|
Name |
Accession |
Description |
Interval |
E-value |
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
75-258 |
6.14e-57 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
:
Pssm-ID: 214560 Cd Length: 184 Bit Score: 194.88 E-value: 6.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 75 NKLEVSGFDLGD-SFSLRRAFC-ESDKTCFKLGS-ALLIRDTIKIFPKGLPEEYSVAAMFRVRrnaKKERWFLWQVLNQQ 151
Cdd:smart00210 1 GQDLLQVFDLPSlSFAIRQVVGpEPGSPAYRLGDpALVPQPTRDLFPSGLPEDFSLLTTFRQT---PKSRGVLFAIYDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 152 NIPQISIVVDGGKKVVEFMFQATEGDVLNYIFRNrelRPLFDRQWHKLGISIQSQVISLYMDCNLIARRQTDEKD--TVD 229
Cdd:smart00210 78 NVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGqpPID 154
|
170 180
....*....|....*....|....*....
gi 767941890 230 FHGRTVIATRASDGKPVDIELHQLKIYCS 258
Cdd:smart00210 155 TDGIEVRGAQAADRKPFQGDLQQLKIVCD 183
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
461-691 |
5.59e-30 |
|
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: 124.63 E-value: 5.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 461 QTLGGYYNKDNKGNDEHEAGGLKGDKGETGLPGFPGSVGPKGQKGEPGEPFTKGEKGDRGEPGVIGSQGVKGEPGDPGPP 540
Cdd:NF038329 97 KKLNSYLEELDEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 541 GLIGSPGLKGQQGSAGSMGPRGPPGDVGLPGEHGIPGKQGIKGEKgdPGGIIGPPGLPGPKGEAGPPGKSlpGEPGLDGN 620
Cdd:NF038329 177 GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA--GEDGPAGPAGDGQQGPDGDPGPT--GEDGPQGP 252
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767941890 621 PGAPGPRGPKGERGLPGVHGSPGDIGPQG-IGIPGRTGAQGPAGEPGIQGPRGLPGLPGTPGTPGNDGVPGR 691
Cdd:NF038329 253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGpVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
769-1020 |
3.82e-19 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 91.89 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 769 GPKGSKGERGYPGIPGEKGDEGLQGIPGIPGAPGPTGPPGLMGRTGHPGPTGAKGEKGSDGPPGKPGppgppgipfnern 848
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG------------- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 849 gmsslykikggvnvpsypgppgppgpkgdpgpvgEPGAMGLPGLEGFPGVKGDRGPAGPPGIAGmSGKPGAPGPPGVPGE 928
Cdd:NF038329 187 ----------------------------------PAGEKGPQGPRGETGPAGEQGPAGPAGPDG-EAGPAGEDGPAGPAG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 929 PGERGPVGDIGFPGPEGPSGKPGINGKDGIPGAQGIMGKPGDRGPKGERGDQGIPGDRGSQGERGKPGLTGMKGAIGPMG 1008
Cdd:NF038329 232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
|
250
....*....|..
gi 767941890 1009 PPGNKGSMGSPG 1020
Cdd:NF038329 312 LPGKDGKDGQPG 323
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
316-439 |
1.47e-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: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 316 KGEAGLPGAPGSPGQKGHKGEPGENGLHGAPGFPGQKGEQGfEGSKGETGEKGEQGEKGDPALAGLNGENGLKGDLGPHG 395
Cdd:NF038329 191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767941890 396 PPGPKGEKGDTGPPGPPALPGSLGIQGPQGPPGKEGQ------RGRRGKT 439
Cdd:NF038329 270 PDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQngkdglPGKDGKD 319
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
75-258 |
6.14e-57 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 194.88 E-value: 6.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 75 NKLEVSGFDLGD-SFSLRRAFC-ESDKTCFKLGS-ALLIRDTIKIFPKGLPEEYSVAAMFRVRrnaKKERWFLWQVLNQQ 151
Cdd:smart00210 1 GQDLLQVFDLPSlSFAIRQVVGpEPGSPAYRLGDpALVPQPTRDLFPSGLPEDFSLLTTFRQT---PKSRGVLFAIYDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 152 NIPQISIVVDGGKKVVEFMFQATEGDVLNYIFRNrelRPLFDRQWHKLGISIQSQVISLYMDCNLIARRQTDEKD--TVD 229
Cdd:smart00210 78 NVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGqpPID 154
|
170 180
....*....|....*....|....*....
gi 767941890 230 FHGRTVIATRASDGKPVDIELHQLKIYCS 258
Cdd:smart00210 155 TDGIEVRGAQAADRKPFQGDLQQLKIVCD 183
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
461-691 |
5.59e-30 |
|
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: 124.63 E-value: 5.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 461 QTLGGYYNKDNKGNDEHEAGGLKGDKGETGLPGFPGSVGPKGQKGEPGEPFTKGEKGDRGEPGVIGSQGVKGEPGDPGPP 540
Cdd:NF038329 97 KKLNSYLEELDEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 541 GLIGSPGLKGQQGSAGSMGPRGPPGDVGLPGEHGIPGKQGIKGEKgdPGGIIGPPGLPGPKGEAGPPGKSlpGEPGLDGN 620
Cdd:NF038329 177 GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA--GEDGPAGPAGDGQQGPDGDPGPT--GEDGPQGP 252
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767941890 621 PGAPGPRGPKGERGLPGVHGSPGDIGPQG-IGIPGRTGAQGPAGEPGIQGPRGLPGLPGTPGTPGNDGVPGR 691
Cdd:NF038329 253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGpVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
357-691 |
3.36e-21 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 98.05 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 357 FEGSKGETGEKGEQGEKGDPalaglngenglkgdlgphgppGPKGEKGDTGPPGPPALPGSLGIQGPQGPPGKEGQRGRR 436
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQ---------------------GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 437 GKTGPPGKPgppgppgppgiqgihqtlggyynkdnkgndeheagGLKGDKGETGLPGFPGSVGPKGQKGEPGEPFTKGEK 516
Cdd:NF038329 174 GPAGKDGEA-----------------------------------GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 517 GDRGEPGVIGSQGVKGEpgdpgppgliGSPGLKGQQGSAGSMGPRGPPGDVGLPGEHGIPGKQGIKGEkgdpggiigppg 596
Cdd:NF038329 219 GPAGEDGPAGPAGDGQQ----------GPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK------------ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 597 lpgpKGEAGPPGKslPGEPGLDGNPGAPGPRGPKGERGLPGVHGSPGDIGPQGI-GIPGRTGAQGPAGEPGIQGPRgLPG 675
Cdd:NF038329 277 ----DGERGPVGP--AGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKdGLPGKDGKDGQPGKPAPKTPE-VPQ 349
|
330
....*....|....*..
gi 767941890 676 LPGT-PGTPGNDGVPGR 691
Cdd:NF038329 350 KPDTaPHTPKTPQIPGQ 366
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
769-1020 |
3.82e-19 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 91.89 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 769 GPKGSKGERGYPGIPGEKGDEGLQGIPGIPGAPGPTGPPGLMGRTGHPGPTGAKGEKGSDGPPGKPGppgppgipfnern 848
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG------------- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 849 gmsslykikggvnvpsypgppgppgpkgdpgpvgEPGAMGLPGLEGFPGVKGDRGPAGPPGIAGmSGKPGAPGPPGVPGE 928
Cdd:NF038329 187 ----------------------------------PAGEKGPQGPRGETGPAGEQGPAGPAGPDG-EAGPAGEDGPAGPAG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 929 PGERGPVGDIGFPGPEGPSGKPGINGKDGIPGAQGIMGKPGDRGPKGERGDQGIPGDRGSQGERGKPGLTGMKGAIGPMG 1008
Cdd:NF038329 232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
|
250
....*....|..
gi 767941890 1009 PPGNKGSMGSPG 1020
Cdd:NF038329 312 LPGKDGKDGQPG 323
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
895-1123 |
6.44e-19 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 91.12 E-value: 6.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 895 FPGVKGDRGPAGPPGIAGmsgkpgapgppgvpgepgERGPVGDIGFPGPEGPSGKPGINGKDGIPGAQGIMGKPGDRGPK 974
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAG------------------EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 975 GERGDQGIPGDRGSQGERGKPGLTGMKGAIGPMGPPGNKGSMGSPGHQGPPGSPGIPGIPADAvsfeeikkyinqevlri 1054
Cdd:NF038329 177 GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG----------------- 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767941890 1055 feermavflsqlkLPAAMLAAQAYGRPGPPGKDGLPGPPGDPGPQGYRGQKGERGEPGI----GLPGSPGLPG 1123
Cdd:NF038329 240 -------------DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPagkdGQNGKDGLPG 299
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
883-1126 |
3.45e-13 |
|
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: 73.02 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 883 EPGAMGLPGLEGFPGVKGDRGPAGPPGIAGMSGKPGAPGPPGVPGEPGERGPVG---------DIGFPGPEGPSGKPGIN 953
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGpagkdgeagAKGPAGEKGPQGPRGET 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 954 GKDGIPGAQGIMGKPGDRGPKGERGDQGIPGDrGSQGERGKPGLTGMKGAIGPMGPPGNKGSMGSPGhqGPPGSPGIPGI 1033
Cdd:NF038329 201 GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG--EAGPDGPDGKD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 1034 PADAVSFEEIKKYINQEVlrifeermavflsqlklpaaMLAAQAyGRPGPPGKDGLPgppgdpgpqgyrGQKGERGEPG- 1112
Cdd:NF038329 278 GERGPVGPAGKDGQNGKD--------------------GLPGKD-GKDGQNGKDGLP------------GKDGKDGQPGk 324
|
250
....*....|....*..
gi 767941890 1113 ---IGLPGSPGLPGTSA 1126
Cdd:NF038329 325 dglPGKDGKDGQPGKPA 341
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
316-439 |
1.47e-07 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 55.30 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 316 KGEAGLPGAPGSPGQKGHKGEPGENGLHGAPGFPGQKGEQGfEGSKGETGEKGEQGEKGDPALAGLNGENGLKGDLGPHG 395
Cdd:NF038329 191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767941890 396 PPGPKGEKGDTGPPGPPALPGSLGIQGPQGPPGKEGQ------RGRRGKT 439
Cdd:NF038329 270 PDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQngkdglPGKDGKD 319
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
317-448 |
3.07e-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: 54.14 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 317 GEAGLPGAPGSPGQKGHKGEPGENGlHGAPGFPGQKGEQGFEGSKGETGEKGEQGEKGDPALAGLNGENGLKGDLGPHGP 396
Cdd:NF038329 207 GPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 767941890 397 PGPKGEKGDTGPPGPPALPGSLGIQGPQGPPGKEGQRGRRGKTGPPGKPGPP 448
Cdd:NF038329 286 AGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
317-369 |
6.17e-07 |
|
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: 47.49 E-value: 6.17e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 767941890 317 GEAGLPGAPGSPGQKGHKGEPGENGLHGAPGFPGQKGEQGFEGSKGETGEKGE 369
Cdd:pfam01391 4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
966-1020 |
7.14e-07 |
|
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: 47.10 E-value: 7.14e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 767941890 966 GKPGDRGPKGERGDQGIPGDRGSQGERGKPGLTGMKGAIGPMGPPGNKGSMGSPG 1020
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
603-665 |
5.64e-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: 41.71 E-value: 5.64e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767941890 603 EAGPPGKslPGEPGLDGNPGAPGPRGPKGERGLPGVHGSPGDigpqgigiPGRTGAQGPAGEP 665
Cdd:pfam01391 5 PPGPPGP--PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGP--------PGPPGAPGAPGPP 57
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
367-682 |
4.68e-04 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 44.25 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 367 KGEQGEKGDPAlaglNGENGLKGDLGPHGPPGPKGEKGDTGPPGPPALPGSLGIQGPQGPPGKEGQRGRRGKTGPPGKPG 446
Cdd:COG5164 1 TGLYGPGKTGP----SDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 447 PPGPpgppgiQGIHQTLGGYYNKDNKGndeheAGGLKGDKGETGLPGFPGSVGPKGQKGEPGEPFT--KGEKGDRGE-PG 523
Cdd:COG5164 77 NQGG------TTPAQNQGGTRPAGNTG-----GTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGgsTTPPGDGGStPP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 524 VIGSQGVKGEPGDPGPPGLIGSPGLKGQQGSAGSMGPRGPP--GDVGLPGEHGIPGKQGIKGEKGDPGGIIGPPGLPGPK 601
Cdd:COG5164 146 GPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 602 GEAGPPGKSLPGEPgldgnpgaPGPRGPKGERGLPGVHGSPGDIGPQGIGIPGRTGAQGPAGEPGIQGPRGLPGLPGTPG 681
Cdd:COG5164 226 GKTGPKDQRPKTNP--------IERRGPERPEAAALPAELTALEAENRAANPEPATKTIPETTTVKDLATVLGKKGSDLV 297
|
.
gi 767941890 682 T 682
Cdd:COG5164 298 T 298
|
|
| PHA03264 |
PHA03264 |
envelope glycoprotein D; Provisional |
606-689 |
9.11e-03 |
|
envelope glycoprotein D; Provisional
Pssm-ID: 223029 [Multi-domain] Cd Length: 416 Bit Score: 39.99 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 606 PPGKSLPgEPGLDGNPGAPGPRGPKGERGLPGVHGSPGDIGPQGIGIPGRTGAQGPAGEPgiQGPRGLPGLPGTPGTPGN 685
Cdd:PHA03264 277 PPGDDRP-EAKPEPGPVEDGAPGRETGGEGEGPEPAGRDGAAGGEPKPGPPRPAPDADRP--EGWPSLEAITFPPPTPAT 353
|
....
gi 767941890 686 DGVP 689
Cdd:PHA03264 354 PAVP 357
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
75-258 |
6.14e-57 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 194.88 E-value: 6.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 75 NKLEVSGFDLGD-SFSLRRAFC-ESDKTCFKLGS-ALLIRDTIKIFPKGLPEEYSVAAMFRVRrnaKKERWFLWQVLNQQ 151
Cdd:smart00210 1 GQDLLQVFDLPSlSFAIRQVVGpEPGSPAYRLGDpALVPQPTRDLFPSGLPEDFSLLTTFRQT---PKSRGVLFAIYDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 152 NIPQISIVVDGGKKVVEFMFQATEGDVLNYIFRNrelRPLFDRQWHKLGISIQSQVISLYMDCNLIARRQTDEKD--TVD 229
Cdd:smart00210 78 NVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGqpPID 154
|
170 180
....*....|....*....|....*....
gi 767941890 230 FHGRTVIATRASDGKPVDIELHQLKIYCS 258
Cdd:smart00210 155 TDGIEVRGAQAADRKPFQGDLQQLKIVCD 183
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
461-691 |
5.59e-30 |
|
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: 124.63 E-value: 5.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 461 QTLGGYYNKDNKGNDEHEAGGLKGDKGETGLPGFPGSVGPKGQKGEPGEPFTKGEKGDRGEPGVIGSQGVKGEPGDPGPP 540
Cdd:NF038329 97 KKLNSYLEELDEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 541 GLIGSPGLKGQQGSAGSMGPRGPPGDVGLPGEHGIPGKQGIKGEKgdPGGIIGPPGLPGPKGEAGPPGKSlpGEPGLDGN 620
Cdd:NF038329 177 GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA--GEDGPAGPAGDGQQGPDGDPGPT--GEDGPQGP 252
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767941890 621 PGAPGPRGPKGERGLPGVHGSPGDIGPQG-IGIPGRTGAQGPAGEPGIQGPRGLPGLPGTPGTPGNDGVPGR 691
Cdd:NF038329 253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGpVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
357-691 |
3.36e-21 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 98.05 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 357 FEGSKGETGEKGEQGEKGDPalaglngenglkgdlgphgppGPKGEKGDTGPPGPPALPGSLGIQGPQGPPGKEGQRGRR 436
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQ---------------------GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 437 GKTGPPGKPgppgppgppgiqgihqtlggyynkdnkgndeheagGLKGDKGETGLPGFPGSVGPKGQKGEPGEPFTKGEK 516
Cdd:NF038329 174 GPAGKDGEA-----------------------------------GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 517 GDRGEPGVIGSQGVKGEpgdpgppgliGSPGLKGQQGSAGSMGPRGPPGDVGLPGEHGIPGKQGIKGEkgdpggiigppg 596
Cdd:NF038329 219 GPAGEDGPAGPAGDGQQ----------GPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK------------ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 597 lpgpKGEAGPPGKslPGEPGLDGNPGAPGPRGPKGERGLPGVHGSPGDIGPQGI-GIPGRTGAQGPAGEPGIQGPRgLPG 675
Cdd:NF038329 277 ----DGERGPVGP--AGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKdGLPGKDGKDGQPGKPAPKTPE-VPQ 349
|
330
....*....|....*..
gi 767941890 676 LPGT-PGTPGNDGVPGR 691
Cdd:NF038329 350 KPDTaPHTPKTPQIPGQ 366
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
769-1020 |
3.82e-19 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 91.89 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 769 GPKGSKGERGYPGIPGEKGDEGLQGIPGIPGAPGPTGPPGLMGRTGHPGPTGAKGEKGSDGPPGKPGppgppgipfnern 848
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG------------- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 849 gmsslykikggvnvpsypgppgppgpkgdpgpvgEPGAMGLPGLEGFPGVKGDRGPAGPPGIAGmSGKPGAPGPPGVPGE 928
Cdd:NF038329 187 ----------------------------------PAGEKGPQGPRGETGPAGEQGPAGPAGPDG-EAGPAGEDGPAGPAG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 929 PGERGPVGDIGFPGPEGPSGKPGINGKDGIPGAQGIMGKPGDRGPKGERGDQGIPGDRGSQGERGKPGLTGMKGAIGPMG 1008
Cdd:NF038329 232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
|
250
....*....|..
gi 767941890 1009 PPGNKGSMGSPG 1020
Cdd:NF038329 312 LPGKDGKDGQPG 323
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
895-1123 |
6.44e-19 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 91.12 E-value: 6.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 895 FPGVKGDRGPAGPPGIAGmsgkpgapgppgvpgepgERGPVGDIGFPGPEGPSGKPGINGKDGIPGAQGIMGKPGDRGPK 974
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAG------------------EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 975 GERGDQGIPGDRGSQGERGKPGLTGMKGAIGPMGPPGNKGSMGSPGHQGPPGSPGIPGIPADAvsfeeikkyinqevlri 1054
Cdd:NF038329 177 GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG----------------- 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767941890 1055 feermavflsqlkLPAAMLAAQAYGRPGPPGKDGLPGPPGDPGPQGYRGQKGERGEPGI----GLPGSPGLPG 1123
Cdd:NF038329 240 -------------DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPagkdGQNGKDGLPG 299
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
883-1126 |
3.45e-13 |
|
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: 73.02 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 883 EPGAMGLPGLEGFPGVKGDRGPAGPPGIAGMSGKPGAPGPPGVPGEPGERGPVG---------DIGFPGPEGPSGKPGIN 953
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGpagkdgeagAKGPAGEKGPQGPRGET 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 954 GKDGIPGAQGIMGKPGDRGPKGERGDQGIPGDrGSQGERGKPGLTGMKGAIGPMGPPGNKGSMGSPGhqGPPGSPGIPGI 1033
Cdd:NF038329 201 GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG--EAGPDGPDGKD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 1034 PADAVSFEEIKKYINQEVlrifeermavflsqlklpaaMLAAQAyGRPGPPGKDGLPgppgdpgpqgyrGQKGERGEPG- 1112
Cdd:NF038329 278 GERGPVGPAGKDGQNGKD--------------------GLPGKD-GKDGQNGKDGLP------------GKDGKDGQPGk 324
|
250
....*....|....*..
gi 767941890 1113 ---IGLPGSPGLPGTSA 1126
Cdd:NF038329 325 dglPGKDGKDGQPGKPA 341
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
316-439 |
1.47e-07 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 55.30 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 316 KGEAGLPGAPGSPGQKGHKGEPGENGLHGAPGFPGQKGEQGfEGSKGETGEKGEQGEKGDPALAGLNGENGLKGDLGPHG 395
Cdd:NF038329 191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767941890 396 PPGPKGEKGDTGPPGPPALPGSLGIQGPQGPPGKEGQ------RGRRGKT 439
Cdd:NF038329 270 PDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQngkdglPGKDGKD 319
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
317-448 |
3.07e-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: 54.14 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 317 GEAGLPGAPGSPGQKGHKGEPGENGlHGAPGFPGQKGEQGFEGSKGETGEKGEQGEKGDPALAGLNGENGLKGDLGPHGP 396
Cdd:NF038329 207 GPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 767941890 397 PGPKGEKGDTGPPGPPALPGSLGIQGPQGPPGKEGQRGRRGKTGPPGKPGPP 448
Cdd:NF038329 286 AGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
317-369 |
6.17e-07 |
|
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: 47.49 E-value: 6.17e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 767941890 317 GEAGLPGAPGSPGQKGHKGEPGENGLHGAPGFPGQKGEQGFEGSKGETGEKGE 369
Cdd:pfam01391 4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
966-1020 |
7.14e-07 |
|
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: 47.10 E-value: 7.14e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 767941890 966 GKPGDRGPKGERGDQGIPGDRGSQGERGKPGLTGMKGAIGPMGPPGNKGSMGSPG 1020
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
954-1010 |
1.58e-06 |
|
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: 46.33 E-value: 1.58e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767941890 954 GKDGIPGAQGIMGKPGDRGPKGERGDQGIPGDRGSQGERGKPGLTGMKGAIGPMGPP 1010
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
945-999 |
6.06e-06 |
|
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: 6.06e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 767941890 945 GPSGKPGINGKDGIPGAQGIMGKPGDRGPKGERGDQGIPGDRGSQGERGKPGLTG 999
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
335-389 |
1.36e-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: 43.64 E-value: 1.36e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 767941890 335 GEPGENGLHGAPGFPGQKGEQGFEGSKGETGEKGEQGEKGDPALAGLNGENGLKG 389
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
317-372 |
1.72e-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: 43.25 E-value: 1.72e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 767941890 317 GEAGLPGAPGSPGQKGHKGEPGENGLHGAPGFPGQKGEQGFEGSKGETGEKGEQGE 372
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
603-665 |
5.64e-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: 41.71 E-value: 5.64e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767941890 603 EAGPPGKslPGEPGLDGNPGAPGPRGPKGERGLPGVHGSPGDigpqgigiPGRTGAQGPAGEP 665
Cdd:pfam01391 5 PPGPPGP--PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGP--------PGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
316-359 |
9.03e-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: 41.33 E-value: 9.03e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767941890 316 KGEAGLPGAPGSPGQKGHKGEPGENGLHGAPGFPGQKGEQGFEG 359
Cdd:pfam01391 12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
933-981 |
3.99e-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: 3.99e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767941890 933 GPVGDIGFPGPEGPSGKPGINGKDGIPGAQGIMGKPGDRGPKGERGDQG 981
Cdd:pfam01391 7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
367-682 |
4.68e-04 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 44.25 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 367 KGEQGEKGDPAlaglNGENGLKGDLGPHGPPGPKGEKGDTGPPGPPALPGSLGIQGPQGPPGKEGQRGRRGKTGPPGKPG 446
Cdd:COG5164 1 TGLYGPGKTGP----SDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 447 PPGPpgppgiQGIHQTLGGYYNKDNKGndeheAGGLKGDKGETGLPGFPGSVGPKGQKGEPGEPFT--KGEKGDRGE-PG 523
Cdd:COG5164 77 NQGG------TTPAQNQGGTRPAGNTG-----GTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGgsTTPPGDGGStPP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 524 VIGSQGVKGEPGDPGPPGLIGSPGLKGQQGSAGSMGPRGPP--GDVGLPGEHGIPGKQGIKGEKGDPGGIIGPPGLPGPK 601
Cdd:COG5164 146 GPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 602 GEAGPPGKSLPGEPgldgnpgaPGPRGPKGERGLPGVHGSPGDIGPQGIGIPGRTGAQGPAGEPGIQGPRGLPGLPGTPG 681
Cdd:COG5164 226 GKTGPKDQRPKTNP--------IERRGPERPEAAALPAELTALEAENRAANPEPATKTIPETTTVKDLATVLGKKGSDLV 297
|
.
gi 767941890 682 T 682
Cdd:COG5164 298 T 298
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
640-690 |
3.06e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.09 E-value: 3.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767941890 640 GSPGDIGPqgigiPGRTGAQGPAGEPGIQGPRGLPGLPGTPGTPGNDGVPG 690
Cdd:pfam01391 1 GPPGPPGP-----PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
322-682 |
6.39e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 40.40 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 322 PGAPGSPGQKGHKGEPGENGLHGAPGFPGQKGEQGFEGSKGETGEKGEQGEKGDPALAGLNGENGlkgdlgphgppgpkg 401
Cdd:COG5164 3 LYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAG--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 402 EKGDTGPPGPPALPGSLGIQGPQGPPGKEGQRGRRGKTGPPGKPGPPgppgppgiqgihQTLGGYYNKDNKGNDEHEAGG 481
Cdd:COG5164 68 NQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDG------------GATGPPDDGGSTTPPSGGSTT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 482 LKGDKGETglPGFPGSVGPKGQKGEPGEPFTKGEKGDRGEPGVIGSQGVKGEPGDpgppgliGSPGLKGQQGSAGSMGPR 561
Cdd:COG5164 136 PPGDGGST--PPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNK-------GETGTDIPTGGTPRQGPD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 562 GPPGDVGLPGEHGIPGKQGIKGEKGDPGGIIGPPGLPGPKGEAGPPGKSLP---GEPGLDGNPGAPGPRGPKGERGLPGV 638
Cdd:COG5164 207 GPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELtalEAENRAANPEPATKTIPETTTVKDLA 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 767941890 639 HGSPGDIGPQGIGIPGRTGAQGPAGEPGIQGPRGLPgLPGTPGT 682
Cdd:COG5164 287 TVLGKKGSDLVTNLMKKGKGTNINAALDFETAATIA-LEGNVIT 329
|
|
| PHA03264 |
PHA03264 |
envelope glycoprotein D; Provisional |
606-689 |
9.11e-03 |
|
envelope glycoprotein D; Provisional
Pssm-ID: 223029 [Multi-domain] Cd Length: 416 Bit Score: 39.99 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767941890 606 PPGKSLPgEPGLDGNPGAPGPRGPKGERGLPGVHGSPGDIGPQGIGIPGRTGAQGPAGEPgiQGPRGLPGLPGTPGTPGN 685
Cdd:PHA03264 277 PPGDDRP-EAKPEPGPVEDGAPGRETGGEGEGPEPAGRDGAAGGEPKPGPPRPAPDADRP--EGWPSLEAITFPPPTPAT 353
|
....
gi 767941890 686 DGVP 689
Cdd:PHA03264 354 PAVP 357
|
|
| |
