|
Name |
Accession |
Description |
Interval |
E-value |
| COLFI |
pfam01410 |
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
813-1042 |
2.02e-131 |
|
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.
Pssm-ID: 460199 Cd Length: 233 Bit Score: 397.10 E-value: 2.02e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 813 GMEEIFGSLNSLKQDIEHMKFPMGTQTNPARTCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTAgGETCIYPDKK 892
Cdd:pfam01410 1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 893 SEGvRISSWPKEKPGSWYSEFKRGKL-LSY-LDVEGNSINMVQMTFLKLLTASARQNFTYNCHQSAAWYDVLSGSYDKAL 970
Cdd:pfam01410 80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720403102 971 RFLGSNDEEMSYE--NNPHIKALYDGCASRKGY-EKTVIEINTPKIDQVPIIDVMINDFGDQNQKFGFEVGPACF 1042
Cdd:pfam01410 159 LLQGSNDEEIRAEgnSRFTYTVLEDGCTKRTGQwGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
|
|
| COLFI |
smart00038 |
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
814-1043 |
1.22e-106 |
|
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.
Pssm-ID: 197483 Cd Length: 232 Bit Score: 332.13 E-value: 1.22e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 814 MEEIFGSLNSLKQDIEHMKFPMGTQTNPARTCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTAgGETCIYPDKKS 893
Cdd:smart00038 1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFET-GETCVSPSPSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 894 EGVRISSWPKEKpGSWYSEFKR-GKLLSYLDVEGNSINMVQMTFLKLLTASARQNFTYNCHQSAAWYDVLSGSYDKALRF 972
Cdd:smart00038 80 IPRKTWYSGKSK-HVWFGETMNgGFKFSYGDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720403102 973 LGSNDEEMSYENN--PHIKALYDGCASRKGY-EKTVIEINTPKIDQVPIIDVMINDFGDQNQKFGFEVGPACFL 1043
Cdd:smart00038 159 RGSNDVELSAEGNskFTYEVLEDGCQKRTGKwGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
298-543 |
4.89e-26 |
|
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: 112.69 E-value: 4.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 298 GERGSAGTAGPIGLPGRPGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGS 377
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 378 KGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPRGqQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGENGDVGPmg 457
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP-- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 458 ppgppgprgpqgpngaDGPQGPPGSIGSVGVVGDKGEPGEAGNPGPPGEAGSGGLKGERGEKGEAGPPGAAGPAGIKGPP 537
Cdd:NF038329 274 ----------------DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
|
....*.
gi 1720403102 538 GDDGPK 543
Cdd:NF038329 338 GKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
342-638 |
2.18e-24 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 107.68 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 342 DGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPpgppglqgpvgaPGIAGGDGEPGPRGQQGMFGQKG 421
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE------------KGPAGPQGEAGPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 422 DEGARGFPGLPGPIGLQGLPGPPGEKGEnGDVGPMGPPGPPGPRGPQGPNGADGPQGPPGSIGSVGVVGDKGEPGEAGNP 501
Cdd:NF038329 184 AKGPAGEKGPQGPRGETGPAGEQGPAGP-AGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 502 GPPGEAGSGGLKGERGEKGEAGPPGAAGPAGIKGPPGDDGPKGnpgpvgfpgdpgppgepgpagQDGVGGDKGEDgdpgq 581
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDG---------------------QNGKDGLPGKD----- 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720403102 582 pgppgpsgeagppgppgkrgppgasGSEGRQGEKGAKGEAGAEGPPGKTGPVGPQGP 638
Cdd:NF038329 317 -------------------------GKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVP 348
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
115-447 |
5.25e-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: 5.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 115 GPRGQRGPTGPRGSRGARGPTGKPGPKgtsggdgppgppgergpqgpqgpvgfpgpkgppGPAGKDGLPGHPGQRGETGF 194
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGET---------------------------------GPAGPAGPPGPQGERGEKGP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 195 QGKtgppgpggvvgpqgpTGETGPIGERghpgppgppgeqglpgaagkeGAKGDPGPQGISGKDGPAGIRGFPGERGLPG 274
Cdd:NF038329 164 AGP---------------QGEAGPQGPA---------------------GKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 275 AQGAPGLKggegpqgpqgpvGSPGERGSAGTAGPiglpgrpGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPA 354
Cdd:NF038329 208 PAGPAGPD------------GEAGPAGEDGPAGP-------AGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 355 GPAGSPGEDGDKGEIGEPGQKGSKGDKGEngppgppglqgpvgapgiAGGDGEPGPRGQQGMFGQKGDEGARGFPGLPGP 434
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGL------------------PGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330
|
330
....*....|...
gi 1720403102 435 IGLQGLPGPPGEK 447
Cdd:NF038329 331 DGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
331-665 |
1.08e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 102.29 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 331 GEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGEngppgppglqgpvgaPGIAGGDGEPGP 410
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE---------------AGPQGPAGKDGE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 411 RGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGENGDvgpmgppgppgprgpqgpngaDGPQGPPGSiGSVGVVG 490
Cdd:NF038329 182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGE---------------------DGPAGPAGD-GQQGPDG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 491 DKGEPGEAGNPGPPGEAGSGGLKGERGEKGEAgppgaagpagikGPPGDDGPKGnpgpvgfpgdpgppgepgpagqdgvg 570
Cdd:NF038329 240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD------------GPDGKDGERG-------------------------- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 571 gdkgedgdpgqpgppgpsgeagppgppgkrgppgasgsegRQGEKGAKGEAGAEGPPGKTGPVGPQGPSGKPGPEGLRGI 650
Cdd:NF038329 282 ----------------------------------------PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321
|
330
....*....|....*
gi 1720403102 651 PGPVGEQGLPGAAGQ 665
Cdd:NF038329 322 PGKDGLPGKDGKDGQ 336
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
475-721 |
1.55e-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: 98.82 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 475 GPQGPPGSIGSVGVVGDKGEPGEAGNPGPPGEAGSGGLKGERGEKGEAgppgaagpagikGPPGDDGPKGnpgpvgfpgd 554
Cdd:NF038329 123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA------------GPQGPAGKDG---------- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 555 pgppgepgpagQDGVGGDKGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGASGSEGRQGEKGaKGEAGAEGPPGKTGPVG 634
Cdd:NF038329 181 -----------EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 635 PQGPSGKPGPEGLRGIPGPVGEQGLPGAAGQDGPPGPLGPPGLPGLKGDPGSKGEKGHPGLIGLIGPPGEQGEKGDRGLP 714
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328
|
....*..
gi 1720403102 715 GTQGSPG 721
Cdd:NF038329 329 GKDGKDG 335
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
103-434 |
6.43e-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: 6.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 103 GEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGtsggdgppgppgergpqgpqgpvgfpgpkgppgpagKDGL 182
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG------------------------------------ERGE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 183 PGHPGQRGETGFQGktgppgpggvvgPQGPTGETGPIGERGhpgppgppgeqglpgAAGKEGAKGDPGPQGISGKDGPAG 262
Cdd:NF038329 161 KGPAGPQGEAGPQG------------PAGKDGEAGAKGPAG---------------EKGPQGPRGETGPAGEQGPAGPAG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 263 IRGFPGERGLPGAQGAPGlkggegpQGPQGPVGSPGERGSAGTAGPiglpgrpgpqgpPgpagekGAPGEKGPQGPAGRD 342
Cdd:NF038329 214 PDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDGPQGP------------D------GPAGKDGPRGDRGEA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 343 GVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGEngppgppglqgpvgaPGIAGGDGEPGPRGQQGMFGQKGD 422
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK---------------DGLPGKDGKDGQPGKDGLPGKDGK 333
|
330
....*....|..
gi 1720403102 423 EGArgfPGLPGP 434
Cdd:NF038329 334 DGQ---PGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
404-709 |
6.73e-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: 6.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 404 GDGEPGPRGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGENGDVGPMGPPGPPGPRGPQGPNGADGPQGPPGSI 483
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 484 GSVGVVGDKGEPGEAGNPGPPGEAGSGGLKGERGEKGeagppgaagpagiKGPPGDDGPKGnpgpvgfpgdpgppgepgp 563
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------------DGQQGPDGDPG------------------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 564 agQDGVGGDKGEDgdpgqpgppgpsgeagppgppgkrgppgasGSEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPSGKPG 643
Cdd:NF038329 243 --PTGEDGPQGPD------------------------------GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720403102 644 PEGLRGIPGPVGEQGLPGAAGQdgppgplgppglpglkgdPGSKGEKGHPGLIGLIGPPGEQGEKG 709
Cdd:NF038329 291 QNGKDGLPGKDGKDGQNGKDGL------------------PGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
91-376 |
1.58e-17 |
|
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: 86.50 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 91 GSTGFPGFPGANGEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPPGERGPQGPQgpvgfpgp 170
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA-------- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 171 kgppgpagkdGLPGHPGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHpgppgppgeqglpgaaGKEGAKGDPG 250
Cdd:NF038329 189 ----------GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------------GQQGPDGDPG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 251 PQGISGKDGPAGIRGFPGERGLPGAQGAPGlkggegpqgpqgPVGSPGERGSAGTAGpiglpgrpgpqgppgpagEKGAP 330
Cdd:NF038329 243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDG------------PDGKDGERGPVGPAG------------------KDGQN 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1720403102 331 GEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKG 376
Cdd:NF038329 293 GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
567-783 |
2.58e-15 |
|
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: 79.56 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 567 DGVGGDKGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGASGSEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPSGKPGPEG 646
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 647 LRGIPGPVGEQGLPGAAGQDGPPGPLGPPGLPGLKGDP-----GSKGEKGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPG 721
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720403102 722 AKGDGGIPGPAGPIGPPGPPGLPGPAGPKGNKGSSGPTGQKGDSGMPGPPGPPGPPGEVIQP 783
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
328-545 |
2.67e-07 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 54.27 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 328 GAPGEKGPQGPAGRDGVQGPVGLPG---PAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGG 404
Cdd:COG5164 10 GPSDPGGVTTPAGSQGSTKPAQNQGstrPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 405 DgepGPRGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGENGDVGPMGPPGPPGPRGPQGPNGADGPQGPPGSIG 484
Cdd:COG5164 90 T---RPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720403102 485 SVGVVGDKGEPGEAGNPGPP--GEAGSGGLKGERGEKGEAGPPGAAGPAGIKGPPGDDGPKGN 545
Cdd:COG5164 167 PPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTG 229
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
90-193 |
1.62e-05 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 48.75 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 90 TGSTGFPGFPGANGEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPPGERGPQGPQGPVGFPG 169
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG 314
|
90 100
....*....|....*....|....
gi 1720403102 170 PKGPPGPAGKDGLPGHPGQRGETG 193
Cdd:NF038329 315 KDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| GGGWT_bact |
NF040941 |
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ... |
844-883 |
2.00e-05 |
|
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.
Pssm-ID: 468872 [Multi-domain] Cd Length: 46 Bit Score: 42.55 E-value: 2.00e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1720403102 844 TCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTAGG 883
Cdd:NF040941 1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTTDG 40
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
91-141 |
7.31e-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: 7.31e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1720403102 91 GSTGFPGFPGANGEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPK 141
Cdd:pfam01391 4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
619-665 |
7.61e-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: 7.61e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720403102 619 GEAGAEGPPGKTGPVGPQGPSGKPGPEGLRGIPGPVGEQGLPGAAGQ 665
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
99-363 |
2.00e-04 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 45.02 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 99 PGANGEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPPGERGPQGPQGPVgfpgpkgppgpag 178
Cdd:COG5164 6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGAT------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 179 kdGLPGHPGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPI--GERGHPGPPGPPGEQGLPGAAGKEGAKG----DPGPQ 252
Cdd:COG5164 73 --GPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPddGGATGPPDDGGSTTPPSGGSTTPPGDGGstppGPGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 253 GISGKDGPAGIRGFPGERGLPGAQGAPGlKGGEGPQGPQGPVGSPGERGSAGTAGPIGLPGRPGPQGPPGPAGEKGAPGE 332
Cdd:COG5164 151 GPGGSTTPPGDGGSTTPPGPGGSTTPPD-DGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTG 229
|
250 260 270
....*....|....*....|....*....|....*
gi 1720403102 333 K----GPQGPAGRDGVQGPVGLPGPAGPAGSPGED 363
Cdd:COG5164 230 PkdqrPKTNPIERRGPERPEAAALPAELTALEAEN 264
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
398-450 |
2.24e-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: 40.17 E-value: 2.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720403102 398 APGIAGGDGEPGPRGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGEN 450
Cdd:pfam01391 5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
624-806 |
6.51e-04 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 43.36 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 624 EGPPGKTGPVGPQGPSGKPGPEGLRGIPGPVGEQGLPGAAGQDgppgplgppglpglkgdpgskgekghpgliGLIGPPG 703
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGER------------------------------GEKGPAG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 704 EQGEKGDRGLPGTQgspgakgdggipgpagpiGPPGPPGLPGPAGPKGNKGSSGPTGQKGDSGMPGPPGPPGPPGEVIQP 783
Cdd:NF038329 166 PQGEAGPQGPAGKD------------------GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPA 227
|
170 180
....*....|....*....|...
gi 1720403102 784 LPILSPKKTRRHTESIQGDAGDN 806
Cdd:NF038329 228 GPAGDGQQGPDGDPGPTGEDGPQ 250
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
473-719 |
1.30e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 42.71 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 473 ADGPQG------PPGSIGSVGVVGDKGEPGEAGNPGPPGEAGSGGLKGERGEKGEAGPPGAAGPAGIKGPPGDDGPKGNP 546
Cdd:COG5164 8 KTGPSDpggvttPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 547 GPVGFPGDPGPPGEPGPAGQDGVGGDKGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGASGSEGRQGEKGAKGEAGAEGP 626
Cdd:COG5164 88 GGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 627 PGKTGPVGPQGPSGKPGPeGLRGIPGPVGEQGLPGAAGQDGPPGPLGPPGLPGLKGDPGSK-GEKGHPGLIGLIGPPGEQ 705
Cdd:COG5164 168 PGPGGSTTPPDDGGSTTP-PNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKtGPKDQRPKTNPIERRGPE 246
|
250
....*....|....
gi 1720403102 706 GEKGDRGLPGTQGS 719
Cdd:COG5164 247 RPEAAALPAELTAL 260
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
683-813 |
1.72e-03 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 42.20 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 683 DPGSKGEKGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPGAKGDGGIPGPAGPIGPPGPPGLPGPAGPKGNKGSSGPTGQK 762
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1720403102 763 GDSGMPGPPGPPGPPGEVIQPLPILSPKKTRRHTESIQGDAGDNILDYSDG 813
Cdd:NF038329 201 GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG 251
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COLFI |
pfam01410 |
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
813-1042 |
2.02e-131 |
|
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.
Pssm-ID: 460199 Cd Length: 233 Bit Score: 397.10 E-value: 2.02e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 813 GMEEIFGSLNSLKQDIEHMKFPMGTQTNPARTCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTAgGETCIYPDKK 892
Cdd:pfam01410 1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 893 SEGvRISSWPKEKPGSWYSEFKRGKL-LSY-LDVEGNSINMVQMTFLKLLTASARQNFTYNCHQSAAWYDVLSGSYDKAL 970
Cdd:pfam01410 80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720403102 971 RFLGSNDEEMSYE--NNPHIKALYDGCASRKGY-EKTVIEINTPKIDQVPIIDVMINDFGDQNQKFGFEVGPACF 1042
Cdd:pfam01410 159 LLQGSNDEEIRAEgnSRFTYTVLEDGCTKRTGQwGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
|
|
| COLFI |
smart00038 |
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
814-1043 |
1.22e-106 |
|
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.
Pssm-ID: 197483 Cd Length: 232 Bit Score: 332.13 E-value: 1.22e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 814 MEEIFGSLNSLKQDIEHMKFPMGTQTNPARTCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTAgGETCIYPDKKS 893
Cdd:smart00038 1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFET-GETCVSPSPSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 894 EGVRISSWPKEKpGSWYSEFKR-GKLLSYLDVEGNSINMVQMTFLKLLTASARQNFTYNCHQSAAWYDVLSGSYDKALRF 972
Cdd:smart00038 80 IPRKTWYSGKSK-HVWFGETMNgGFKFSYGDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720403102 973 LGSNDEEMSYENN--PHIKALYDGCASRKGY-EKTVIEINTPKIDQVPIIDVMINDFGDQNQKFGFEVGPACFL 1043
Cdd:smart00038 159 RGSNDVELSAEGNskFTYEVLEDGCQKRTGKwGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
298-543 |
4.89e-26 |
|
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: 112.69 E-value: 4.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 298 GERGSAGTAGPIGLPGRPGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGS 377
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 378 KGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPRGqQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGENGDVGPmg 457
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP-- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 458 ppgppgprgpqgpngaDGPQGPPGSIGSVGVVGDKGEPGEAGNPGPPGEAGSGGLKGERGEKGEAGPPGAAGPAGIKGPP 537
Cdd:NF038329 274 ----------------DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
|
....*.
gi 1720403102 538 GDDGPK 543
Cdd:NF038329 338 GKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
342-638 |
2.18e-24 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 107.68 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 342 DGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPpgppglqgpvgaPGIAGGDGEPGPRGQQGMFGQKG 421
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE------------KGPAGPQGEAGPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 422 DEGARGFPGLPGPIGLQGLPGPPGEKGEnGDVGPMGPPGPPGPRGPQGPNGADGPQGPPGSIGSVGVVGDKGEPGEAGNP 501
Cdd:NF038329 184 AKGPAGEKGPQGPRGETGPAGEQGPAGP-AGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 502 GPPGEAGSGGLKGERGEKGEAGPPGAAGPAGIKGPPGDDGPKGnpgpvgfpgdpgppgepgpagQDGVGGDKGEDgdpgq 581
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDG---------------------QNGKDGLPGKD----- 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720403102 582 pgppgpsgeagppgppgkrgppgasGSEGRQGEKGAKGEAGAEGPPGKTGPVGPQGP 638
Cdd:NF038329 317 -------------------------GKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVP 348
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
115-447 |
5.25e-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: 5.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 115 GPRGQRGPTGPRGSRGARGPTGKPGPKgtsggdgppgppgergpqgpqgpvgfpgpkgppGPAGKDGLPGHPGQRGETGF 194
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGET---------------------------------GPAGPAGPPGPQGERGEKGP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 195 QGKtgppgpggvvgpqgpTGETGPIGERghpgppgppgeqglpgaagkeGAKGDPGPQGISGKDGPAGIRGFPGERGLPG 274
Cdd:NF038329 164 AGP---------------QGEAGPQGPA---------------------GKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 275 AQGAPGLKggegpqgpqgpvGSPGERGSAGTAGPiglpgrpGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPA 354
Cdd:NF038329 208 PAGPAGPD------------GEAGPAGEDGPAGP-------AGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 355 GPAGSPGEDGDKGEIGEPGQKGSKGDKGEngppgppglqgpvgapgiAGGDGEPGPRGQQGMFGQKGDEGARGFPGLPGP 434
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGL------------------PGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330
|
330
....*....|...
gi 1720403102 435 IGLQGLPGPPGEK 447
Cdd:NF038329 331 DGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
331-665 |
1.08e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 102.29 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 331 GEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGEngppgppglqgpvgaPGIAGGDGEPGP 410
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE---------------AGPQGPAGKDGE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 411 RGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGENGDvgpmgppgppgprgpqgpngaDGPQGPPGSiGSVGVVG 490
Cdd:NF038329 182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGE---------------------DGPAGPAGD-GQQGPDG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 491 DKGEPGEAGNPGPPGEAGSGGLKGERGEKGEAgppgaagpagikGPPGDDGPKGnpgpvgfpgdpgppgepgpagqdgvg 570
Cdd:NF038329 240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD------------GPDGKDGERG-------------------------- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 571 gdkgedgdpgqpgppgpsgeagppgppgkrgppgasgsegRQGEKGAKGEAGAEGPPGKTGPVGPQGPSGKPGPEGLRGI 650
Cdd:NF038329 282 ----------------------------------------PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321
|
330
....*....|....*
gi 1720403102 651 PGPVGEQGLPGAAGQ 665
Cdd:NF038329 322 PGKDGLPGKDGKDGQ 336
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
475-721 |
1.55e-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: 98.82 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 475 GPQGPPGSIGSVGVVGDKGEPGEAGNPGPPGEAGSGGLKGERGEKGEAgppgaagpagikGPPGDDGPKGnpgpvgfpgd 554
Cdd:NF038329 123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA------------GPQGPAGKDG---------- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 555 pgppgepgpagQDGVGGDKGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGASGSEGRQGEKGaKGEAGAEGPPGKTGPVG 634
Cdd:NF038329 181 -----------EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 635 PQGPSGKPGPEGLRGIPGPVGEQGLPGAAGQDGPPGPLGPPGLPGLKGDPGSKGEKGHPGLIGLIGPPGEQGEKGDRGLP 714
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328
|
....*..
gi 1720403102 715 GTQGSPG 721
Cdd:NF038329 329 GKDGKDG 335
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
103-434 |
6.43e-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: 6.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 103 GEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGtsggdgppgppgergpqgpqgpvgfpgpkgppgpagKDGL 182
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG------------------------------------ERGE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 183 PGHPGQRGETGFQGktgppgpggvvgPQGPTGETGPIGERGhpgppgppgeqglpgAAGKEGAKGDPGPQGISGKDGPAG 262
Cdd:NF038329 161 KGPAGPQGEAGPQG------------PAGKDGEAGAKGPAG---------------EKGPQGPRGETGPAGEQGPAGPAG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 263 IRGFPGERGLPGAQGAPGlkggegpQGPQGPVGSPGERGSAGTAGPiglpgrpgpqgpPgpagekGAPGEKGPQGPAGRD 342
Cdd:NF038329 214 PDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDGPQGP------------D------GPAGKDGPRGDRGEA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 343 GVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGEngppgppglqgpvgaPGIAGGDGEPGPRGQQGMFGQKGD 422
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK---------------DGLPGKDGKDGQPGKDGLPGKDGK 333
|
330
....*....|..
gi 1720403102 423 EGArgfPGLPGP 434
Cdd:NF038329 334 DGQ---PGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
404-709 |
6.73e-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: 6.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 404 GDGEPGPRGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGENGDVGPMGPPGPPGPRGPQGPNGADGPQGPPGSI 483
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 484 GSVGVVGDKGEPGEAGNPGPPGEAGSGGLKGERGEKGeagppgaagpagiKGPPGDDGPKGnpgpvgfpgdpgppgepgp 563
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------------DGQQGPDGDPG------------------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 564 agQDGVGGDKGEDgdpgqpgppgpsgeagppgppgkrgppgasGSEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPSGKPG 643
Cdd:NF038329 243 --PTGEDGPQGPD------------------------------GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720403102 644 PEGLRGIPGPVGEQGLPGAAGQdgppgplgppglpglkgdPGSKGEKGHPGLIGLIGPPGEQGEKG 709
Cdd:NF038329 291 QNGKDGLPGKDGKDGQNGKDGL------------------PGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
91-376 |
1.58e-17 |
|
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: 86.50 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 91 GSTGFPGFPGANGEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPPGERGPQGPQgpvgfpgp 170
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA-------- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 171 kgppgpagkdGLPGHPGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHpgppgppgeqglpgaaGKEGAKGDPG 250
Cdd:NF038329 189 ----------GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------------GQQGPDGDPG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 251 PQGISGKDGPAGIRGFPGERGLPGAQGAPGlkggegpqgpqgPVGSPGERGSAGTAGpiglpgrpgpqgppgpagEKGAP 330
Cdd:NF038329 243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDG------------PDGKDGERGPVGPAG------------------KDGQN 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1720403102 331 GEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKG 376
Cdd:NF038329 293 GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
567-783 |
2.58e-15 |
|
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: 79.56 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 567 DGVGGDKGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGASGSEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPSGKPGPEG 646
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 647 LRGIPGPVGEQGLPGAAGQDGPPGPLGPPGLPGLKGDP-----GSKGEKGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPG 721
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720403102 722 AKGDGGIPGPAGPIGPPGPPGLPGPAGPKGNKGSSGPTGQKGDSGMPGPPGPPGPPGEVIQP 783
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
328-545 |
2.67e-07 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 54.27 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 328 GAPGEKGPQGPAGRDGVQGPVGLPG---PAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGG 404
Cdd:COG5164 10 GPSDPGGVTTPAGSQGSTKPAQNQGstrPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 405 DgepGPRGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGENGDVGPMGPPGPPGPRGPQGPNGADGPQGPPGSIG 484
Cdd:COG5164 90 T---RPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720403102 485 SVGVVGDKGEPGEAGNPGPP--GEAGSGGLKGERGEKGEAGPPGAAGPAGIKGPPGDDGPKGN 545
Cdd:COG5164 167 PPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTG 229
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
179-444 |
2.99e-07 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 54.27 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 179 KDGLPGHPGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGErghpgppgppgeqglPGAAGKEGAKGDPGPQGISGKD 258
Cdd:COG5164 8 KTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQN---------------QGSTTPAGNTGGTRPAGNQGAT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 259 GPAGIRGFPGERGLPGAQGAPGLKGGEGPQGPQGPVGSPGERGSAGTA---GPIGLPGRPGPQGPPGPAGEKGAPGEKGP 335
Cdd:COG5164 73 GPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPddgGSTTPPSGGSTTPPGDGGSTPPGPGSTGP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 336 QGPAGRDGVQGPVGLPGPAGPAGSPGEDG-----DKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGGDGepGP 410
Cdd:COG5164 153 GGSTTPPGDGGSTTPPGPGGSTTPPDDGGsttppNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKT--GP 230
|
250 260 270
....*....|....*....|....*....|....
gi 1720403102 411 RGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPP 444
Cdd:COG5164 231 KDQRPKTNPIERRGPERPEAAALPAELTALEAEN 264
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
90-193 |
1.62e-05 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 48.75 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 90 TGSTGFPGFPGANGEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPPGERGPQGPQGPVGFPG 169
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG 314
|
90 100
....*....|....*....|....
gi 1720403102 170 PKGPPGPAGKDGLPGHPGQRGETG 193
Cdd:NF038329 315 KDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| GGGWT_bact |
NF040941 |
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ... |
844-883 |
2.00e-05 |
|
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.
Pssm-ID: 468872 [Multi-domain] Cd Length: 46 Bit Score: 42.55 E-value: 2.00e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1720403102 844 TCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTAGG 883
Cdd:NF040941 1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTTDG 40
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
91-141 |
7.31e-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: 7.31e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1720403102 91 GSTGFPGFPGANGEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPK 141
Cdd:pfam01391 4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
619-665 |
7.61e-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: 7.61e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720403102 619 GEAGAEGPPGKTGPVGPQGPSGKPGPEGLRGIPGPVGEQGLPGAAGQ 665
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
99-363 |
2.00e-04 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 45.02 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 99 PGANGEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPPGERGPQGPQGPVgfpgpkgppgpag 178
Cdd:COG5164 6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGAT------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 179 kdGLPGHPGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPI--GERGHPGPPGPPGEQGLPGAAGKEGAKG----DPGPQ 252
Cdd:COG5164 73 --GPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPddGGATGPPDDGGSTTPPSGGSTTPPGDGGstppGPGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 253 GISGKDGPAGIRGFPGERGLPGAQGAPGlKGGEGPQGPQGPVGSPGERGSAGTAGPIGLPGRPGPQGPPGPAGEKGAPGE 332
Cdd:COG5164 151 GPGGSTTPPGDGGSTTPPGPGGSTTPPD-DGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTG 229
|
250 260 270
....*....|....*....|....*....|....*
gi 1720403102 333 K----GPQGPAGRDGVQGPVGLPGPAGPAGSPGED 363
Cdd:COG5164 230 PkdqrPKTNPIERRGPERPEAAALPAELTALEAEN 264
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
398-450 |
2.24e-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: 40.17 E-value: 2.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720403102 398 APGIAGGDGEPGPRGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGEN 450
Cdd:pfam01391 5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
399-449 |
3.53e-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: 3.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1720403102 399 PGIAGGDGEPGPRGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGE 449
Cdd:pfam01391 3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
90-138 |
5.83e-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: 39.01 E-value: 5.83e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720403102 90 TGSTGFPGFPGANGEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKP 138
Cdd:pfam01391 9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
624-806 |
6.51e-04 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 43.36 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 624 EGPPGKTGPVGPQGPSGKPGPEGLRGIPGPVGEQGLPGAAGQDgppgplgppglpglkgdpgskgekghpgliGLIGPPG 703
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGER------------------------------GEKGPAG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 704 EQGEKGDRGLPGTQgspgakgdggipgpagpiGPPGPPGLPGPAGPKGNKGSSGPTGQKGDSGMPGPPGPPGPPGEVIQP 783
Cdd:NF038329 166 PQGEAGPQGPAGKD------------------GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPA 227
|
170 180
....*....|....*....|...
gi 1720403102 784 LPILSPKKTRRHTESIQGDAGDN 806
Cdd:NF038329 228 GPAGDGQQGPDGDPGPTGEDGPQ 250
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
97-141 |
1.15e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.86 E-value: 1.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1720403102 97 GFPGANGEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPK 141
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPP 45
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
337-383 |
1.16e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.86 E-value: 1.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720403102 337 GPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGE 383
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
473-719 |
1.30e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 42.71 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 473 ADGPQG------PPGSIGSVGVVGDKGEPGEAGNPGPPGEAGSGGLKGERGEKGEAGPPGAAGPAGIKGPPGDDGPKGNP 546
Cdd:COG5164 8 KTGPSDpggvttPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 547 GPVGFPGDPGPPGEPGPAGQDGVGGDKGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGASGSEGRQGEKGAKGEAGAEGP 626
Cdd:COG5164 88 GGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 627 PGKTGPVGPQGPSGKPGPeGLRGIPGPVGEQGLPGAAGQDGPPGPLGPPGLPGLKGDPGSK-GEKGHPGLIGLIGPPGEQ 705
Cdd:COG5164 168 PGPGGSTTPPDDGGSTTP-PNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKtGPKDQRPKTNPIERRGPE 246
|
250
....*....|....
gi 1720403102 706 GEKGDRGLPGTQGS 719
Cdd:COG5164 247 RPEAAALPAELTAL 260
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
324-372 |
1.35e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.86 E-value: 1.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720403102 324 AGEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEP 372
Cdd:pfam01391 9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
683-813 |
1.72e-03 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 42.20 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 683 DPGSKGEKGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPGAKGDGGIPGPAGPIGPPGPPGLPGPAGPKGNKGSSGPTGQK 762
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1720403102 763 GDSGMPGPPGPPGPPGEVIQPLPILSPKKTRRHTESIQGDAGDNILDYSDG 813
Cdd:NF038329 201 GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG 251
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
475-521 |
1.79e-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: 1.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720403102 475 GPQGPPGSIGSVGVVGDKGEPGEAGNPGPPGEAGSGGLKGERGEKGE 521
Cdd:pfam01391 10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
429-664 |
4.17e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 40.78 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 429 PGLPGPIGLQGLPGPPGEKGENGDVGPMGPPGPPGPRGPQGPNGADGPQGPPGSIGSVGVVGDKGEPGEAGNPGPPGEAG 508
Cdd:COG5164 6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720403102 509 SGGLKGERGEKGEAGPPGAAGPAGIKGPPGDDGPKGNPGPVGFPGDPGPPGepgpagqDGVGGDKGEDGDPGQPGPPGps 588
Cdd:COG5164 86 NQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTP-------PGDGGSTPPGPGSTGPGGST-- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720403102 589 geagppgppGKRGPPGASGSEGRQGEKGAKGEAGAEGPP--GKTGPVGPQGPSGKPGPEGLRGIPGPVGEQGLPGAAG 664
Cdd:COG5164 157 ---------TPPGDGGSTTPPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG 225
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
604-654 |
5.09e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.32 E-value: 5.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1720403102 604 GASGSEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPSGKPGPEGLRGIPGPV 654
Cdd:pfam01391 7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
295-362 |
5.34e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.32 E-value: 5.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720403102 295 GSPGERGSAGTAGPiglpgrpgpqgpPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGE 362
Cdd:pfam01391 1 GPPGPPGPPGPPGP------------PGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| GON |
pfam08685 |
GON domain; The GON domain is found in the ADAMTS (a disintegrin and metalloproteinase domain ... |
842-877 |
5.86e-03 |
|
GON domain; The GON domain is found in the ADAMTS (a disintegrin and metalloproteinase domain with thrombospondin type-1 modules) family of proteins. It contains several conserved cysteine residues.
Pssm-ID: 462559 Cd Length: 200 Bit Score: 39.14 E-value: 5.86e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1720403102 842 ARTCKDLQLSHPDFPDGEYWIDPNqgcsGDSFKVYC 877
Cdd:pfam08685 1 PRSCKEIQSRSGVRKDGEYTLNVR----GRNVRIYC 32
|
|
| |
