|
Name |
Accession |
Description |
Interval |
E-value |
| COLFI |
pfam01410 |
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1575-1804 |
2.31e-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: 403.65 E-value: 2.31e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1575 GMEEIFGSLNSLKQDIEHMKFPMGTQTNPARTCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTSgGETCIYPDKK 1654
Cdd:pfam01410 1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1655 SEGvRISSWPKEKPGSWFSEFKRGKL-LSY-LDVEGNSINMVQMTFLKLLTASARQNFTYHCHQSAAWYDVSSGSYDKAL 1732
Cdd:pfam01410 80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966919058 1733 RFLGSNDEEMSYD--NNPFIKALYDGCASRKGY-EKTVIEINTPKIDQVPIVDVMINDFGDQNQKFGFEVGPVCF 1804
Cdd:pfam01410 159 LLQGSNDEEIRAEgnSRFTYTVLEDGCTKRTGQwGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
|
|
| COLFI |
smart00038 |
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1576-1805 |
3.15e-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: 338.68 E-value: 3.15e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1576 MEEIFGSLNSLKQDIEHMKFPMGTQTNPARTCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTsGGETCIYPDKKS 1655
Cdd:smart00038 1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFE-TGETCVSPSPSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1656 EGVRISSWPKEKpGSWFSEFKR-GKLLSYLDVEGNSINMVQMTFLKLLTASARQNFTYHCHQSAAWYDVSSGSYDKALRF 1734
Cdd:smart00038 80 IPRKTWYSGKSK-HVWFGETMNgGFKFSYGDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966919058 1735 LGSNDEEMSYDNN--PFIKALYDGCASRKGY-EKTVIEINTPKIDQVPIVDVMINDFGDQNQKFGFEVGPVCFL 1805
Cdd:smart00038 159 RGSNDVELSAEGNskFTYEVLEDGCQKRTGKwGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
38-229 |
2.80e-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: 2.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 38 PVDVLKALDFHNSPEGISKTTGFCtnrknskGSDTAYRVSKQAQLSAPTKQLFPGGpFPEDFSILFTVKPKKGIQSFLLS 117
Cdd:smart00210 1 GQDLLQVFDLPSLSFAIRQVVGPE-------PGSPAYRLGDPALVPQPTRDLFPSG-LPEDFSLLTTFRQTPKSRGVLFA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 118 IYNEHGIQQIGVEV-GRSPVFLFEDHtGKPAPEDYPLFRTVNIADGKWHRVAISVEKKTVTMIVDCKKKTTKPLDRSERA 196
Cdd:smart00210 73 IYDAQNVRQFGLEVdGRANTLLLRYQ-GVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQP 151
|
170 180 190
....*....|....*....|....*....|...
gi 966919058 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 ... |
602-903 |
5.38e-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: 131.57 E-value: 5.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 602 FDGLPGLPGDkGHRGERGPQGPpgppgddgmRGEDGEIGPRGLPGEAGPRGLLGPRGTPGAPGQPGMAGVDGPPGPKGnm 681
Cdd:NF038329 107 DEGLQQLKGD-GEKGEPGPAGP---------AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 682 gpqgepgppgqqgnpgpqglpgpqgpigppgEKGPQGKPGLAGLPGADGPPGHPGKEGQSGEKGALgppgpqgpigypgp 761
Cdd:NF038329 175 -------------------------------PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA-------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 762 rGVKGADGVRGLKGSKGEKGEDGfPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKlgvpg 841
Cdd:NF038329 210 -GPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP----- 282
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966919058 842 lPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPK 903
Cdd:NF038329 283 -VGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
579-843 |
7.79e-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: 125.02 E-value: 7.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 579 RGRPGADGGRGMPGEPGSKGDRGFDGLPGLPGDKGHRGERGPQGPPgppgddgmrGEDGEIGPRGLPGEAGPRGLLGPRG 658
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA---------GPQGEAGPQGPAGKDGEAGAKGPAG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 659 TPGAPGQPGMAGVDGPPGPKGNMGPQGEPGPPGQQGNPGPQGLPgpqgpigppgEKGPQGKPGLAGLPGADGPPGHPGKE 738
Cdd:NF038329 190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG----------QQGPDGDPGPTGEDGPQGPDGPAGKD 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 739 GQsgekgalgppgpqgpigypgprgvKGADGVRGLKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGR 818
Cdd:NF038329 260 GP------------------------RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK 315
|
250 260
....*....|....*....|....*
gi 966919058 819 AGPTGDPGPSGQAGEKGKLGVPGLP 843
Cdd:NF038329 316 DGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
791-1043 |
5.37e-26 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 113.46 E-value: 5.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 791 DMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKlgvPGLPGYPGRQGPKGSTGFPGFPGANGEKGAR 870
Cdd:NF038329 112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE---RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 871 GVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPpgergpqgpqgpvgfpgpkgppgppgkdglpghpGQ 950
Cdd:NF038329 189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------------------------------GQ 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 951 RGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHPGPPGPPGEQGLPGAAGKEGAKGDPGPQGISGKDGPAGLRGFPG 1030
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG 314
|
250
....*....|...
gi 966919058 1031 ERGLPGAQGAPGL 1043
Cdd:NF038329 315 KDGKDGQPGKDGL 327
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
829-1171 |
2.22e-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: 105.37 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 829 GQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTsgg 908
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 909 dgppgppgergpqgpqgpvgfpgpkgppgppgkdglpghPGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGErghpg 988
Cdd:NF038329 194 ---------------------------------------QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP----- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 989 ppgppgeqglpGAAGKEGAKGDPGPQGISGKDGPAGLRGFPGERGlpgaqgapglkggegpqgppgpvgspgERGSAGTA 1068
Cdd:NF038329 230 -----------AGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG---------------------------DRGEAGPD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1069 GPiglpgrpgpqgppgpageKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGdkgengp 1148
Cdd:NF038329 272 GP------------------DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG------- 326
|
330 340
....*....|....*....|...
gi 966919058 1149 pgppglqgpvgAPGIAGGDGEPG 1171
Cdd:NF038329 327 -----------LPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1255-1483 |
8.54e-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: 8.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1255 GEPGEAGNPGPPGEAGVGGPKGERGEKGEAGPPGAAGPPGAKGPPGDDGPKGnpgpvgfpgDPGPPGEPGPAGQDGVGGD 1334
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------EAGPQGPAGKDGEAGAKGP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1335 KGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGAAGAEGRQGEKGaKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPG 1414
Cdd:NF038329 188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966919058 1415 PVGEQGLPGAAGQDGPPGPMGPPGLPGLKGDPGSKGEKGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPG 1483
Cdd:NF038329 267 EAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
529-815 |
1.07e-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: 100.36 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 529 GPPGPMGLTGRPGPVGGPGSAGAKGESGDPGPQGPRGVQGPPGPTGKPGKRGRPGADGGRGMPGEPGSKGDRGFDGLPGL 608
Cdd:NF038329 135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGP 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 609 PGDKGHRGERGPQGPPGppgddgmrgeDGEIGPRGLPGEAGPRGLLGPRGTPGAPGQPGMAGVDGPPGPKGnmgpqgepg 688
Cdd:NF038329 215 DGEAGPAGEDGPAGPAG----------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG--------- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 689 ppgqqgnpgpqglpgpqgpigppgEKGPQGKPGLAGLPGADGPPGHPGKEGQsgekgalgppgpqgpigypgprgvkgaD 768
Cdd:NF038329 276 ------------------------KDGERGPVGPAGKDGQNGKDGLPGKDGK---------------------------D 304
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 966919058 769 GVRGLKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGP 815
Cdd:NF038329 305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKP 351
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
877-1183 |
8.51e-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: 97.67 E-value: 8.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 877 GPRGQRGPTGPRGSRGARGPTGKpgpkgtsggdgppgppgergpqgpqgpvgfpgpkgppgppgkdglpghpgqRGETGF 956
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGD---------------------------------------------------RGETGP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 957 QGKtgppgpggvvgpqgpTGETGPIGERGHpgppgppgeqglpgaAGKEGAKGDPGPQGISGKDGPAGLRGFPGERGLPG 1036
Cdd:NF038329 146 AGP---------------AGPPGPQGERGE---------------KGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1037 AQGAPGLKGGEGPQGPPGPVGSPGERGSAGTAGPiglpgrpGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPA 1116
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP-------AGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966919058 1117 GPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPRGQQGMFGQKG 1183
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1104-1471 |
5.04e-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: 92.28 E-value: 5.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1104 DGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPpgppglqgpvgaPGIAGGDGEPGPRGQQGMFGQKG 1183
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE------------KGPAGPQGEAGPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1184 DEgargfpgppgpiglqglpGPPGEKGENgdvgpmgppgppgprgpqgpngadgpqgppgsvgsvggvgekGEPGEAGNP 1263
Cdd:NF038329 184 AK------------------GPAGEKGPQ------------------------------------------GPRGETGPA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1264 GPPGEAGVGGPKGERGEKGEagppgaagppgakgppgdDGPKGnpgpvgfpgdpgppgePGPAGQDGVGGDKGEDgdpgq 1343
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGE------------------DGPAG----------------PAGDGQQGPDGDPGPT----- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1344 pgppgpsgeagppgppgkrgppgaaGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPG 1423
Cdd:NF038329 245 -------------------------GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPG 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 966919058 1424 AAGQDGPPGPMgppglpglkGDPGSKGEKGHPGLIGLIGPPGEQGEKG 1471
Cdd:NF038329 300 KDGKDGQNGKD---------GLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1093-1427 |
7.16e-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: 88.42 E-value: 7.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1093 GEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGP 1172
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1173 RGQQGMFGQKGDEGARGFPGPPGPIGLQGLPGPPGEkgengdvgpmgppgppgprgpqgpnGADGPQGppgsvgsvggvg 1252
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------------------------GQQGPDG------------ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1253 EKGEPGEAGNPGPPGEAGVGGPKGERGEKGEagppgaagppgakgppgdDGPKGNpgpvgfpgdpgppgepgpagqdgvg 1332
Cdd:NF038329 240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP------------------DGPDGK------------------------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1333 gdkgedgdpgqpgppgpsgeagppgppgkrgppgaAGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGI 1412
Cdd:NF038329 277 -----------------------------------DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321
|
330
....*....|....*
gi 966919058 1413 PGPVGEQGLPGAAGQ 1427
Cdd:NF038329 322 PGKDGLPGKDGKDGQ 336
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1061-1282 |
1.44e-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: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1061 ERGSAGTAGPIGLPGRPGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSK 1140
Cdd:NF038329 118 EKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1141 GDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPRGqQGMFGQKGDEGARGFPGPPGPIGLQGLPGPPGEKGENGDVGPMGP 1220
Cdd:NF038329 198 GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966919058 1221 PGPPGPRGPQGPNGADGPQGPPGSVGSVGGVGEKGEPGEAGNPGPPGEAGVGGPKGERGEKG 1282
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1329-1483 |
5.81e-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: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1329 DGVGGDKGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGAAGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEG 1408
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1409 LRGIPGPVGEQGLPGAAGQDGPPGPMGPPGLPGLKGDP-----GSKGEKGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPG 1483
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1367-1528 |
1.13e-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: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1367 AAGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPGAAGQDGPPGPMGPPGLPGLKGDP 1446
Cdd:NF038329 145 PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGED 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1447 GSKGE--KGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPGAKGDGGIPGPAGPLGPPGPPGLPGPQGPKGNKGSTGPAGQK 1524
Cdd:NF038329 225 GPAGPagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKD 304
|
....
gi 966919058 1525 GDSG 1528
Cdd:NF038329 305 GQNG 308
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
660-902 |
5.05e-09 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 60.81 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 660 PGAPGQPGMAGVDGPPGPKGNMGPQGEPGPPGQQGNPGPQGLPGPQGPIGPPGEKGPQGKPGLAGLPGADGPPGHPGKEG 739
Cdd:COG5164 3 LYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 740 QSGEKGALGPPGPQGPIGYPGPRGVKGADGVRGLKGSKGEKGEDGfPGFKGDMGLKGDRGEV----GQIGPRGEDGPEGP 815
Cdd:COG5164 83 PAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-PPSGGSTTPPGDGGSTppgpGSTGPGGSTTPPGD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 816 KGRAGPTGDPGPSGQAGEKGKlGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKP-------GPRGQRGPTGPR 888
Cdd:COG5164 162 GGSTTPPGPGGSTTPPDDGGS-TTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPddrggktGPKDQRPKTNPI 240
|
250
....*....|....
gi 966919058 889 GSRGARGPTGKPGP 902
Cdd:COG5164 241 ERRGPERPEAAALP 254
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
420-669 |
7.49e-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: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 420 GAYGEKGQKGEPAVVEPgMLVEGPPGPAGPAGIMGPPGLQGPTGPPGDPGDRGPPGRPGLPGADGLPGPPGTmlmlPFRY 499
Cdd:NF038329 135 GPRGDRGETGPAGPAGP-PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE----QGPA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 500 GGDGSKGPTISAQEAQAQAILQQARIALRGPPGPMGLTGRPGPVGGPGSAGAKGESGDPGPQGPRGVQGPPGPTgkpgkr 579
Cdd:NF038329 210 GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV------ 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 580 GRPGADGGRGMPGEPGSKGDRGFDGLPGLPGDkghrgergpqgppgppgddgmRGEDGEIGPRGLPGEAGPRGLLGPRG- 658
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK---------------------DGKDGQPGKDGLPGKDGKDGQPGKPAp 342
|
250
....*....|..
gi 966919058 659 -TPGAPGQPGMA 669
Cdd:NF038329 343 kTPEVPQKPDTA 354
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
73-225 |
1.04e-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: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 73 AYRVSKQAQLSAPTKQLFPggpfpEDFSILFTVKPKK--GIqsfLLSIYNEHGIQQIGVE-VGRSPVFLFEDHTGKPape 149
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPR-----TRLSISFSFRTTSpnGL---LLYAGSQNGGDFLALElEDGRLVLRYDLGSGSL--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 150 dypLFRTVN-IADGKWHRVAISVEKKTVTMIVDCKKKTTKPLDRSErAIVDTNGITVFGTRILDEEV--------FEGDI 220
Cdd:cd00110 70 ---VLSSKTpLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGS-ALLNLDGPLYLGGLPEDLKSpglpvspgFVGCI 145
|
....*
gi 966919058 221 QQFLI 225
Cdd:cd00110 146 RDLKV 150
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
844-900 |
2.95e-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: 48.64 E-value: 2.95e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 966919058 844 GYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKP 900
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1378-1575 |
7.77e-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: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1378 GAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPGAAGQDgppgpmgppglpglkgdpgskgekghpgl 1457
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ----------------------------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1458 igliGPPGEQGEKGDRGLPGTQGSPGAKgdggipgpagplgppgppglpGPQGPKGNKGSTGPAGQKGDSGLPGPPGPPG 1537
Cdd:NF038329 168 ----GEAGPQGPAGKDGEAGAKGPAGEK---------------------GPQGPRGETGPAGEQGPAGPAGPDGEAGPAG 222
|
170 180 190
....*....|....*....|....*....|....*...
gi 966919058 1538 PPGEVIQPLPILSSKKTRRHTEGMQADADDNILDYSDG 1575
Cdd:NF038329 223 EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
781-1041 |
8.65e-06 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 50.41 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 781 GEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGF 860
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 861 PGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPPGERGPQGPQGPVGFPGPKGPPGPPG 940
Cdd:COG5164 87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 941 KDGLPghpGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHPGPPGPPGEQGLPGAAGKEGAKGDPGPQGISGKD 1020
Cdd:COG5164 167 PPGPG---GSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERR 243
|
250 260
....*....|....*....|.
gi 966919058 1021 GPAGLRGFPGERGLPGAQGAP 1041
Cdd:COG5164 244 GPERPEAAALPAELTALEAEN 264
|
|
| GGGWT_bact |
NF040941 |
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ... |
1606-1645 |
1.14e-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: 1.14e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 966919058 1606 TCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTSGG 1645
Cdd:NF040941 1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTTDG 40
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1381-1427 |
1.22e-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: 1.22e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 966919058 1381 GEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPGAAGQ 1427
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1099-1145 |
2.90e-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: 2.90e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 966919058 1099 GPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGE 1145
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
949-1173 |
3.36e-04 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 45.41 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 949 GQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGErghpgppgppgeqglPGAAGKEGAKGDPGPQGISGKDGPAGLRGF 1028
Cdd:COG5164 16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQN---------------QGSTTPAGNTGGTRPAGNQGATGPAQNQGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1029 PGERGLPGAQGAPGLKGGEGPQGPPGPVGSPGERGSAGTA---GPIGLPGRPGPQGPPGPAGEKGAPGEKGPQGPAGRDG 1105
Cdd:COG5164 81 TTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPddgGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966919058 1106 VQGPVGLPGPAGPAGSPGEDG-----DKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPR 1173
Cdd:COG5164 161 DGGSTTPPGPGGSTTPPDDGGsttppNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQ 233
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
806-902 |
6.98e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.59 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 806 PRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPT 885
Cdd:PRK07764 615 PAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA 694
|
90
....*....|....*..
gi 966919058 886 GPRGSRGARGPTGKPGP 902
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 |
8.82e-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: 8.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 966919058 156 TVNIADGKWHRVAISVEKKTVTMIVDCKKKTTKPLDrSERAIVDTNGITVFG 207
Cdd:pfam02210 47 GKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP-GESLLLNLNGPLYLG 97
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
1090-1307 |
6.77e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 41.17 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1090 GAPGEKGPQGPAGRDGVQGPVGLPG---PAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGG 1166
Cdd:COG5164 10 GPSDPGGVTTPAGSQGSTKPAQNQGstrPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1167 DgepGPRGQQGMFGQKGDEGARGFPGPPGPIGLQGLPGPPGEKGENGDVGPMGPPGPPGPRGPQGPNGADGPQGPPGSVG 1246
Cdd:COG5164 90 T---RPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966919058 1247 SVGGVGEKGEPGEAGNPGPP--GEAGVGGPKGERGEKGEAGPPGAAGPPGAKGPPGDDGPKGN 1307
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 ... |
1575-1804 |
2.31e-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: 403.65 E-value: 2.31e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1575 GMEEIFGSLNSLKQDIEHMKFPMGTQTNPARTCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTSgGETCIYPDKK 1654
Cdd:pfam01410 1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1655 SEGvRISSWPKEKPGSWFSEFKRGKL-LSY-LDVEGNSINMVQMTFLKLLTASARQNFTYHCHQSAAWYDVSSGSYDKAL 1732
Cdd:pfam01410 80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966919058 1733 RFLGSNDEEMSYD--NNPFIKALYDGCASRKGY-EKTVIEINTPKIDQVPIVDVMINDFGDQNQKFGFEVGPVCF 1804
Cdd:pfam01410 159 LLQGSNDEEIRAEgnSRFTYTVLEDGCTKRTGQwGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
|
|
| COLFI |
smart00038 |
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1576-1805 |
3.15e-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: 338.68 E-value: 3.15e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1576 MEEIFGSLNSLKQDIEHMKFPMGTQTNPARTCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTsGGETCIYPDKKS 1655
Cdd:smart00038 1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFE-TGETCVSPSPSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1656 EGVRISSWPKEKpGSWFSEFKR-GKLLSYLDVEGNSINMVQMTFLKLLTASARQNFTYHCHQSAAWYDVSSGSYDKALRF 1734
Cdd:smart00038 80 IPRKTWYSGKSK-HVWFGETMNgGFKFSYGDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966919058 1735 LGSNDEEMSYDNN--PFIKALYDGCASRKGY-EKTVIEINTPKIDQVPIVDVMINDFGDQNQKFGFEVGPVCFL 1805
Cdd:smart00038 159 RGSNDVELSAEGNskFTYEVLEDGCQKRTGKwGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
38-229 |
2.80e-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: 2.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 38 PVDVLKALDFHNSPEGISKTTGFCtnrknskGSDTAYRVSKQAQLSAPTKQLFPGGpFPEDFSILFTVKPKKGIQSFLLS 117
Cdd:smart00210 1 GQDLLQVFDLPSLSFAIRQVVGPE-------PGSPAYRLGDPALVPQPTRDLFPSG-LPEDFSLLTTFRQTPKSRGVLFA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 118 IYNEHGIQQIGVEV-GRSPVFLFEDHtGKPAPEDYPLFRTVNIADGKWHRVAISVEKKTVTMIVDCKKKTTKPLDRSERA 196
Cdd:smart00210 73 IYDAQNVRQFGLEVdGRANTLLLRYQ-GVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQP 151
|
170 180 190
....*....|....*....|....*....|...
gi 966919058 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 ... |
602-903 |
5.38e-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: 131.57 E-value: 5.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 602 FDGLPGLPGDkGHRGERGPQGPpgppgddgmRGEDGEIGPRGLPGEAGPRGLLGPRGTPGAPGQPGMAGVDGPPGPKGnm 681
Cdd:NF038329 107 DEGLQQLKGD-GEKGEPGPAGP---------AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 682 gpqgepgppgqqgnpgpqglpgpqgpigppgEKGPQGKPGLAGLPGADGPPGHPGKEGQSGEKGALgppgpqgpigypgp 761
Cdd:NF038329 175 -------------------------------PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA-------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 762 rGVKGADGVRGLKGSKGEKGEDGfPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKlgvpg 841
Cdd:NF038329 210 -GPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP----- 282
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966919058 842 lPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPK 903
Cdd:NF038329 283 -VGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
579-843 |
7.79e-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: 125.02 E-value: 7.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 579 RGRPGADGGRGMPGEPGSKGDRGFDGLPGLPGDKGHRGERGPQGPPgppgddgmrGEDGEIGPRGLPGEAGPRGLLGPRG 658
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA---------GPQGEAGPQGPAGKDGEAGAKGPAG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 659 TPGAPGQPGMAGVDGPPGPKGNMGPQGEPGPPGQQGNPGPQGLPgpqgpigppgEKGPQGKPGLAGLPGADGPPGHPGKE 738
Cdd:NF038329 190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG----------QQGPDGDPGPTGEDGPQGPDGPAGKD 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 739 GQsgekgalgppgpqgpigypgprgvKGADGVRGLKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGR 818
Cdd:NF038329 260 GP------------------------RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK 315
|
250 260
....*....|....*....|....*
gi 966919058 819 AGPTGDPGPSGQAGEKGKLGVPGLP 843
Cdd:NF038329 316 DGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
791-1043 |
5.37e-26 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 113.46 E-value: 5.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 791 DMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKlgvPGLPGYPGRQGPKGSTGFPGFPGANGEKGAR 870
Cdd:NF038329 112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE---RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 871 GVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPpgergpqgpqgpvgfpgpkgppgppgkdglpghpGQ 950
Cdd:NF038329 189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------------------------------GQ 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 951 RGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHPGPPGPPGEQGLPGAAGKEGAKGDPGPQGISGKDGPAGLRGFPG 1030
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG 314
|
250
....*....|...
gi 966919058 1031 ERGLPGAQGAPGL 1043
Cdd:NF038329 315 KDGKDGQPGKDGL 327
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
829-1171 |
2.22e-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: 105.37 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 829 GQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTsgg 908
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 909 dgppgppgergpqgpqgpvgfpgpkgppgppgkdglpghPGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGErghpg 988
Cdd:NF038329 194 ---------------------------------------QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP----- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 989 ppgppgeqglpGAAGKEGAKGDPGPQGISGKDGPAGLRGFPGERGlpgaqgapglkggegpqgppgpvgspgERGSAGTA 1068
Cdd:NF038329 230 -----------AGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG---------------------------DRGEAGPD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1069 GPiglpgrpgpqgppgpageKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGdkgengp 1148
Cdd:NF038329 272 GP------------------DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG------- 326
|
330 340
....*....|....*....|...
gi 966919058 1149 pgppglqgpvgAPGIAGGDGEPG 1171
Cdd:NF038329 327 -----------LPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1255-1483 |
8.54e-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: 8.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1255 GEPGEAGNPGPPGEAGVGGPKGERGEKGEAGPPGAAGPPGAKGPPGDDGPKGnpgpvgfpgDPGPPGEPGPAGQDGVGGD 1334
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------EAGPQGPAGKDGEAGAKGP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1335 KGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGAAGAEGRQGEKGaKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPG 1414
Cdd:NF038329 188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966919058 1415 PVGEQGLPGAAGQDGPPGPMGPPGLPGLKGDPGSKGEKGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPG 1483
Cdd:NF038329 267 EAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
529-815 |
1.07e-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: 100.36 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 529 GPPGPMGLTGRPGPVGGPGSAGAKGESGDPGPQGPRGVQGPPGPTGKPGKRGRPGADGGRGMPGEPGSKGDRGFDGLPGL 608
Cdd:NF038329 135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGP 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 609 PGDKGHRGERGPQGPPGppgddgmrgeDGEIGPRGLPGEAGPRGLLGPRGTPGAPGQPGMAGVDGPPGPKGnmgpqgepg 688
Cdd:NF038329 215 DGEAGPAGEDGPAGPAG----------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG--------- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 689 ppgqqgnpgpqglpgpqgpigppgEKGPQGKPGLAGLPGADGPPGHPGKEGQsgekgalgppgpqgpigypgprgvkgaD 768
Cdd:NF038329 276 ------------------------KDGERGPVGPAGKDGQNGKDGLPGKDGK---------------------------D 304
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 966919058 769 GVRGLKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGP 815
Cdd:NF038329 305 GQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKP 351
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
877-1183 |
8.51e-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: 97.67 E-value: 8.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 877 GPRGQRGPTGPRGSRGARGPTGKpgpkgtsggdgppgppgergpqgpqgpvgfpgpkgppgppgkdglpghpgqRGETGF 956
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGD---------------------------------------------------RGETGP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 957 QGKtgppgpggvvgpqgpTGETGPIGERGHpgppgppgeqglpgaAGKEGAKGDPGPQGISGKDGPAGLRGFPGERGLPG 1036
Cdd:NF038329 146 AGP---------------AGPPGPQGERGE---------------KGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1037 AQGAPGLKGGEGPQGPPGPVGSPGERGSAGTAGPiglpgrpGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPA 1116
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP-------AGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966919058 1117 GPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPRGQQGMFGQKG 1183
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1104-1471 |
5.04e-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: 92.28 E-value: 5.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1104 DGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPpgppglqgpvgaPGIAGGDGEPGPRGQQGMFGQKG 1183
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE------------KGPAGPQGEAGPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1184 DEgargfpgppgpiglqglpGPPGEKGENgdvgpmgppgppgprgpqgpngadgpqgppgsvgsvggvgekGEPGEAGNP 1263
Cdd:NF038329 184 AK------------------GPAGEKGPQ------------------------------------------GPRGETGPA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1264 GPPGEAGVGGPKGERGEKGEagppgaagppgakgppgdDGPKGnpgpvgfpgdpgppgePGPAGQDGVGGDKGEDgdpgq 1343
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGE------------------DGPAG----------------PAGDGQQGPDGDPGPT----- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1344 pgppgpsgeagppgppgkrgppgaaGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPG 1423
Cdd:NF038329 245 -------------------------GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPG 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 966919058 1424 AAGQDGPPGPMgppglpglkGDPGSKGEKGHPGLIGLIGPPGEQGEKG 1471
Cdd:NF038329 300 KDGKDGQNGKD---------GLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1093-1427 |
7.16e-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: 88.42 E-value: 7.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1093 GEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGP 1172
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1173 RGQQGMFGQKGDEGARGFPGPPGPIGLQGLPGPPGEkgengdvgpmgppgppgprgpqgpnGADGPQGppgsvgsvggvg 1252
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------------------------GQQGPDG------------ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1253 EKGEPGEAGNPGPPGEAGVGGPKGERGEKGEagppgaagppgakgppgdDGPKGNpgpvgfpgdpgppgepgpagqdgvg 1332
Cdd:NF038329 240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP------------------DGPDGK------------------------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1333 gdkgedgdpgqpgppgpsgeagppgppgkrgppgaAGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGI 1412
Cdd:NF038329 277 -----------------------------------DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321
|
330
....*....|....*
gi 966919058 1413 PGPVGEQGLPGAAGQ 1427
Cdd:NF038329 322 PGKDGLPGKDGKDGQ 336
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1061-1282 |
1.44e-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: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1061 ERGSAGTAGPIGLPGRPGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSK 1140
Cdd:NF038329 118 EKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1141 GDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPRGqQGMFGQKGDEGARGFPGPPGPIGLQGLPGPPGEKGENGDVGPMGP 1220
Cdd:NF038329 198 GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966919058 1221 PGPPGPRGPQGPNGADGPQGPPGSVGSVGGVGEKGEPGEAGNPGPPGEAGVGGPKGERGEKG 1282
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1329-1483 |
5.81e-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: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1329 DGVGGDKGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGAAGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEG 1408
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1409 LRGIPGPVGEQGLPGAAGQDGPPGPMGPPGLPGLKGDP-----GSKGEKGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPG 1483
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1367-1528 |
1.13e-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: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1367 AAGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPGAAGQDGPPGPMGPPGLPGLKGDP 1446
Cdd:NF038329 145 PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGED 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1447 GSKGE--KGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPGAKGDGGIPGPAGPLGPPGPPGLPGPQGPKGNKGSTGPAGQK 1524
Cdd:NF038329 225 GPAGPagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKD 304
|
....
gi 966919058 1525 GDSG 1528
Cdd:NF038329 305 GQNG 308
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
660-902 |
5.05e-09 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 60.81 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 660 PGAPGQPGMAGVDGPPGPKGNMGPQGEPGPPGQQGNPGPQGLPGPQGPIGPPGEKGPQGKPGLAGLPGADGPPGHPGKEG 739
Cdd:COG5164 3 LYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 740 QSGEKGALGPPGPQGPIGYPGPRGVKGADGVRGLKGSKGEKGEDGfPGFKGDMGLKGDRGEV----GQIGPRGEDGPEGP 815
Cdd:COG5164 83 PAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-PPSGGSTTPPGDGGSTppgpGSTGPGGSTTPPGD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 816 KGRAGPTGDPGPSGQAGEKGKlGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKP-------GPRGQRGPTGPR 888
Cdd:COG5164 162 GGSTTPPGPGGSTTPPDDGGS-TTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPddrggktGPKDQRPKTNPI 240
|
250
....*....|....
gi 966919058 889 GSRGARGPTGKPGP 902
Cdd:COG5164 241 ERRGPERPEAAALP 254
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
420-669 |
7.49e-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: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 420 GAYGEKGQKGEPAVVEPgMLVEGPPGPAGPAGIMGPPGLQGPTGPPGDPGDRGPPGRPGLPGADGLPGPPGTmlmlPFRY 499
Cdd:NF038329 135 GPRGDRGETGPAGPAGP-PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE----QGPA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 500 GGDGSKGPTISAQEAQAQAILQQARIALRGPPGPMGLTGRPGPVGGPGSAGAKGESGDPGPQGPRGVQGPPGPTgkpgkr 579
Cdd:NF038329 210 GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV------ 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 580 GRPGADGGRGMPGEPGSKGDRGFDGLPGLPGDkghrgergpqgppgppgddgmRGEDGEIGPRGLPGEAGPRGLLGPRG- 658
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK---------------------DGKDGQPGKDGLPGKDGKDGQPGKPAp 342
|
250
....*....|..
gi 966919058 659 -TPGAPGQPGMA 669
Cdd:NF038329 343 kTPEVPQKPDTA 354
|
|
| LamG |
smart00282 |
Laminin G domain; |
100-227 |
2.06e-08 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 54.65 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 100 SILFTVKP--KKGIqsfLLSIYNEHGIQQIGVE-VGRSPVFLFEDHTGKPAPEdyplFRTVNIADGKWHRVAISVEKKTV 176
Cdd:smart00282 1 SISFSFRTtsPNGL---LLYAGSKGGGDYLALElRDGRLVLRYDLGSGPARLT----SDPTPLNDGQWHRVAVERNGRSV 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 966919058 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 |
1.04e-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: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 73 AYRVSKQAQLSAPTKQLFPggpfpEDFSILFTVKPKK--GIqsfLLSIYNEHGIQQIGVE-VGRSPVFLFEDHTGKPape 149
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPR-----TRLSISFSFRTTSpnGL---LLYAGSQNGGDFLALElEDGRLVLRYDLGSGSL--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 150 dypLFRTVN-IADGKWHRVAISVEKKTVTMIVDCKKKTTKPLDRSErAIVDTNGITVFGTRILDEEV--------FEGDI 220
Cdd:cd00110 70 ---VLSSKTpLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGS-ALLNLDGPLYLGGLPEDLKSpglpvspgFVGCI 145
|
....*
gi 966919058 221 QQFLI 225
Cdd:cd00110 146 RDLKV 150
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
844-900 |
2.95e-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: 48.64 E-value: 2.95e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 966919058 844 GYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKP 900
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1378-1575 |
7.77e-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: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1378 GAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPGAAGQDgppgpmgppglpglkgdpgskgekghpgl 1457
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ----------------------------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1458 igliGPPGEQGEKGDRGLPGTQGSPGAKgdggipgpagplgppgppglpGPQGPKGNKGSTGPAGQKGDSGLPGPPGPPG 1537
Cdd:NF038329 168 ----GEAGPQGPAGKDGEAGAKGPAGEK---------------------GPQGPRGETGPAGEQGPAGPAGPDGEAGPAG 222
|
170 180 190
....*....|....*....|....*....|....*...
gi 966919058 1538 PPGEVIQPLPILSSKKTRRHTEGMQADADDNILDYSDG 1575
Cdd:NF038329 223 EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
814-870 |
1.53e-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: 1.53e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 966919058 814 GPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGAR 870
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
850-903 |
1.92e-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: 1.92e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 966919058 850 GPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPK 903
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
841-896 |
5.44e-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: 45.18 E-value: 5.44e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 966919058 841 GLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGP 896
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
835-891 |
6.30e-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: 45.18 E-value: 6.30e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 966919058 835 GKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSR 891
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
781-1041 |
8.65e-06 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 50.41 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 781 GEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGF 860
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 861 PGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPPGERGPQGPQGPVGFPGPKGPPGPPG 940
Cdd:COG5164 87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 941 KDGLPghpGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHPGPPGPPGEQGLPGAAGKEGAKGDPGPQGISGKD 1020
Cdd:COG5164 167 PPGPG---GSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERR 243
|
250 260
....*....|....*....|.
gi 966919058 1021 GPAGLRGFPGERGLPGAQGAP 1041
Cdd:COG5164 244 GPERPEAAALPAELTALEAEN 264
|
|
| GGGWT_bact |
NF040941 |
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ... |
1606-1645 |
1.14e-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: 1.14e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 966919058 1606 TCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTSGG 1645
Cdd:NF040941 1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTTDG 40
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1381-1427 |
1.22e-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: 1.22e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 966919058 1381 GEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPGAAGQ 1427
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
802-856 |
1.48e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 44.02 E-value: 1.48e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 966919058 802 GQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTG 856
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
826-882 |
1.91e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 43.64 E-value: 1.91e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 966919058 826 GPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQR 882
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
793-847 |
5.10e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 42.48 E-value: 5.10e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 966919058 793 GLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPG 847
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
637-679 |
1.14e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 41.71 E-value: 1.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 966919058 637 GEIGPRGLPGEAGPRGLLGPRGTPGAPGQPGMAGVDGPPGPKG 679
Cdd:pfam01391 10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
778-833 |
2.34e-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: 2.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 966919058 778 GEKGEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGE 833
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1099-1145 |
2.90e-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: 2.90e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 966919058 1099 GPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGE 1145
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
949-1173 |
3.36e-04 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 45.41 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 949 GQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGErghpgppgppgeqglPGAAGKEGAKGDPGPQGISGKDGPAGLRGF 1028
Cdd:COG5164 16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQN---------------QGSTTPAGNTGGTRPAGNQGATGPAQNQGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1029 PGERGLPGAQGAPGLKGGEGPQGPPGPVGSPGERGSAGTA---GPIGLPGRPGPQGPPGPAGEKGAPGEKGPQGPAGRDG 1105
Cdd:COG5164 81 TTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPddgGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966919058 1106 VQGPVGLPGPAGPAGSPGEDG-----DKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPR 1173
Cdd:COG5164 161 DGGSTTPPGPGGSTTPPDDGGsttppNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQ 233
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1086-1134 |
3.61e-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: 3.61e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 966919058 1086 AGEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEP 1134
Cdd:pfam01391 9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
856-905 |
4.02e-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: 4.02e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 966919058 856 GFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGT 905
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
787-843 |
4.70e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.78 E-value: 4.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 966919058 787 GFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLP 843
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1366-1416 |
6.13e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.40 E-value: 6.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 966919058 1366 GAAGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPV 1416
Cdd:pfam01391 7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
806-902 |
6.98e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.59 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 806 PRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPT 885
Cdd:PRK07764 615 PAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA 694
|
90
....*....|....*..
gi 966919058 886 GPRGSRGARGPTGKPGP 902
Cdd:PRK07764 695 GAAPAQPAPAPAATPPA 711
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
594-850 |
8.47e-04 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 43.87 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 594 PGSKGDRGFDGLPGLPGDKGHRGERGPQGPPGPPGDDgmrGEDGEIGPRGLPGEAGPRGLLGPRGTPGAPGQPGMAGVDG 673
Cdd:COG5164 6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNT---GGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 674 PPGPKGNMGPQGEPGPPGQQGNPGPQGLPGPQGPIGPPGEKGPQGKPGLAGLPGADGPPGHPGKEGQSGEKGALGPPGPQ 753
Cdd:COG5164 83 PAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 754 GPIGYPGPRGVKGADGVRGlKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQIGPRGE-DGPEGPKGRAGPTGDPGPSGQAG 832
Cdd:COG5164 163 GSTTPPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKgNPPDDRGGKTGPKDQRPKTNPIE 241
|
250
....*....|....*...
gi 966919058 833 EKGKLGVPGLPGYPGRQG 850
Cdd:COG5164 242 RRGPERPEAAALPAELTA 259
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
156-207 |
8.82e-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: 8.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 966919058 156 TVNIADGKWHRVAISVEKKTVTMIVDCKKKTTKPLDrSERAIVDTNGITVFG 207
Cdd:pfam02210 47 GKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP-GESLLLNLNGPLYLG 97
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
729-901 |
1.19e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 43.42 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 729 DGPPGHPGKEGQSGEKGALGPPGPQGPIGYPGPRGVKGADGV---RGLKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQIG 805
Cdd:PHA03169 89 QGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESpasHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQ 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 806 PRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGyPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPR----GQ 881
Cdd:PHA03169 169 PSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSP-PDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEregpPF 247
|
170 180
....*....|....*....|
gi 966919058 882 RGPTGPRGSRGARGPTGKPG 901
Cdd:PHA03169 248 PGHRSHSYTVVGWKPSTRPG 267
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
1090-1307 |
6.77e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 41.17 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1090 GAPGEKGPQGPAGRDGVQGPVGLPG---PAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGG 1166
Cdd:COG5164 10 GPSDPGGVTTPAGSQGSTKPAQNQGstrPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966919058 1167 DgepGPRGQQGMFGQKGDEGARGFPGPPGPIGLQGLPGPPGEKGENGDVGPMGPPGPPGPRGPQGPNGADGPQGPPGSVG 1246
Cdd:COG5164 90 T---RPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966919058 1247 SVGGVGEKGEPGEAGNPGPP--GEAGVGGPKGERGEKGEAGPPGAAGPPGAKGPPGDDGPKGN 1307
Cdd:COG5164 167 PPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTG 229
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1083-1124 |
8.59e-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: 8.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 966919058 1083 PGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGE 1124
Cdd:pfam01391 15 PGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| |
