|
Name |
Accession |
Description |
Interval |
E-value |
| COLFI |
pfam01410 |
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1534-1763 |
3.34e-127 |
|
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: 3.34e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1534 GMEEIFGSLNSLKQDIEHMKFPMGTQTNPARTCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTAgGETCIYPDKK 1613
Cdd:pfam01410 1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1614 SEGvRISSWPKEKPGSWYSEFKRGKL-LSY-LDVEGNSINMVQMTFLKLLTASARQNFTYNCHQSAAWYDVLSGSYDKAL 1691
Cdd:pfam01410 80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568921732 1692 RFLGSNDEEMSYE--NNPHIKALYDGCASRKGY-EKTVIEINTPKIDQVPIIDVMINDFGDQNQKFGFEVGPACF 1763
Cdd:pfam01410 159 LLQGSNDEEIRAEgnSRFTYTVLEDGCTKRTGQwGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
|
|
| COLFI |
smart00038 |
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1535-1764 |
5.52e-104 |
|
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: 5.52e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1535 MEEIFGSLNSLKQDIEHMKFPMGTQTNPARTCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTAgGETCIYPDKKS 1614
Cdd:smart00038 1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFET-GETCVSPSPSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1615 EGVRISSWPKEKpGSWYSEFKR-GKLLSYLDVEGNSINMVQMTFLKLLTASARQNFTYNCHQSAAWYDVLSGSYDKALRF 1693
Cdd:smart00038 80 IPRKTWYSGKSK-HVWFGETMNgGFKFSYGDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568921732 1694 LGSNDEEMSYENN--PHIKALYDGCASRKGY-EKTVIEINTPKIDQVPIIDVMINDFGDQNQKFGFEVGPACFL 1764
Cdd:smart00038 159 RGSNDVELSAEGNskFTYEVLEDGCQKRTGKwGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
37-228 |
6.71e-53 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 183.71 E-value: 6.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 37 PVDILKALDFHNSPVGISKTTGFCTnrknskdPDVAYRVTEEAQISAPTKQLFPGGiFPQDFSILFTIKPKKGTQAFLLS 116
Cdd:smart00210 1 GQDLLQVFDLPSLSFAIRQVVGPEP-------GSPAYRLGDPALVPQPTRDLFPSG-LPEDFSLLTTFRQTPKSRGVLFA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 117 LYNEHGIQQLGVEV-GRSPVFLFEDHtGKPTPENYPLFSTVNIADGKWHRVAISVEKKTVTMIVDCKKKITKPLDRSERS 195
Cdd:smart00210 73 IYDAQNVRQFGLEVdGRANTLLLRYQ-GVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQP 151
|
170 180 190
....*....|....*....|....*....|...
gi 568921732 196 IVDTNGIMVFGTRILETDVFQGDIQQFLITGDP 228
Cdd:smart00210 152 PIDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
561-862 |
2.28e-28 |
|
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: 120.40 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 561 FDGLPGLPGDkGHRGERGPQGPPGLPGDDGMRGEDGEIGPRGLPGEAGPRGllgprgtpgppgqpgIGGIDGPQGPKGnm 640
Cdd:NF038329 107 DEGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG---------------ERGEKGPAGPQG-- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 641 gpqgepgppgqqgnpgpqglpgpqgpigppgEKGPQGKPGLAGLPGADGPPGHPGKEGQSGEKgalgppgpqgpigypGP 720
Cdd:NF038329 169 -------------------------------EAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET---------------GP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 721 RGVKGADGVRGLKGSKGEKGEDGFPGFKGDmGLKGDRGEVGQVGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPG 800
Cdd:NF038329 203 AGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568921732 801 LPGYPGRQGPKGSTGFPGFPGANGEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPK 862
Cdd:NF038329 282 PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
750-1003 |
6.04e-27 |
|
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: 116.16 E-value: 6.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 750 DMGLKGDRGEVGQVGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKlgvPGLPGYPGRQGPKGSTGFPGFPGANGEKGAR 829
Cdd:NF038329 112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE---RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 830 GIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKgtsggdgPPGPPGERGPQGPQGPVGFPGPKGPPGPAGKDGLPGHPGQ 909
Cdd:NF038329 189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA-------GEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGP 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 910 RGETGFQGKtgppgpggvvgpQGPTGETGPIGERGHPGPPGPPGEQGLPGAAGKEGAKGDPGPQGISGKDGPAGIRGFPG 989
Cdd:NF038329 262 RGDRGEAGP------------DGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
|
250
....*....|....
gi 568921732 990 ERGLPGAQGAPGLK 1003
Cdd:NF038329 330 KDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1019-1264 |
8.26e-27 |
|
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: 115.77 E-value: 8.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1019 GERGSAGTAGPIGLPGRPGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGS 1098
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1099 KGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPRGqQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGEngdvgpmg 1178
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE-------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1179 ppgppgprgpQGPNGADGPQGPPGSIGSVGVVGDKGEPGEAGNPGPPGEAGSGGLKGERGEKGEAGPPGAAGPAGIKGPP 1258
Cdd:NF038329 268 ----------AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
|
....*.
gi 568921732 1259 GDDGPK 1264
Cdd:NF038329 338 GKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
512-847 |
5.47e-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: 113.46 E-value: 5.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 512 GESGDPGPQGPRGVQgppgptgkpgkrgrpgadggrgmpGESGSKGDRGFDGLPGLPGDKGHRGERgpqgppglpGDDGM 591
Cdd:NF038329 117 GEKGEPGPAGPAGPA------------------------GEQGPRGDRGETGPAGPAGPPGPQGER---------GEKGP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 592 RGEDGEIGPRGLPGEAGPRGLlgprgtpgppgqpgiggiDGPQGPKGnmgpqgepgppgqqgnpgpqglpgpqgpigppg 671
Cdd:NF038329 164 AGPQGEAGPQGPAGKDGEAGA------------------KGPAGEKG--------------------------------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 672 EKGPQGKPGLAGLPGADGPPGHPGKEGQSGEkgalgppgpqgpigypgpRGVKGADGvrglkgsKGEKGEDGFPGFKGDM 751
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGE------------------DGPAGPAG-------DGQQGPDGDPGPTGED 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 752 GLKGDRGEVGQVGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGI 831
Cdd:NF038329 248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327
|
330
....*....|....*.
gi 568921732 832 AGKPGPRGQRGPTGPR 847
Cdd:NF038329 328 PGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1063-1359 |
1.77e-25 |
|
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: 111.92 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1063 DGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPpgppglqgpvgaPGIAGGDGEPGPRGQQGMFGQKG 1142
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE------------KGPAGPQGEAGPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1143 DEGARGFPGLPGPIGLQGLPGPPGEKGEnGDVGPMGPPGPPGPRGPQGPNGADGPQGPPGSIGSVGVVGDKGEPGEAGNP 1222
Cdd:NF038329 184 AKGPAGEKGPQGPRGETGPAGEQGPAGP-AGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1223 GPPGEAGSGGLKGERGEKGEAGPPGAAGPAGIKGPPGDDGPKGnpgpvgfpgdpgppgepgpagQDGVGGDKGEDgdpgq 1302
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDG---------------------QNGKDGLPGKD----- 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 568921732 1303 pgppgpsgeagppgppgkrgppgasGSEGRQGEKGAKGEAGAEGPPGKTGPVGPQGP 1359
Cdd:NF038329 317 -------------------------GKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVP 348
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
836-1168 |
2.50e-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: 108.45 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 836 GPRGQRGPTGPRGSRGARGPTGKPGPKgtsggdgppgppgergpqgpqgpvgfpgpkgppGPAGKDGLPGHPGQRGETGF 915
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGET---------------------------------GPAGPAGPPGPQGERGEKGP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 916 QGKtgppgpggvvgpqgpTGETGPIGERghpgppgppgeqglpgaagkeGAKGDPGPQGISGKDGPAGIRGFPGERGLPG 995
Cdd:NF038329 164 AGP---------------QGEAGPQGPA---------------------GKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 996 AQGAPGLKggegpqgpqgpvGSPGERGSAGTAGPiglpgrpGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPA 1075
Cdd:NF038329 208 PAGPAGPD------------GEAGPAGEDGPAGP-------AGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1076 GPAGSPGEDGDKGEIGEPGQKGSKGDKGEngppgppglqgpvgapgiAGGDGEPGPRGQQGMFGQKGDEGARGFPGLPGP 1155
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGL------------------PGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330
|
330
....*....|...
gi 568921732 1156 IGLQGLPGPPGEK 1168
Cdd:NF038329 331 DGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1052-1386 |
4.57e-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: 4.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1052 GEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGEngppgppglqgpvgaPGIAGGDGEPGP 1131
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE---------------AGPQGPAGKDGE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1132 RGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGENGDvgpmgppgppgprgpqgpngaDGPQGPPGSiGSVGVVG 1211
Cdd:NF038329 182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGE---------------------DGPAGPAGD-GQQGPDG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1212 DKGEPGEAGNPGPPGEAGSGGLKGERGEKGEAgppgaagpagikGPPGDDGPKGnpgpvgfpgdpgppgepgpagqdgvg 1291
Cdd:NF038329 240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD------------GPDGKDGERG-------------------------- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1292 gdkgedgdpgqpgppgpsgeagppgppgkrgppgasgsegRQGEKGAKGEAGAEGPPGKTGPVGPQGPSGKPGPEGLRGI 1371
Cdd:NF038329 282 ----------------------------------------PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321
|
330
....*....|....*
gi 568921732 1372 PGPVGEQGLPGAAGQ 1386
Cdd:NF038329 322 PGKDGLPGKDGKDGQ 336
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
788-1097 |
1.29e-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: 106.14 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 788 GQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKgtsgg 867
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK----- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 868 dgppgppgergpqgpqgpvgfpgpkgppgpagkdglpGHPGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHpg 947
Cdd:NF038329 192 -------------------------------------GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 948 ppgppgeqglpgaaGKEGAKGDPGPQGISGKDGPAGIRGFPGERGLPGAQGAPGlkggegpqgpqgPVGSPGERGSAGTA 1027
Cdd:NF038329 233 --------------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG------------PDGKDGERGPVGPA 286
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1028 GpiglpgrpgpqgppgpagEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKG 1097
Cdd:NF038329 287 G------------------KDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
824-1155 |
2.80e-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: 101.91 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 824 GEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGtsggdgppgppgergpqgpqgpvgfpgpkgppgpagKDGL 903
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG------------------------------------ERGE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 904 PGHPGQRGETGFQGktgppgpggvvgPQGPTGETGPIGERGhpgppgppgeqglpgAAGKEGAKGDPGPQGISGKDGPAG 983
Cdd:NF038329 161 KGPAGPQGEAGPQG------------PAGKDGEAGAKGPAG---------------EKGPQGPRGETGPAGEQGPAGPAG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 984 IRGFPGERGLPGAQGAPGlkggegpQGPQGPVGSPGERGSAGTAGPiglpgrpgpqgpPgpagekGAPGEKGPQGPAGRD 1063
Cdd:NF038329 214 PDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDGPQGP------------D------GPAGKDGPRGDRGEA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1064 GVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGEngppgppglqgpvgaPGIAGGDGEPGPRGQQGMFGQKGD 1143
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK---------------DGLPGKDGKDGQPGKDGLPGKDGK 333
|
330
....*....|..
gi 568921732 1144 EGArgfPGLPGP 1155
Cdd:NF038329 334 DGQ---PGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1196-1442 |
2.82e-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: 101.91 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1196 GPQGPPGSIGSVGVVGDKGEPGEAGNPGPPGEAGSGGLKGERGEKGEAgppgaagpagikGPPGDDGPKGnpgpvgfpgd 1275
Cdd:NF038329 123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA------------GPQGPAGKDG---------- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1276 pgppgepgpagQDGVGGDKGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGASGSEGRQGEKGaKGEAGAEGPPGKTGPVG 1355
Cdd:NF038329 181 -----------EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1356 PQGPSGKPGPEGLRGIPGPVGEQGLPGAAGQDGPPGPLGPPGLPGLKGDPGSKGEKGHPGLIGLIGPPGEQGEKGDRGLP 1435
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328
|
....*..
gi 568921732 1436 GTQGSPG 1442
Cdd:NF038329 329 GKDGKDG 335
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1125-1430 |
5.57e-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: 101.14 E-value: 5.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1125 GDGEPGPRGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGENGDVGPMGPPgppgprgpqgpngadGPQGPPGSI 1204
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA---------------GPQGPAGKD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1205 GSVGVVGDKGEPGEAGNPGPPGEAGSGGLKGERGEKGEAgppgaagpagikGPPGDDGPKGnpgpvgfpgdpgppgePGP 1284
Cdd:NF038329 180 GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEA------------GPAGEDGPAG----------------PAG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1285 AGQDGVGGDKGEDGDPGQPGPPgpsgeagppgppgkrgppgasGSEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPSGKPG 1364
Cdd:NF038329 232 DGQQGPDGDPGPTGEDGPQGPD---------------------GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568921732 1365 PEGLRGIPGPVGEQGLPGAAGQdgppgplgppglpglkgdPGSKGEKGHPGLIGLIGPPGEQGEKG 1430
Cdd:NF038329 291 QNGKDGLPGKDGKDGQNGKDGL------------------PGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
487-775 |
2.27e-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: 86.88 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 487 RGPPGPMGLTGRPGPVGGPGSAGAKGESGDPGPQGPRGVQGPPGPTGKPGKRGRPGADGGRGMPGESGSKGDRGFDGLPG 566
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 567 LPGDKGHRGERGPQGPPGLPGDDGMRGEDG--EIGPRGLPGEAGPrgllgprgtpgppgqpgiggiDGPQGPKGnmgpqg 644
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGE---------------------DGPQGPDG------ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 645 epgppgqqgNPGPQglpgpqgpiGPPGEKGPQGKPGLAGLPGADGPPGHPGKEGQsgekgalgppgpqgpigypgprgvK 724
Cdd:NF038329 255 ---------PAGKD---------GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ------------------------N 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568921732 725 GADGVRGLKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQVGPRGEDGPEGPK 775
Cdd:NF038329 293 GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1288-1504 |
1.63e-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: 81.10 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1288 DGVGGDKGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGASGSEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPSGKPGPEG 1367
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1368 LRGIPGPVGEQGLPGAAGQDGPPGPLGPPGLPGLKGDP-----GSKGEKGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPG 1442
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568921732 1443 AKGDGGIPGPAGPIGPPGPPGLPGPAGPKGNKGSSGPTGQKGDSGMPGPPGPPGPPGEVIQP 1504
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
72-224 |
1.24e-11 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 64.36 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 72 AYRVTEEAQISAPTKQlfpggIFPQDFSILFTIKPKKgTQAFLLSLYNEHGIQQLGVE-VGRSPVFLFEDHTGKPTpeny 150
Cdd:cd00110 1 GVSFSGSSYVRLPTLP-----APRTRLSISFSFRTTS-PNGLLLYAGSQNGGDFLALElEDGRLVLRYDLGSGSLV---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 151 pLFSTVNIADGKWHRVAISVEKKTVTMIVDCKKKITKPLDRSErSIVDTNGIMVFG--------TRILETDVFQGDIQQF 222
Cdd:cd00110 71 -LSSKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGS-ALLNLDGPLYLGglpedlksPGLPVSPGFVGCIRDL 148
|
..
gi 568921732 223 LI 224
Cdd:cd00110 149 KV 150
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
379-610 |
1.27e-11 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 68.78 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 379 GAYGEKGQKGEPAVVEPgMLVEGPPGPAGPAGLMGPPGLQGPSGLPGDPGDRGPPGRPGLPGADGLPGPPGTmlmlPFRY 458
Cdd:NF038329 135 GPRGDRGETGPAGPAGP-PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE----QGPA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 459 GGDGSKGPTISAQEAQAQAILQQARIALRGPPGPMGLTGRPGPVGGPGSAGAKGESGDPGPQGPRGVQGPPGPTgkpgkr 538
Cdd:NF038329 210 GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV------ 283
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568921732 539 GRPGADGGRGMPGESGSKGDRGFDGLPGLPGDKGHRGErgpqgppglpgdDGMRGEDGEIGPRGLPGEAGPR 610
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ------------PGKDGLPGKDGKDGQPGKPAPK 343
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
1049-1266 |
3.43e-07 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 55.04 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1049 GAPGEKGPQGPAGRDGVQGPVGLPG---PAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGG 1125
Cdd:COG5164 10 GPSDPGGVTTPAGSQGSTKPAQNQGstrPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1126 DgepGPRGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGENGDVGPMGPPGPPGPRGPQGPNGADGPQGPPGSIG 1205
Cdd:COG5164 90 T---RPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568921732 1206 SVGVVGDKGEPGEAGNPGPP--GEAGSGGLKGERGEKGEAGPPGAAGPAGIKGPPGDDGPKGN 1266
Cdd:COG5164 167 PPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTG 229
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
604-861 |
3.83e-07 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 54.65 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 604 PGEAGPRGLLGPRGTPGPPGQPGIGGIDGPQGPKGNMGPQGEPGPPGQQGNPGPQGLPGPQGPIGPPGEKGPQGKPGLAG 683
Cdd:COG5164 6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 684 LPGADGPPGHPGKEGQSGEKGALGPPGPQGPIGYPGPRGVKGAdgvrglkGSKGEKGEDGFPG-FKGDMGLKGDRGEVGQ 762
Cdd:COG5164 86 NQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTP-------PSGGSTTPPGDGGsTPPGPGSTGPGGSTTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 763 VGPRGEDGPEGPKGRAGPTGDPGpSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGiaGKPGPRGQRG 842
Cdd:COG5164 159 PGDGGSTTPPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGPKDQRP 235
|
250
....*....|....*....
gi 568921732 843 PTGPRGSRGARGPTGKPGP 861
Cdd:COG5164 236 KTNPIERRGPERPEAAALP 254
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
803-859 |
1.48e-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: 46.72 E-value: 1.48e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568921732 803 GYPGRQGPKGSTGFPGFPGANGEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKP 859
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
740-1000 |
2.58e-06 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 51.95 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 740 GEDGFPGFKGDMGLKGDRGEVGQVGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGF 819
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 820 PGANGEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPPGERGPQGPQGPVGFPGPKGPPGPAg 899
Cdd:COG5164 87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGST- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 900 kdGLPGHPGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHPGPPGPPGEQGLPGAAGKEGAKGDPGPQGISGKD 979
Cdd:COG5164 166 --TPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERR 243
|
250 260
....*....|....*....|.
gi 568921732 980 GPAGIRGFPGERGLPGAQGAP 1000
Cdd:COG5164 244 GPERPEAAALPAELTALEAEN 264
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1340-1386 |
3.98e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 42.87 E-value: 3.98e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568921732 1340 GEAGAEGPPGKTGPVGPQGPSGKPGPEGLRGIPGPVGEQGLPGAAGQ 1386
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
|
|
| GGGWT_bact |
NF040941 |
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ... |
1565-1604 |
4.17e-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: 4.17e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 568921732 1565 TCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTAGG 1604
Cdd:NF040941 1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTTDG 40
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
152-220 |
5.75e-05 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 44.33 E-value: 5.75e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568921732 152 LFSTVNIADGKWHRVAISVEKKTVTMIVDCKKKITKPLDrSERSIVDTNGIMVFG--------TRILETDVFQGDIQ 220
Cdd:pfam02210 44 LSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP-GESLLLNLNGPLYLGglppllllPALPVRAGFVGCIR 119
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1119-1171 |
1.24e-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: 41.33 E-value: 1.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568921732 1119 APGIAGGDGEPGPRGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGEN 1171
Cdd:pfam01391 5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1345-1527 |
3.48e-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: 45.28 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1345 EGPPGKTGPVGPQGPSGKPGPEGLRGIPGPVGEQGLPGAAGQDgppgplgppglpglkgdpgskgekghpgliGLIGPPG 1424
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGER------------------------------GEKGPAG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1425 EQGEKGDRGLPGTQgspgakgdggipgpagpiGPPGPPGLPGPAGPKGNKGSSGPTGQKGDSGMPGPPGPPGPPGEVIQP 1504
Cdd:NF038329 166 PQGEAGPQGPAGKD------------------GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPA 227
|
170 180
....*....|....*....|...
gi 568921732 1505 LPILSPKKTRRHTESIQGDAGDN 1527
Cdd:NF038329 228 GPAGDGQQGPDGDPGPTGEDGPQ 250
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
688-860 |
9.03e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 43.81 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 688 DGPPGHPGKEGQSGEKGALGPPGPQGPIGYPGPRGVKGADGV---RGLKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQVG 764
Cdd:PHA03169 89 QGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESpasHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQ 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 765 PRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGyPGRQGPKGSTGFPGFPGANGEKGARGIAGKPGPR----GQ 840
Cdd:PHA03169 169 PSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSP-PDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEregpPF 247
|
170 180
....*....|....*....|
gi 568921732 841 RGPTGPRGSRGARGPTGKPG 860
Cdd:PHA03169 248 PGHRSHSYTVVGWKPSTRPG 267
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1404-1534 |
2.15e-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: 42.58 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1404 DPGSKGEKGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPGAKGDGGIPGPAGPIGPPGPPGLPGPAGPKGNKGSSGPTGQK 1483
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 568921732 1484 GDSGMPGPPGPPGPPGEVIQPLPILSPKKTRRHTESIQGDAGDNILDYSDG 1534
Cdd:NF038329 201 GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG 251
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
1194-1440 |
2.41e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 42.71 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1194 ADGPQG------PPGSIGSVGVVGDKGEPGEAGNPGPPGEAGSGGLKGERGEKGEAGPPGAAGPAGIKGPPGDDGPKGNP 1267
Cdd:COG5164 8 KTGPSDpggvttPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1268 GPVGFPGDPGPPGEPGPAGQDGVGGDKGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGASGSEGRQGEKGAKGEAGAEGP 1347
Cdd:COG5164 88 GGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1348 PGKTGPVGPQGPSGKPGPeGLRGIPGPVGEQGLPGAAGQDGPPGPLGPPGLPGLKGDPGSK-GEKGHPGLIGLIGPPGEQ 1426
Cdd:COG5164 168 PGPGGSTTPPDDGGSTTP-PNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKtGPKDQRPKTNPIERRGPE 246
|
250
....*....|....
gi 568921732 1427 GEKGDRGLPGTQGS 1440
Cdd:COG5164 247 RPEAAALPAELTAL 260
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COLFI |
pfam01410 |
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1534-1763 |
3.34e-127 |
|
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: 3.34e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1534 GMEEIFGSLNSLKQDIEHMKFPMGTQTNPARTCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTAgGETCIYPDKK 1613
Cdd:pfam01410 1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1614 SEGvRISSWPKEKPGSWYSEFKRGKL-LSY-LDVEGNSINMVQMTFLKLLTASARQNFTYNCHQSAAWYDVLSGSYDKAL 1691
Cdd:pfam01410 80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568921732 1692 RFLGSNDEEMSYE--NNPHIKALYDGCASRKGY-EKTVIEINTPKIDQVPIIDVMINDFGDQNQKFGFEVGPACF 1763
Cdd:pfam01410 159 LLQGSNDEEIRAEgnSRFTYTVLEDGCTKRTGQwGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
|
|
| COLFI |
smart00038 |
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1535-1764 |
5.52e-104 |
|
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: 5.52e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1535 MEEIFGSLNSLKQDIEHMKFPMGTQTNPARTCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTAgGETCIYPDKKS 1614
Cdd:smart00038 1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFET-GETCVSPSPSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1615 EGVRISSWPKEKpGSWYSEFKR-GKLLSYLDVEGNSINMVQMTFLKLLTASARQNFTYNCHQSAAWYDVLSGSYDKALRF 1693
Cdd:smart00038 80 IPRKTWYSGKSK-HVWFGETMNgGFKFSYGDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568921732 1694 LGSNDEEMSYENN--PHIKALYDGCASRKGY-EKTVIEINTPKIDQVPIIDVMINDFGDQNQKFGFEVGPACFL 1764
Cdd:smart00038 159 RGSNDVELSAEGNskFTYEVLEDGCQKRTGKwGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
37-228 |
6.71e-53 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 183.71 E-value: 6.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 37 PVDILKALDFHNSPVGISKTTGFCTnrknskdPDVAYRVTEEAQISAPTKQLFPGGiFPQDFSILFTIKPKKGTQAFLLS 116
Cdd:smart00210 1 GQDLLQVFDLPSLSFAIRQVVGPEP-------GSPAYRLGDPALVPQPTRDLFPSG-LPEDFSLLTTFRQTPKSRGVLFA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 117 LYNEHGIQQLGVEV-GRSPVFLFEDHtGKPTPENYPLFSTVNIADGKWHRVAISVEKKTVTMIVDCKKKITKPLDRSERS 195
Cdd:smart00210 73 IYDAQNVRQFGLEVdGRANTLLLRYQ-GVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQP 151
|
170 180 190
....*....|....*....|....*....|...
gi 568921732 196 IVDTNGIMVFGTRILETDVFQGDIQQFLITGDP 228
Cdd:smart00210 152 PIDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
561-862 |
2.28e-28 |
|
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: 120.40 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 561 FDGLPGLPGDkGHRGERGPQGPPGLPGDDGMRGEDGEIGPRGLPGEAGPRGllgprgtpgppgqpgIGGIDGPQGPKGnm 640
Cdd:NF038329 107 DEGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG---------------ERGEKGPAGPQG-- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 641 gpqgepgppgqqgnpgpqglpgpqgpigppgEKGPQGKPGLAGLPGADGPPGHPGKEGQSGEKgalgppgpqgpigypGP 720
Cdd:NF038329 169 -------------------------------EAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET---------------GP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 721 RGVKGADGVRGLKGSKGEKGEDGFPGFKGDmGLKGDRGEVGQVGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPG 800
Cdd:NF038329 203 AGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568921732 801 LPGYPGRQGPKGSTGFPGFPGANGEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPK 862
Cdd:NF038329 282 PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
750-1003 |
6.04e-27 |
|
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: 116.16 E-value: 6.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 750 DMGLKGDRGEVGQVGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKlgvPGLPGYPGRQGPKGSTGFPGFPGANGEKGAR 829
Cdd:NF038329 112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE---RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 830 GIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKgtsggdgPPGPPGERGPQGPQGPVGFPGPKGPPGPAGKDGLPGHPGQ 909
Cdd:NF038329 189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA-------GEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGP 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 910 RGETGFQGKtgppgpggvvgpQGPTGETGPIGERGHPGPPGPPGEQGLPGAAGKEGAKGDPGPQGISGKDGPAGIRGFPG 989
Cdd:NF038329 262 RGDRGEAGP------------DGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
|
250
....*....|....
gi 568921732 990 ERGLPGAQGAPGLK 1003
Cdd:NF038329 330 KDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1019-1264 |
8.26e-27 |
|
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: 115.77 E-value: 8.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1019 GERGSAGTAGPIGLPGRPGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGS 1098
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1099 KGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPRGqQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGEngdvgpmg 1178
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE-------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1179 ppgppgprgpQGPNGADGPQGPPGSIGSVGVVGDKGEPGEAGNPGPPGEAGSGGLKGERGEKGEAGPPGAAGPAGIKGPP 1258
Cdd:NF038329 268 ----------AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
|
....*.
gi 568921732 1259 GDDGPK 1264
Cdd:NF038329 338 GKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
512-847 |
5.47e-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: 113.46 E-value: 5.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 512 GESGDPGPQGPRGVQgppgptgkpgkrgrpgadggrgmpGESGSKGDRGFDGLPGLPGDKGHRGERgpqgppglpGDDGM 591
Cdd:NF038329 117 GEKGEPGPAGPAGPA------------------------GEQGPRGDRGETGPAGPAGPPGPQGER---------GEKGP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 592 RGEDGEIGPRGLPGEAGPRGLlgprgtpgppgqpgiggiDGPQGPKGnmgpqgepgppgqqgnpgpqglpgpqgpigppg 671
Cdd:NF038329 164 AGPQGEAGPQGPAGKDGEAGA------------------KGPAGEKG--------------------------------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 672 EKGPQGKPGLAGLPGADGPPGHPGKEGQSGEkgalgppgpqgpigypgpRGVKGADGvrglkgsKGEKGEDGFPGFKGDM 751
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGE------------------DGPAGPAG-------DGQQGPDGDPGPTGED 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 752 GLKGDRGEVGQVGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGI 831
Cdd:NF038329 248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327
|
330
....*....|....*.
gi 568921732 832 AGKPGPRGQRGPTGPR 847
Cdd:NF038329 328 PGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1063-1359 |
1.77e-25 |
|
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: 111.92 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1063 DGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPpgppglqgpvgaPGIAGGDGEPGPRGQQGMFGQKG 1142
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE------------KGPAGPQGEAGPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1143 DEGARGFPGLPGPIGLQGLPGPPGEKGEnGDVGPMGPPGPPGPRGPQGPNGADGPQGPPGSIGSVGVVGDKGEPGEAGNP 1222
Cdd:NF038329 184 AKGPAGEKGPQGPRGETGPAGEQGPAGP-AGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1223 GPPGEAGSGGLKGERGEKGEAGPPGAAGPAGIKGPPGDDGPKGnpgpvgfpgdpgppgepgpagQDGVGGDKGEDgdpgq 1302
Cdd:NF038329 263 GDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDG---------------------QNGKDGLPGKD----- 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 568921732 1303 pgppgpsgeagppgppgkrgppgasGSEGRQGEKGAKGEAGAEGPPGKTGPVGPQGP 1359
Cdd:NF038329 317 -------------------------GKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVP 348
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
836-1168 |
2.50e-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: 108.45 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 836 GPRGQRGPTGPRGSRGARGPTGKPGPKgtsggdgppgppgergpqgpqgpvgfpgpkgppGPAGKDGLPGHPGQRGETGF 915
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGET---------------------------------GPAGPAGPPGPQGERGEKGP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 916 QGKtgppgpggvvgpqgpTGETGPIGERghpgppgppgeqglpgaagkeGAKGDPGPQGISGKDGPAGIRGFPGERGLPG 995
Cdd:NF038329 164 AGP---------------QGEAGPQGPA---------------------GKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 996 AQGAPGLKggegpqgpqgpvGSPGERGSAGTAGPiglpgrpGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPA 1075
Cdd:NF038329 208 PAGPAGPD------------GEAGPAGEDGPAGP-------AGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1076 GPAGSPGEDGDKGEIGEPGQKGSKGDKGEngppgppglqgpvgapgiAGGDGEPGPRGQQGMFGQKGDEGARGFPGLPGP 1155
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGL------------------PGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330
|
330
....*....|...
gi 568921732 1156 IGLQGLPGPPGEK 1168
Cdd:NF038329 331 DGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1052-1386 |
4.57e-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: 4.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1052 GEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGEngppgppglqgpvgaPGIAGGDGEPGP 1131
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE---------------AGPQGPAGKDGE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1132 RGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGENGDvgpmgppgppgprgpqgpngaDGPQGPPGSiGSVGVVG 1211
Cdd:NF038329 182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGE---------------------DGPAGPAGD-GQQGPDG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1212 DKGEPGEAGNPGPPGEAGSGGLKGERGEKGEAgppgaagpagikGPPGDDGPKGnpgpvgfpgdpgppgepgpagqdgvg 1291
Cdd:NF038329 240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD------------GPDGKDGERG-------------------------- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1292 gdkgedgdpgqpgppgpsgeagppgppgkrgppgasgsegRQGEKGAKGEAGAEGPPGKTGPVGPQGPSGKPGPEGLRGI 1371
Cdd:NF038329 282 ----------------------------------------PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321
|
330
....*....|....*
gi 568921732 1372 PGPVGEQGLPGAAGQ 1386
Cdd:NF038329 322 PGKDGLPGKDGKDGQ 336
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
788-1097 |
1.29e-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: 106.14 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 788 GQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKgtsgg 867
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK----- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 868 dgppgppgergpqgpqgpvgfpgpkgppgpagkdglpGHPGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHpg 947
Cdd:NF038329 192 -------------------------------------GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 948 ppgppgeqglpgaaGKEGAKGDPGPQGISGKDGPAGIRGFPGERGLPGAQGAPGlkggegpqgpqgPVGSPGERGSAGTA 1027
Cdd:NF038329 233 --------------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG------------PDGKDGERGPVGPA 286
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1028 GpiglpgrpgpqgppgpagEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKG 1097
Cdd:NF038329 287 G------------------KDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
824-1155 |
2.80e-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: 101.91 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 824 GEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGtsggdgppgppgergpqgpqgpvgfpgpkgppgpagKDGL 903
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG------------------------------------ERGE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 904 PGHPGQRGETGFQGktgppgpggvvgPQGPTGETGPIGERGhpgppgppgeqglpgAAGKEGAKGDPGPQGISGKDGPAG 983
Cdd:NF038329 161 KGPAGPQGEAGPQG------------PAGKDGEAGAKGPAG---------------EKGPQGPRGETGPAGEQGPAGPAG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 984 IRGFPGERGLPGAQGAPGlkggegpQGPQGPVGSPGERGSAGTAGPiglpgrpgpqgpPgpagekGAPGEKGPQGPAGRD 1063
Cdd:NF038329 214 PDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDGPQGP------------D------GPAGKDGPRGDRGEA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1064 GVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGEngppgppglqgpvgaPGIAGGDGEPGPRGQQGMFGQKGD 1143
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK---------------DGLPGKDGKDGQPGKDGLPGKDGK 333
|
330
....*....|..
gi 568921732 1144 EGArgfPGLPGP 1155
Cdd:NF038329 334 DGQ---PGKPAP 342
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1196-1442 |
2.82e-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: 101.91 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1196 GPQGPPGSIGSVGVVGDKGEPGEAGNPGPPGEAGSGGLKGERGEKGEAgppgaagpagikGPPGDDGPKGnpgpvgfpgd 1275
Cdd:NF038329 123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA------------GPQGPAGKDG---------- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1276 pgppgepgpagQDGVGGDKGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGASGSEGRQGEKGaKGEAGAEGPPGKTGPVG 1355
Cdd:NF038329 181 -----------EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1356 PQGPSGKPGPEGLRGIPGPVGEQGLPGAAGQDGPPGPLGPPGLPGLKGDPGSKGEKGHPGLIGLIGPPGEQGEKGDRGLP 1435
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328
|
....*..
gi 568921732 1436 GTQGSPG 1442
Cdd:NF038329 329 GKDGKDG 335
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1125-1430 |
5.57e-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: 101.14 E-value: 5.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1125 GDGEPGPRGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGENGDVGPMGPPgppgprgpqgpngadGPQGPPGSI 1204
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA---------------GPQGPAGKD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1205 GSVGVVGDKGEPGEAGNPGPPGEAGSGGLKGERGEKGEAgppgaagpagikGPPGDDGPKGnpgpvgfpgdpgppgePGP 1284
Cdd:NF038329 180 GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEA------------GPAGEDGPAG----------------PAG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1285 AGQDGVGGDKGEDGDPGQPGPPgpsgeagppgppgkrgppgasGSEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPSGKPG 1364
Cdd:NF038329 232 DGQQGPDGDPGPTGEDGPQGPD---------------------GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG 290
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568921732 1365 PEGLRGIPGPVGEQGLPGAAGQdgppgplgppglpglkgdPGSKGEKGHPGLIGLIGPPGEQGEKG 1430
Cdd:NF038329 291 QNGKDGLPGKDGKDGQNGKDGL------------------PGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
487-775 |
2.27e-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: 86.88 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 487 RGPPGPMGLTGRPGPVGGPGSAGAKGESGDPGPQGPRGVQGPPGPTGKPGKRGRPGADGGRGMPGESGSKGDRGFDGLPG 566
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 567 LPGDKGHRGERGPQGPPGLPGDDGMRGEDG--EIGPRGLPGEAGPrgllgprgtpgppgqpgiggiDGPQGPKGnmgpqg 644
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGE---------------------DGPQGPDG------ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 645 epgppgqqgNPGPQglpgpqgpiGPPGEKGPQGKPGLAGLPGADGPPGHPGKEGQsgekgalgppgpqgpigypgprgvK 724
Cdd:NF038329 255 ---------PAGKD---------GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ------------------------N 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568921732 725 GADGVRGLKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQVGPRGEDGPEGPK 775
Cdd:NF038329 293 GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1288-1504 |
1.63e-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: 81.10 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1288 DGVGGDKGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGASGSEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPSGKPGPEG 1367
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1368 LRGIPGPVGEQGLPGAAGQDGPPGPLGPPGLPGLKGDP-----GSKGEKGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPG 1442
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568921732 1443 AKGDGGIPGPAGPIGPPGPPGLPGPAGPKGNKGSSGPTGQKGDSGMPGPPGPPGPPGEVIQP 1504
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
72-224 |
1.24e-11 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 64.36 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 72 AYRVTEEAQISAPTKQlfpggIFPQDFSILFTIKPKKgTQAFLLSLYNEHGIQQLGVE-VGRSPVFLFEDHTGKPTpeny 150
Cdd:cd00110 1 GVSFSGSSYVRLPTLP-----APRTRLSISFSFRTTS-PNGLLLYAGSQNGGDFLALElEDGRLVLRYDLGSGSLV---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 151 pLFSTVNIADGKWHRVAISVEKKTVTMIVDCKKKITKPLDRSErSIVDTNGIMVFG--------TRILETDVFQGDIQQF 222
Cdd:cd00110 71 -LSSKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGS-ALLNLDGPLYLGglpedlksPGLPVSPGFVGCIRDL 148
|
..
gi 568921732 223 LI 224
Cdd:cd00110 149 KV 150
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
379-610 |
1.27e-11 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 68.78 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 379 GAYGEKGQKGEPAVVEPgMLVEGPPGPAGPAGLMGPPGLQGPSGLPGDPGDRGPPGRPGLPGADGLPGPPGTmlmlPFRY 458
Cdd:NF038329 135 GPRGDRGETGPAGPAGP-PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE----QGPA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 459 GGDGSKGPTISAQEAQAQAILQQARIALRGPPGPMGLTGRPGPVGGPGSAGAKGESGDPGPQGPRGVQGPPGPTgkpgkr 538
Cdd:NF038329 210 GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV------ 283
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568921732 539 GRPGADGGRGMPGESGSKGDRGFDGLPGLPGDKGHRGErgpqgppglpgdDGMRGEDGEIGPRGLPGEAGPR 610
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ------------PGKDGLPGKDGKDGQPGKPAPK 343
|
|
| LamG |
smart00282 |
Laminin G domain; |
99-226 |
2.65e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 62.74 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 99 SILFTIKPKKgTQAFLLSLYNEHGIQQLGVE-VGRSPVFLFEDHTGKPTPENyplfSTVNIADGKWHRVAISVEKKTVTM 177
Cdd:smart00282 1 SISFSFRTTS-PNGLLLYAGSKGGGDYLALElRDGRLVLRYDLGSGPARLTS----DPTPLNDGQWHRVAVERNGRSVTL 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568921732 178 IVDCKKKITKPLDRSErSIVDTNGIMVFG--------TRILETDVFQGDIQQFLITG 226
Cdd:smart00282 76 SVDGGNRVSGESPGGL-TILNLDGPLYLGglpedlklPPLPVTPGFRGCIRNLKVNG 131
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
1049-1266 |
3.43e-07 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 55.04 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1049 GAPGEKGPQGPAGRDGVQGPVGLPG---PAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGG 1125
Cdd:COG5164 10 GPSDPGGVTTPAGSQGSTKPAQNQGstrPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1126 DgepGPRGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGENGDVGPMGPPGPPGPRGPQGPNGADGPQGPPGSIG 1205
Cdd:COG5164 90 T---RPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568921732 1206 SVGVVGDKGEPGEAGNPGPP--GEAGSGGLKGERGEKGEAGPPGAAGPAGIKGPPGDDGPKGN 1266
Cdd:COG5164 167 PPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTG 229
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
604-861 |
3.83e-07 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 54.65 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 604 PGEAGPRGLLGPRGTPGPPGQPGIGGIDGPQGPKGNMGPQGEPGPPGQQGNPGPQGLPGPQGPIGPPGEKGPQGKPGLAG 683
Cdd:COG5164 6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 684 LPGADGPPGHPGKEGQSGEKGALGPPGPQGPIGYPGPRGVKGAdgvrglkGSKGEKGEDGFPG-FKGDMGLKGDRGEVGQ 762
Cdd:COG5164 86 NQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTP-------PSGGSTTPPGDGGsTPPGPGSTGPGGSTTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 763 VGPRGEDGPEGPKGRAGPTGDPGpSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGiaGKPGPRGQRG 842
Cdd:COG5164 159 PGDGGSTTPPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGPKDQRP 235
|
250
....*....|....*....
gi 568921732 843 PTGPRGSRGARGPTGKPGP 861
Cdd:COG5164 236 KTNPIERRGPERPEAAALP 254
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
900-1165 |
3.90e-07 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 54.65 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 900 KDGLPGHPGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGErghpgppgppgeqglPGAAGKEGAKGDPGPQGISGKD 979
Cdd:COG5164 8 KTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQN---------------QGSTTPAGNTGGTRPAGNQGAT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 980 GPAGIRGFPGERGLPGAQGAPGLKGGEGPQGPQGPVGSPGERGSAGTA---GPIGLPGRPGPQGPPGPAGEKGAPGEKGP 1056
Cdd:COG5164 73 GPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPddgGSTTPPSGGSTTPPGDGGSTPPGPGSTGP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1057 QGPAGRDGVQGPVGLPGPAGPAGSPGEDG-----DKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGGDGepGP 1131
Cdd:COG5164 153 GGSTTPPGDGGSTTPPGPGGSTTPPDDGGsttppNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKT--GP 230
|
250 260 270
....*....|....*....|....*....|....
gi 568921732 1132 RGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPP 1165
Cdd:COG5164 231 KDQRPKTNPIERRGPERPEAAALPAELTALEAEN 264
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
803-859 |
1.48e-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: 46.72 E-value: 1.48e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568921732 803 GYPGRQGPKGSTGFPGFPGANGEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKP 859
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
740-1000 |
2.58e-06 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 51.95 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 740 GEDGFPGFKGDMGLKGDRGEVGQVGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGF 819
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 820 PGANGEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPPGERGPQGPQGPVGFPGPKGPPGPAg 899
Cdd:COG5164 87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGST- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 900 kdGLPGHPGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHPGPPGPPGEQGLPGAAGKEGAKGDPGPQGISGKD 979
Cdd:COG5164 166 --TPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERR 243
|
250 260
....*....|....*....|.
gi 568921732 980 GPAGIRGFPGERGLPGAQGAP 1000
Cdd:COG5164 244 GPERPEAAALPAELTALEAEN 264
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
773-829 |
4.04e-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: 45.56 E-value: 4.04e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568921732 773 GPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGAR 829
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
809-862 |
4.72e-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: 45.56 E-value: 4.72e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568921732 809 GPKGSTGFPGFPGANGEKGARGIAGKPGPRGQRGPTGPRGSRGARGPTGKPGPK 862
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
800-855 |
8.94e-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: 44.79 E-value: 8.94e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568921732 800 GLPGYPGRQGPKGSTGFPGFPGANGEKGARGIAGKPGPRGQRGPTGPRGSRGARGP 855
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
794-850 |
1.85e-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: 1.85e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568921732 794 GKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGIAGKPGPRGQRGPTGPRGSR 850
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
761-815 |
2.21e-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: 2.21e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568921732 761 GQVGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTG 815
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
785-841 |
2.48e-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: 2.48e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568921732 785 GPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGIAGKPGPRGQR 841
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1340-1386 |
3.98e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 42.87 E-value: 3.98e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568921732 1340 GEAGAEGPPGKTGPVGPQGPSGKPGPEGLRGIPGPVGEQGLPGAAGQ 1386
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
|
|
| GGGWT_bact |
NF040941 |
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ... |
1565-1604 |
4.17e-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: 4.17e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 568921732 1565 TCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTAGG 1604
Cdd:NF040941 1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTTDG 40
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
152-220 |
5.75e-05 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 44.33 E-value: 5.75e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568921732 152 LFSTVNIADGKWHRVAISVEKKTVTMIVDCKKKITKPLDrSERSIVDTNGIMVFG--------TRILETDVFQGDIQ 220
Cdd:pfam02210 44 LSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP-GESLLLNLNGPLYLGglppllllPALPVRAGFVGCIR 119
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1119-1171 |
1.24e-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: 41.33 E-value: 1.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568921732 1119 APGIAGGDGEPGPRGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGEN 1171
Cdd:pfam01391 5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
752-806 |
1.81e-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: 40.94 E-value: 1.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568921732 752 GLKGDRGEVGQVGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPG 806
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1120-1170 |
1.95e-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: 40.94 E-value: 1.95e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568921732 1120 PGIAGGDGEPGPRGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGE 1170
Cdd:pfam01391 3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1345-1527 |
3.48e-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: 45.28 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1345 EGPPGKTGPVGPQGPSGKPGPEGLRGIPGPVGEQGLPGAAGQDgppgplgppglpglkgdpgskgekghpgliGLIGPPG 1424
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGER------------------------------GEKGPAG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1425 EQGEKGDRGLPGTQgspgakgdggipgpagpiGPPGPPGLPGPAGPKGNKGSSGPTGQKGDSGMPGPPGPPGPPGEVIQP 1504
Cdd:NF038329 166 PQGEAGPQGPAGKD------------------GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPA 227
|
170 180
....*....|....*....|...
gi 568921732 1505 LPILSPKKTRRHTESIQGDAGDN 1527
Cdd:NF038329 228 GPAGDGQQGPDGDPGPTGEDGPQ 250
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
737-792 |
4.78e-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: 39.78 E-value: 4.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568921732 737 GEKGEDGFPGFKGDMGLKGDRGEVGQVGPRGEDGPEGPKGRAGPTGDPGPSGQAGE 792
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1058-1104 |
6.75e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.40 E-value: 6.75e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568921732 1058 GPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGE 1104
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1045-1093 |
7.97e-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: 7.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568921732 1045 AGEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEP 1093
Cdd:pfam01391 9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
688-860 |
9.03e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 43.81 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 688 DGPPGHPGKEGQSGEKGALGPPGPQGPIGYPGPRGVKGADGV---RGLKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQVG 764
Cdd:PHA03169 89 QGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESpasHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQ 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 765 PRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGyPGRQGPKGSTGFPGFPGANGEKGARGIAGKPGPR----GQ 840
Cdd:PHA03169 169 PSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSP-PDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEregpPF 247
|
170 180
....*....|....*....|
gi 568921732 841 RGPTGPRGSRGARGPTGKPG 860
Cdd:PHA03169 248 PGHRSHSYTVVGWKPSTRPG 267
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
765-861 |
9.31e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.21 E-value: 9.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 765 PRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGIAGKPGPRGQRGPT 844
Cdd:PRK07764 615 PAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA 694
|
90
....*....|....*..
gi 568921732 845 GPRGSRGARGPTGKPGP 861
Cdd:PRK07764 695 GAAPAQPAPAPAATPPA 711
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
746-802 |
9.71e-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: 9.71e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568921732 746 GFKGDMGLKGDRGEVGQVGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLP 802
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1196-1242 |
1.04e-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: 38.63 E-value: 1.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568921732 1196 GPQGPPGSIGSVGVVGDKGEPGEAGNPGPPGEAGSGGLKGERGEKGE 1242
Cdd:pfam01391 10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1404-1534 |
2.15e-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: 42.58 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1404 DPGSKGEKGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPGAKGDGGIPGPAGPIGPPGPPGLPGPAGPKGNKGSSGPTGQK 1483
Cdd:NF038329 121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 568921732 1484 GDSGMPGPPGPPGPPGEVIQPLPILSPKKTRRHTESIQGDAGDNILDYSDG 1534
Cdd:NF038329 201 GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG 251
|
|
| Laminin_G_3 |
pfam13385 |
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
89-224 |
2.40e-03 |
|
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
Pssm-ID: 463865 [Multi-domain] Cd Length: 151 Bit Score: 40.45 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 89 FPGGIFP-QDFSILFTIKPK--KGTQAFLLSLYNEHGIqqlGVEVGRSPVFLFEDHTGKPTPENYPlfSTVNIADGKWHR 165
Cdd:pfam13385 9 LPDALLPtSDFTVSAWVKPDslPGWARAIISSSGGGGY---SLGLDGDGRLRFAVNGGNGGWDTVT--SGASVPLGQWTH 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568921732 166 VAISVEKKTVTMIVDCKKKITKPLdrSERSIVDTNGIMVFGTRILETDVFQGDIQQFLI 224
Cdd:pfam13385 84 VAVTYDGGTLRLYVNGVLVGSSTL--TGGPPPGTGGPLYIGRSPGGDDYFNGLIDEVRI 140
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
1194-1440 |
2.41e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 42.71 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1194 ADGPQG------PPGSIGSVGVVGDKGEPGEAGNPGPPGEAGSGGLKGERGEKGEAGPPGAAGPAGIKGPPGDDGPKGNP 1267
Cdd:COG5164 8 KTGPSDpggvttPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1268 GPVGFPGDPGPPGEPGPAGQDGVGGDKGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGASGSEGRQGEKGAKGEAGAEGP 1347
Cdd:COG5164 88 GGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1348 PGKTGPVGPQGPSGKPGPeGLRGIPGPVGEQGLPGAAGQDGPPGPLGPPGLPGLKGDPGSK-GEKGHPGLIGLIGPPGEQ 1426
Cdd:COG5164 168 PGPGGSTTPPDDGGSTTP-PNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKtGPKDQRPKTNPIERRGPE 246
|
250
....*....|....
gi 568921732 1427 GEKGDRGLPGTQGS 1440
Cdd:COG5164 247 RPEAAALPAELTAL 260
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1016-1083 |
2.65e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.47 E-value: 2.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568921732 1016 GSPGERGSAGTAGPiglpgrpgpqgpPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGE 1083
Cdd:pfam01391 1 GPPGPPGPPGPPGP------------PGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1325-1375 |
3.20e-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: 3.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568921732 1325 GASGSEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPSGKPGPEGLRGIPGPV 1375
Cdd:pfam01391 7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
1124-1385 |
5.29e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 41.55 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1124 GGDGEPGPRGQQGMFGQKGDEGARGFPGLPGPIGLQGLPGPPGEKGENGDVGPMgppgppgprgpqgpngadGPQGPPGS 1203
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNT------------------GGTRPAGN 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1204 IGSVGVVGDKGEPGEAGNPGPPGEAGSGGLKGERGEKGEAGPPGAAGPAgikGPPGDDGPKGNPGPVGFPGDPGPPGEPG 1283
Cdd:COG5164 69 QGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGAT---GPPDDGGSTTPPSGGSTTPPGDGGSTPP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921732 1284 PAGQDGVGGdkgedgdpgqpgppgpsgEAgppgppGKRGPPGASGSEGRQGEKGAKGEAGAEGPP--GKTGPVGPQGPSG 1361
Cdd:COG5164 146 GPGSTGPGG------------------ST------TPPGDGGSTTPPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTP 201
|
250 260
....*....|....*....|....
gi 568921732 1362 KPGPEGLRGIPGPVGEQGLPGAAG 1385
Cdd:COG5164 202 RQGPDGPVKKDDKNGKGNPPDDRG 225
|
|
| |
