|
Name |
Accession |
Description |
Interval |
E-value |
| COLFI |
pfam01410 |
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1536-1765 |
2.84e-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: 402.87 E-value: 2.84e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1536 GMEEIFGSLNSLKQDIEHMKFPMGTQTNPARTCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTSgGETCIYPDKK 1615
Cdd:pfam01410 1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1616 SEGvRISSWPKEKPGSWFSEFKRGKL-LSY-LDVEGNSINMVQMTFLKLLTASARQNFTYHCHQSAAWYDVSSGSYDKAL 1693
Cdd:pfam01410 80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6165881 1694 RFLGSNDEEMSYD--NNPFIKTLYDGCASRKGY-EKTVIEINTPKIDQVPIVDVMINDFGDQNQKFGFEVGPVCF 1765
Cdd:pfam01410 159 LLQGSNDEEIRAEgnSRFTYTVLEDGCTKRTGQwGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
|
|
| COLFI |
smart00038 |
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1537-1766 |
4.45e-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: 337.90 E-value: 4.45e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1537 MEEIFGSLNSLKQDIEHMKFPMGTQTNPARTCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTsGGETCIYPDKKS 1616
Cdd:smart00038 1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFE-TGETCVSPSPSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1617 EGVRISSWPKEKpGSWFSEFKR-GKLLSYLDVEGNSINMVQMTFLKLLTASARQNFTYHCHQSAAWYDVSSGSYDKALRF 1695
Cdd:smart00038 80 IPRKTWYSGKSK-HVWFGETMNgGFKFSYGDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6165881 1696 LGSNDEEMSYDNN--PFIKTLYDGCASRKGY-EKTVIEINTPKIDQVPIVDVMINDFGDQNQKFGFEVGPVCFL 1766
Cdd:smart00038 159 RGSNDVELSAEGNskFTYEVLEDGCQKRTGKwGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
38-229 |
4.57e-57 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 195.65 E-value: 4.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 38 PVDVLKALDFHNSPEGISKTTGFCtnrknskGSDTAYRVSKQAQLSAPTKQLFPGGtFPEDFSILFTVKPKKGIQSFLLS 117
Cdd:smart00210 1 GQDLLQVFDLPSLSFAIRQVVGPE-------PGSPAYRLGDPALVPQPTRDLFPSG-LPEDFSLLTTFRQTPKSRGVLFA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 118 IYNEHGIQQIGVEV-GRSPVFLFEDHtGKPAPEDYPLFRTVNIADGKWHRVAISVEKKTVTMIVDCKKKTTKPLDRSERA 196
Cdd:smart00210 73 IYDAQNVRQFGLEVdGRANTLLLRYQ-GVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQP 151
|
170 180 190
....*....|....*....|....*....|...
gi 6165881 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 ... |
563-864 |
1.45e-31 |
|
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: 130.03 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 563 FDGLPGLPGDkGHRGERGPQGPpgppgddgmRGEDGEIGPRGLPGEAGPRGLLGPRGTPGAPGQPGMAGVDGPPGPKGnm 642
Cdd:NF038329 107 DEGLQQLKGD-GEKGEPGPAGP---------AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 643 gpqgepgppgqqgnpgpqglpgpqgpigppgEKGPQGKPGLAGLPGADGPPGHPGKEGQSGEKGALgppgpqgpigypgp 722
Cdd:NF038329 175 -------------------------------PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA-------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 723 rGVKGADGVRGLKGSKGEKGEDGfPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKlgvpg 802
Cdd:NF038329 210 -GPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP----- 282
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6165881 803 lPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPK 864
Cdd:NF038329 283 -VGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
540-804 |
1.23e-29 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 124.25 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 540 RGRPGADGGRGMPGEPGAKGDRGFDGLPGLPGDKGHRGERGPQGPPgppgddgmrGEDGEIGPRGLPGEAGPRGLLGPRG 619
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA---------GPQGEAGPQGPAGKDGEAGAKGPAG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 620 TPGAPGQPGMAGVDGPPGPKGNMGPQGEPGPPGQQGNPGPQGLPgpqgpigppgEKGPQGKPGLAGLPGADGPPGHPGKE 699
Cdd:NF038329 190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG----------QQGPDGDPGPTGEDGPQGPDGPAGKD 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 700 GQsgekgalgppgpqgpigypgprgvKGADGVRGLKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGR 779
Cdd:NF038329 260 GP------------------------RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK 315
|
250 260
....*....|....*....|....*
gi 6165881 780 AGPTGDPGPSGQAGEKGKLGVPGLP 804
Cdd:NF038329 316 DGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
752-1004 |
1.03e-25 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 112.69 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 752 DMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKlgvPGLPGYPGRQGPKGSTGFPGFPGANGEKGAR 831
Cdd:NF038329 112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE---RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 832 GVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPpgergpqgpqgpvgfpgpkgppgppgkdglpghpGQ 911
Cdd:NF038329 189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------------------------------GQ 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 912 RGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHPGPPGPPGEQGLPGAAGKEGAKGDPGPQGISGKDGPAGLRGFPG 991
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG 314
|
250
....*....|...
gi 6165881 992 ERGLPGAQGAPGL 1004
Cdd:NF038329 315 KDGKDGQPGKDGL 327
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
790-1132 |
5.07e-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: 104.22 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 790 GQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTsgg 869
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 870 dgppgppgergpqgpqgpvgfpgpkgppgppgkdglpghPGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHpg 949
Cdd:NF038329 194 ---------------------------------------QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 950 ppgppgeqglpgaaGKEGAKGDPGPQGISGKDGPAGLRGFPGERGlpgaqgapglkggegpqgppgpvgspgERGSAGTA 1029
Cdd:NF038329 233 --------------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG---------------------------DRGEAGPD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1030 GPiglpgrpgpqgppgpageKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGdkgengp 1109
Cdd:NF038329 272 GP------------------DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG------- 326
|
330 340
....*....|....*....|...
gi 6165881 1110 pgppglqgpvgAPGIAGGDGEPG 1132
Cdd:NF038329 327 -----------LPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1216-1444 |
1.28e-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: 99.98 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1216 GEPGEAGNPGPPGEAGVGGPKGERGEKGEAGPPGAAGPPGAKGPPGDDGPKGnpgpvgfpgDPGPPGELGPAGQDGVGGD 1295
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------EAGPQGPAGKDGEAGAKGP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1296 KGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGAAGAEGRQGEKGaKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPG 1375
Cdd:NF038329 188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6165881 1376 PVGEQGLPGAAGQDGPPGPMGPPGLPGLKGDPGSKGEKGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPG 1444
Cdd:NF038329 267 EAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
489-776 |
1.43e-21 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 99.98 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 489 RGPPGPMGLTGRPGPVGGPGSSGAKGESGDPGPQGPRGVQGPPGPTGKPGKRGRPGADGGRGMPGEPGAKGDRGFDGLPG 568
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 569 LPGDKGHRGERGPQGPPGPPGDDGMRGEDG--EIGPRGLPGEAGPRGLLGPRGTPGAPGQPGMAGVDGPPGPKGnmgpqg 646
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG------ 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 647 epgppgqqgnpgpqglpgpqgpigppgEKGPQGKPGLAGLPGADGPPGHPGKEGQsgekgalgppgpqgpigypgprgvk 726
Cdd:NF038329 276 ---------------------------KDGERGPVGPAGKDGQNGKDGLPGKDGK------------------------- 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 6165881 727 gaDGVRGLKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGP 776
Cdd:NF038329 304 --DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKP 351
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
838-1144 |
1.69e-20 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 96.51 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 838 GPRGQRGPTGPRGSRGARGPTGKpgpkgtsggdgppgppgergpqgpqgpvgfpgpkgppgppgkdglpghpgqRGETGF 917
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGD---------------------------------------------------RGETGP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 918 QGKtgppgpggvvgpqgpTGETGPIGERGHpgppgppgeqglpgaAGKEGAKGDPGPQGISGKDGPAGLRGFPGERGLPG 997
Cdd:NF038329 146 AGP---------------AGPPGPQGERGE---------------KGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 998 AQGAPGLKGGEGPQGPPGPVGSPGERGSAGTAGPiglpgrpGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPA 1077
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP-------AGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6165881 1078 GPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPRGQQGMFGQKG 1144
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1065-1432 |
1.26e-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: 90.73 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1065 DGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPpgppglqgpvgaPGIAGGDGEPGPRGQQGMFGQKG 1144
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE------------KGPAGPQGEAGPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1145 DEgargfpgppgpiglqglpGPPGEKGENgdvgpmgppgppgprgpqgpngadgpqgppgsvgsvggvgekGEPGEAGNP 1224
Cdd:NF038329 184 AK------------------GPAGEKGPQ------------------------------------------GPRGETGPA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1225 GPPGEAGVGGPKGERGEKGEagppgaagppgakgppgdDGPKGnpgpvgfpgdpgppgeLGPAGQDGVGGDKGEDgdpgq 1304
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGE------------------DGPAG----------------PAGDGQQGPDGDPGPT----- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1305 pgppgpsgeagppgppgkrgppgaaGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPG 1384
Cdd:NF038329 245 -------------------------GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPG 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 6165881 1385 AAGQDGPPGPMgppglpglkGDPGSKGEKGHPGLIGLIGPPGEQGEKG 1432
Cdd:NF038329 300 KDGKDGQNGKD---------GLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1054-1388 |
1.43e-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: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1054 GEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGP 1133
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1134 RGQQGMFGQKGDEGARGFPGPPGPIGLQGLPGPPGEkgengdvgpmgppgppgprgpqgpnGADGPQGppgsvgsvggvg 1213
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------------------------GQQGPDG------------ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1214 EKGEPGEAGNPGPPGEAGVGGPKGERGEKGEagppgaagppgakgppgdDGPKGNpgpvgfpgdpgppgelgpagqdgvg 1293
Cdd:NF038329 240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP------------------DGPDGK------------------------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1294 gdkgedgdpgqpgppgpsgeagppgppgkrgppgaAGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGI 1373
Cdd:NF038329 277 -----------------------------------DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321
|
330
....*....|....*
gi 6165881 1374 PGPVGEQGLPGAAGQ 1388
Cdd:NF038329 322 PGKDGLPGKDGKDGQ 336
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1022-1243 |
1.97e-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: 87.27 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1022 ERGSAGTAGPIGLPGRPGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSK 1101
Cdd:NF038329 118 EKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1102 GDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPRGqQGMFGQKGDEGARGFPGPPGPIGLQGLPGPPGEKGENGDVGPMGP 1181
Cdd:NF038329 198 GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6165881 1182 PGPPGPRGPQGPNGADGPQGPPGSVGSVGGVGEKGEPGEAGNPGPPGEAGVGGPKGERGEKG 1243
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1290-1444 |
9.07e-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: 81.88 E-value: 9.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1290 DGVGGDKGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGAAGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEG 1369
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1370 LRGIPGPVGEQGLPGAAGQDGPPGPMGPPGLPGLKGDP-----GSKGEKGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPG 1444
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1328-1489 |
1.70e-15 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 81.10 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1328 AAGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPGAAGQDGPPGPMGPPGLPGLKGDP 1407
Cdd:NF038329 145 PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGED 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1408 GSKGE--KGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPGAKGDGGIPGPAGPLGPPGPPGLPGPQGPKGNKGSTGPAGQK 1485
Cdd:NF038329 225 GPAGPagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKD 304
|
....
gi 6165881 1486 GDSG 1489
Cdd:NF038329 305 GQNG 308
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
621-863 |
8.78e-09 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 60.04 E-value: 8.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 621 PGAPGQPGMAGVDGPPGPKGNMGPQGEPGPPGQQGNPGPQGLPGPQGPIGPPGEKGPQGKPGLAGLPGADGPPGHPGKEG 700
Cdd:COG5164 3 LYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 701 QSGEKGALGPPGPQGPIGYPGPRGVKGADGVRGLKGSKGEKGEDGfPGFKGDMGLKGDRGEV----GQIGPRGEDGPEGP 776
Cdd:COG5164 83 PAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-PPSGGSTTPPGDGGSTppgpGSTGPGGSTTPPGD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 777 KGRAGPTGDPGPSGQAGEKGKlGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKP-------GPRGQRGPTGPR 849
Cdd:COG5164 162 GGSTTPPGPGGSTTPPDDGGS-TTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPddrggktGPKDQRPKTNPI 240
|
250
....*....|....
gi 6165881 850 GSRGARGPTGKPGP 863
Cdd:COG5164 241 ERRGPERPEAAALP 254
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
381-630 |
1.16e-08 |
|
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: 59.53 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 381 GAYGEKGQKGEPAVVEPgMLVEGPPGPAGPAGIMGPPGLQGPTGPPGDPGDRGPPGRPGLPGADGLPGPPGTmlmlPFRY 460
Cdd:NF038329 135 GPRGDRGETGPAGPAGP-PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE----QGPA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 461 GGDGSKGPTISAQEAQAQAILQQARIALRGPPGPMGLTGRPGPVGGPGSSGAKGESGDPGPQGPRGVQGPPGPTgkpgkr 540
Cdd:NF038329 210 GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV------ 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 541 GRPGADGGRGMPGEPGAKGDRGFDGLPGLPGDkghrgergpqgppgppgddgmRGEDGEIGPRGLPGEAGPRGLLGPRG- 619
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK---------------------DGKDGQPGKDGLPGKDGKDGQPGKPAp 342
|
250
....*....|..
gi 6165881 620 -TPGAPGQPGMA 630
Cdd:NF038329 343 kTPEVPQKPDTA 354
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
73-225 |
1.01e-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: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 73 AYRVSKQAQLSAPTKQLFPggtfpEDFSILFTVKPKK--GIqsfLLSIYNEHGIQQIGVE-VGRSPVFLFEDHTGKPape 149
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPR-----TRLSISFSFRTTSpnGL---LLYAGSQNGGDFLALElEDGRLVLRYDLGSGSL--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 150 dypLFRTVN-IADGKWHRVAISVEKKTVTMIVDCKKKTTKPLDRSErAIVDTNGITVFGTRILDEEV--------FEGDI 220
Cdd:cd00110 70 ---VLSSKTpLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGS-ALLNLDGPLYLGGLPEDLKSpglpvspgFVGCI 145
|
....*
gi 6165881 221 QQFLI 225
Cdd:cd00110 146 RDLKV 150
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
805-861 |
6.27e-07 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 47.87 E-value: 6.27e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 6165881 805 GYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKP 861
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1339-1536 |
1.19e-06 |
|
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: 52.99 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1339 GAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPGAAGQDgppgpmgppglpglkgdpgskgekghpgl 1418
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ----------------------------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1419 igliGPPGEQGEKGDRGLPGTQGSPGAKgdggipgpagplgppgppglpGPQGPKGNKGSTGPAGQKGDSGLPGPPGPPG 1498
Cdd:NF038329 168 ----GEAGPQGPAGKDGEAGAKGPAGEK---------------------GPQGPRGETGPAGEQGPAGPAGPDGEAGPAG 222
|
170 180 190
....*....|....*....|....*....|....*...
gi 6165881 1499 PPGEVIQPLPILSSKKTRRHTEGMQADADDNILDYSDG 1536
Cdd:NF038329 223 EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260
|
|
| GGGWT_bact |
NF040941 |
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ... |
1567-1606 |
1.21e-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: 1.21e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 6165881 1567 TCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTSGG 1606
Cdd:NF040941 1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTTDG 40
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
742-1002 |
1.23e-05 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 50.03 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 742 GEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGF 821
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 822 PGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPPGERGPQGPQGPVGFPGPKGPPGPPG 901
Cdd:COG5164 87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 902 KDGLPghpGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHPGPPGPPGEQGLPGAAGKEGAKGDPGPQGISGKD 981
Cdd:COG5164 167 PPGPG---GSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERR 243
|
250 260
....*....|....*....|.
gi 6165881 982 GPAGLRGFPGERGLPGAQGAP 1002
Cdd:COG5164 244 GPERPEAAALPAELTALEAEN 264
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1342-1388 |
2.27e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 43.64 E-value: 2.27e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 6165881 1342 GEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPGAAGQ 1388
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
910-1134 |
4.58e-04 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 45.02 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 910 GQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGErghpgppgppgeqglPGAAGKEGAKGDPGPQGISGKDGPAGLRGF 989
Cdd:COG5164 16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQN---------------QGSTTPAGNTGGTRPAGNQGATGPAQNQGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 990 PGERGLPGAQGAPGLKGGEGPQGPPGPVGSPGERGSAGTA---GPIGLPGRPGPQGPPGPAGEKGAPGEKGPQGPAGRDG 1066
Cdd:COG5164 81 TTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPddgGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6165881 1067 VQGPVGLPGPAGPAGSPGEDG-----DKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPR 1134
Cdd:COG5164 161 DGGSTTPPGPGGSTTPPDDGGsttppNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQ 233
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1060-1106 |
5.18e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.78 E-value: 5.18e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 6165881 1060 GPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGE 1106
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
767-863 |
6.81e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.59 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 767 PRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPT 846
Cdd:PRK07764 615 PAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA 694
|
90
....*....|....*..
gi 6165881 847 GPRGSRGARGPTGKPGP 863
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 |
8.63e-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: 8.63e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 6165881 156 TVNIADGKWHRVAISVEKKTVTMIVDCKKKTTKPLDrSERAIVDTNGITVFG 207
Cdd:pfam02210 47 GKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP-GESLLLNLNGPLYLG 97
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COLFI |
pfam01410 |
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1536-1765 |
2.84e-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: 402.87 E-value: 2.84e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1536 GMEEIFGSLNSLKQDIEHMKFPMGTQTNPARTCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTSgGETCIYPDKK 1615
Cdd:pfam01410 1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1616 SEGvRISSWPKEKPGSWFSEFKRGKL-LSY-LDVEGNSINMVQMTFLKLLTASARQNFTYHCHQSAAWYDVSSGSYDKAL 1693
Cdd:pfam01410 80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6165881 1694 RFLGSNDEEMSYD--NNPFIKTLYDGCASRKGY-EKTVIEINTPKIDQVPIVDVMINDFGDQNQKFGFEVGPVCF 1765
Cdd:pfam01410 159 LLQGSNDEEIRAEgnSRFTYTVLEDGCTKRTGQwGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
|
|
| COLFI |
smart00038 |
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ... |
1537-1766 |
4.45e-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: 337.90 E-value: 4.45e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1537 MEEIFGSLNSLKQDIEHMKFPMGTQTNPARTCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTsGGETCIYPDKKS 1616
Cdd:smart00038 1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFE-TGETCVSPSPSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1617 EGVRISSWPKEKpGSWFSEFKR-GKLLSYLDVEGNSINMVQMTFLKLLTASARQNFTYHCHQSAAWYDVSSGSYDKALRF 1695
Cdd:smart00038 80 IPRKTWYSGKSK-HVWFGETMNgGFKFSYGDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6165881 1696 LGSNDEEMSYDNN--PFIKTLYDGCASRKGY-EKTVIEINTPKIDQVPIVDVMINDFGDQNQKFGFEVGPVCFL 1766
Cdd:smart00038 159 RGSNDVELSAEGNskFTYEVLEDGCQKRTGKwGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
38-229 |
4.57e-57 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 195.65 E-value: 4.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 38 PVDVLKALDFHNSPEGISKTTGFCtnrknskGSDTAYRVSKQAQLSAPTKQLFPGGtFPEDFSILFTVKPKKGIQSFLLS 117
Cdd:smart00210 1 GQDLLQVFDLPSLSFAIRQVVGPE-------PGSPAYRLGDPALVPQPTRDLFPSG-LPEDFSLLTTFRQTPKSRGVLFA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 118 IYNEHGIQQIGVEV-GRSPVFLFEDHtGKPAPEDYPLFRTVNIADGKWHRVAISVEKKTVTMIVDCKKKTTKPLDRSERA 196
Cdd:smart00210 73 IYDAQNVRQFGLEVdGRANTLLLRYQ-GVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQP 151
|
170 180 190
....*....|....*....|....*....|...
gi 6165881 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 ... |
563-864 |
1.45e-31 |
|
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: 130.03 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 563 FDGLPGLPGDkGHRGERGPQGPpgppgddgmRGEDGEIGPRGLPGEAGPRGLLGPRGTPGAPGQPGMAGVDGPPGPKGnm 642
Cdd:NF038329 107 DEGLQQLKGD-GEKGEPGPAGP---------AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 643 gpqgepgppgqqgnpgpqglpgpqgpigppgEKGPQGKPGLAGLPGADGPPGHPGKEGQSGEKGALgppgpqgpigypgp 722
Cdd:NF038329 175 -------------------------------PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA-------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 723 rGVKGADGVRGLKGSKGEKGEDGfPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKlgvpg 802
Cdd:NF038329 210 -GPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP----- 282
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6165881 803 lPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPK 864
Cdd:NF038329 283 -VGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
540-804 |
1.23e-29 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 124.25 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 540 RGRPGADGGRGMPGEPGAKGDRGFDGLPGLPGDKGHRGERGPQGPPgppgddgmrGEDGEIGPRGLPGEAGPRGLLGPRG 619
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA---------GPQGEAGPQGPAGKDGEAGAKGPAG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 620 TPGAPGQPGMAGVDGPPGPKGNMGPQGEPGPPGQQGNPGPQGLPgpqgpigppgEKGPQGKPGLAGLPGADGPPGHPGKE 699
Cdd:NF038329 190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG----------QQGPDGDPGPTGEDGPQGPDGPAGKD 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 700 GQsgekgalgppgpqgpigypgprgvKGADGVRGLKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGR 779
Cdd:NF038329 260 GP------------------------RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK 315
|
250 260
....*....|....*....|....*
gi 6165881 780 AGPTGDPGPSGQAGEKGKLGVPGLP 804
Cdd:NF038329 316 DGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
752-1004 |
1.03e-25 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 112.69 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 752 DMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKlgvPGLPGYPGRQGPKGSTGFPGFPGANGEKGAR 831
Cdd:NF038329 112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE---RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 832 GVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPpgergpqgpqgpvgfpgpkgppgppgkdglpghpGQ 911
Cdd:NF038329 189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------------------------------GQ 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 912 RGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHPGPPGPPGEQGLPGAAGKEGAKGDPGPQGISGKDGPAGLRGFPG 991
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPG 314
|
250
....*....|...
gi 6165881 992 ERGLPGAQGAPGL 1004
Cdd:NF038329 315 KDGKDGQPGKDGL 327
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
790-1132 |
5.07e-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: 104.22 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 790 GQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTsgg 869
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 870 dgppgppgergpqgpqgpvgfpgpkgppgppgkdglpghPGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHpg 949
Cdd:NF038329 194 ---------------------------------------QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 950 ppgppgeqglpgaaGKEGAKGDPGPQGISGKDGPAGLRGFPGERGlpgaqgapglkggegpqgppgpvgspgERGSAGTA 1029
Cdd:NF038329 233 --------------GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG---------------------------DRGEAGPD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1030 GPiglpgrpgpqgppgpageKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGdkgengp 1109
Cdd:NF038329 272 GP------------------DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG------- 326
|
330 340
....*....|....*....|...
gi 6165881 1110 pgppglqgpvgAPGIAGGDGEPG 1132
Cdd:NF038329 327 -----------LPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1216-1444 |
1.28e-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: 99.98 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1216 GEPGEAGNPGPPGEAGVGGPKGERGEKGEAGPPGAAGPPGAKGPPGDDGPKGnpgpvgfpgDPGPPGELGPAGQDGVGGD 1295
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------EAGPQGPAGKDGEAGAKGP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1296 KGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGAAGAEGRQGEKGaKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPG 1375
Cdd:NF038329 188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6165881 1376 PVGEQGLPGAAGQDGPPGPMGPPGLPGLKGDPGSKGEKGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPG 1444
Cdd:NF038329 267 EAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
489-776 |
1.43e-21 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 99.98 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 489 RGPPGPMGLTGRPGPVGGPGSSGAKGESGDPGPQGPRGVQGPPGPTGKPGKRGRPGADGGRGMPGEPGAKGDRGFDGLPG 568
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 569 LPGDKGHRGERGPQGPPGPPGDDGMRGEDG--EIGPRGLPGEAGPRGLLGPRGTPGAPGQPGMAGVDGPPGPKGnmgpqg 646
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG------ 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 647 epgppgqqgnpgpqglpgpqgpigppgEKGPQGKPGLAGLPGADGPPGHPGKEGQsgekgalgppgpqgpigypgprgvk 726
Cdd:NF038329 276 ---------------------------KDGERGPVGPAGKDGQNGKDGLPGKDGK------------------------- 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 6165881 727 gaDGVRGLKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGP 776
Cdd:NF038329 304 --DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKP 351
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
838-1144 |
1.69e-20 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 96.51 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 838 GPRGQRGPTGPRGSRGARGPTGKpgpkgtsggdgppgppgergpqgpqgpvgfpgpkgppgppgkdglpghpgqRGETGF 917
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGD---------------------------------------------------RGETGP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 918 QGKtgppgpggvvgpqgpTGETGPIGERGHpgppgppgeqglpgaAGKEGAKGDPGPQGISGKDGPAGLRGFPGERGLPG 997
Cdd:NF038329 146 AGP---------------AGPPGPQGERGE---------------KGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 998 AQGAPGLKGGEGPQGPPGPVGSPGERGSAGTAGPiglpgrpGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPA 1077
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP-------AGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6165881 1078 GPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPRGQQGMFGQKG 1144
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1065-1432 |
1.26e-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: 90.73 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1065 DGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPpgppglqgpvgaPGIAGGDGEPGPRGQQGMFGQKG 1144
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE------------KGPAGPQGEAGPQGPAGKDGEAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1145 DEgargfpgppgpiglqglpGPPGEKGENgdvgpmgppgppgprgpqgpngadgpqgppgsvgsvggvgekGEPGEAGNP 1224
Cdd:NF038329 184 AK------------------GPAGEKGPQ------------------------------------------GPRGETGPA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1225 GPPGEAGVGGPKGERGEKGEagppgaagppgakgppgdDGPKGnpgpvgfpgdpgppgeLGPAGQDGVGGDKGEDgdpgq 1304
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGE------------------DGPAG----------------PAGDGQQGPDGDPGPT----- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1305 pgppgpsgeagppgppgkrgppgaaGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPG 1384
Cdd:NF038329 245 -------------------------GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPG 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 6165881 1385 AAGQDGPPGPMgppglpglkGDPGSKGEKGHPGLIGLIGPPGEQGEKG 1432
Cdd:NF038329 300 KDGKDGQNGKD---------GLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1054-1388 |
1.43e-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: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1054 GEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGP 1133
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1134 RGQQGMFGQKGDEGARGFPGPPGPIGLQGLPGPPGEkgengdvgpmgppgppgprgpqgpnGADGPQGppgsvgsvggvg 1213
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------------------------GQQGPDG------------ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1214 EKGEPGEAGNPGPPGEAGVGGPKGERGEKGEagppgaagppgakgppgdDGPKGNpgpvgfpgdpgppgelgpagqdgvg 1293
Cdd:NF038329 240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP------------------DGPDGK------------------------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1294 gdkgedgdpgqpgppgpsgeagppgppgkrgppgaAGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGI 1373
Cdd:NF038329 277 -----------------------------------DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321
|
330
....*....|....*
gi 6165881 1374 PGPVGEQGLPGAAGQ 1388
Cdd:NF038329 322 PGKDGLPGKDGKDGQ 336
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1022-1243 |
1.97e-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: 87.27 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1022 ERGSAGTAGPIGLPGRPGPQGPPGPAGEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSK 1101
Cdd:NF038329 118 EKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1102 GDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPRGqQGMFGQKGDEGARGFPGPPGPIGLQGLPGPPGEKGENGDVGPMGP 1181
Cdd:NF038329 198 GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6165881 1182 PGPPGPRGPQGPNGADGPQGPPGSVGSVGGVGEKGEPGEAGNPGPPGEAGVGGPKGERGEKG 1243
Cdd:NF038329 277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1290-1444 |
9.07e-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: 81.88 E-value: 9.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1290 DGVGGDKGEDGDPGQPGPPGPSGEAGPPGPPGKRGPPGAAGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEG 1369
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1370 LRGIPGPVGEQGLPGAAGQDGPPGPMGPPGLPGLKGDP-----GSKGEKGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPG 1444
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1328-1489 |
1.70e-15 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 81.10 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1328 AAGAEGRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPGAAGQDGPPGPMGPPGLPGLKGDP 1407
Cdd:NF038329 145 PAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGED 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1408 GSKGE--KGHPGLIGLIGPPGEQGEKGDRGLPGTQGSPGAKGDGGIPGPAGPLGPPGPPGLPGPQGPKGNKGSTGPAGQK 1485
Cdd:NF038329 225 GPAGPagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKD 304
|
....
gi 6165881 1486 GDSG 1489
Cdd:NF038329 305 GQNG 308
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
621-863 |
8.78e-09 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 60.04 E-value: 8.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 621 PGAPGQPGMAGVDGPPGPKGNMGPQGEPGPPGQQGNPGPQGLPGPQGPIGPPGEKGPQGKPGLAGLPGADGPPGHPGKEG 700
Cdd:COG5164 3 LYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 701 QSGEKGALGPPGPQGPIGYPGPRGVKGADGVRGLKGSKGEKGEDGfPGFKGDMGLKGDRGEV----GQIGPRGEDGPEGP 776
Cdd:COG5164 83 PAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-PPSGGSTTPPGDGGSTppgpGSTGPGGSTTPPGD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 777 KGRAGPTGDPGPSGQAGEKGKlGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKP-------GPRGQRGPTGPR 849
Cdd:COG5164 162 GGSTTPPGPGGSTTPPDDGGS-TTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPddrggktGPKDQRPKTNPI 240
|
250
....*....|....
gi 6165881 850 GSRGARGPTGKPGP 863
Cdd:COG5164 241 ERRGPERPEAAALP 254
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
381-630 |
1.16e-08 |
|
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: 59.53 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 381 GAYGEKGQKGEPAVVEPgMLVEGPPGPAGPAGIMGPPGLQGPTGPPGDPGDRGPPGRPGLPGADGLPGPPGTmlmlPFRY 460
Cdd:NF038329 135 GPRGDRGETGPAGPAGP-PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE----QGPA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 461 GGDGSKGPTISAQEAQAQAILQQARIALRGPPGPMGLTGRPGPVGGPGSSGAKGESGDPGPQGPRGVQGPPGPTgkpgkr 540
Cdd:NF038329 210 GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV------ 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 541 GRPGADGGRGMPGEPGAKGDRGFDGLPGLPGDkghrgergpqgppgppgddgmRGEDGEIGPRGLPGEAGPRGLLGPRG- 619
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK---------------------DGKDGQPGKDGLPGKDGKDGQPGKPAp 342
|
250
....*....|..
gi 6165881 620 -TPGAPGQPGMA 630
Cdd:NF038329 343 kTPEVPQKPDTA 354
|
|
| LamG |
smart00282 |
Laminin G domain; |
100-227 |
2.59e-08 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 54.27 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 100 SILFTVKP--KKGIqsfLLSIYNEHGIQQIGVE-VGRSPVFLFEDHTGKPAPEdyplFRTVNIADGKWHRVAISVEKKTV 176
Cdd:smart00282 1 SISFSFRTtsPNGL---LLYAGSKGGGDYLALElRDGRLVLRYDLGSGPARLT----SDPTPLNDGQWHRVAVERNGRSV 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 6165881 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 |
1.01e-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: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 73 AYRVSKQAQLSAPTKQLFPggtfpEDFSILFTVKPKK--GIqsfLLSIYNEHGIQQIGVE-VGRSPVFLFEDHTGKPape 149
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPR-----TRLSISFSFRTTSpnGL---LLYAGSQNGGDFLALElEDGRLVLRYDLGSGSL--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 150 dypLFRTVN-IADGKWHRVAISVEKKTVTMIVDCKKKTTKPLDRSErAIVDTNGITVFGTRILDEEV--------FEGDI 220
Cdd:cd00110 70 ---VLSSKTpLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGS-ALLNLDGPLYLGGLPEDLKSpglpvspgFVGCI 145
|
....*
gi 6165881 221 QQFLI 225
Cdd:cd00110 146 RDLKV 150
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
805-861 |
6.27e-07 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 47.87 E-value: 6.27e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 6165881 805 GYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKP 861
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1339-1536 |
1.19e-06 |
|
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: 52.99 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1339 GAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPGAAGQDgppgpmgppglpglkgdpgskgekghpgl 1418
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ----------------------------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 1419 igliGPPGEQGEKGDRGLPGTQGSPGAKgdggipgpagplgppgppglpGPQGPKGNKGSTGPAGQKGDSGLPGPPGPPG 1498
Cdd:NF038329 168 ----GEAGPQGPAGKDGEAGAKGPAGEK---------------------GPQGPRGETGPAGEQGPAGPAGPDGEAGPAG 222
|
170 180 190
....*....|....*....|....*....|....*...
gi 6165881 1499 PPGEVIQPLPILSSKKTRRHTEGMQADADDNILDYSDG 1536
Cdd:NF038329 223 EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
775-831 |
3.01e-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: 45.95 E-value: 3.01e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 6165881 775 GPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGAR 831
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
811-864 |
3.63e-06 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 45.56 E-value: 3.63e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 6165881 811 GPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPK 864
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
802-857 |
1.07e-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: 1.07e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 6165881 802 GLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGP 857
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
796-852 |
1.14e-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: 1.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 6165881 796 GKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSR 852
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| GGGWT_bact |
NF040941 |
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ... |
1567-1606 |
1.21e-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: 1.21e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 6165881 1567 TCKDLQLSHPDFPDGEYWIDPNQGCSGDSFKVYCNFTSGG 1606
Cdd:NF040941 1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTTDG 40
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
742-1002 |
1.23e-05 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 50.03 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 742 GEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGF 821
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 822 PGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGTSGGDGPPGPPGERGPQGPQGPVGFPGPKGPPGPPG 901
Cdd:COG5164 87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 902 KDGLPghpGQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGERGHPGPPGPPGEQGLPGAAGKEGAKGDPGPQGISGKD 981
Cdd:COG5164 167 PPGPG---GSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERR 243
|
250 260
....*....|....*....|.
gi 6165881 982 GPAGLRGFPGERGLPGAQGAP 1002
Cdd:COG5164 244 GPERPEAAALPAELTALEAEN 264
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1342-1388 |
2.27e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 43.64 E-value: 2.27e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 6165881 1342 GEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPVGEQGLPGAAGQ 1388
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
763-817 |
2.79e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 43.25 E-value: 2.79e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 6165881 763 GQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTG 817
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
787-843 |
3.68e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 42.87 E-value: 3.68e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 6165881 787 GPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQR 843
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
754-808 |
9.08e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 41.71 E-value: 9.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 6165881 754 GLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPG 808
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
598-640 |
2.05e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 40.94 E-value: 2.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 6165881 598 GEIGPRGLPGEAGPRGLLGPRGTPGAPGQPGMAGVDGPPGPKG 640
Cdd:pfam01391 10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
739-794 |
4.05e-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: 4.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 6165881 739 GEKGEDGFPGFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGE 794
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
910-1134 |
4.58e-04 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 45.02 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 910 GQRGETGFQGKTGPPGPGGVVGPQGPTGETGPIGErghpgppgppgeqglPGAAGKEGAKGDPGPQGISGKDGPAGLRGF 989
Cdd:COG5164 16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQN---------------QGSTTPAGNTGGTRPAGNQGATGPAQNQGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 990 PGERGLPGAQGAPGLKGGEGPQGPPGPVGSPGERGSAGTA---GPIGLPGRPGPQGPPGPAGEKGAPGEKGPQGPAGRDG 1066
Cdd:COG5164 81 TTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPddgGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6165881 1067 VQGPVGLPGPAGPAGSPGEDG-----DKGEIGEPGQKGSKGDKGENGPPGPPGLQGPVGAPGIAGGDGEPGPR 1134
Cdd:COG5164 161 DGGSTTPPGPGGSTTPPDDGGsttppNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQ 233
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1060-1106 |
5.18e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.78 E-value: 5.18e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 6165881 1060 GPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEPGQKGSKGDKGE 1106
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1047-1095 |
6.30e-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: 6.30e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 6165881 1047 AGEKGAPGEKGPQGPAGRDGVQGPVGLPGPAGPAGSPGEDGDKGEIGEP 1095
Cdd:pfam01391 9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
767-863 |
6.81e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.59 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 767 PRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGYPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPRGQRGPT 846
Cdd:PRK07764 615 PAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA 694
|
90
....*....|....*..
gi 6165881 847 GPRGSRGARGPTGKPGP 863
Cdd:PRK07764 695 GAAPAQPAPAPAATPPA 711
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
817-866 |
7.23e-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: 7.23e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 6165881 817 GFPGFPGANGEKGARGVAGKPGPRGQRGPTGPRGSRGARGPTGKPGPKGT 866
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
748-804 |
8.55e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.01 E-value: 8.55e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 6165881 748 GFKGDMGLKGDRGEVGQIGPRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLP 804
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
156-207 |
8.63e-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: 8.63e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 6165881 156 TVNIADGKWHRVAISVEKKTVTMIVDCKKKTTKPLDrSERAIVDTNGITVFG 207
Cdd:pfam02210 47 GKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP-GESLLLNLNGPLYLG 97
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
690-862 |
1.13e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 43.42 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 690 DGPPGHPGKEGQSGEKGALGPPGPQGPIGYPGPRGVKGADGV---RGLKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQIG 766
Cdd:PHA03169 89 QGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESpasHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQ 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 767 PRGEDGPEGPKGRAGPTGDPGPSGQAGEKGKLGVPGLPGyPGRQGPKGSTGFPGFPGANGEKGARGVAGKPGPR----GQ 842
Cdd:PHA03169 169 PSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSP-PDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEregpPF 247
|
170 180
....*....|....*....|
gi 6165881 843 RGPTGPRGSRGARGPTGKPG 862
Cdd:PHA03169 248 PGHRSHSYTVVGWKPSTRPG 267
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
555-811 |
1.25e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 43.48 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 555 PGAKGDRGFDGLPGLPGDKGHRGERGPQGPPGPPGDDgmrGEDGEIGPRGLPGEAGPRGLLGPRGTPGAPGQPGMAGVDG 634
Cdd:COG5164 6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNT---GGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 635 PPGPKGNMGPQGEPGPPGQQGNPGPQGLPGPQGPIGPPGEKGPQGKPGLAGLPGADGPPGHPGKEGQSGEKGALGPPGPQ 714
Cdd:COG5164 83 PAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6165881 715 GPIGYPGPRGVKGADGVRGlKGSKGEKGEDGFPGFKGDMGLKGDRGEVGQIGPRGE-DGPEGPKGRAGPTGDPGPSGQAG 793
Cdd:COG5164 163 GSTTPPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKgNPPDDRGGKTGPKDQRPKTNPIE 241
|
250
....*....|....*...
gi 6165881 794 EKGKLGVPGLPGYPGRQG 811
Cdd:COG5164 242 RRGPERPEAAALPAELTA 259
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1333-1377 |
2.01e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.86 E-value: 2.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 6165881 1333 GRQGEKGAKGEAGAEGPPGKTGPVGPQGPAGKPGPEGLRGIPGPV 1377
Cdd:pfam01391 13 GPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| |
