|
Name |
Accession |
Description |
Interval |
E-value |
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1584-1694 |
7.06e-69 |
|
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: 226.32 E-value: 7.06e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1584 VIAVHSQTIQIPHCPQGWDSLWIGYSFMMHTSAGaEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYANSYSFWLATV 1663
Cdd:pfam01413 2 LIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYASNDYSYWLSTV 80
|
90 100 110
....*....|....*....|....*....|..
gi 1034673478 1664 DvsDMFSKPQSETLKAGD-LRTRISRCQVCMK 1694
Cdd:pfam01413 81 E--EQFRKPMSQTPKAGNeLRSYISRCVVCEA 110
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1473-1580 |
6.70e-63 |
|
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: 209.37 E-value: 6.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1473 FLITRHSQTTDAPQCPQGTLQVYEGFSLLYVQGNKRAHGQDLGTAGSCLRRFSTMPFMFCNINNVCNFASrNDYSYWLST 1552
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|.
gi 1034673478 1553 PE---PMPMSMQPLKGQSIQPFISRCAVCEA 1580
Cdd:pfam01413 80 VEeqfRKPMSQTPKAGNELRSYISRCVVCEA 110
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
469-703 |
8.16e-14 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 75.71 E-value: 8.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 469 DKGLQGEQGVKGDKGDTCfnciGTGISGPPGQPGLPGLPGPPGSLGFPGQKGEKGQAGATGPKGLPGIPGAPGAPGFPGS 548
Cdd:NF038329 151 PPGPQGERGEKGPAGPQG----EAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGP 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 549 KGEPGDILTfpGMKGDKGELGSPGAPGLPGLPGTPGQDGLPGLPGPKGEPGGITFKGERgppgnpglpglpgnigpmgpp 628
Cdd:NF038329 227 AGPAGDGQQ--GPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV--------------------- 283
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034673478 629 gfgppgpvgekGIQGVAGNPGQPGIPGPKGDPGQTitqpGKPGLPGNPGRDGDVGLPGDPGLPGQPGLPGIPGSK 703
Cdd:NF038329 284 -----------GPAGKDGQNGKDGLPGKDGKDGQN----GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
969-1231 |
1.09e-12 |
|
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: 72.25 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 969 GEKGEPGLPGIPGVSGPKGYQGLPGDPGQPGLSGQPGLPGPPGPKGNPGLPGQPGLIGPPGLKGTIGDMGFPGPQGVEGP 1048
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1049 PGPSGVPGQPGSPGLPGQKGDKGDPGISSIGLPGLPGPKGEPGLPGYPGNPGIKGSVGDPGLPGLPGTPGAKGqpglpgf 1128
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG------- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1129 pgtpgppgpkgisgppgnpglpgepgPVGGGGHPGQPGPPGEKGKPGQ---DGIPGPAGQKGEpgqpgfgnpgpPGLPGL 1205
Cdd:NF038329 270 --------------------------PDGPDGKDGERGPVGPAGKDGQngkDGLPGKDGKDGQ-----------NGKDGL 312
|
250 260
....*....|....*....|....*.
gi 1034673478 1206 SGQKGDGGLPGIPGNPGLPGPKGEPG 1231
Cdd:NF038329 313 PGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1085-1356 |
2.33e-08 |
|
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: 58.38 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1085 GPKGEPGLPGYPGNPGIKGSVGDPGLPGLPGTPGAKGqpglpgfpgtpgppgpkgisgppgnpglpgepgpvgggghpgQ 1164
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPG------------------------------------------P 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1165 PGPPGEKGKPGQDGIPGPAGQKGEPGQPgfgnpgppglpglsGQKGDGGLPGIPGNPGLPGPKGEPGFHGFPGVQGPPGP 1244
Cdd:NF038329 155 QGERGEKGPAGPQGEAGPQGPAGKDGEA--------------GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1245 PGSPGPALEGPKGNPGPQGPPGRPGPTGFQGLPGPEGPPGLPGNGGIKGEKGNPGQPGLPGLPGLKGDQGPPGLQGNPGR 1324
Cdd:NF038329 221 AGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGK 300
|
250 260 270
....*....|....*....|....*....|..
gi 1034673478 1325 PGLNGMKGDPGLPGVPGFPGMKGPSGVPGSAG 1356
Cdd:NF038329 301 DGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1293-1449 |
2.23e-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.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 55.30 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1293 GEKGNPGQPGLPGLPGLKGDQGPPGLQGNPGRPGLNGMKGDPGLPGVPGFPGMKGPSGVPGSAGPEGEPGLIGPPGPPGL 1372
Cdd:NF038329 147 GPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGP 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1373 PGPSGQSIIIK-GDAGPPGIPGQPGLKGLPGPQGPQGLPGPTGPPGDPGRNG------------------LPGFDGAGGR 1433
Cdd:NF038329 227 AGPAGDGQQGPdGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGergpvgpagkdgqngkdgLPGKDGKDGQ 306
|
170 180
....*....|....*....|..
gi 1034673478 1434 KGDPGLPG------QPGTRGLD 1449
Cdd:NF038329 307 NGKDGLPGkdgkdgQPGKDGLP 328
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
767-995 |
3.74e-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.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 48.36 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 767 PGLPGFKGALGPKGDRGFPGPPGPPGRTGLDGLPGPKGDVGPNGQPGPMGPPGLPGIGVQGPPGPPGIPGPIGQPGlhGI 846
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA--GE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 847 PGEKGDPGPPGLDVPGPPGERGSPGIPGAPGPIGPPGSPGLPGKAGASGFPGTKGEMGMMGPPGPPGPLGIPGRSGVPGL 926
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034673478 927 KGDDGLQGQPGLPGPTGEKGSKGEPglpgppgpmdpnllGSKGEKGEPGLPGIPGVSGPKGYQGLPGDP 995
Cdd:NF038329 286 AGKDGQNGKDGLPGKDGKDGQNGKD--------------GLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1584-1694 |
7.06e-69 |
|
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: 226.32 E-value: 7.06e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1584 VIAVHSQTIQIPHCPQGWDSLWIGYSFMMHTSAGaEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYANSYSFWLATV 1663
Cdd:pfam01413 2 LIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYASNDYSYWLSTV 80
|
90 100 110
....*....|....*....|....*....|..
gi 1034673478 1664 DvsDMFSKPQSETLKAGD-LRTRISRCQVCMK 1694
Cdd:pfam01413 81 E--EQFRKPMSQTPKAGNeLRSYISRCVVCEA 110
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1473-1580 |
6.70e-63 |
|
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: 209.37 E-value: 6.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1473 FLITRHSQTTDAPQCPQGTLQVYEGFSLLYVQGNKRAHGQDLGTAGSCLRRFSTMPFMFCNINNVCNFASrNDYSYWLST 1552
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|.
gi 1034673478 1553 PE---PMPMSMQPLKGQSIQPFISRCAVCEA 1580
Cdd:pfam01413 80 VEeqfRKPMSQTPKAGNELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1582-1695 |
3.46e-62 |
|
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: 207.63 E-value: 3.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1582 AVVIAVHSQTIQIPHCPQGWDSLWIGYSFMMHTsAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYA-NSYSFWL 1660
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASrNDYSFWL 79
|
90 100 110
....*....|....*....|....*....|....*
gi 1034673478 1661 ATVDVSDMFSKPQSETLKAGDLRTRISRCQVCMKR 1695
Cdd:smart00111 80 STIEPSDQFTAPRPMTPKAGDLRPYISRCQVCEKP 114
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1472-1581 |
2.20e-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: 187.98 E-value: 2.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1472 GFLITRHSQTTDAPQCPQGTLQVYEGFSLLYVQGNKRAHGQDLGTAGSCLRRFSTMPFMFCNINNVCNFASRNDYSYWLS 1551
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80
|
90 100 110
....*....|....*....|....*....|....*
gi 1034673478 1552 TPEP-----MPMSMQPLKGQsIQPFISRCAVCEAP 1581
Cdd:smart00111 81 TIEPsdqftAPRPMTPKAGD-LRPYISRCQVCEKP 114
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
469-703 |
8.16e-14 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 75.71 E-value: 8.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 469 DKGLQGEQGVKGDKGDTCfnciGTGISGPPGQPGLPGLPGPPGSLGFPGQKGEKGQAGATGPKGLPGIPGAPGAPGFPGS 548
Cdd:NF038329 151 PPGPQGERGEKGPAGPQG----EAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGP 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 549 KGEPGDILTfpGMKGDKGELGSPGAPGLPGLPGTPGQDGLPGLPGPKGEPGGITFKGERgppgnpglpglpgnigpmgpp 628
Cdd:NF038329 227 AGPAGDGQQ--GPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV--------------------- 283
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034673478 629 gfgppgpvgekGIQGVAGNPGQPGIPGPKGDPGQTitqpGKPGLPGNPGRDGDVGLPGDPGLPGQPGLPGIPGSK 703
Cdd:NF038329 284 -----------GPAGKDGQNGKDGLPGKDGKDGQN----GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
969-1231 |
1.09e-12 |
|
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: 72.25 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 969 GEKGEPGLPGIPGVSGPKGYQGLPGDPGQPGLSGQPGLPGPPGPKGNPGLPGQPGLIGPPGLKGTIGDMGFPGPQGVEGP 1048
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1049 PGPSGVPGQPGSPGLPGQKGDKGDPGISSIGLPGLPGPKGEPGLPGYPGNPGIKGSVGDPGLPGLPGTPGAKGqpglpgf 1128
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG------- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1129 pgtpgppgpkgisgppgnpglpgepgPVGGGGHPGQPGPPGEKGKPGQ---DGIPGPAGQKGEpgqpgfgnpgpPGLPGL 1205
Cdd:NF038329 270 --------------------------PDGPDGKDGERGPVGPAGKDGQngkDGLPGKDGKDGQ-----------NGKDGL 312
|
250 260
....*....|....*....|....*.
gi 1034673478 1206 SGQKGDGGLPGIPGNPGLPGPKGEPG 1231
Cdd:NF038329 313 PGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
848-1117 |
9.21e-11 |
|
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: 66.08 E-value: 9.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 848 GEKGDPGPPGldVPGPPGERGSPGIPGAPGPIGPPGSPGLPGKAGASGFPGTKGEmgmmgppgpPGPLGIPGRSGVPGLK 927
Cdd:NF038329 117 GEKGEPGPAG--PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE---------AGPQGPAGKDGEAGAK 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 928 GDDGLQGQPGLPGPTGEKGSKGEPglpgppgpmdpnllGSKGEKGEPGLPGIPGVSGPKGyQGLPGDPGQPGLSGQPGLP 1007
Cdd:NF038329 186 GPAGEKGPQGPRGETGPAGEQGPA--------------GPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1008 GPPGPKGNPGLPGQPGLIGPPGLKGTIGDMGFPGPQGVEGPPGPSgvpgqpgspGLPGQKGDKGDPgissiGLPGLPGPK 1087
Cdd:NF038329 251 GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKD---------GLPGKDGKDGQN-----GKDGLPGKD 316
|
250 260 270
....*....|....*....|....*....|
gi 1034673478 1088 GEPGLPGYPGNPGIKGSVGDPGLPGlPGTP 1117
Cdd:NF038329 317 GKDGQPGKDGLPGKDGKDGQPGKPA-PKTP 345
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1085-1356 |
2.33e-08 |
|
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: 58.38 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1085 GPKGEPGLPGYPGNPGIKGSVGDPGLPGLPGTPGAKGqpglpgfpgtpgppgpkgisgppgnpglpgepgpvgggghpgQ 1164
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPG------------------------------------------P 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1165 PGPPGEKGKPGQDGIPGPAGQKGEPGQPgfgnpgppglpglsGQKGDGGLPGIPGNPGLPGPKGEPGFHGFPGVQGPPGP 1244
Cdd:NF038329 155 QGERGEKGPAGPQGEAGPQGPAGKDGEA--------------GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1245 PGSPGPALEGPKGNPGPQGPPGRPGPTGFQGLPGPEGPPGLPGNGGIKGEKGNPGQPGLPGLPGLKGDQGPPGLQGNPGR 1324
Cdd:NF038329 221 AGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGK 300
|
250 260 270
....*....|....*....|....*....|..
gi 1034673478 1325 PGLNGMKGDPGLPGVPGFPGMKGPSGVPGSAG 1356
Cdd:NF038329 301 DGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1205-1443 |
5.17e-08 |
|
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: 57.22 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1205 LSGQKGDGGLPGIPGNPGLPGPKGEPGFHGFPGVQGPPGPPGSPGPALEGPKGNPGPQGPPGRPgptgfQGLPGPEGPPG 1284
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK-----DGEAGAKGPAG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1285 LPGNGGIKGEKGNPGQPGLPGLPGLKGDQGPPGLQGNPGRPGlNGMKGDPGLPGVPGFPGMKGPSGVPGSAGPEGEPGLI 1364
Cdd:NF038329 190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034673478 1365 GPPGPPGLPGPsgqsiiiKGDAGPPGIPGQPGLKGLPGPQGPQGLPGPTGPPGDPGRNGLPGFDGAGGRKGDPGLPGQP 1443
Cdd:NF038329 269 GPDGPDGKDGE-------RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1293-1449 |
2.23e-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: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1293 GEKGNPGQPGLPGLPGLKGDQGPPGLQGNPGRPGLNGMKGDPGLPGVPGFPGMKGPSGVPGSAGPEGEPGLIGPPGPPGL 1372
Cdd:NF038329 147 GPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGP 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1373 PGPSGQSIIIK-GDAGPPGIPGQPGLKGLPGPQGPQGLPGPTGPPGDPGRNG------------------LPGFDGAGGR 1433
Cdd:NF038329 227 AGPAGDGQQGPdGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGergpvgpagkdgqngkdgLPGKDGKDGQ 306
|
170 180
....*....|....*....|..
gi 1034673478 1434 KGDPGLPG------QPGTRGLD 1449
Cdd:NF038329 307 NGKDGLPGkdgkdgQPGKDGLP 328
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1262-1449 |
2.93e-06 |
|
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: 51.83 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1262 QGPPGRPGPTGFQGLPGPEGPpglpgnggiKGEKGNPGQPGLPGLPGLKGDQGPPGLQGNPGRPGLNGMKGDPGLPGVPG 1341
Cdd:NF038329 125 AGPAGPAGEQGPRGDRGETGP---------AGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1342 FPGMKGPSGVPGSAGPEGEPGLIGPPGPPGLPGPSGQSII----IKGDAGPPGIPGQPGLKGLPGPQGPQGLPGPTGPPG 1417
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQgpdgDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
|
170 180 190
....*....|....*....|....*....|..
gi 1034673478 1418 DPGRNGLPGFDGAGGRKGDPGLPGQPGTRGLD 1449
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN 307
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
532-592 |
1.14e-05 |
|
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: 44.41 E-value: 1.14e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034673478 532 GLPGIPGAPGAPGFPGSKGEPGdiltFPGMKGDKGELGSPGAPGLPGLPGTPGQDGLPGLP 592
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPG----PPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1299-1355 |
3.39e-05 |
|
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: 42.87 E-value: 3.39e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034673478 1299 GQPGLPGLPGLKGDQGPPGLQGNPGRPGLNGMKGDPGLPGVPGFPGMKGPSGVPGSA 1355
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
767-995 |
3.74e-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: 48.36 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 767 PGLPGFKGALGPKGDRGFPGPPGPPGRTGLDGLPGPKGDVGPNGQPGPMGPPGLPGIGVQGPPGPPGIPGPIGQPGlhGI 846
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA--GE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 847 PGEKGDPGPPGLDVPGPPGERGSPGIPGAPGPIGPPGSPGLPGKAGASGFPGTKGEMGMMGPPGPPGPLGIPGRSGVPGL 926
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034673478 927 KGDDGLQGQPGLPGPTGEKGSKGEPglpgppgpmdpnllGSKGEKGEPGLPGIPGVSGPKGYQGLPGDP 995
Cdd:NF038329 286 AGKDGQNGKDGLPGKDGKDGQNGKD--------------GLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
773-986 |
8.35e-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: 43.74 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 773 KGALGPKGDRGFPGPPGPPGRTGLDGLPGPKGDVGPNGQPGPMGPPGLPGIGVQGPPGPPGIPGPIGQPGLHGIPGEKGD 852
Cdd:NF038329 161 KGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 853 PGPPGLDVP-GPPGERGSPGIPGAPGPIGPPGSPGLPGKAGASGFPGTKGEMGmmgppgppgplgipgRSGVPGLKGDDG 931
Cdd:NF038329 241 PGPTGEDGPqGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG---------------KDGLPGKDGKDG 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034673478 932 LQGQPGLPGPTGEKGskgepglpgppgpmdpnLLGSKGEKGEPGLPGIPGVSGPK 986
Cdd:NF038329 306 QNGKDGLPGKDGKDG-----------------QPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
294-595 |
1.79e-03 |
|
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: 42.97 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 294 GEQGEPGKRGKPGKDGENGQPGIPGLPGDPGYPGEPGRDGEKGQKGDTGPPGPPGLVIPRPGTGIT-IGEKGNIGLPGLP 372
Cdd:NF038329 165 GPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgDGQQGPDGDPGPT 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 373 GEKGERGfpgiqgppglpgppgaavmgppgppgfpgergqkgdegppgisipgppgldgqpgapglpgppgpagphipps 452
Cdd:NF038329 245 GEDGPQG------------------------------------------------------------------------- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 453 deicepgppgppgspgDKGLQGEQGVKGDKGDtcfncigtgisgppgqpglpglpgppgslgfPGQKGEKGQAGATGPKG 532
Cdd:NF038329 252 ----------------PDGPAGKDGPRGDRGE-------------------------------AGPDGPDGKDGERGPVG 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034673478 533 LPGIPGAPGAPGFPGSKGEPGDiltfPGMKGDKGELGSPGAPGLPGLPGTPGQDGLPGLPGPK 595
Cdd:NF038329 285 PAGKDGQNGKDGLPGKDGKDGQ----NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1584-1694 |
7.06e-69 |
|
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: 226.32 E-value: 7.06e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1584 VIAVHSQTIQIPHCPQGWDSLWIGYSFMMHTSAGaEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYANSYSFWLATV 1663
Cdd:pfam01413 2 LIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYASNDYSYWLSTV 80
|
90 100 110
....*....|....*....|....*....|..
gi 1034673478 1664 DvsDMFSKPQSETLKAGD-LRTRISRCQVCMK 1694
Cdd:pfam01413 81 E--EQFRKPMSQTPKAGNeLRSYISRCVVCEA 110
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1473-1580 |
6.70e-63 |
|
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: 209.37 E-value: 6.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1473 FLITRHSQTTDAPQCPQGTLQVYEGFSLLYVQGNKRAHGQDLGTAGSCLRRFSTMPFMFCNINNVCNFASrNDYSYWLST 1552
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|.
gi 1034673478 1553 PE---PMPMSMQPLKGQSIQPFISRCAVCEA 1580
Cdd:pfam01413 80 VEeqfRKPMSQTPKAGNELRSYISRCVVCEA 110
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1582-1695 |
3.46e-62 |
|
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: 207.63 E-value: 3.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1582 AVVIAVHSQTIQIPHCPQGWDSLWIGYSFMMHTsAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYA-NSYSFWL 1660
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASrNDYSFWL 79
|
90 100 110
....*....|....*....|....*....|....*
gi 1034673478 1661 ATVDVSDMFSKPQSETLKAGDLRTRISRCQVCMKR 1695
Cdd:smart00111 80 STIEPSDQFTAPRPMTPKAGDLRPYISRCQVCEKP 114
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1472-1581 |
2.20e-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: 187.98 E-value: 2.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1472 GFLITRHSQTTDAPQCPQGTLQVYEGFSLLYVQGNKRAHGQDLGTAGSCLRRFSTMPFMFCNINNVCNFASRNDYSYWLS 1551
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80
|
90 100 110
....*....|....*....|....*....|....*
gi 1034673478 1552 TPEP-----MPMSMQPLKGQsIQPFISRCAVCEAP 1581
Cdd:smart00111 81 TIEPsdqftAPRPMTPKAGD-LRPYISRCQVCEKP 114
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
469-703 |
8.16e-14 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 75.71 E-value: 8.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 469 DKGLQGEQGVKGDKGDTCfnciGTGISGPPGQPGLPGLPGPPGSLGFPGQKGEKGQAGATGPKGLPGIPGAPGAPGFPGS 548
Cdd:NF038329 151 PPGPQGERGEKGPAGPQG----EAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGP 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 549 KGEPGDILTfpGMKGDKGELGSPGAPGLPGLPGTPGQDGLPGLPGPKGEPGGITFKGERgppgnpglpglpgnigpmgpp 628
Cdd:NF038329 227 AGPAGDGQQ--GPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV--------------------- 283
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034673478 629 gfgppgpvgekGIQGVAGNPGQPGIPGPKGDPGQTitqpGKPGLPGNPGRDGDVGLPGDPGLPGQPGLPGIPGSK 703
Cdd:NF038329 284 -----------GPAGKDGQNGKDGLPGKDGKDGQN----GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
969-1231 |
1.09e-12 |
|
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: 72.25 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 969 GEKGEPGLPGIPGVSGPKGYQGLPGDPGQPGLSGQPGLPGPPGPKGNPGLPGQPGLIGPPGLKGTIGDMGFPGPQGVEGP 1048
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1049 PGPSGVPGQPGSPGLPGQKGDKGDPGISSIGLPGLPGPKGEPGLPGYPGNPGIKGSVGDPGLPGLPGTPGAKGqpglpgf 1128
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG------- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1129 pgtpgppgpkgisgppgnpglpgepgPVGGGGHPGQPGPPGEKGKPGQ---DGIPGPAGQKGEpgqpgfgnpgpPGLPGL 1205
Cdd:NF038329 270 --------------------------PDGPDGKDGERGPVGPAGKDGQngkDGLPGKDGKDGQ-----------NGKDGL 312
|
250 260
....*....|....*....|....*.
gi 1034673478 1206 SGQKGDGGLPGIPGNPGLPGPKGEPG 1231
Cdd:NF038329 313 PGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
848-1117 |
9.21e-11 |
|
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: 66.08 E-value: 9.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 848 GEKGDPGPPGldVPGPPGERGSPGIPGAPGPIGPPGSPGLPGKAGASGFPGTKGEmgmmgppgpPGPLGIPGRSGVPGLK 927
Cdd:NF038329 117 GEKGEPGPAG--PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE---------AGPQGPAGKDGEAGAK 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 928 GDDGLQGQPGLPGPTGEKGSKGEPglpgppgpmdpnllGSKGEKGEPGLPGIPGVSGPKGyQGLPGDPGQPGLSGQPGLP 1007
Cdd:NF038329 186 GPAGEKGPQGPRGETGPAGEQGPA--------------GPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1008 GPPGPKGNPGLPGQPGLIGPPGLKGTIGDMGFPGPQGVEGPPGPSgvpgqpgspGLPGQKGDKGDPgissiGLPGLPGPK 1087
Cdd:NF038329 251 GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKD---------GLPGKDGKDGQN-----GKDGLPGKD 316
|
250 260 270
....*....|....*....|....*....|
gi 1034673478 1088 GEPGLPGYPGNPGIKGSVGDPGLPGlPGTP 1117
Cdd:NF038329 317 GKDGQPGKDGLPGKDGKDGQPGKPA-PKTP 345
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1085-1356 |
2.33e-08 |
|
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: 58.38 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1085 GPKGEPGLPGYPGNPGIKGSVGDPGLPGLPGTPGAKGqpglpgfpgtpgppgpkgisgppgnpglpgepgpvgggghpgQ 1164
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPG------------------------------------------P 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1165 PGPPGEKGKPGQDGIPGPAGQKGEPGQPgfgnpgppglpglsGQKGDGGLPGIPGNPGLPGPKGEPGFHGFPGVQGPPGP 1244
Cdd:NF038329 155 QGERGEKGPAGPQGEAGPQGPAGKDGEA--------------GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1245 PGSPGPALEGPKGNPGPQGPPGRPGPTGFQGLPGPEGPPGLPGNGGIKGEKGNPGQPGLPGLPGLKGDQGPPGLQGNPGR 1324
Cdd:NF038329 221 AGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGK 300
|
250 260 270
....*....|....*....|....*....|..
gi 1034673478 1325 PGLNGMKGDPGLPGVPGFPGMKGPSGVPGSAG 1356
Cdd:NF038329 301 DGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1205-1443 |
5.17e-08 |
|
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: 57.22 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1205 LSGQKGDGGLPGIPGNPGLPGPKGEPGFHGFPGVQGPPGPPGSPGPALEGPKGNPGPQGPPGRPgptgfQGLPGPEGPPG 1284
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK-----DGEAGAKGPAG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1285 LPGNGGIKGEKGNPGQPGLPGLPGLKGDQGPPGLQGNPGRPGlNGMKGDPGLPGVPGFPGMKGPSGVPGSAGPEGEPGLI 1364
Cdd:NF038329 190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034673478 1365 GPPGPPGLPGPsgqsiiiKGDAGPPGIPGQPGLKGLPGPQGPQGLPGPTGPPGDPGRNGLPGFDGAGGRKGDPGLPGQP 1443
Cdd:NF038329 269 GPDGPDGKDGE-------RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1293-1449 |
2.23e-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: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1293 GEKGNPGQPGLPGLPGLKGDQGPPGLQGNPGRPGLNGMKGDPGLPGVPGFPGMKGPSGVPGSAGPEGEPGLIGPPGPPGL 1372
Cdd:NF038329 147 GPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGP 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1373 PGPSGQSIIIK-GDAGPPGIPGQPGLKGLPGPQGPQGLPGPTGPPGDPGRNG------------------LPGFDGAGGR 1433
Cdd:NF038329 227 AGPAGDGQQGPdGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGergpvgpagkdgqngkdgLPGKDGKDGQ 306
|
170 180
....*....|....*....|..
gi 1034673478 1434 KGDPGLPG------QPGTRGLD 1449
Cdd:NF038329 307 NGKDGLPGkdgkdgQPGKDGLP 328
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1262-1449 |
2.93e-06 |
|
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: 51.83 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1262 QGPPGRPGPTGFQGLPGPEGPpglpgnggiKGEKGNPGQPGLPGLPGLKGDQGPPGLQGNPGRPGLNGMKGDPGLPGVPG 1341
Cdd:NF038329 125 AGPAGPAGEQGPRGDRGETGP---------AGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 1342 FPGMKGPSGVPGSAGPEGEPGLIGPPGPPGLPGPSGQSII----IKGDAGPPGIPGQPGLKGLPGPQGPQGLPGPTGPPG 1417
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQgpdgDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
|
170 180 190
....*....|....*....|....*....|..
gi 1034673478 1418 DPGRNGLPGFDGAGGRKGDPGLPGQPGTRGLD 1449
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN 307
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
532-592 |
1.14e-05 |
|
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: 44.41 E-value: 1.14e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034673478 532 GLPGIPGAPGAPGFPGSKGEPGdiltFPGMKGDKGELGSPGAPGLPGLPGTPGQDGLPGLP 592
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPG----PPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1299-1355 |
3.39e-05 |
|
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: 42.87 E-value: 3.39e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034673478 1299 GQPGLPGLPGLKGDQGPPGLQGNPGRPGLNGMKGDPGLPGVPGFPGMKGPSGVPGSA 1355
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
767-995 |
3.74e-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: 48.36 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 767 PGLPGFKGALGPKGDRGFPGPPGPPGRTGLDGLPGPKGDVGPNGQPGPMGPPGLPGIGVQGPPGPPGIPGPIGQPGlhGI 846
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA--GE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 847 PGEKGDPGPPGLDVPGPPGERGSPGIPGAPGPIGPPGSPGLPGKAGASGFPGTKGEMGMMGPPGPPGPLGIPGRSGVPGL 926
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034673478 927 KGDDGLQGQPGLPGPTGEKGSKGEPglpgppgpmdpnllGSKGEKGEPGLPGIPGVSGPKGYQGLPGDP 995
Cdd:NF038329 286 AGKDGQNGKDGLPGKDGKDGQNGKD--------------GLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
646-705 |
5.93e-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: 5.93e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 646 GNPGQPGIPGPKGDPGQtitqPGKPGLPGNPGRDGDVGLPGDPGLPGQPGLPGIPGSKGE 705
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGP----PGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
535-598 |
6.74e-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: 6.74e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034673478 535 GIPGAPGAPGFPGSKGEPGDIltfpgmkGDKGELGSPGAPGLPGLPGTPGQDGLPGLPGPKGEP 598
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPP-------GPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
773-986 |
8.35e-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: 43.74 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 773 KGALGPKGDRGFPGPPGPPGRTGLDGLPGPKGDVGPNGQPGPMGPPGLPGIGVQGPPGPPGIPGPIGQPGLHGIPGEKGD 852
Cdd:NF038329 161 KGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 853 PGPPGLDVP-GPPGERGSPGIPGAPGPIGPPGSPGLPGKAGASGFPGTKGEMGmmgppgppgplgipgRSGVPGLKGDDG 931
Cdd:NF038329 241 PGPTGEDGPqGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG---------------KDGLPGKDGKDG 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034673478 932 LQGQPGLPGPTGEKGskgepglpgppgpmdpnLLGSKGEKGEPGLPGIPGVSGPK 986
Cdd:NF038329 306 QNGKDGLPGKDGKDG-----------------QPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
294-595 |
1.79e-03 |
|
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: 42.97 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 294 GEQGEPGKRGKPGKDGENGQPGIPGLPGDPGYPGEPGRDGEKGQKGDTGPPGPPGLVIPRPGTGIT-IGEKGNIGLPGLP 372
Cdd:NF038329 165 GPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgDGQQGPDGDPGPT 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 373 GEKGERGfpgiqgppglpgppgaavmgppgppgfpgergqkgdegppgisipgppgldgqpgapglpgppgpagphipps 452
Cdd:NF038329 245 GEDGPQG------------------------------------------------------------------------- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034673478 453 deicepgppgppgspgDKGLQGEQGVKGDKGDtcfncigtgisgppgqpglpglpgppgslgfPGQKGEKGQAGATGPKG 532
Cdd:NF038329 252 ----------------PDGPAGKDGPRGDRGE-------------------------------AGPDGPDGKDGERGPVG 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034673478 533 LPGIPGAPGAPGFPGSKGEPGDiltfPGMKGDKGELGSPGAPGLPGLPGTPGQDGLPGLPGPK 595
Cdd:NF038329 285 PAGKDGQNGKDGLPGKDGKDGQ----NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1311-1357 |
2.75e-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: 37.47 E-value: 2.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1034673478 1311 GDQGPPGLQGNPGRPGLNGMKGDPGLPGVPGFPGMKGPSGVPGSAGP 1357
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
|
|
| |
