|
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 ... |
436-671 |
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.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 104.22 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 436 EIGLPGPPGHDGDKGPRGKPGDmgpagpqgppgkdgppgmKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRP 515
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGE------------------TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 516 GATGLPGPIGLPGFTGEKGEAGEKGDPGAEVPGPPGPEGPPGPPGLQGFPGPKGEAGLEGSKGEKGSQGEKGDRGPLGLP 595
Cdd:NF038329 183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755534030 596 GASGLDGRPGPPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPG 671
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
303-546 |
3.97e-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: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 303 GTKGEKGAAGSPGLLGQKGEKGDAGNAigGGRGEPGPPGLPGPPGPKGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPK 382
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGET--GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 383 GAKGEPGKGEMVDYNGsinealqeirtLALMGPPGLPGQTGPPGPPGTPGQRGEIGLPGPPGHDGDKGPRGKPGDMGPAG 462
Cdd:NF038329 195 GPRGETGPAGEQGPAG-----------PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 463 PQGPPGKDGPPGMKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEAGEKGDP 542
Cdd:NF038329 264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
....
gi 755534030 543 GAEV 546
Cdd:NF038329 344 TPEV 347
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
150-390 |
1.07e-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.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 67.62 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 150 GFPGFPGPIGLDGRPGLVGPRGQPGPQGQKGEKGQCGEyphrllpllnsvrlapppvikrrtfQGEQSQTGIQGPPGPPG 229
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGP-------------------------QGERGEKGPAGPQGEAG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 230 PPGPSGPLGHPGLPGPIGPPGLPGPPGPKGDPGIQGYHGRKGERGMPGMPGKHGAKGVPGIAVAGMKGEPGTPGTKGEKG 309
Cdd:NF038329 172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 310 AAGSPGLLGQKGEKGDAGNAigGGRGEPGPPGLPGPPGPKGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPKGAKGEPG 389
Cdd:NF038329 252 PDGPAGKDGPRGDRGEAGPD--GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
|
.
gi 755534030 390 K 390
Cdd:NF038329 330 K 330
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
436-671 |
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: 104.22 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 436 EIGLPGPPGHDGDKGPRGKPGDmgpagpqgppgkdgppgmKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRP 515
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGE------------------TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 516 GATGLPGPIGLPGFTGEKGEAGEKGDPGAEVPGPPGPEGPPGPPGLQGFPGPKGEAGLEGSKGEKGSQGEKGDRGPLGLP 595
Cdd:NF038329 183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755534030 596 GASGLDGRPGPPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPG 671
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
303-546 |
3.97e-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: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 303 GTKGEKGAAGSPGLLGQKGEKGDAGNAigGGRGEPGPPGLPGPPGPKGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPK 382
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGET--GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 383 GAKGEPGKGEMVDYNGsinealqeirtLALMGPPGLPGQTGPPGPPGTPGQRGEIGLPGPPGHDGDKGPRGKPGDMGPAG 462
Cdd:NF038329 195 GPRGETGPAGEQGPAG-----------PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 463 PQGPPGKDGPPGMKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEAGEKGDP 542
Cdd:NF038329 264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
....
gi 755534030 543 GAEV 546
Cdd:NF038329 344 TPEV 347
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
476-678 |
4.39e-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: 4.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 476 KGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEAGEKGDPGAevPGPPGPEGP 555
Cdd:NF038329 131 AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE--TGPAGEQGP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 556 PGPPGLQGFPGPKGEAGLEGSKGeKGSQGEKGDRGPLGLPGASGLDGRPGPPGTPGPIGVPGPAGPKGERGSKGDPGMTG 635
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 755534030 636 PTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPGLDGLDAP 678
Cdd:NF038329 288 KDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
150-390 |
1.07e-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: 67.62 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 150 GFPGFPGPIGLDGRPGLVGPRGQPGPQGQKGEKGQCGEyphrllpllnsvrlapppvikrrtfQGEQSQTGIQGPPGPPG 229
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGP-------------------------QGERGEKGPAGPQGEAG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 230 PPGPSGPLGHPGLPGPIGPPGLPGPPGPKGDPGIQGYHGRKGERGMPGMPGKHGAKGVPGIAVAGMKGEPGTPGTKGEKG 309
Cdd:NF038329 172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 310 AAGSPGLLGQKGEKGDAGNAigGGRGEPGPPGLPGPPGPKGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPKGAKGEPG 389
Cdd:NF038329 252 PDGPAGKDGPRGDRGEAGPD--GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
|
.
gi 755534030 390 K 390
Cdd:NF038329 330 K 330
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
159-510 |
1.26e-10 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 64.16 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 159 GLDGRPGLVGPRGQPGPQGQKGEKGQCGEYphrllpllnsvrlapppviKRRTFQGEQSQTGIQGPPGPPgppgpsgplg 238
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPA-------------------GPAGPPGPQGERGEKGPAGPQ---------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 239 hpglpgpigppglpgppgpkgdpgiqgyhGRKGERGMPGMPGKHGAKGVPGIA-VAGMKGEPGTPGTKGEKGAAGSPGLL 317
Cdd:NF038329 168 -----------------------------GEAGPQGPAGKDGEAGAKGPAGEKgPQGPRGETGPAGEQGPAGPAGPDGEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 318 GQKGEKGDAGNAigggrgepgppglpgppgpkgEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPKGAKGEPGKGEMVDYN 397
Cdd:NF038329 219 GPAGEDGPAGPA---------------------GDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 398 GsinealqeirtlalmgppglpgqtgppgppgtpgqrgEIGLPGPPGHDGDKGPRGKPGdmgpagpqgppgkdgPPGMKG 477
Cdd:NF038329 278 G-------------------------------------ERGPVGPAGKDGQNGKDGLPG---------------KDGKDG 305
|
330 340 350
....*....|....*....|....*....|...
gi 755534030 478 EVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPG 510
Cdd:NF038329 306 QNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
477-528 |
1.55e-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: 1.55e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 755534030 477 GEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPG 528
Cdd:pfam01391 4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
133-390 |
8.13e-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: 45.67 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 133 DKGAIGMPGRVGQPGTRgfpGFPGPIGLDGRPGLVGPRGQPGPQGQKGEKGQCGeyphrllpllnsvrlapppvikrrtf 212
Cdd:NF038329 181 EAGAKGPAGEKGPQGPR---GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------------------------- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 213 QGEQSQTGiqgppgppgppgpsgplghpglpgpigppglpgppgpkgdpgIQGYHGRKGERGMPGMPGKHGAKGVPGIAv 292
Cdd:NF038329 232 DGQQGPDG------------------------------------------DPGPTGEDGPQGPDGPAGKDGPRGDRGEA- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 293 agmkGEPGTPGTKGEKGAAGSPGLLGQKGEKGDAGNAigggrgepgppglpgppgpkgeaGVDGQAGPPGQQGDKGQPGA 372
Cdd:NF038329 269 ----GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD-----------------------GKDGQNGKDGLPGKDGKDGQ 321
|
250
....*....|....*...
gi 755534030 373 AGEQGPSGPKGAKGEPGK 390
Cdd:NF038329 322 PGKDGLPGKDGKDGQPGK 339
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
134-185 |
1.87e-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: 1.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 755534030 134 KGAIGMPGRVGQPGTRGFPGFPGPIGLDGRPGLVGPRGQPGPQGQKGEKGQC 185
Cdd:pfam01391 6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
436-671 |
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: 104.22 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 436 EIGLPGPPGHDGDKGPRGKPGDmgpagpqgppgkdgppgmKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRP 515
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGE------------------TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 516 GATGLPGPIGLPGFTGEKGEAGEKGDPGAEVPGPPGPEGPPGPPGLQGFPGPKGEAGLEGSKGEKGSQGEKGDRGPLGLP 595
Cdd:NF038329 183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755534030 596 GASGLDGRPGPPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPG 671
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
303-546 |
3.97e-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: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 303 GTKGEKGAAGSPGLLGQKGEKGDAGNAigGGRGEPGPPGLPGPPGPKGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPK 382
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGET--GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 383 GAKGEPGKGEMVDYNGsinealqeirtLALMGPPGLPGQTGPPGPPGTPGQRGEIGLPGPPGHDGDKGPRGKPGDMGPAG 462
Cdd:NF038329 195 GPRGETGPAGEQGPAG-----------PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 463 PQGPPGKDGPPGMKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEAGEKGDP 542
Cdd:NF038329 264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
....
gi 755534030 543 GAEV 546
Cdd:NF038329 344 TPEV 347
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
476-678 |
4.39e-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: 4.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 476 KGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEAGEKGDPGAevPGPPGPEGP 555
Cdd:NF038329 131 AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE--TGPAGEQGP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 556 PGPPGLQGFPGPKGEAGLEGSKGeKGSQGEKGDRGPLGLPGASGLDGRPGPPGTPGPIGVPGPAGPKGERGSKGDPGMTG 635
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 755534030 636 PTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPGLDGLDAP 678
Cdd:NF038329 288 KDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
150-390 |
1.07e-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: 67.62 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 150 GFPGFPGPIGLDGRPGLVGPRGQPGPQGQKGEKGQCGEyphrllpllnsvrlapppvikrrtfQGEQSQTGIQGPPGPPG 229
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGP-------------------------QGERGEKGPAGPQGEAG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 230 PPGPSGPLGHPGLPGPIGPPGLPGPPGPKGDPGIQGYHGRKGERGMPGMPGKHGAKGVPGIAVAGMKGEPGTPGTKGEKG 309
Cdd:NF038329 172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 310 AAGSPGLLGQKGEKGDAGNAigGGRGEPGPPGLPGPPGPKGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPKGAKGEPG 389
Cdd:NF038329 252 PDGPAGKDGPRGDRGEAGPD--GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
|
.
gi 755534030 390 K 390
Cdd:NF038329 330 K 330
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
159-510 |
1.26e-10 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 64.16 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 159 GLDGRPGLVGPRGQPGPQGQKGEKGQCGEYphrllpllnsvrlapppviKRRTFQGEQSQTGIQGPPGPPgppgpsgplg 238
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPA-------------------GPAGPPGPQGERGEKGPAGPQ---------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 239 hpglpgpigppglpgppgpkgdpgiqgyhGRKGERGMPGMPGKHGAKGVPGIA-VAGMKGEPGTPGTKGEKGAAGSPGLL 317
Cdd:NF038329 168 -----------------------------GEAGPQGPAGKDGEAGAKGPAGEKgPQGPRGETGPAGEQGPAGPAGPDGEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 318 GQKGEKGDAGNAigggrgepgppglpgppgpkgEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPKGAKGEPGKGEMVDYN 397
Cdd:NF038329 219 GPAGEDGPAGPA---------------------GDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 398 GsinealqeirtlalmgppglpgqtgppgppgtpgqrgEIGLPGPPGHDGDKGPRGKPGdmgpagpqgppgkdgPPGMKG 477
Cdd:NF038329 278 G-------------------------------------ERGPVGPAGKDGQNGKDGLPG---------------KDGKDG 305
|
330 340 350
....*....|....*....|....*....|...
gi 755534030 478 EVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPG 510
Cdd:NF038329 306 QNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
477-528 |
1.55e-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: 1.55e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 755534030 477 GEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPG 528
Cdd:pfam01391 4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
480-536 |
1.78e-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: 1.78e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 755534030 480 GPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEA 536
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
133-390 |
8.13e-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: 45.67 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 133 DKGAIGMPGRVGQPGTRgfpGFPGPIGLDGRPGLVGPRGQPGPQGQKGEKGQCGeyphrllpllnsvrlapppvikrrtf 212
Cdd:NF038329 181 EAGAKGPAGEKGPQGPR---GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------------------------- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 213 QGEQSQTGiqgppgppgppgpsgplghpglpgpigppglpgppgpkgdpgIQGYHGRKGERGMPGMPGKHGAKGVPGIAv 292
Cdd:NF038329 232 DGQQGPDG------------------------------------------DPGPTGEDGPQGPDGPAGKDGPRGDRGEA- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534030 293 agmkGEPGTPGTKGEKGAAGSPGLLGQKGEKGDAGNAigggrgepgppglpgppgpkgeaGVDGQAGPPGQQGDKGQPGA 372
Cdd:NF038329 269 ----GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD-----------------------GKDGQNGKDGLPGKDGKDGQ 321
|
250
....*....|....*...
gi 755534030 373 AGEQGPSGPKGAKGEPGK 390
Cdd:NF038329 322 PGKDGLPGKDGKDGQPGK 339
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
626-674 |
1.80e-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: 1.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 755534030 626 GSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPGLDG 674
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
134-185 |
1.87e-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: 1.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 755534030 134 KGAIGMPGRVGQPGTRGFPGFPGPIGLDGRPGLVGPRGQPGPQGQKGEKGQC 185
Cdd:pfam01391 6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
623-671 |
3.44e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.32 E-value: 3.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 755534030 623 GERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPG 671
Cdd:pfam01391 7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
138-187 |
5.21e-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: 5.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 755534030 138 GMPGRVGQPGTRGFPGFPGPIGLDGRPGLVGPRGQPGPQGQKGEKGQCGE 187
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
|
|
| |
