|
Name |
Accession |
Description |
Interval |
E-value |
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
430-665 |
2.89e-23 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats. The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 103.45 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 430 EIGLPGPPGHDGDKGPRGKPGDmgpagpqgppgkdgppgmKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRP 509
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGE------------------TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 510 GATGLPGPIGLPGFTGEKGEAGEKGDPGAEVPGPPGPEGPPGPPGLQGFPGPKGEAGLEGSKGEKGSQGEKGDRGPLGLP 589
Cdd:NF038329 183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360270 590 GASGLDGRPGPPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPG 665
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
297-540 |
7.18e-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: 96.13 E-value: 7.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 297 GTKGEKGAAGSPGLLGQKGEKGDAGNAigGGRGEPGPPGLPGPPGPKGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPK 376
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGET--GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 377 GAKGEPGKGEMVDYNGsinealqeirtLALMGPPGLPGQTGPPGPPGTPGQRGEIGLPGPPGHDGDKGPRGKPGDMGPAG 456
Cdd:NF038329 195 GPRGETGPAGEQGPAG-----------PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 457 PQGPPGKDGPPGMKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEAGEKGDP 536
Cdd:NF038329 264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
....
gi 1720360270 537 GAEV 540
Cdd:NF038329 344 TPEV 347
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
133-384 |
8.54e-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. The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 42.58 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 133 QPGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQkGEKGQCGEyphreypggmlaalrsnpimslkgeqsq 212
Cdd:NF038329 190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGD---------------------------- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 213 tgiqgppgppgppgpsgplghpglpgpigppglpgppgpkgdpgiQGYHGRKGERGMPGMPGKHGAKGVPGIAvagmkGE 292
Cdd:NF038329 241 ---------------------------------------------PGPTGEDGPQGPDGPAGKDGPRGDRGEA-----GP 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 293 PGTPGTKGEKGAAGSPGLLGQKGEKGDAGNAigggrgepgppglpgppgpkgeaGVDGQAGPPGQQGDKGQPGAAGEQGP 372
Cdd:NF038329 271 DGPDGKDGERGPVGPAGKDGQNGKDGLPGKD-----------------------GKDGQNGKDGLPGKDGKDGQPGKDGL 327
|
250
....*....|..
gi 1720360270 373 SGPKGAKGEPGK 384
Cdd:NF038329 328 PGKDGKDGQPGK 339
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
430-665 |
2.89e-23 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 103.45 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 430 EIGLPGPPGHDGDKGPRGKPGDmgpagpqgppgkdgppgmKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRP 509
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGE------------------TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 510 GATGLPGPIGLPGFTGEKGEAGEKGDPGAEVPGPPGPEGPPGPPGLQGFPGPKGEAGLEGSKGEKGSQGEKGDRGPLGLP 589
Cdd:NF038329 183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360270 590 GASGLDGRPGPPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPG 665
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
297-540 |
7.18e-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: 96.13 E-value: 7.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 297 GTKGEKGAAGSPGLLGQKGEKGDAGNAigGGRGEPGPPGLPGPPGPKGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPK 376
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGET--GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 377 GAKGEPGKGEMVDYNGsinealqeirtLALMGPPGLPGQTGPPGPPGTPGQRGEIGLPGPPGHDGDKGPRGKPGDMGPAG 456
Cdd:NF038329 195 GPRGETGPAGEQGPAG-----------PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 457 PQGPPGKDGPPGMKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEAGEKGDP 536
Cdd:NF038329 264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
....
gi 1720360270 537 GAEV 540
Cdd:NF038329 344 TPEV 347
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
470-672 |
7.78e-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: 96.13 E-value: 7.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 470 KGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEAGEKGDPGAevPGPPGPEGP 549
Cdd:NF038329 131 AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE--TGPAGEQGP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 550 PGPPGLQGFPGPKGEAGLEGSKGeKGSQGEKGDRGPLGLPGASGLDGRPGPPGTPGPIGVPGPAGPKGERGSKGDPGMTG 629
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720360270 630 PTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPGLDGLDAP 672
Cdd:NF038329 288 KDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
148-504 |
3.89e-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: 68.78 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 148 LDGRPGHPGPKGEMGlvgPRGQPGPQGQKGEKGQcgeyphreypggmlaalrsnpimslkgeqsqtgiqgppgppgppgp 227
Cdd:NF038329 115 GDGEKGEPGPAGPAG---PAGEQGPRGDRGETGP---------------------------------------------- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 228 sgplghpglpgpigppglpgppgpkgdpgiQGYHGRKGERGMPGMPGKHGAKGVPGiaVAGMKGEPGTPGTKGEKGAAGS 307
Cdd:NF038329 146 ------------------------------AGPAGPPGPQGERGEKGPAGPQGEAG--PQGPAGKDGEAGAKGPAGEKGP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 308 PGLLGQKGEKGDAGNAIGGGRGEPGPPGLPGPPGPKGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPKGAKGEPGKGEM 387
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 388 VDYNGsinealqeirtlalmgppglpgqtgppgppgtpgqrgEIGLPGPPGHDGDKGPRGKPGdmgpagpqgppgkdgPP 467
Cdd:NF038329 274 DGKDG-------------------------------------ERGPVGPAGKDGQNGKDGLPG---------------KD 301
|
330 340 350
....*....|....*....|....*....|....*..
gi 1720360270 468 GMKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPG 504
Cdd:NF038329 302 GKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
471-522 |
1.54e-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: 1.54e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1720360270 471 GEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPG 522
Cdd:pfam01391 4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
133-384 |
8.54e-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: 42.58 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 133 QPGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQkGEKGQCGEyphreypggmlaalrsnpimslkgeqsq 212
Cdd:NF038329 190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGD---------------------------- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 213 tgiqgppgppgppgpsgplghpglpgpigppglpgppgpkgdpgiQGYHGRKGERGMPGMPGKHGAKGVPGIAvagmkGE 292
Cdd:NF038329 241 ---------------------------------------------PGPTGEDGPQGPDGPAGKDGPRGDRGEA-----GP 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 293 PGTPGTKGEKGAAGSPGLLGQKGEKGDAGNAigggrgepgppglpgppgpkgeaGVDGQAGPPGQQGDKGQPGAAGEQGP 372
Cdd:NF038329 271 DGPDGKDGERGPVGPAGKDGQNGKDGLPGKD-----------------------GKDGQNGKDGLPGKDGKDGQPGKDGL 327
|
250
....*....|..
gi 1720360270 373 SGPKGAKGEPGK 384
Cdd:NF038329 328 PGKDGKDGQPGK 339
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
134-182 |
1.27e-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: 1.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720360270 134 PGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQKGEKGQC 182
Cdd:pfam01391 9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
430-665 |
2.89e-23 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 103.45 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 430 EIGLPGPPGHDGDKGPRGKPGDmgpagpqgppgkdgppgmKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRP 509
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGE------------------TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 510 GATGLPGPIGLPGFTGEKGEAGEKGDPGAEVPGPPGPEGPPGPPGLQGFPGPKGEAGLEGSKGEKGSQGEKGDRGPLGLP 589
Cdd:NF038329 183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360270 590 GASGLDGRPGPPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPG 665
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
297-540 |
7.18e-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: 96.13 E-value: 7.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 297 GTKGEKGAAGSPGLLGQKGEKGDAGNAigGGRGEPGPPGLPGPPGPKGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPK 376
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGET--GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 377 GAKGEPGKGEMVDYNGsinealqeirtLALMGPPGLPGQTGPPGPPGTPGQRGEIGLPGPPGHDGDKGPRGKPGDMGPAG 456
Cdd:NF038329 195 GPRGETGPAGEQGPAG-----------PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 457 PQGPPGKDGPPGMKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEAGEKGDP 536
Cdd:NF038329 264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
....
gi 1720360270 537 GAEV 540
Cdd:NF038329 344 TPEV 347
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
470-672 |
7.78e-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: 96.13 E-value: 7.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 470 KGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEAGEKGDPGAevPGPPGPEGP 549
Cdd:NF038329 131 AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE--TGPAGEQGP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 550 PGPPGLQGFPGPKGEAGLEGSKGeKGSQGEKGDRGPLGLPGASGLDGRPGPPGTPGPIGVPGPAGPKGERGSKGDPGMTG 629
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720360270 630 PTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPGLDGLDAP 672
Cdd:NF038329 288 KDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
148-504 |
3.89e-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: 68.78 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 148 LDGRPGHPGPKGEMGlvgPRGQPGPQGQKGEKGQcgeyphreypggmlaalrsnpimslkgeqsqtgiqgppgppgppgp 227
Cdd:NF038329 115 GDGEKGEPGPAGPAG---PAGEQGPRGDRGETGP---------------------------------------------- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 228 sgplghpglpgpigppglpgppgpkgdpgiQGYHGRKGERGMPGMPGKHGAKGVPGiaVAGMKGEPGTPGTKGEKGAAGS 307
Cdd:NF038329 146 ------------------------------AGPAGPPGPQGERGEKGPAGPQGEAG--PQGPAGKDGEAGAKGPAGEKGP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 308 PGLLGQKGEKGDAGNAIGGGRGEPGPPGLPGPPGPKGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPKGAKGEPGKGEM 387
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 388 VDYNGsinealqeirtlalmgppglpgqtgppgppgtpgqrgEIGLPGPPGHDGDKGPRGKPGdmgpagpqgppgkdgPP 467
Cdd:NF038329 274 DGKDG-------------------------------------ERGPVGPAGKDGQNGKDGLPG---------------KD 301
|
330 340 350
....*....|....*....|....*....|....*..
gi 1720360270 468 GMKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPG 504
Cdd:NF038329 302 GKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
471-522 |
1.54e-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: 1.54e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1720360270 471 GEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPG 522
Cdd:pfam01391 4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
474-530 |
1.77e-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: 42.48 E-value: 1.77e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360270 474 GPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEA 530
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
133-384 |
8.54e-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: 42.58 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 133 QPGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQkGEKGQCGEyphreypggmlaalrsnpimslkgeqsq 212
Cdd:NF038329 190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGD---------------------------- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 213 tgiqgppgppgppgpsgplghpglpgpigppglpgppgpkgdpgiQGYHGRKGERGMPGMPGKHGAKGVPGIAvagmkGE 292
Cdd:NF038329 241 ---------------------------------------------PGPTGEDGPQGPDGPAGKDGPRGDRGEA-----GP 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360270 293 PGTPGTKGEKGAAGSPGLLGQKGEKGDAGNAigggrgepgppglpgppgpkgeaGVDGQAGPPGQQGDKGQPGAAGEQGP 372
Cdd:NF038329 271 DGPDGKDGERGPVGPAGKDGQNGKDGLPGKD-----------------------GKDGQNGKDGLPGKDGKDGQPGKDGL 327
|
250
....*....|..
gi 1720360270 373 SGPKGAKGEPGK 384
Cdd:NF038329 328 PGKDGKDGQPGK 339
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
134-182 |
1.27e-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: 1.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720360270 134 PGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQKGEKGQC 182
Cdd:pfam01391 9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
620-668 |
1.78e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.09 E-value: 1.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720360270 620 GSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPGLDG 668
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
617-665 |
3.41e-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: 3.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720360270 617 GERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPG 665
Cdd:pfam01391 7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
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