmGTPGKIGQPGDP 892
Cdd:NF038329 301 DGKDGQNGKDGLPGKDGKDGQPGKDGLP---GKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
767-1007 |
1.44e-23 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 105.37 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 767 GKQGSKGQKGDQGSPGLQGPAGTPGAPGISLPSVIAGQPGDPGRPGLDGERGRPGPPGPPGPPGPSSDQGDPGDSGFPGI 846
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 847 PGLQGFKGNQGLPGFSGLSGELGLKGMRGEPGLMGtPGKIGQPGDPGFPGMKGKAGPRGFSGPQGapghtpiaeamqvPP 926
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDG-------------PR 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 927 GPLGLPGIDGIPGLIGDPGSQGSVGLQGSKGLPGIPGKDGPSGLPGPSGIlgdPGLPGLQGPPGFEGAPGNQGPIGQPGM 1006
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGL---PGKDGKDGQPGKDGLPGKDGKDGQPGK 339
|
.
gi 148682815 1007 P 1007
Cdd:NF038329 340 P 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
186-428 |
4.33e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 100.75 E-value: 4.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 186 DGLPGQQGLRGAQGVTLPCIIPGSYGPSGFPGAPGFPGSKGARGLPGIPGKPGTHGSKGGPGSPGLMHLPGLPGFPGVRG 265
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 266 EKGLPGFPGLPGKDGYPGKAGSPGLPGFKGAAGDIFGAENGASGEQGLQGLPGDKGFPGDSGLPGPKGLNGKPGMLGPKG 345
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 346 ERGnpgtsgppgqpgpsgstdPFGIKGTSGFPGAPGLPGISGHPGKKGQRGDIGQPGSTGKRGLPGIKGLPGPQGSPGFL 425
Cdd:NF038329 276 KDG------------------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
|
...
gi 148682815 426 GSP 428
Cdd:NF038329 338 GKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
265-508 |
4.37e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 100.75 E-value: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 265 GEKGLPGFPGLPGKDGYPGKAGSPGLPGFKGAAGdifgaENGASGEQGLQGLPGDKGFPGDSGLPGPKGLNGKPGMLGPK 344
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAG-----PPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 345 GERGNPGTSGPPGQPGPSGSTDPFGIKGTSGFPGAPGLPGiSGHPGKKGQRGDIGQPGSTGKRGLPGIKGLPGPQGSPGF 424
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 425 LGSPGLSGVTGLPGIEGQKGEKGSSGPVGfpglpgLPGLPGADGLKGFSGSFGKVGQPGQTGTSGEKGDRGDPGPVGISS 504
Cdd:NF038329 271 DGPDGKDGERGPVGPAGKDGQNGKDGLPG------KDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKT 344
|
....
gi 148682815 505 PRPP 508
Cdd:NF038329 345 PEVP 348
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
730-988 |
6.69e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 100.36 E-value: 6.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 730 KGTHGTPGASITGVPGPAGLPGPKGERGVPGivigDPGKQGSKGQKGDQGSPGLQGPAGTPGApgislpsviAGQPGDPG 809
Cdd:NF038329 108 EGLQQLKGDGEKGEPGPAGPAGPAGEQGPRG----DRGETGPAGPAGPPGPQGERGEKGPAGP---------QGEAGPQG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 810 RPGLDGERGRPGPPGPPGPPGPSSDQGDPGDSGFPGIPGLQGFKGNQGLPGFSGLSGelglKGMRGEPGLMGTPGKIGQP 889
Cdd:NF038329 175 PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQ 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 890 GDPGFPGMKGKAGPRGFSGPQGAPGHTPiaeamqvPPGPLGLPGIDGIPGLIGDPGSQGSVGLQGSKGLPGIPGKDGPSG 969
Cdd:NF038329 251 GPDGPAGKDGPRGDRGEAGPDGPDGKDG-------ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323
|
250
....*....|....*....
gi 148682815 970 LPGPSGILGDPGLPGLQGP 988
Cdd:NF038329 324 KDGLPGKDGKDGQPGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
55-344 |
7.87e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 99.98 E-value: 7.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 55 LQGFKGTKGDpGSRGASGPAGTPGLFGPRGQTGLKGKKGEPtvsrgskmsGDKGDPGPQGTPGLAGTPGKDGRPGLPGLP 134
Cdd:NF038329 107 DEGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPA---------GPAGPPGPQGERGEKGPAGPQGEAGPQGPA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 135 GIQG-DGGSGFPGERGLPGLPGEKGHDGPIGPPGIGlpgppgprglpgdkGVDGLPGQQGLRGAQGVTLpciiPGSYGPS 213
Cdd:NF038329 177 GKDGeAGAKGPAGEKGPQGPRGETGPAGEQGPAGPA--------------GPDGEAGPAGEDGPAGPAG----DGQQGPD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 214 GFPGAPGFPGSKGARGLPGIPGKPGthgskggpgspglmhLPGLPGFPGVRGEKGLPGFPGLPGKDGYPGKAGSPGLPGf 293
Cdd:NF038329 239 GDPGPTGEDGPQGPDGPAGKDGPRG---------------DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG- 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 148682815 294 kgaagdifgaENGASGEQGLQGLPGDKGFPGDSGLPGPKGLNGKPGMLGPK 344
Cdd:NF038329 303 ----------KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
492-730 |
2.53e-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: 98.44 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 492 GDRGDPGPVGISSPRppmlnlwfkGEKGSRGSAGSDGFPGPRGDKGEPGIPGLPGPPGATGQTntikGLNGRPGSPGSMG 571
Cdd:NF038329 117 GEKGEPGPAGPAGPA---------GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA----GPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 572 RRGLPGLKGSLGIAGFPGMPGKSGSQGLTGTSGLLGATGIPGLKGDQGQ-TLGISGSPGPKGQPGELGFKGVKGKDGLVG 650
Cdd:NF038329 184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 651 DRGYPGNKGDGGKVGITGDPGFPGSPGLQGISGMNGDPGLPGSSGHLGSIGRPGPSGLIGPKGFPGAPGLHGLNGLPGTK 730
Cdd:NF038329 264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
577-820 |
2.93e-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: 98.44 E-value: 2.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 577 GLKGSLGIAGFPGMPGKSGSQGLTGTSGLLGATGIPGLKGDQGQTlgisGSPGPKGQPGELGFKGVKGKDGLVGDRGYPG 656
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEK----GPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 657 NKGDGGKVGITGDPGFPGSPGLQGISGMNGDPGLPGSSGHlgsiGRPGPSGLIGPKGFPGAPGLHGLNGLPGTKGTHGTP 736
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 737 GasitgvpgPAGLPGPKGERGvpgivigDPGKQGSKGQKGDQGSPGLQGPAGTPGAPGISLPSVIAGQPGDPGRPGLDGE 816
Cdd:NF038329 269 G--------PDGPDGKDGERG-------PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333
|
....
gi 148682815 817 RGRP 820
Cdd:NF038329 334 DGQP 337
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
311-593 |
7.63e-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: 96.90 E-value: 7.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 311 QGLQGLPGDkgfpGDSGLPGPKGLNGKPGMLGPKGERGnpgtsgppgqpgpsgstdPFGIKGTSGFPGAPGLPGISGHPG 390
Cdd:NF038329 108 EGLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRG------------------ETGPAGPAGPPGPQGERGEKGPAG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 391 KKGQRGDIGQPGSTGKRGLPGIKGLPGPQGSPGFLGSPGLSGVTGLPGIEGQKGEKGSSGPVGfpglPGLPGLPGADGLK 470
Cdd:NF038329 166 PQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG----PAGDGQQGPDGDP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 471 GFSGSFGKVGQPGQTGTSGEKGDRGDPGPVGISSPRppmlnlwfkGEKGSRGSAGSDGFPGPRGDKGEPGIpglpgppga 550
Cdd:NF038329 242 GPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD---------GERGPVGPAGKDGQNGKDGLPGKDGK--------- 303
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 148682815 551 tgqtntiKGLNGRPGSPGSMGRRGLPGLKGSLGIAGFPGMPGK 593
Cdd:NF038329 304 -------DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
803-1014 |
1.52e-20 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 96.13 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 803 GQPGDPGRPGLDGERGRPGPPGPPGPPGPSSDQGDPGDSGFPGIPGLQGFKGNQGLPGFSGLSGELGLKGMRGEPGLMGT 882
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 883 PGKIGQPGDPGFPGMKGKAGPRGFSGPQGAPGHTPiaeamQVPPGPLGLPGIDGIPGLIGDPGSQGSVGLQGSKGLPGIP 962
Cdd:NF038329 200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ-----QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 148682815 963 GKDGPSGLPGPSGILGDPGLPGLQGPPG------FEGAPGNQGPIGQPGMPGHGVRVG 1014
Cdd:NF038329 275 GKDGERGPVGPAGKDGQNGKDGLPGKDGkdgqngKDGLPGKDGKDGQPGKDGLPGKDG 332
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
813-1008 |
6.43e-19 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 91.12 E-value: 6.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 813 LDGERGRPGPPGPPGPPGPSSDQGDPGDSGFPGIPGLQGFKGNQGLPGFSGLSGELGLKGMRGEPGLMGTPGKIGQPGDP 892
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 893 GFPGMKGKAGPRGFSGPQGAPGHT-PIAEAMQVPPGPLGLPGIDGIPGLIGDPGSQGSVGLQGSKGLPGIPGKDGPSGLP 971
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAgPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274
|
170 180 190
....*....|....*....|....*....|....*..
gi 148682815 972 GPSGILGDPGLPGLQGPPGFEGAPGNQGPIGQPGMPG 1008
Cdd:NF038329 275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
345-616 |
8.57e-19 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 90.73 E-value: 8.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 345 GERGNPgtsgppgqpgpsGSTDPFGIKGTSGFPGAPGLPGISGHPGKKGQRGDIGQPGSTGKRGLPGIKGLPGPQGSPGF 424
Cdd:NF038329 117 GEKGEP------------GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 425 LGSPGLSGVTGLPGIEGQKGEKGSSGPVGfpglpglpglpgADGLKGFSGSFGKVGQPGQtgtsGEKGDRGDPGPVGISS 504
Cdd:NF038329 185 KGPAGEKGPQGPRGETGPAGEQGPAGPAG------------PDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 505 PRPPMLNLWFKGEKGSRGSAGSDGFPGPRGDkgepgipglpgppgatgqtntiKGLNGRPGSPGSMGRRGLPGLKGSLGI 584
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGE----------------------RGPVGPAGKDGQNGKDGLPGKDGKDGQ 306
|
250 260 270
....*....|....*....|....*....|..
gi 148682815 585 AGFPGMPGKSGSQGLTGTSGLLGATGIPGLKG 616
Cdd:NF038329 307 NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
925-1032 |
1.79e-07 |
|
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: 55.30 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 925 PPGPLGLPGIDGIPGLIGDPGS---QGSVGLQGSKGLPGIPGKDGPSGLPGPSGILGDPGLPGLQGPPGFEGAPGNQGPI 1001
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGEtgpAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200
|
90 100 110
....*....|....*....|....*....|.
gi 148682815 1002 GQPGMPGHGVRVGYTLVKHSQSEQVPLCPTG 1032
Cdd:NF038329 201 GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG 231
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
951-1007 |
1.03e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 41.33 E-value: 1.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 148682815 951 GLQGSKGLPGIPGKDGPSGLPGPSGILGDPGLPGLQGPPGFEGAPGNQGPIGQPGMP 1007
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
939-995 |
8.18e-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: 38.63 E-value: 8.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 148682815 939 GLIGDPGSQGSVGLQGSKGLPGIPGKDGPSGLPGPSGILGDPGLPGLQGPPGFEGAP 995
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
925-980 |
1.06e-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: 38.24 E-value: 1.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 148682815 925 PPGPLGLPGIDGIPGLIGDPGSQGSVGLQGSKGLPGIPGKDGPSGLPGPSGILGDP 980
Cdd:pfam01391 2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
945-1004 |
1.18e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 38.24 E-value: 1.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 945 GSQGSVGLQGSKGLPGIPGKDGPSGLPGPSGilgDPGLPGLQGPPGFEGAPGNQGPIGQP 1004
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPG---EPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
930-984 |
1.39e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.86 E-value: 1.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 148682815 930 GLPGIDGIPGLIGDPGSQGSVGLQGSKGLPGIPGKDGPSGLPGPSGILGDPGLPG 984
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
393-447 |
1.61e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.86 E-value: 1.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 148682815 393 GQRGDIGQPGSTGKRGLPGIKGLPGPQGSPGFLGSPGLSGVTGLPGIEGQKGEKG 447
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
375-429 |
2.97e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.09 E-value: 2.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 148682815 375 GFPGAPGLPGISGHPGKKGQRGDIGQPGSTGKRGLPGIKGLPGPQGSPGFLGSPG 429
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
369-422 |
3.09e-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: 3.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 148682815 369 GIKGTSGFPGAPGLPGISGHPGKKGQRGDIGQPGSTGKRGLPGIKGLPGPQGSP 422
Cdd:pfam01391 4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
960-1008 |
3.62e-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: 3.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 148682815 960 GIPGKDGPSGLPGPSGILGDPGLPGLQGPPGFEGAPGNQGPIGQPGMPG 1008
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
860-914 |
4.68e-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: 4.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 148682815 860 GFSGLSGELGLKGMRGEPGLMGTPGKIGQPGDPGFPGMKGKAGPRGFSGPQGAPG 914
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
39-95 |
5.81e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.32 E-value: 5.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 148682815 39 GPHGEPGLPGIQGPIGLQGFKGTKGDPGSRGASGPAGTPGLFGPRGQTGLKGKKGEP 95
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
942-996 |
5.81e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.32 E-value: 5.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 148682815 942 GDPGSQGSVGLQGSKGLPGIPGKDGPSGLPGPSGILGDPGLPGLQGPPGFEGAPG 996
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
668-722 |
7.58e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 35.93 E-value: 7.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 148682815 668 GDPGFPGSPGLQGISGMNGDPGLPGSSGHLGSIGRPGPSGLIGPKGFPGAPGLHG 722
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| PRK14959 |
PRK14959 |
DNA polymerase III subunits gamma and tau; Provisional |
925-1040 |
7.59e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 40.43 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148682815 925 PPGPLGLPG-IDGIPGLIGDPGSQGSVGLQGSKGLP---GIPGKDGPSGLPGPSGILGD-PGLPGLQGPPGFeGAPGNQG 999
Cdd:PRK14959 380 APSGSAAEGpASGGAATIPTPGTQGPQGTAPAAGMTpssAAPATPAPSAAPSPRVPWDDaPPAPPRSGIPPR-PAPRMPE 458
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 148682815 1000 PIGQPGMPGHGVRVGYTLVKHSQSEQVPLCPTGMSRLWVGY 1040
Cdd:PRK14959 459 ASPVPGAPDSVASASDAPPTLGDPSDTAEHTPSGPRTWDGF 499
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
214-285 |
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: 35.55 E-value: 9.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148682815 214 GFPGAPGFPGSKGARGLPGIPGKPGthgskggpgspglmhLPGLPGFPGVRGEKGLPGFPGLPGKDGYPGKA 285
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPG---------------PPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
680-736 |
9.99e-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: 35.55 E-value: 9.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 148682815 680 GISGMNGDPGLPGSSGHLGSIGRPGPSGLIGPKGFPGAPGLHGLNGLPGTKGTHGTP 736
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| |
