|
Name |
Accession |
Description |
Interval |
E-value |
| COLFI |
pfam01410 |
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1624-1853 |
3.64e-129 |
|
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: 403.26 E-value: 3.64e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1624 GMEEIFGSLNSLKQDIEHMKFPMGTQTNPARTCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTSgGETCIYPDKK 1703
Cdd:pfam01410 1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1704 SEGvRISSWPKEKPGSWFSEFKRGKL-LSY-LDVEGNSINMVQMTFLKLLTASARQNFTYHCHQSAAWYDVSSGSYDKAL 1781
Cdd:pfam01410 80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966919056 1782 RFLGSNDEEMSYD--NNPFIKALYDGCASRKGY-EKTVIEINTPKIDQVPIVDVMINDFGDQNQKFGFEVGPVCF 1853
Cdd:pfam01410 159 LLQGSNDEEIRAEgnSRFTYTVLEDGCTKRTGQwGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
|
|
| COLFI |
smart00038 |
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1625-1854 |
3.70e-106 |
|
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.
Pssm-ID: 197483 Cd Length: 232 Bit Score: 338.29 E-value: 3.70e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1625 MEEIFGSLNSLKQDIEHMKFPMGTQTNPARTCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTsGGETCIYPDKKS 1704
Cdd:smart00038 1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFE-TGETCVSPSPSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1705 EGVRISSWPKEKpGSWFSEFKR-GKLLSYLDVEGNSINMVQMTFLKLLTASARQNFTYHCHQSAAWYDVSSGSYDKALRF 1783
Cdd:smart00038 80 IPRKTWYSGKSK-HVWFGETMNgGFKFSYGDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966919056 1784 LGSNDEEMSYDNN--PFIKALYDGCASRKGY-EKTVIEINTPKIDQVPIVDVMINDFGDQNQKFGFEVGPVCFL 1854
Cdd:smart00038 159 RGSNDVELSAEGNskFTYEVLEDGCQKRTGKwGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
38-229 |
2.49e-57 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 196.42 E-value: 2.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 38 PVDVLKALDFHNSPEGISKTTGFCtnrknskGSDTAYRVSKQAQLSAPTKQLFPGGpFPEDFSILFTVKPKKGIQSFLLS 117
Cdd:smart00210 1 GQDLLQVFDLPSLSFAIRQVVGPE-------PGSPAYRLGDPALVPQPTRDLFPSG-LPEDFSLLTTFRQTPKSRGVLFA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 118 IYNEHGIQQIGVEV-GRSPVFLFEDHtGKPAPEDYPLFRTVNIADGKWHRVAISVEKKTVTMIVDCKKKTTKPLDRSERA 196
Cdd:smart00210 73 IYDAQNVRQFGLEVdGRANTLLLRYQ-GVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQP 151
|
170 180 190
....*....|....*....|....*....|...
gi 966919056 197 IVDTNGITVFGTRILDEEVFEGDIQQFLITGDP 229
Cdd:smart00210 152 PIDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
651-952 |
3.80e-32 |
|
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: 131.95 E-value: 3.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 651 FDGLPGLPGDkGHRGERGPQGPpgppgddgmRGEDGEIGPRGLPGEAGPRGLLGPRGTPGAPGQPGMAGVDGPPGPKGnm 730
Cdd:NF038329 107 DEGLQQLKGD-GEKGEPGPAGP---------AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 731 gpqgepgppgqqgnpgpqglpgpqgpigppgEKGPQGKPGLAGLPGADGPPGHPGKEGQSGEKGALgppgpqgpigypgp 810
Cdd:NF038329 175 -------------------------------PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA-------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 811 rGVKGADGVRGLKGSKGEKGEDGfPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKlgvpg 890
Cdd:NF038329 210 -GPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP----- 282
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966919056 891 lPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPK 952
Cdd:NF038329 283 -VGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
628-892 |
5.56e-30 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 125.40 E-value: 5.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 628 RGRPGADGGRGMPGEPGSKGDRGFDGLPGLPGDKGHRGERGPQGPPgppgddgmrGEDGEIGPRGLPGEAGPRGLLGPRG 707
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA---------GPQGEAGPQGPAGKDGEAGAKGPAG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 708 TPGAPGQPGMAGVDGPPGPKGNMGPQGEPGPPGQQGNPGPQGLPgpqgpigppgEKGPQGKPGLAGLPGADGPPGHPGKE 787
Cdd:NF038329 190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG----------QQGPDGDPGPTGEDGPQGPDGPAGKD 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 788 GQsgekgalgppgpqgpigypgprgvKGADGVRGLKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGR 867
Cdd:NF038329 260 GP------------------------RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK 315
|
250 260
....*....|....*....|....*
gi 966919056 868 AGPTGDPGPSGQAGEKGKLGVPGLP 892
Cdd:NF038329 316 DGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
840-1092 |
4.18e-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: 113.85 E-value: 4.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 840 DMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKlgvPGLPGYPGRQGPKGSTGFPGFPGANGEKGAR 919
Cdd:NF038329 112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE---RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 920 GVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPpgergpqgpqgpvgfpgpkgppgppgkdglpghpGQ 999
Cdd:NF038329 189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------------------------------GQ 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1000 RGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHPGPPGPPGEQGLPGAAGKEGAKGDPGPQGISGKDGPAGLRGFPG 1079
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG 314
|
250
....*....|...
gi 966919056 1080 ERGLPGAQGAPGL 1092
Cdd:NF038329 315 KDGKDGQPGKDGL 327
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
878-1220 |
1.62e-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: 105.76 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 878 GQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTsgg 957
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 958 dgppgppgergpqgpqgpvgfpgpkgppgppgkdglpghPGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGErghpg 1037
Cdd:NF038329 194 ---------------------------------------QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP----- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1038 ppgppgeqglpGAAGKEGAKGDPGPQGISGKDGPAGLRGFPGERGlpgaqgapglkggegpqgppgpvgspgERGSAGTA 1117
Cdd:NF038329 230 -----------AGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG---------------------------DRGEAGPD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1118 GPiglpgrpgpqgppgpageKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGdkgengp 1197
Cdd:NF038329 272 GP------------------DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG------- 326
|
330 340
....*....|....*....|...
gi 966919056 1198 pgppglqgpvgAPGIAGGDGEPG 1220
Cdd:NF038329 327 -----------LPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1304-1532 |
7.36e-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: 100.75 E-value: 7.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1304 GEPGEAGNPGPPGEAGVGGPKGERGEKGEAGPPGAAGPPGAKGPPGDDGPKGnpgpvgfpgDPGPPGEPGPAGQDGVGGD 1383
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------EAGPQGPAGKDGEAGAKGP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1384 KGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGAAGAEGRQGEKGaKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPG 1463
Cdd:NF038329 188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966919056 1464 PVGEQGLPGAAGQDGPPGPMGPPGLPGLKGDPGSKGEKGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPG 1532
Cdd:NF038329 267 EAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
578-864 |
8.58e-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: 100.75 E-value: 8.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 578 GPPGPMGLTGRPGPVGGPGSAGAKGESGDPGPQGPRGVQGPPGPTGKPGKRGRPGADGGRGMPGEPGSKGDRGFDGLPGL 657
Cdd:NF038329 135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGP 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 658 PGDKGHRGERGPQGPPGppgddgmrgeDGEIGPRGLPGEAGPRGLLGPRGTPGAPGQPGMAGVDGPPGPKGnmgpqgepg 737
Cdd:NF038329 215 DGEAGPAGEDGPAGPAG----------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG--------- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 738 ppgqqgnpgpqglpgpqgpigppgEKGPQGKPGLAGLPGADGPPGHPGKEGQsgekgalgppgpqgpigypgprgvkgaD 817
Cdd:NF038329 276 ------------------------KDGERGPVGPAGKDGQNGKDGLPGKDGK---------------------------D 304
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 966919056 818 GVRGLKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGP 864
Cdd:NF038329 305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKP 351
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
926-1232 |
6.70e-21 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 98.05 E-value: 6.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 926 GPRGQRGPTGPRGSRGARGPTGKpgpkgtsggdgppgppgergpqgpqgpvgfpgpkgppgppgkdglpghpgqRGETGF 1005
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGD---------------------------------------------------RGETGP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1006 QGKtgppgpggvvgpqgpTGETGPIGERGHpgppgppgeqglpgaAGKEGAKGDPGPQGISGKDGPAGLRGFPGERGLPG 1085
Cdd:NF038329 146 AGP---------------AGPPGPQGERGE---------------KGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1086 AQGAPGLKGGEGPQGPPGPVGSPGERGSAGTAGPiglpgrpGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPA 1165
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP-------AGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966919056 1166 GPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPRGQQGMFGQKG 1232
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1153-1520 |
3.50e-19 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 92.66 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1153 DGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPpgppglqgpvgaPGIAGGDGEPGPRGQQGMFGQKG 1232
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE------------KGPAGPQGEAGPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1233 DEgargfpgppgpiglqglpGPPGEKGENgdvgpmgppgppgprgpqgpngadgpqgppgsvgsvggvgekGEPGEAGNP 1312
Cdd:NF038329 184 AK------------------GPAGEKGPQ------------------------------------------GPRGETGPA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1313 GPPGEAGVGGPKGERGEKGEagppgaagppgakgppgdDGPKGnpgpvgfpgdpgppgePGPAGQDGVGGDKGEDgdpgq 1392
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGE------------------DGPAG----------------PAGDGQQGPDGDPGPT----- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1393 pgppgpsgeagppgppgkrgppgaaGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPG 1472
Cdd:NF038329 245 -------------------------GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPG 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 966919056 1473 AAGQDGPPGPMgppglpglkGDPGSKGEKGHPGLIGLIGPPGEQGEKG 1520
Cdd:NF038329 300 KDGKDGQNGKD---------GLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1142-1476 |
5.36e-18 |
|
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: 88.81 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1142 GEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGP 1221
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1222 RGQQGMFGQKGDEGARGFPGPPGPIGLQGLPGPPGEkgengdvgpmgppgppgprgpqgpnGADGPQGppgsvgsvggvg 1301
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------------------------GQQGPDG------------ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1302 EKGEPGEAGNPGPPGEAGVGGPKGERGEKGEagppgaagppgakgppgdDGPKGNpgpvgfpgdpgppgepgpagqdgvg 1381
Cdd:NF038329 240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP------------------DGPDGK------------------------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1382 gdkgedgdpgqpgppgpsgeagppgppgkrgppgaAGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGI 1461
Cdd:NF038329 277 -----------------------------------DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321
|
330
....*....|....*
gi 966919056 1462 PGPVGEQGLPGAAGQ 1476
Cdd:NF038329 322 PGKDGLPGKDGKDGQ 336
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1110-1331 |
1.30e-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: 87.65 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1110 ERGSAGTAGPIGLPGRPGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSK 1189
Cdd:NF038329 118 EKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1190 GDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPRGqQGMFGQKGDEGARGFPGPPGPIGLQGLPGPPGEKGENGDVGPMGP 1269
Cdd:NF038329 198 GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966919056 1270 PGPPGPRGPQGPNGADGPQGPPGSVGSVGGVGEKGEPGEAGNPGPPGEAGVGGPKGERGEKG 1331
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1378-1532 |
5.34e-16 |
|
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: 82.65 E-value: 5.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1378 DGVGGDKGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGAAGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEG 1457
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1458 LRGIPGPVGEQGLPGAAGQDGPPGPMGPPGLPGLKGDP-----GSKGEKGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPG 1532
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1416-1577 |
1.04e-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: 81.88 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1416 AAGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPGAAGQDGPPGPMGPPGLPGLKGDP 1495
Cdd:NF038329 145 PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGED 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1496 GSKGE--KGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPGAKGDGGIPGPAGPLGPPGPPGLPGPQGPKGNKGSTGPAGQK 1573
Cdd:NF038329 225 GPAGPagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKD 304
|
....
gi 966919056 1574 GDSG 1577
Cdd:NF038329 305 GQNG 308
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
709-951 |
5.03e-09 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 60.81 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 709 PGAPGQPGMAGVDGPPGPKGNMGPQGEPGPPGQQGNPGPQGLPGPQGPIGPPGEKGPQGKPGLAGLPGADGPPGHPGKEG 788
Cdd:COG5164 3 LYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 789 QSGEKGALGPPGPQGPIGYPGPRGVKGADGVRGLKGSKGEKGEDGfPGFKGDMGLKGDRGEV----GQIGPRGEDGPEGP 864
Cdd:COG5164 83 PAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-PPSGGSTTPPGDGGSTppgpGSTGPGGSTTPPGD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 865 KGRAGPTGDPGPSGQAGEKGKlGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKP-------GPRGQRGPTGPR 937
Cdd:COG5164 162 GGSTTPPGPGGSTTPPDDGGS-TTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPddrggktGPKDQRPKTNPI 240
|
250
....*....|....
gi 966919056 938 GSRGARGPTGKPGP 951
Cdd:COG5164 241 ERRGPERPEAAALP 254
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
469-718 |
6.44e-09 |
|
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: 60.30 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 469 GAYGEKGQKGEPAVVEPgMLVEGPPGPAGPAGIMGPPGLQGPTGPPGDPGDRGPPGRPGLPGADGLPGPPGTmlmlPFRY 548
Cdd:NF038329 135 GPRGDRGETGPAGPAGP-PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE----QGPA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 549 GGDGSKGPTISAQEAQAQAILQQARIALRGPPGPMGLTGRPGPVGGPGSAGAKGESGDPGPQGPRGVQGPPGPTgkpgkr 628
Cdd:NF038329 210 GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV------ 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 629 GRPGADGGRGMPGEPGSKGDRGFDGLPGLPGDkghrgergpqgppgppgddgmRGEDGEIGPRGLPGEAGPRGLLGPRG- 707
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK---------------------DGKDGQPGKDGLPGKDGKDGQPGKPAp 342
|
250
....*....|..
gi 966919056 708 -TPGAPGQPGMA 718
Cdd:NF038329 343 kTPEVPQKPDTA 354
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
73-225 |
1.07e-07 |
|
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: 53.19 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 73 AYRVSKQAQLSAPTKQLFPggpfpEDFSILFTVKPKK--GIqsfLLSIYNEHGIQQIGVE-VGRSPVFLFEDHTGKPape 149
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPR-----TRLSISFSFRTTSpnGL---LLYAGSQNGGDFLALElEDGRLVLRYDLGSGSL--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 150 dypLFRTVN-IADGKWHRVAISVEKKTVTMIVDCKKKTTKPLDRSErAIVDTNGITVFGTRILDEEV--------FEGDI 220
Cdd:cd00110 70 ---VLSSKTpLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGS-ALLNLDGPLYLGGLPEDLKSpglpvspgFVGCI 145
|
....*
gi 966919056 221 QQFLI 225
Cdd:cd00110 146 RDLKV 150
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
893-949 |
2.37e-07 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 49.03 E-value: 2.37e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 966919056 893 GYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKP 949
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1427-1624 |
6.98e-07 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 53.76 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1427 GAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPGAAGQDgppgpmgppglpglkgdpgskgekghpgl 1506
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ----------------------------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1507 igliGPPGEQGEKGDRGLPGTQGSPGAKgdggipgpagplgppgppglpGPQGPKGNKGSTGPAGQKGDSGLPGPPGPPG 1586
Cdd:NF038329 168 ----GEAGPQGPAGKDGEAGAKGPAGEK---------------------GPQGPRGETGPAGEQGPAGPAGPDGEAGPAG 222
|
170 180 190
....*....|....*....|....*....|....*...
gi 966919056 1587 PPGEVIQPLPILSSKKTRRHTEGMQADADDNILDYSDG 1624
Cdd:NF038329 223 EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
830-1090 |
8.76e-06 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 50.41 E-value: 8.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 830 GEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGF 909
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 910 PGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPPGERGPQGPQGPVGFPGPKGPPGPPG 989
Cdd:COG5164 87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 990 KDGLPghpGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHPGPPGPPGEQGLPGAAGKEGAKGDPGPQGISGKD 1069
Cdd:COG5164 167 PPGPG---GSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERR 243
|
250 260
....*....|....*....|.
gi 966919056 1070 GPAGLRGFPGERGLPGAQGAP 1090
Cdd:COG5164 244 GPERPEAAALPAELTALEAEN 264
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1430-1476 |
9.30e-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: 9.30e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 966919056 1430 GEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPGAAGQ 1476
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
|
|
| GGGWT_bact |
NF040941 |
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ... |
1655-1694 |
1.07e-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: 44.09 E-value: 1.07e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 966919056 1655 TCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTSGG 1694
Cdd:NF040941 1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTTDG 40
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1148-1194 |
2.38e-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: 40.55 E-value: 2.38e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 966919056 1148 GPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGE 1194
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
998-1222 |
3.32e-04 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 45.41 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 998 GQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGErghpgppgppgeqglPGAAGKEGAKGDPGPQGISGKDGPAGLRGF 1077
Cdd:COG5164 16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQN---------------QGSTTPAGNTGGTRPAGNQGATGPAQNQGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1078 PGERGLPGAQGAPGLKGGEGPQGPPGPVGSPGERGSAGTA---GPIGLPGRPGPQGPPGPAGEKGAPGEKGPQGPAGRDG 1154
Cdd:COG5164 81 TTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPddgGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966919056 1155 VQGPVGLPGPAGPAGSPGEDG-----DKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPR 1222
Cdd:COG5164 161 DGGSTTPPGPGGSTTPPDDGGsttppNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQ 233
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
855-951 |
6.95e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.59 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 855 PRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPT 934
Cdd:PRK07764 615 PAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA 694
|
90
....*....|....*..
gi 966919056 935 GPRGSRGARGPTGKPGP 951
Cdd:PRK07764 695 GAAPAQPAPAPAATPPA 711
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
156-207 |
9.07e-04 |
|
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: 41.25 E-value: 9.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 966919056 156 TVNIADGKWHRVAISVEKKTVTMIVDCKKKTTKPLDrSERAIVDTNGITVFG 207
Cdd:pfam02210 47 GKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP-GESLLLNLNGPLYLG 97
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
1139-1356 |
7.40e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 41.17 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1139 GAPGEKGPQGPAGRDGVQGPVGLPG---PAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGG 1215
Cdd:COG5164 10 GPSDPGGVTTPAGSQGSTKPAQNQGstrPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1216 DgepGPRGQQGMFGQKGDEGARGFPGPPGPIGLQGLPGPPGEKGENGDVGPMGPPGPPGPRGPQGPNGADGPQGPPGSVG 1295
Cdd:COG5164 90 T---RPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966919056 1296 SVGGVGEKGEPGEAGNPGPP--GEAGVGGPKGERGEKGEAGPPGAAGPPGAKGPPGDDGPKGN 1356
Cdd:COG5164 167 PPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTG 229
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COLFI |
pfam01410 |
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1624-1853 |
3.64e-129 |
|
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: 403.26 E-value: 3.64e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1624 GMEEIFGSLNSLKQDIEHMKFPMGTQTNPARTCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTSgGETCIYPDKK 1703
Cdd:pfam01410 1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1704 SEGvRISSWPKEKPGSWFSEFKRGKL-LSY-LDVEGNSINMVQMTFLKLLTASARQNFTYHCHQSAAWYDVSSGSYDKAL 1781
Cdd:pfam01410 80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966919056 1782 RFLGSNDEEMSYD--NNPFIKALYDGCASRKGY-EKTVIEINTPKIDQVPIVDVMINDFGDQNQKFGFEVGPVCF 1853
Cdd:pfam01410 159 LLQGSNDEEIRAEgnSRFTYTVLEDGCTKRTGQwGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
|
|
| COLFI |
smart00038 |
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1625-1854 |
3.70e-106 |
|
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.
Pssm-ID: 197483 Cd Length: 232 Bit Score: 338.29 E-value: 3.70e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1625 MEEIFGSLNSLKQDIEHMKFPMGTQTNPARTCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTsGGETCIYPDKKS 1704
Cdd:smart00038 1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFE-TGETCVSPSPSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1705 EGVRISSWPKEKpGSWFSEFKR-GKLLSYLDVEGNSINMVQMTFLKLLTASARQNFTYHCHQSAAWYDVSSGSYDKALRF 1783
Cdd:smart00038 80 IPRKTWYSGKSK-HVWFGETMNgGFKFSYGDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966919056 1784 LGSNDEEMSYDNN--PFIKALYDGCASRKGY-EKTVIEINTPKIDQVPIVDVMINDFGDQNQKFGFEVGPVCFL 1854
Cdd:smart00038 159 RGSNDVELSAEGNskFTYEVLEDGCQKRTGKwGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
38-229 |
2.49e-57 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 196.42 E-value: 2.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 38 PVDVLKALDFHNSPEGISKTTGFCtnrknskGSDTAYRVSKQAQLSAPTKQLFPGGpFPEDFSILFTVKPKKGIQSFLLS 117
Cdd:smart00210 1 GQDLLQVFDLPSLSFAIRQVVGPE-------PGSPAYRLGDPALVPQPTRDLFPSG-LPEDFSLLTTFRQTPKSRGVLFA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 118 IYNEHGIQQIGVEV-GRSPVFLFEDHtGKPAPEDYPLFRTVNIADGKWHRVAISVEKKTVTMIVDCKKKTTKPLDRSERA 196
Cdd:smart00210 73 IYDAQNVRQFGLEVdGRANTLLLRYQ-GVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQP 151
|
170 180 190
....*....|....*....|....*....|...
gi 966919056 197 IVDTNGITVFGTRILDEEVFEGDIQQFLITGDP 229
Cdd:smart00210 152 PIDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
651-952 |
3.80e-32 |
|
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: 131.95 E-value: 3.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 651 FDGLPGLPGDkGHRGERGPQGPpgppgddgmRGEDGEIGPRGLPGEAGPRGLLGPRGTPGAPGQPGMAGVDGPPGPKGnm 730
Cdd:NF038329 107 DEGLQQLKGD-GEKGEPGPAGP---------AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 731 gpqgepgppgqqgnpgpqglpgpqgpigppgEKGPQGKPGLAGLPGADGPPGHPGKEGQSGEKGALgppgpqgpigypgp 810
Cdd:NF038329 175 -------------------------------PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA-------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 811 rGVKGADGVRGLKGSKGEKGEDGfPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKlgvpg 890
Cdd:NF038329 210 -GPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP----- 282
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966919056 891 lPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPK 952
Cdd:NF038329 283 -VGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
628-892 |
5.56e-30 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 125.40 E-value: 5.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 628 RGRPGADGGRGMPGEPGSKGDRGFDGLPGLPGDKGHRGERGPQGPPgppgddgmrGEDGEIGPRGLPGEAGPRGLLGPRG 707
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA---------GPQGEAGPQGPAGKDGEAGAKGPAG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 708 TPGAPGQPGMAGVDGPPGPKGNMGPQGEPGPPGQQGNPGPQGLPgpqgpigppgEKGPQGKPGLAGLPGADGPPGHPGKE 787
Cdd:NF038329 190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG----------QQGPDGDPGPTGEDGPQGPDGPAGKD 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 788 GQsgekgalgppgpqgpigypgprgvKGADGVRGLKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGR 867
Cdd:NF038329 260 GP------------------------RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK 315
|
250 260
....*....|....*....|....*
gi 966919056 868 AGPTGDPGPSGQAGEKGKLGVPGLP 892
Cdd:NF038329 316 DGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
840-1092 |
4.18e-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: 113.85 E-value: 4.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 840 DMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKlgvPGLPGYPGRQGPKGSTGFPGFPGANGEKGAR 919
Cdd:NF038329 112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE---RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 920 GVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPpgergpqgpqgpvgfpgpkgppgppgkdglpghpGQ 999
Cdd:NF038329 189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------------------------------GQ 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1000 RGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHPGPPGPPGEQGLPGAAGKEGAKGDPGPQGISGKDGPAGLRGFPG 1079
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG 314
|
250
....*....|...
gi 966919056 1080 ERGLPGAQGAPGL 1092
Cdd:NF038329 315 KDGKDGQPGKDGL 327
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
878-1220 |
1.62e-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: 105.76 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 878 GQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTsgg 957
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 958 dgppgppgergpqgpqgpvgfpgpkgppgppgkdglpghPGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGErghpg 1037
Cdd:NF038329 194 ---------------------------------------QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP----- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1038 ppgppgeqglpGAAGKEGAKGDPGPQGISGKDGPAGLRGFPGERGlpgaqgapglkggegpqgppgpvgspgERGSAGTA 1117
Cdd:NF038329 230 -----------AGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG---------------------------DRGEAGPD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1118 GPiglpgrpgpqgppgpageKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGdkgengp 1197
Cdd:NF038329 272 GP------------------DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG------- 326
|
330 340
....*....|....*....|...
gi 966919056 1198 pgppglqgpvgAPGIAGGDGEPG 1220
Cdd:NF038329 327 -----------LPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1304-1532 |
7.36e-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: 100.75 E-value: 7.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1304 GEPGEAGNPGPPGEAGVGGPKGERGEKGEAGPPGAAGPPGAKGPPGDDGPKGnpgpvgfpgDPGPPGEPGPAGQDGVGGD 1383
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------EAGPQGPAGKDGEAGAKGP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1384 KGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGAAGAEGRQGEKGaKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPG 1463
Cdd:NF038329 188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966919056 1464 PVGEQGLPGAAGQDGPPGPMGPPGLPGLKGDPGSKGEKGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPG 1532
Cdd:NF038329 267 EAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
578-864 |
8.58e-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: 100.75 E-value: 8.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 578 GPPGPMGLTGRPGPVGGPGSAGAKGESGDPGPQGPRGVQGPPGPTGKPGKRGRPGADGGRGMPGEPGSKGDRGFDGLPGL 657
Cdd:NF038329 135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGP 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 658 PGDKGHRGERGPQGPPGppgddgmrgeDGEIGPRGLPGEAGPRGLLGPRGTPGAPGQPGMAGVDGPPGPKGnmgpqgepg 737
Cdd:NF038329 215 DGEAGPAGEDGPAGPAG----------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG--------- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 738 ppgqqgnpgpqglpgpqgpigppgEKGPQGKPGLAGLPGADGPPGHPGKEGQsgekgalgppgpqgpigypgprgvkgaD 817
Cdd:NF038329 276 ------------------------KDGERGPVGPAGKDGQNGKDGLPGKDGK---------------------------D 304
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 966919056 818 GVRGLKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGP 864
Cdd:NF038329 305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKP 351
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
926-1232 |
6.70e-21 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 98.05 E-value: 6.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 926 GPRGQRGPTGPRGSRGARGPTGKpgpkgtsggdgppgppgergpqgpqgpvgfpgpkgppgppgkdglpghpgqRGETGF 1005
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGD---------------------------------------------------RGETGP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1006 QGKtgppgpggvvgpqgpTGETGPIGERGHpgppgppgeqglpgaAGKEGAKGDPGPQGISGKDGPAGLRGFPGERGLPG 1085
Cdd:NF038329 146 AGP---------------AGPPGPQGERGE---------------KGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1086 AQGAPGLKGGEGPQGPPGPVGSPGERGSAGTAGPiglpgrpGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPA 1165
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP-------AGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966919056 1166 GPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPRGQQGMFGQKG 1232
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1153-1520 |
3.50e-19 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 92.66 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1153 DGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPpgppglqgpvgaPGIAGGDGEPGPRGQQGMFGQKG 1232
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE------------KGPAGPQGEAGPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1233 DEgargfpgppgpiglqglpGPPGEKGENgdvgpmgppgppgprgpqgpngadgpqgppgsvgsvggvgekGEPGEAGNP 1312
Cdd:NF038329 184 AK------------------GPAGEKGPQ------------------------------------------GPRGETGPA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1313 GPPGEAGVGGPKGERGEKGEagppgaagppgakgppgdDGPKGnpgpvgfpgdpgppgePGPAGQDGVGGDKGEDgdpgq 1392
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGE------------------DGPAG----------------PAGDGQQGPDGDPGPT----- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1393 pgppgpsgeagppgppgkrgppgaaGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPG 1472
Cdd:NF038329 245 -------------------------GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPG 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 966919056 1473 AAGQDGPPGPMgppglpglkGDPGSKGEKGHPGLIGLIGPPGEQGEKG 1520
Cdd:NF038329 300 KDGKDGQNGKD---------GLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1142-1476 |
5.36e-18 |
|
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: 88.81 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1142 GEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGP 1221
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1222 RGQQGMFGQKGDEGARGFPGPPGPIGLQGLPGPPGEkgengdvgpmgppgppgprgpqgpnGADGPQGppgsvgsvggvg 1301
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------------------------GQQGPDG------------ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1302 EKGEPGEAGNPGPPGEAGVGGPKGERGEKGEagppgaagppgakgppgdDGPKGNpgpvgfpgdpgppgepgpagqdgvg 1381
Cdd:NF038329 240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP------------------DGPDGK------------------------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1382 gdkgedgdpgqpgppgpsgeagppgppgkrgppgaAGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGI 1461
Cdd:NF038329 277 -----------------------------------DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321
|
330
....*....|....*
gi 966919056 1462 PGPVGEQGLPGAAGQ 1476
Cdd:NF038329 322 PGKDGLPGKDGKDGQ 336
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1110-1331 |
1.30e-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: 87.65 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1110 ERGSAGTAGPIGLPGRPGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSK 1189
Cdd:NF038329 118 EKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1190 GDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPRGqQGMFGQKGDEGARGFPGPPGPIGLQGLPGPPGEKGENGDVGPMGP 1269
Cdd:NF038329 198 GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966919056 1270 PGPPGPRGPQGPNGADGPQGPPGSVGSVGGVGEKGEPGEAGNPGPPGEAGVGGPKGERGEKG 1331
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1378-1532 |
5.34e-16 |
|
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: 82.65 E-value: 5.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1378 DGVGGDKGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGAAGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEG 1457
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1458 LRGIPGPVGEQGLPGAAGQDGPPGPMGPPGLPGLKGDP-----GSKGEKGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPG 1532
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1416-1577 |
1.04e-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: 81.88 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1416 AAGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPGAAGQDGPPGPMGPPGLPGLKGDP 1495
Cdd:NF038329 145 PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGED 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1496 GSKGE--KGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPGAKGDGGIPGPAGPLGPPGPPGLPGPQGPKGNKGSTGPAGQK 1573
Cdd:NF038329 225 GPAGPagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKD 304
|
....
gi 966919056 1574 GDSG 1577
Cdd:NF038329 305 GQNG 308
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
709-951 |
5.03e-09 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 60.81 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 709 PGAPGQPGMAGVDGPPGPKGNMGPQGEPGPPGQQGNPGPQGLPGPQGPIGPPGEKGPQGKPGLAGLPGADGPPGHPGKEG 788
Cdd:COG5164 3 LYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 789 QSGEKGALGPPGPQGPIGYPGPRGVKGADGVRGLKGSKGEKGEDGfPGFKGDMGLKGDRGEV----GQIGPRGEDGPEGP 864
Cdd:COG5164 83 PAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-PPSGGSTTPPGDGGSTppgpGSTGPGGSTTPPGD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 865 KGRAGPTGDPGPSGQAGEKGKlGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKP-------GPRGQRGPTGPR 937
Cdd:COG5164 162 GGSTTPPGPGGSTTPPDDGGS-TTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPddrggktGPKDQRPKTNPI 240
|
250
....*....|....
gi 966919056 938 GSRGARGPTGKPGP 951
Cdd:COG5164 241 ERRGPERPEAAALP 254
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
469-718 |
6.44e-09 |
|
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: 60.30 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 469 GAYGEKGQKGEPAVVEPgMLVEGPPGPAGPAGIMGPPGLQGPTGPPGDPGDRGPPGRPGLPGADGLPGPPGTmlmlPFRY 548
Cdd:NF038329 135 GPRGDRGETGPAGPAGP-PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE----QGPA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 549 GGDGSKGPTISAQEAQAQAILQQARIALRGPPGPMGLTGRPGPVGGPGSAGAKGESGDPGPQGPRGVQGPPGPTgkpgkr 628
Cdd:NF038329 210 GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV------ 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 629 GRPGADGGRGMPGEPGSKGDRGFDGLPGLPGDkghrgergpqgppgppgddgmRGEDGEIGPRGLPGEAGPRGLLGPRG- 707
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK---------------------DGKDGQPGKDGLPGKDGKDGQPGKPAp 342
|
250
....*....|..
gi 966919056 708 -TPGAPGQPGMA 718
Cdd:NF038329 343 kTPEVPQKPDTA 354
|
|
| LamG |
smart00282 |
Laminin G domain; |
100-227 |
1.85e-08 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 54.65 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 100 SILFTVKP--KKGIqsfLLSIYNEHGIQQIGVE-VGRSPVFLFEDHTGKPAPEdyplFRTVNIADGKWHRVAISVEKKTV 176
Cdd:smart00282 1 SISFSFRTtsPNGL---LLYAGSKGGGDYLALElRDGRLVLRYDLGSGPARLT----SDPTPLNDGQWHRVAVERNGRSV 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 966919056 177 TMIVDCKKKTTKPLDRSERaIVDTNGITVFG--------TRILDEEVFEGDIQQFLITG 227
Cdd:smart00282 74 TLSVDGGNRVSGESPGGLT-ILNLDGPLYLGglpedlklPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
73-225 |
1.07e-07 |
|
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: 53.19 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 73 AYRVSKQAQLSAPTKQLFPggpfpEDFSILFTVKPKK--GIqsfLLSIYNEHGIQQIGVE-VGRSPVFLFEDHTGKPape 149
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPR-----TRLSISFSFRTTSpnGL---LLYAGSQNGGDFLALElEDGRLVLRYDLGSGSL--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 150 dypLFRTVN-IADGKWHRVAISVEKKTVTMIVDCKKKTTKPLDRSErAIVDTNGITVFGTRILDEEV--------FEGDI 220
Cdd:cd00110 70 ---VLSSKTpLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGS-ALLNLDGPLYLGGLPEDLKSpglpvspgFVGCI 145
|
....*
gi 966919056 221 QQFLI 225
Cdd:cd00110 146 RDLKV 150
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
893-949 |
2.37e-07 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 49.03 E-value: 2.37e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 966919056 893 GYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKP 949
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1427-1624 |
6.98e-07 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 53.76 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1427 GAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPGAAGQDgppgpmgppglpglkgdpgskgekghpgl 1506
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ----------------------------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1507 igliGPPGEQGEKGDRGLPGTQGSPGAKgdggipgpagplgppgppglpGPQGPKGNKGSTGPAGQKGDSGLPGPPGPPG 1586
Cdd:NF038329 168 ----GEAGPQGPAGKDGEAGAKGPAGEK---------------------GPQGPRGETGPAGEQGPAGPAGPDGEAGPAG 222
|
170 180 190
....*....|....*....|....*....|....*...
gi 966919056 1587 PPGEVIQPLPILSSKKTRRHTEGMQADADDNILDYSDG 1624
Cdd:NF038329 223 EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
863-919 |
1.21e-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: 47.10 E-value: 1.21e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 966919056 863 GPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGAR 919
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
899-952 |
1.47e-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: 1.47e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 966919056 899 GPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPK 952
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
890-945 |
4.33e-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: 4.33e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 966919056 890 GLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGP 945
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
884-940 |
4.96e-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: 4.96e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 966919056 884 GKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSR 940
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
830-1090 |
8.76e-06 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 50.41 E-value: 8.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 830 GEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGF 909
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 910 PGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPPGERGPQGPQGPVGFPGPKGPPGPPG 989
Cdd:COG5164 87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 990 KDGLPghpGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHPGPPGPPGEQGLPGAAGKEGAKGDPGPQGISGKD 1069
Cdd:COG5164 167 PPGPG---GSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERR 243
|
250 260
....*....|....*....|.
gi 966919056 1070 GPAGLRGFPGERGLPGAQGAP 1090
Cdd:COG5164 244 GPERPEAAALPAELTALEAEN 264
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1430-1476 |
9.30e-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: 9.30e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 966919056 1430 GEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPGAAGQ 1476
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
|
|
| GGGWT_bact |
NF040941 |
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ... |
1655-1694 |
1.07e-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: 44.09 E-value: 1.07e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 966919056 1655 TCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTSGG 1694
Cdd:NF040941 1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTTDG 40
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
851-905 |
1.20e-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: 44.41 E-value: 1.20e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 966919056 851 GQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTG 905
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
875-931 |
1.52e-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: 44.02 E-value: 1.52e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 966919056 875 GPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQR 931
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
842-896 |
4.02e-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: 4.02e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 966919056 842 GLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPG 896
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
686-728 |
8.99e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 41.71 E-value: 8.99e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 966919056 686 GEIGPRGLPGEAGPRGLLGPRGTPGAPGQPGMAGVDGPPGPKG 728
Cdd:pfam01391 10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
827-882 |
1.96e-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: 1.96e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 966919056 827 GEKGEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGE 882
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1148-1194 |
2.38e-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: 40.55 E-value: 2.38e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 966919056 1148 GPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGE 1194
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1135-1183 |
2.93e-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: 40.55 E-value: 2.93e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 966919056 1135 AGEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEP 1183
Cdd:pfam01391 9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
998-1222 |
3.32e-04 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 45.41 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 998 GQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGErghpgppgppgeqglPGAAGKEGAKGDPGPQGISGKDGPAGLRGF 1077
Cdd:COG5164 16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQN---------------QGSTTPAGNTGGTRPAGNQGATGPAQNQGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1078 PGERGLPGAQGAPGLKGGEGPQGPPGPVGSPGERGSAGTA---GPIGLPGRPGPQGPPGPAGEKGAPGEKGPQGPAGRDG 1154
Cdd:COG5164 81 TTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPddgGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966919056 1155 VQGPVGLPGPAGPAGSPGEDG-----DKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPR 1222
Cdd:COG5164 161 DGGSTTPPGPGGSTTPPDDGGsttppNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQ 233
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
905-954 |
3.46e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 40.17 E-value: 3.46e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 966919056 905 GFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGT 954
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
836-892 |
3.78e-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: 40.17 E-value: 3.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 966919056 836 GFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLP 892
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1415-1465 |
5.03e-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: 5.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 966919056 1415 GAAGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPV 1465
Cdd:pfam01391 7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
855-951 |
6.95e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.59 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 855 PRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPT 934
Cdd:PRK07764 615 PAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA 694
|
90
....*....|....*..
gi 966919056 935 GPRGSRGARGPTGKPGP 951
Cdd:PRK07764 695 GAAPAQPAPAPAATPPA 711
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
156-207 |
9.07e-04 |
|
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: 41.25 E-value: 9.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 966919056 156 TVNIADGKWHRVAISVEKKTVTMIVDCKKKTTKPLDrSERAIVDTNGITVFG 207
Cdd:pfam02210 47 GKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP-GESLLLNLNGPLYLG 97
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
643-899 |
9.42e-04 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 43.87 E-value: 9.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 643 PGSKGDRGFDGLPGLPGDKGHRGERGPQGPPGPPGDDgmrGEDGEIGPRGLPGEAGPRGLLGPRGTPGAPGQPGMAGVDG 722
Cdd:COG5164 6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNT---GGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 723 PPGPKGNMGPQGEPGPPGQQGNPGPQGLPGPQGPIGPPGEKGPQGKPGLAGLPGADGPPGHPGKEGQSGEKGALGPPGPQ 802
Cdd:COG5164 83 PAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 803 GPIGYPGPRGVKGADGVRGlKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQIGPRGE-DGPEGPKGRAGPTGDPGPSGQAG 881
Cdd:COG5164 163 GSTTPPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKgNPPDDRGGKTGPKDQRPKTNPIE 241
|
250
....*....|....*...
gi 966919056 882 EKGKLGVPGLPGYPGRQG 899
Cdd:COG5164 242 RRGPERPEAAALPAELTA 259
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
778-950 |
1.23e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 43.42 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 778 DGPPGHPGKEGQSGEKGALGPPGPQGPIGYPGPRGVKGADGV---RGLKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQIG 854
Cdd:PHA03169 89 QGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESpasHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQ 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 855 PRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGyPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPR----GQ 930
Cdd:PHA03169 169 PSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSP-PDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEregpPF 247
|
170 180
....*....|....*....|
gi 966919056 931 RGPTGPRGSRGARGPTGKPG 950
Cdd:PHA03169 248 PGHRSHSYTVVGWKPSTRPG 267
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1132-1173 |
7.17e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.32 E-value: 7.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 966919056 1132 PGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGE 1173
Cdd:pfam01391 15 PGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
1139-1356 |
7.40e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 41.17 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1139 GAPGEKGPQGPAGRDGVQGPVGLPG---PAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGG 1215
Cdd:COG5164 10 GPSDPGGVTTPAGSQGSTKPAQNQGstrPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919056 1216 DgepGPRGQQGMFGQKGDEGARGFPGPPGPIGLQGLPGPPGEKGENGDVGPMGPPGPPGPRGPQGPNGADGPQGPPGSVG 1295
Cdd:COG5164 90 T---RPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966919056 1296 SVGGVGEKGEPGEAGNPGPP--GEAGVGGPKGERGEKGEAGPPGAAGPPGAKGPPGDDGPKGN 1356
Cdd:COG5164 167 PPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTG 229
|
|
| |
