|
Name |
Accession |
Description |
Interval |
E-value |
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1625-1737 |
2.73e-57 |
|
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.
:
Pssm-ID: 128421 Cd Length: 114 Bit Score: 193.76 E-value: 2.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1625 TRIIALHSQSMSIPDCPGGWEEMWTGYSYFMSTLdNVGGVGQNLVSPGSCLEEFRAQPVIECHGHGRCNYYD-ALASFWL 1703
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTG-NGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASrNDYSFWL 79
|
90 100 110
....*....|....*....|....*....|....*
gi 442626069 1704 TVIEEQDQFVQPRQQTLKA-DFTSKISRCTVCRRR 1737
Cdd:smart00111 80 STIEPSDQFTAPRPMTPKAgDLRPYISRCQVCEKP 114
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1515-1624 |
2.02e-55 |
|
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.
:
Pssm-ID: 128421 Cd Length: 114 Bit Score: 188.37 E-value: 2.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1515 GFIFARHSQSVHVPQCPANTNLLWEGYSLSGNVAASRAVGQDLGQSGSCMMRFTTMPYMLCDITNVCHFAQNNDDSLWLS 1594
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80
|
90 100 110
....*....|....*....|....*....|....*
gi 442626069 1595 TAEP-----MPMTMTPIQGrDLMKYISRCVVCETT 1624
Cdd:smart00111 81 TIEPsdqftAPRPMTPKAG-DLRPYISRCQVCEKP 114
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
894-1132 |
1.99e-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.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 126.94 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 894 GAKGQKGEVGSLGQNGQNGAKGSIGFSGRRGLLGNAGLQGLPGSPGIPGLPGMIGEIGERGEIGYNGRQGDIGPRGPNGE 973
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 974 FGPKGLSGDDGPDGYPGANGLPGRKGETGNPGFPGRP-----GAKGVAAYSGIKGDDGESGLTGPIGYPGAPGAKGQRGP 1048
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1049 VGDsqpalDGVAGRKGEVGSPGPNGLPGRHGLKGQRGDRGLPGQQGRPGEPGAKGLGGYPGRNginglkGATGFPGPQGP 1128
Cdd:NF038329 277 DGE-----RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD------GQPGKPAPKTP 345
|
....
gi 442626069 1129 KGPQ 1132
Cdd:NF038329 346 EVPQ 349
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
637-871 |
3.73e-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.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 126.17 E-value: 3.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 637 DGSKGERGETGQRGDYGDAGYQGRDGEPGRDGRDGAPGRNATTPKVYLIGEPGYDGIKGERGDDGDTGFKGVKGEpnpgq 716
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE----- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 717 iydnTGEPGEDGYTGPKGVKGAKGEQGAIGLRGEIGDRGPAGEVIPGPVGAKGYPGPTGDYGQQGAPGLPGRDGEPGLDG 796
Cdd:NF038329 191 ----KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626069 797 GIGYKGQRGVPGQeviQGEIGPPGRSGIKGFPGDVGAPGQYGLAGRPGPKGVKGEQGPDGAVGQTGLPGNKGQRG 871
Cdd:NF038329 267 EAGPDGPDGKDGE---RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
465-712 |
2.56e-28 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 120.40 E-value: 2.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 465 LEGYRGDRGEVGLPGDKGLPGEgynivgppgsqgppgfrglPGDDGYNGLRGLPGEKGLRGDDCPVCNAGPRGPRGQEGD 544
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGP-------------------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 545 TGYPGSHGNRGAIGLTGPRGVQGLQGNPGRAGHKGLPGPAGIPGEPGKVGAAGPDGKAievgslRKGEIGDTGDSGHRGD 624
Cdd:NF038329 176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG------QQGPDGDPGPTGEDGP 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 625 TGDDGEKGRDGSDGSKGERGETGQRGDYGDAGYQGRDGEPGRDGRDGAPGRNATTPKVYLIGEPGYDGIKGERGDDGDTG 704
Cdd:NF038329 250 QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
|
....*...
gi 442626069 705 FKGVKGEP 712
Cdd:NF038329 330 KDGKDGQP 337
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
63-349 |
3.14e-28 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 120.40 E-value: 3.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 63 GDIGPPGRAGPLGEKGDVGEYGEQGEKGHRGDIGPKGEMGYPGIMGKSGEPGTPGPRGIDGCDGRPGMQGPSGAPGQNGV 142
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 143 RGPPGKPGQQgppgeagegginskgtkgnrgetgqpggvgppgfdgdrGSKGDTGYAGLTGEKGDPGLPGPKGDtgavse 222
Cdd:NF038329 197 RGETGPAGEQ--------------------------------------GPAGPAGPDGEAGPAGEDGPAGPAGD------ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 223 lpysliGPPGAKGEPGDslsgvlkpddtlkgykgyVGLQGDEGPQGPTGEQGAVGRNGLPGARGEIGGPGERGKPGKDGE 302
Cdd:NF038329 233 ------GQQGPDGDPGP------------------TGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK 288
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 442626069 303 PGRFGDKGMKGAPGWTGADGLDGSPGERGEDGFTGMPGVQGGAGPPG 349
Cdd:NF038329 289 DGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1078-1342 |
3.81e-28 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 120.01 E-value: 3.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1078 HGLKGQRGDRGLPGQQGRPGEPGAKGLGGYPGRNGINGLKGATGFPGPQGPKGPQGESGVVGLDGRNGQIGDQGPRGlig 1157
Cdd:NF038329 113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG--- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1158 eqgeqgeqgdegevgipgrlenlrdrsfYRGFTGDQGLQGERGEQGDMGPIGFIGPPGAKGERGDIGYAGQlGFDGAEGL 1237
Cdd:NF038329 190 ----------------------------EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGD 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1238 KGFQGDQGPRGPPGitLPAEKGDEGVAGLDGRAGRPGHFGQKGAPGPPGENGPNGAIGhrgpqIQGPPGPQGDVGFPGAP 1317
Cdd:NF038329 241 PGPTGEDGPQGPDG--PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG-----LPGKDGKDGQNGKDGLP 313
|
250 260
....*....|....*....|....*
gi 442626069 1318 GHNGRHGLIGPKGELGDMGRQGERG 1342
Cdd:NF038329 314 GKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1228-1515 |
1.88e-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.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 115.00 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1228 QLGFDGAEGLKGFQGDQGPRGPPGitlpaEKGDEGVAGLDGRAGRPGHFGQKGAPGPPGENGPNGAIGHRGPQiqGPPGP 1307
Cdd:NF038329 112 QLKGDGEKGEPGPAGPAGPAGEQG-----PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD--GEAGA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1308 QGDVGFPGAPGHNGRHGLIGPKGELGDMGRQGERGESGYAIVGRQGDIGDIGFQGEPGWDGAKGEQGYPGLPGKNGRVGA 1387
Cdd:NF038329 185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1388 PGPRGPTGDAGWGGIDGMDGLVGPKGQPGvtysysmarpgDRGEPGLDGFQGEEGDGGAPGLIGFQGQRGAVGYRGDQGE 1467
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNG-----------KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 442626069 1468 VGYTGADGPQGQRGDKGYMGLTGAPGLRGLPGPQGEPAPAPPAPKSRG 1515
Cdd:NF038329 334 DGQPGKPAPKTPEVPQKPDTAPHTPKTPQIPGQSKDVTPAPQNPSNRG 381
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1625-1737 |
2.73e-57 |
|
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.
Pssm-ID: 128421 Cd Length: 114 Bit Score: 193.76 E-value: 2.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1625 TRIIALHSQSMSIPDCPGGWEEMWTGYSYFMSTLdNVGGVGQNLVSPGSCLEEFRAQPVIECHGHGRCNYYD-ALASFWL 1703
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTG-NGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASrNDYSFWL 79
|
90 100 110
....*....|....*....|....*....|....*
gi 442626069 1704 TVIEEQDQFVQPRQQTLKA-DFTSKISRCTVCRRR 1737
Cdd:smart00111 80 STIEPSDQFTAPRPMTPKAgDLRPYISRCQVCEKP 114
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1515-1624 |
2.02e-55 |
|
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.
Pssm-ID: 128421 Cd Length: 114 Bit Score: 188.37 E-value: 2.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1515 GFIFARHSQSVHVPQCPANTNLLWEGYSLSGNVAASRAVGQDLGQSGSCMMRFTTMPYMLCDITNVCHFAQNNDDSLWLS 1594
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80
|
90 100 110
....*....|....*....|....*....|....*
gi 442626069 1595 TAEP-----MPMTMTPIQGrDLMKYISRCVVCETT 1624
Cdd:smart00111 81 TIEPsdqftAPRPMTPKAG-DLRPYISRCQVCEKP 114
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1516-1623 |
2.08e-54 |
|
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.
Pssm-ID: 460201 Cd Length: 110 Bit Score: 185.11 E-value: 2.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1516 FIFARHSQSVHVPQCPANTNLLWEGYSLSGNVAASRAVGQDLGQSGSCMMRFTTMPYMLCDITNVCHFAQnNDDSLWLST 1595
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|.
gi 442626069 1596 AE---PMPMTMTPIQGRDLMKYISRCVVCET 1623
Cdd:pfam01413 80 VEeqfRKPMSQTPKAGNELRSYISRCVVCEA 110
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1626-1736 |
2.05e-53 |
|
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.
Pssm-ID: 460201 Cd Length: 110 Bit Score: 182.41 E-value: 2.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1626 RIIALHSQSMSIPDCPGGWEEMWTGYSYFMSTLDNVGGvGQNLVSPGSCLEEFRAQPVIECHGHGRCNYYDALASFWLTV 1705
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGH-GQDLGSPGSCLERFRTMPFIECNGNGTCNYASNDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|...
gi 442626069 1706 IEEqdQFVQPRQQTLKAD--FTSKISRCTVCRR 1736
Cdd:pfam01413 80 VEE--QFRKPMSQTPKAGneLRSYISRCVVCEA 110
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
894-1132 |
1.99e-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: 126.94 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 894 GAKGQKGEVGSLGQNGQNGAKGSIGFSGRRGLLGNAGLQGLPGSPGIPGLPGMIGEIGERGEIGYNGRQGDIGPRGPNGE 973
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 974 FGPKGLSGDDGPDGYPGANGLPGRKGETGNPGFPGRP-----GAKGVAAYSGIKGDDGESGLTGPIGYPGAPGAKGQRGP 1048
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1049 VGDsqpalDGVAGRKGEVGSPGPNGLPGRHGLKGQRGDRGLPGQQGRPGEPGAKGLGGYPGRNginglkGATGFPGPQGP 1128
Cdd:NF038329 277 DGE-----RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD------GQPGKPAPKTP 345
|
....
gi 442626069 1129 KGPQ 1132
Cdd:NF038329 346 EVPQ 349
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
637-871 |
3.73e-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: 126.17 E-value: 3.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 637 DGSKGERGETGQRGDYGDAGYQGRDGEPGRDGRDGAPGRNATTPKVYLIGEPGYDGIKGERGDDGDTGFKGVKGEpnpgq 716
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE----- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 717 iydnTGEPGEDGYTGPKGVKGAKGEQGAIGLRGEIGDRGPAGEVIPGPVGAKGYPGPTGDYGQQGAPGLPGRDGEPGLDG 796
Cdd:NF038329 191 ----KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626069 797 GIGYKGQRGVPGQeviQGEIGPPGRSGIKGFPGDVGAPGQYGLAGRPGPKGVKGEQGPDGAVGQTGLPGNKGQRG 871
Cdd:NF038329 267 EAGPDGPDGKDGE---RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
465-712 |
2.56e-28 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 120.40 E-value: 2.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 465 LEGYRGDRGEVGLPGDKGLPGEgynivgppgsqgppgfrglPGDDGYNGLRGLPGEKGLRGDDCPVCNAGPRGPRGQEGD 544
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGP-------------------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 545 TGYPGSHGNRGAIGLTGPRGVQGLQGNPGRAGHKGLPGPAGIPGEPGKVGAAGPDGKAievgslRKGEIGDTGDSGHRGD 624
Cdd:NF038329 176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG------QQGPDGDPGPTGEDGP 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 625 TGDDGEKGRDGSDGSKGERGETGQRGDYGDAGYQGRDGEPGRDGRDGAPGRNATTPKVYLIGEPGYDGIKGERGDDGDTG 704
Cdd:NF038329 250 QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
|
....*...
gi 442626069 705 FKGVKGEP 712
Cdd:NF038329 330 KDGKDGQP 337
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
63-349 |
3.14e-28 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 120.40 E-value: 3.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 63 GDIGPPGRAGPLGEKGDVGEYGEQGEKGHRGDIGPKGEMGYPGIMGKSGEPGTPGPRGIDGCDGRPGMQGPSGAPGQNGV 142
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 143 RGPPGKPGQQgppgeagegginskgtkgnrgetgqpggvgppgfdgdrGSKGDTGYAGLTGEKGDPGLPGPKGDtgavse 222
Cdd:NF038329 197 RGETGPAGEQ--------------------------------------GPAGPAGPDGEAGPAGEDGPAGPAGD------ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 223 lpysliGPPGAKGEPGDslsgvlkpddtlkgykgyVGLQGDEGPQGPTGEQGAVGRNGLPGARGEIGGPGERGKPGKDGE 302
Cdd:NF038329 233 ------GQQGPDGDPGP------------------TGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK 288
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 442626069 303 PGRFGDKGMKGAPGWTGADGLDGSPGERGEDGFTGMPGVQGGAGPPG 349
Cdd:NF038329 289 DGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1078-1342 |
3.81e-28 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 120.01 E-value: 3.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1078 HGLKGQRGDRGLPGQQGRPGEPGAKGLGGYPGRNGINGLKGATGFPGPQGPKGPQGESGVVGLDGRNGQIGDQGPRGlig 1157
Cdd:NF038329 113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG--- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1158 eqgeqgeqgdegevgipgrlenlrdrsfYRGFTGDQGLQGERGEQGDMGPIGFIGPPGAKGERGDIGYAGQlGFDGAEGL 1237
Cdd:NF038329 190 ----------------------------EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGD 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1238 KGFQGDQGPRGPPGitLPAEKGDEGVAGLDGRAGRPGHFGQKGAPGPPGENGPNGAIGhrgpqIQGPPGPQGDVGFPGAP 1317
Cdd:NF038329 241 PGPTGEDGPQGPDG--PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG-----LPGKDGKDGQNGKDGLP 313
|
250 260
....*....|....*....|....*
gi 442626069 1318 GHNGRHGLIGPKGELGDMGRQGERG 1342
Cdd:NF038329 314 GKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
542-809 |
4.33e-28 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 120.01 E-value: 4.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 542 EGDTGYPGSHGNRGAIGLTGPRGVQGLQGNPGRAGHKGLPGPAGIPGEPGKVGAAGPDGKAievgslrkgeigdtgdsgh 621
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA------------------- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 622 rGDTGDDGEKGRDGSDGSKGERGETGQRGDYGDAGYQGRDGEPGRDGRDGAPGrnattpkvyligePGYDGIKGERGDDG 701
Cdd:NF038329 177 -GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG-------------PAGDGQQGPDGDPG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 702 DTGFKGVKGEpnpgqiydnTGEPGEDgytGPKGVKGAKGEQGAIGLRGEIGDRGPAGEviPGPVGAKGYPGPTGDYGQQG 781
Cdd:NF038329 243 PTGEDGPQGP---------DGPAGKD---GPRGDRGEAGPDGPDGKDGERGPVGPAGK--DGQNGKDGLPGKDGKDGQNG 308
|
250 260
....*....|....*....|....*...
gi 442626069 782 APGLPGRDGEPGLDGGIGYKGQRGVPGQ 809
Cdd:NF038329 309 KDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
813-1047 |
6.20e-28 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 119.24 E-value: 6.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 813 QGEIGPPGRSGIKGFPGDVGAPGQYGLAGRPGPKGVKGEQGPDGAVGQTGLPGNKGQRGDflvgppgpkgqpgrNGRQAP 892
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK--------------DGEAGA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 893 HGAKGQKGEVGSLGQNGQNGAKGSIGFSGRRGLLGNAGLQGLPGSPGIpglpgmiGEIGERGEIGYNGRQGDIGPRGPNG 972
Cdd:NF038329 185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------GQQGPDGDPGPTGEDGPQGPDGPAG 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 973 EFGPKGLSGDDGPDGYPGAN------GLPGRKGETGNPGFPGRPGAKGVAAYSGIKGDDGESGLTGPIGYPGAPGAKGQR 1046
Cdd:NF038329 258 KDGPRGDRGEAGPDGPDGKDgergpvGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
|
.
gi 442626069 1047 G 1047
Cdd:NF038329 338 G 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
45-307 |
6.07e-27 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 116.54 E-value: 6.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 45 GRMGAPGPIGVPGLEGPAGDIGPPGRAGPLGEKGDVGEYGEQGEKGHRGdigPKGEMGYPGIMGKSGEPGTPGPRGIDGC 124
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG---PQGEAGPQGPAGKDGEAGAKGPAGEKGP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 125 DGRPGMQGPSGAPGQNGVRGPPGKPGQQGPPGEAGEGGINSKGTKGNRGETGQPggvgppgfdgdrGSKGDTGYAGLTGE 204
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGED------------GPQGPDGPAGKDGP 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 205 KGDPGLPGPKGDTGAVselpysliGPPGAKGEPGDSlsgvlkpddtlkgykgyvGLQGDEGPQGPTGEQGAVGRNGLPGA 284
Cdd:NF038329 262 RGDRGEAGPDGPDGKD--------GERGPVGPAGKD------------------GQNGKDGLPGKDGKDGQNGKDGLPGK 315
|
250 260
....*....|....*....|...
gi 442626069 285 RGEIGGPGERGKPGKDGEPGRFG 307
Cdd:NF038329 316 DGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
766-1014 |
1.21e-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: 115.39 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 766 GAKGYPGPTGDYGQQGAPGLPGRDGEPGLDGGIGYKGQRGVPGQeviQGEIGPPGRSGIKGFPGDVGAPGQYGLAGRPGP 845
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE---KGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 846 KGVKGEQGPDGAVGQTGLPGNKGQrgdflvgppgpkgqpgrNGRQAPHGAKGQKGEvgslGQNGQNGAKGSIGFSGRRGL 925
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGE-----------------AGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGP 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 926 LGNAGLQGLPGSPGIPGLPGMIGEIGERGEIGyngrqgdigPRGPNGEFGPKGLSGDDGPDGYPGANGLPGRKGETGNPG 1005
Cdd:NF038329 253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVG---------PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323
|
....*....
gi 442626069 1006 FPGRPGAKG 1014
Cdd:NF038329 324 KDGLPGKDG 332
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1228-1515 |
1.88e-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: 115.00 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1228 QLGFDGAEGLKGFQGDQGPRGPPGitlpaEKGDEGVAGLDGRAGRPGHFGQKGAPGPPGENGPNGAIGHRGPQiqGPPGP 1307
Cdd:NF038329 112 QLKGDGEKGEPGPAGPAGPAGEQG-----PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD--GEAGA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1308 QGDVGFPGAPGHNGRHGLIGPKGELGDMGRQGERGESGYAIVGRQGDIGDIGFQGEPGWDGAKGEQGYPGLPGKNGRVGA 1387
Cdd:NF038329 185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1388 PGPRGPTGDAGWGGIDGMDGLVGPKGQPGvtysysmarpgDRGEPGLDGFQGEEGDGGAPGLIGFQGQRGAVGYRGDQGE 1467
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNG-----------KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 442626069 1468 VGYTGADGPQGQRGDKGYMGLTGAPGLRGLPGPQGEPAPAPPAPKSRG 1515
Cdd:NF038329 334 DGQPGKPAPKTPEVPQKPDTAPHTPKTPQIPGQSKDVTPAPQNPSNRG 381
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
957-1221 |
2.36e-25 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 111.54 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 957 GYNGRQGDIGPRGPNGEFGPKGLSGDDGPDGYPGANGLPGRKGETGNPGFPGRPGAKGVAaysgikGDDGESGLTGPIGY 1036
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA------GKDGEAGAKGPAGE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1037 PGAPGAKGQRGPVGDSQPalDGVAGRKGEVGSPGPNGLPGRHGlKGQRGDRGLPGQQGRPGEPGAKGLggyPGRNGINGL 1116
Cdd:NF038329 191 KGPQGPRGETGPAGEQGP--AGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGP---AGKDGPRGD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1117 KGATGFPGPQGPKGPQGESGVVGLDGRNGQIGDQGPRGligeqgeqgeqgdegevgipgrlenlrdrsfYRGFTGDQGLQ 1196
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG-------------------------------KDGQNGKDGLP 313
|
250 260
....*....|....*....|....*
gi 442626069 1197 GERGEQGDMGPIGFIGPPGAKGERG 1221
Cdd:NF038329 314 GKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
398-682 |
1.21e-24 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 109.22 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 398 DPGLNGSRGPPGRSERGEAGDYGFIGPPGPQGPPGEAGLPGRYGLHGEPGQNvvGPKGEPGLNGQPGLEGYRGDRGEVGL 477
Cdd:NF038329 107 DEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGER--GEKGPAGPQGEAGPQGPAGKDGEAGA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 478 PGDkglpgegynivgppgsqgppgfrglPGDDGYNGLRGLPGEKGLRGDDcpvcnaGPRGPRGQEGDTGYPGSHGNRGAi 557
Cdd:NF038329 185 KGP-------------------------AGEKGPQGPRGETGPAGEQGPA------GPAGPDGEAGPAGEDGPAGPAGD- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 558 GLTGPRGVQGLQGNPGRAGHKGLPGPAGIPGEPGKVGAAGPDGKAievgslrkGEIGDTGDSGHRGDTGDDGEKGRDGSD 637
Cdd:NF038329 233 GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD--------GERGPVGPAGKDGQNGKDGLPGKDGKD 304
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 442626069 638 GSKGERGETGQRgdyGDAGYQGRDGEPGRDGRDGAPGRNA-TTPKV 682
Cdd:NF038329 305 GQNGKDGLPGKD---GKDGQPGKDGLPGKDGKDGQPGKPApKTPEV 347
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
256-485 |
2.32e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 102.29 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 256 GYVGLQGDEGPQGPTGEQGAVGRNGLPGARGEIGGPGERGKPGKDGEPGRFGDKGMKGAPGWTGADGLDGSPGERGEDGF 335
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 336 TGMPGVQGGAGPPGIYDPSLTKSLPGPIGSQGdigppgeqgppglPGKPGRRGPIGLAGQSGDPGLNGSRGPPGRSerGE 415
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG-------------PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKD--GP 261
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 416 AGDYGFIGPPGPQGPPGEAGLPGRYGLHGEPGQNvvGPKGEPGLNGQPGLEGYRGDRGEVGLPGDKGLPG 485
Cdd:NF038329 262 RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKD--GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
290-578 |
1.64e-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: 96.90 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 290 GPGERGKPGKDGEPGRFGDKGMKGAPGWTGADGLDGSPGERGEDGFTGMPGVQGGAGPPGiydpsltksLPGPIGSQGDi 369
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG---------PAGKDGEAGA- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 370 gppgeQGPPGLPGKPGRRGPIGLAGQSGDPGLNGSRGppgrsergeagdygfigppgpqgppgEAGLPGRYGLHGEPGQN 449
Cdd:NF038329 185 -----KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG--------------------------EAGPAGEDGPAGPAGDG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 450 VVGPKGEPGLNGQPGLEGYRGDRGEVGLPGDKGLPGEgynivgppgsqgppgfRGLPGDDGYNGLRGLPGEKGLRGDDCP 529
Cdd:NF038329 234 QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP----------------DGPDGKDGERGPVGPAGKDGQNGKDGL 297
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 442626069 530 vcnAGPRGPRGQEGDTGYPGSHGNRGAIGLTGPRGVQGLQGNPGRAGHK 578
Cdd:NF038329 298 ---PGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
41-238 |
6.64e-18 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 88.81 E-value: 6.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 41 KGIKGRMGAPGPIGVPGLEGPAGDIGPPGRAGPLGEKGDVGEYGEQGEKGHRGDIGPKGEMGYPGIMGKSGEpGTPGPRG 120
Cdd:NF038329 161 KGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDG 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 121 IDGCDGRPGMQGPSGAPGQNGVRGPPGKPGQQGPPGEAgegginskGTKGNRGETGQPGGVGPPGFDGDRGSKGDTGYAG 200
Cdd:NF038329 240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD--------GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
|
170 180 190
....*....|....*....|....*....|....*...
gi 442626069 201 LTGEKGDPGLPGPKGdtgavselpysLIGPPGAKGEPG 238
Cdd:NF038329 312 LPGKDGKDGQPGKDG-----------LPGKDGKDGQPG 338
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
609-769 |
2.72e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 51.90 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 609 RKGEIGDTGDSGHRGDTGDDGEKGRDGSDGSKGERGETGQRGDYGDAGyqgrDGEPGRDGRDGAPGrnattpkvyligEP 688
Cdd:PHA03169 86 ERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPAS----HSPPPSPPSHPGPH------------EP 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 689 GYDGIKGERGDDGDTGFKGVKGEPNPGQIYDNTGEPGEDGYTGPKGVKGAKGEQGAIGLRGEIGDRGPAGEVIPGPVGAK 768
Cdd:PHA03169 150 APPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQ 229
|
.
gi 442626069 769 G 769
Cdd:PHA03169 230 A 230
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
1188-1418 |
1.96e-05 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 49.26 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1188 GFTGDQGLQGERGEQGDMGPIGFIGPPGAKGERGDIGYAGQLGFDGAEGLKGFQGDQGPRGPP----GITLPAEKGDEGV 1263
Cdd:COG5164 13 DPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAqnqgGTTPAQNQGGTRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1264 AGLDGRAGRPGHFGQKGAPGPPGENGPNGAIGHRGPQIQGPPGPQGDVG-FPGAPGHNGRHGLIGPKGELGDMGRQGERG 1342
Cdd:COG5164 93 AGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGsTPPGPGSTGPGGSTTPPGDGGSTTPPGPGG 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626069 1343 ESGYAIVGRQGDIGDIGFQGEPGWDGAKGEQGYPGLPGKNGRVGAPGPrgPTGDAGWGGIDGMDGLVGPKGQPGVT 1418
Cdd:COG5164 173 STTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNP--PDDRGGKTGPKDQRPKTNPIERRGPE 246
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
41-119 |
4.15e-05 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 48.36 E-value: 4.15e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626069 41 KGIKGRMGAPGPIGVPGLEGPAGDIGPPGRAGPLGEKGDVGEYGEQGEKGHRGDIGPKGEMGYPGIMGKSGEPGTPGPR 119
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
764-1151 |
3.85e-04 |
|
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.
Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 45.38 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 764 PVGAKGYPGP-----TGDYGQQGAPGLPGRDGEPGldggigyKGQRGVPGQEVIQGEIGPPGRSGIKGFPGDVGAPGQYG 838
Cdd:pfam09606 133 PMGGAGFPSQmsrvgRMQPGGQAGGMMQPSSGQPG-------SGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 839 LAGRPGPkGVKGEQGPDGAVGQTGLPGNKGQRGdflvgppgpkgQPGRNGRQAPHGAKGQKGEVGSLGQNGQNGAKGSig 918
Cdd:pfam09606 206 VPGMPGP-ADAGAQMGQQAQANGGMNPQQMGGA-----------PNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGV-- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 919 fsgrrgllGNAGLQGLPGSPGIPglpgmigeigergeigYNGRQGDIGPRGPNGEFGPKGLSGDDGPDGYPGANGLPGRK 998
Cdd:pfam09606 272 --------GGGAGQGGPGQPMGP----------------PGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 999 GETGNPGFPGrpgakgvaaysgikgddgesGLTGPIGYPGAPGAKGQRGPVGDSQPAldgvAGRKGEVGSPGPNGLPGRH 1078
Cdd:pfam09606 328 QQMNQSVGQG--------------------GQVVALGGLNHLETWNPGNFGGLGANP----MQRGQPGMMSSPSPVPGQQ 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626069 1079 gLKGQRGDRGLPgQQGRPGEPGAKGLGGYPGRNGINGLKGATGF---PGPQGPKGPQGESgVVGLDGRNGQIGDQG 1151
Cdd:pfam09606 384 -VRQVTPNQFMR-QSPQPSVPSPQGPGSQPPQSHPGGMIPSPALipsPSPQMSQQPAQQR-TIGQDSPGGSLNTPG 456
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
561-702 |
9.21e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 44.12 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 561 GPRGVQGLQGNPGRAGHKGLPGPAGIPGEPGKVGAAGPDGKAIEVGSLRK----------GEIGDTGDSGHRGDTGDDGE 630
Cdd:PRK12678 125 AQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRrgdredrqaeAERGERGRREERGRDGDDRD 204
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626069 631 KGRDGSDGSKGERGETGQRGDYGDAGYQGRDGEPGRDGRDGAPGRNATTpkvyliGEPGYDGIKGERGDDGD 702
Cdd:PRK12678 205 RRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGD------DGEGRGGRRGRRFRDRD 270
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
87-361 |
1.42e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 43.48 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 87 GEKGHRGDIGPKGEMGYPGIMGKSGEPGTPGPRGIDGCDGRPGMQGPSGAPGQNGVRGPPGKPGqqgppgeagegginSK 166
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQG--------------AT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 167 GTKGNRGETGQPGGVGPPGFDGDRGSKGDTGYAGLTGEKGDPGLPGPKGDTGAVSELPYSLIGPPGAKGEPgdslsgvlK 246
Cdd:COG5164 73 GPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGST--------P 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 247 PDDTLKGYKGYVGLQGDEGPQGPTGEQGAVGRNGLPGARGEiGGPGERGKPGKDGEPGRFGDKGMKGAPGWTGA-DGLDG 325
Cdd:COG5164 145 PGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTP-PNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKgNPPDD 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 442626069 326 SPGERGEDGFTGMPGVQGGAGPPGIYDPSLTKSLPG 361
Cdd:COG5164 224 RGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTA 259
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
534-590 |
2.04e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 38.24 E-value: 2.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 442626069 534 GPRGPRGQEGDTGYPGSHGNRGAIGLTGPRGVQGLQGNPGRAGHKGLPGPAGIPGEP 590
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
280-334 |
2.39e-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: 2.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 442626069 280 GLPGARGEIGGPGERGKPGKDGEPGRFGDKGMKGAPGWTGADGLDGSPGERGEDG 334
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
314-599 |
2.96e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 42.32 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 314 APGWTGADGLDGSPGERGEDGFTGMPGVQGGAGPPGiydpslTKSLPGPIGSQGDIGPPGEQGPPGLPGKPGRRGPIGLA 393
Cdd:COG5164 5 GPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAG------NTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 394 GQSGDPGLNGSRGPPGRSerGEAGDYGFIGPPGPQGPPGEAGLPGRYGLHGEPGQNVVGPKGEPGLN-GQPGLEGYRGDR 472
Cdd:COG5164 79 GGTTPAQNQGGTRPAGNT--GGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTpPGPGSTGPGGST 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 473 GEVGLPGDKGLPGEGYNIVgppgsqgppgfrglPGDDGYNGLRGLPGEKGLRGDDCPVCNAGPRGPRGQEGDTGYPGSHG 552
Cdd:COG5164 157 TPPGDGGSTTPPGPGGSTT--------------PPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPD 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 442626069 553 NRGAI-GLTGPRGVQGLQGNPGRAGHKGLPGPAGIPGEPGKVGAAGPD 599
Cdd:COG5164 223 DRGGKtGPKDQRPKTNPIERRGPERPEAAALPAELTALEAENRAANPE 270
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
817-871 |
3.12e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.47 E-value: 3.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 442626069 817 GPPGRSGIKGFPGDVGAPGQYGLAGRPGPKGVKGEQGPDGAVGQTGLPGNKGQRG 871
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1625-1737 |
2.73e-57 |
|
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.
Pssm-ID: 128421 Cd Length: 114 Bit Score: 193.76 E-value: 2.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1625 TRIIALHSQSMSIPDCPGGWEEMWTGYSYFMSTLdNVGGVGQNLVSPGSCLEEFRAQPVIECHGHGRCNYYD-ALASFWL 1703
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTG-NGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASrNDYSFWL 79
|
90 100 110
....*....|....*....|....*....|....*
gi 442626069 1704 TVIEEQDQFVQPRQQTLKA-DFTSKISRCTVCRRR 1737
Cdd:smart00111 80 STIEPSDQFTAPRPMTPKAgDLRPYISRCQVCEKP 114
|
|
| C4 |
smart00111 |
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ... |
1515-1624 |
2.02e-55 |
|
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.
Pssm-ID: 128421 Cd Length: 114 Bit Score: 188.37 E-value: 2.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1515 GFIFARHSQSVHVPQCPANTNLLWEGYSLSGNVAASRAVGQDLGQSGSCMMRFTTMPYMLCDITNVCHFAQNNDDSLWLS 1594
Cdd:smart00111 1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80
|
90 100 110
....*....|....*....|....*....|....*
gi 442626069 1595 TAEP-----MPMTMTPIQGrDLMKYISRCVVCETT 1624
Cdd:smart00111 81 TIEPsdqftAPRPMTPKAG-DLRPYISRCQVCEKP 114
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1516-1623 |
2.08e-54 |
|
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.
Pssm-ID: 460201 Cd Length: 110 Bit Score: 185.11 E-value: 2.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1516 FIFARHSQSVHVPQCPANTNLLWEGYSLSGNVAASRAVGQDLGQSGSCMMRFTTMPYMLCDITNVCHFAQnNDDSLWLST 1595
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|.
gi 442626069 1596 AE---PMPMTMTPIQGRDLMKYISRCVVCET 1623
Cdd:pfam01413 80 VEeqfRKPMSQTPKAGNELRSYISRCVVCEA 110
|
|
| C4 |
pfam01413 |
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ... |
1626-1736 |
2.05e-53 |
|
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.
Pssm-ID: 460201 Cd Length: 110 Bit Score: 182.41 E-value: 2.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1626 RIIALHSQSMSIPDCPGGWEEMWTGYSYFMSTLDNVGGvGQNLVSPGSCLEEFRAQPVIECHGHGRCNYYDALASFWLTV 1705
Cdd:pfam01413 1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGH-GQDLGSPGSCLERFRTMPFIECNGNGTCNYASNDYSYWLST 79
|
90 100 110
....*....|....*....|....*....|...
gi 442626069 1706 IEEqdQFVQPRQQTLKAD--FTSKISRCTVCRR 1736
Cdd:pfam01413 80 VEE--QFRKPMSQTPKAGneLRSYISRCVVCEA 110
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
894-1132 |
1.99e-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: 126.94 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 894 GAKGQKGEVGSLGQNGQNGAKGSIGFSGRRGLLGNAGLQGLPGSPGIPGLPGMIGEIGERGEIGYNGRQGDIGPRGPNGE 973
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 974 FGPKGLSGDDGPDGYPGANGLPGRKGETGNPGFPGRP-----GAKGVAAYSGIKGDDGESGLTGPIGYPGAPGAKGQRGP 1048
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1049 VGDsqpalDGVAGRKGEVGSPGPNGLPGRHGLKGQRGDRGLPGQQGRPGEPGAKGLGGYPGRNginglkGATGFPGPQGP 1128
Cdd:NF038329 277 DGE-----RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD------GQPGKPAPKTP 345
|
....
gi 442626069 1129 KGPQ 1132
Cdd:NF038329 346 EVPQ 349
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
637-871 |
3.73e-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: 126.17 E-value: 3.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 637 DGSKGERGETGQRGDYGDAGYQGRDGEPGRDGRDGAPGRNATTPKVYLIGEPGYDGIKGERGDDGDTGFKGVKGEpnpgq 716
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE----- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 717 iydnTGEPGEDGYTGPKGVKGAKGEQGAIGLRGEIGDRGPAGEVIPGPVGAKGYPGPTGDYGQQGAPGLPGRDGEPGLDG 796
Cdd:NF038329 191 ----KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626069 797 GIGYKGQRGVPGQeviQGEIGPPGRSGIKGFPGDVGAPGQYGLAGRPGPKGVKGEQGPDGAVGQTGLPGNKGQRG 871
Cdd:NF038329 267 EAGPDGPDGKDGE---RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
465-712 |
2.56e-28 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 120.40 E-value: 2.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 465 LEGYRGDRGEVGLPGDKGLPGEgynivgppgsqgppgfrglPGDDGYNGLRGLPGEKGLRGDDCPVCNAGPRGPRGQEGD 544
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGP-------------------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 545 TGYPGSHGNRGAIGLTGPRGVQGLQGNPGRAGHKGLPGPAGIPGEPGKVGAAGPDGKAievgslRKGEIGDTGDSGHRGD 624
Cdd:NF038329 176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG------QQGPDGDPGPTGEDGP 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 625 TGDDGEKGRDGSDGSKGERGETGQRGDYGDAGYQGRDGEPGRDGRDGAPGRNATTPKVYLIGEPGYDGIKGERGDDGDTG 704
Cdd:NF038329 250 QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
|
....*...
gi 442626069 705 FKGVKGEP 712
Cdd:NF038329 330 KDGKDGQP 337
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
63-349 |
3.14e-28 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 120.40 E-value: 3.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 63 GDIGPPGRAGPLGEKGDVGEYGEQGEKGHRGDIGPKGEMGYPGIMGKSGEPGTPGPRGIDGCDGRPGMQGPSGAPGQNGV 142
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 143 RGPPGKPGQQgppgeagegginskgtkgnrgetgqpggvgppgfdgdrGSKGDTGYAGLTGEKGDPGLPGPKGDtgavse 222
Cdd:NF038329 197 RGETGPAGEQ--------------------------------------GPAGPAGPDGEAGPAGEDGPAGPAGD------ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 223 lpysliGPPGAKGEPGDslsgvlkpddtlkgykgyVGLQGDEGPQGPTGEQGAVGRNGLPGARGEIGGPGERGKPGKDGE 302
Cdd:NF038329 233 ------GQQGPDGDPGP------------------TGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK 288
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 442626069 303 PGRFGDKGMKGAPGWTGADGLDGSPGERGEDGFTGMPGVQGGAGPPG 349
Cdd:NF038329 289 DGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1078-1342 |
3.81e-28 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 120.01 E-value: 3.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1078 HGLKGQRGDRGLPGQQGRPGEPGAKGLGGYPGRNGINGLKGATGFPGPQGPKGPQGESGVVGLDGRNGQIGDQGPRGlig 1157
Cdd:NF038329 113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG--- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1158 eqgeqgeqgdegevgipgrlenlrdrsfYRGFTGDQGLQGERGEQGDMGPIGFIGPPGAKGERGDIGYAGQlGFDGAEGL 1237
Cdd:NF038329 190 ----------------------------EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGD 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1238 KGFQGDQGPRGPPGitLPAEKGDEGVAGLDGRAGRPGHFGQKGAPGPPGENGPNGAIGhrgpqIQGPPGPQGDVGFPGAP 1317
Cdd:NF038329 241 PGPTGEDGPQGPDG--PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG-----LPGKDGKDGQNGKDGLP 313
|
250 260
....*....|....*....|....*
gi 442626069 1318 GHNGRHGLIGPKGELGDMGRQGERG 1342
Cdd:NF038329 314 GKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
542-809 |
4.33e-28 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 120.01 E-value: 4.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 542 EGDTGYPGSHGNRGAIGLTGPRGVQGLQGNPGRAGHKGLPGPAGIPGEPGKVGAAGPDGKAievgslrkgeigdtgdsgh 621
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA------------------- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 622 rGDTGDDGEKGRDGSDGSKGERGETGQRGDYGDAGYQGRDGEPGRDGRDGAPGrnattpkvyligePGYDGIKGERGDDG 701
Cdd:NF038329 177 -GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG-------------PAGDGQQGPDGDPG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 702 DTGFKGVKGEpnpgqiydnTGEPGEDgytGPKGVKGAKGEQGAIGLRGEIGDRGPAGEviPGPVGAKGYPGPTGDYGQQG 781
Cdd:NF038329 243 PTGEDGPQGP---------DGPAGKD---GPRGDRGEAGPDGPDGKDGERGPVGPAGK--DGQNGKDGLPGKDGKDGQNG 308
|
250 260
....*....|....*....|....*...
gi 442626069 782 APGLPGRDGEPGLDGGIGYKGQRGVPGQ 809
Cdd:NF038329 309 KDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
813-1047 |
6.20e-28 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 119.24 E-value: 6.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 813 QGEIGPPGRSGIKGFPGDVGAPGQYGLAGRPGPKGVKGEQGPDGAVGQTGLPGNKGQRGDflvgppgpkgqpgrNGRQAP 892
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK--------------DGEAGA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 893 HGAKGQKGEVGSLGQNGQNGAKGSIGFSGRRGLLGNAGLQGLPGSPGIpglpgmiGEIGERGEIGYNGRQGDIGPRGPNG 972
Cdd:NF038329 185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------GQQGPDGDPGPTGEDGPQGPDGPAG 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 973 EFGPKGLSGDDGPDGYPGAN------GLPGRKGETGNPGFPGRPGAKGVAAYSGIKGDDGESGLTGPIGYPGAPGAKGQR 1046
Cdd:NF038329 258 KDGPRGDRGEAGPDGPDGKDgergpvGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
|
.
gi 442626069 1047 G 1047
Cdd:NF038329 338 G 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
45-307 |
6.07e-27 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 116.54 E-value: 6.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 45 GRMGAPGPIGVPGLEGPAGDIGPPGRAGPLGEKGDVGEYGEQGEKGHRGdigPKGEMGYPGIMGKSGEPGTPGPRGIDGC 124
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG---PQGEAGPQGPAGKDGEAGAKGPAGEKGP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 125 DGRPGMQGPSGAPGQNGVRGPPGKPGQQGPPGEAGEGGINSKGTKGNRGETGQPggvgppgfdgdrGSKGDTGYAGLTGE 204
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGED------------GPQGPDGPAGKDGP 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 205 KGDPGLPGPKGDTGAVselpysliGPPGAKGEPGDSlsgvlkpddtlkgykgyvGLQGDEGPQGPTGEQGAVGRNGLPGA 284
Cdd:NF038329 262 RGDRGEAGPDGPDGKD--------GERGPVGPAGKD------------------GQNGKDGLPGKDGKDGQNGKDGLPGK 315
|
250 260
....*....|....*....|...
gi 442626069 285 RGEIGGPGERGKPGKDGEPGRFG 307
Cdd:NF038329 316 DGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
766-1014 |
1.21e-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: 115.39 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 766 GAKGYPGPTGDYGQQGAPGLPGRDGEPGLDGGIGYKGQRGVPGQeviQGEIGPPGRSGIKGFPGDVGAPGQYGLAGRPGP 845
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE---KGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 846 KGVKGEQGPDGAVGQTGLPGNKGQrgdflvgppgpkgqpgrNGRQAPHGAKGQKGEvgslGQNGQNGAKGSIGFSGRRGL 925
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGE-----------------AGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGP 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 926 LGNAGLQGLPGSPGIPGLPGMIGEIGERGEIGyngrqgdigPRGPNGEFGPKGLSGDDGPDGYPGANGLPGRKGETGNPG 1005
Cdd:NF038329 253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVG---------PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323
|
....*....
gi 442626069 1006 FPGRPGAKG 1014
Cdd:NF038329 324 KDGLPGKDG 332
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
1228-1515 |
1.88e-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: 115.00 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1228 QLGFDGAEGLKGFQGDQGPRGPPGitlpaEKGDEGVAGLDGRAGRPGHFGQKGAPGPPGENGPNGAIGHRGPQiqGPPGP 1307
Cdd:NF038329 112 QLKGDGEKGEPGPAGPAGPAGEQG-----PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD--GEAGA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1308 QGDVGFPGAPGHNGRHGLIGPKGELGDMGRQGERGESGYAIVGRQGDIGDIGFQGEPGWDGAKGEQGYPGLPGKNGRVGA 1387
Cdd:NF038329 185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1388 PGPRGPTGDAGWGGIDGMDGLVGPKGQPGvtysysmarpgDRGEPGLDGFQGEEGDGGAPGLIGFQGQRGAVGYRGDQGE 1467
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNG-----------KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 442626069 1468 VGYTGADGPQGQRGDKGYMGLTGAPGLRGLPGPQGEPAPAPPAPKSRG 1515
Cdd:NF038329 334 DGQPGKPAPKTPEVPQKPDTAPHTPKTPQIPGQSKDVTPAPQNPSNRG 381
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
957-1221 |
2.36e-25 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 111.54 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 957 GYNGRQGDIGPRGPNGEFGPKGLSGDDGPDGYPGANGLPGRKGETGNPGFPGRPGAKGVAaysgikGDDGESGLTGPIGY 1036
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA------GKDGEAGAKGPAGE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1037 PGAPGAKGQRGPVGDSQPalDGVAGRKGEVGSPGPNGLPGRHGlKGQRGDRGLPGQQGRPGEPGAKGLggyPGRNGINGL 1116
Cdd:NF038329 191 KGPQGPRGETGPAGEQGP--AGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGP---AGKDGPRGD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1117 KGATGFPGPQGPKGPQGESGVVGLDGRNGQIGDQGPRGligeqgeqgeqgdegevgipgrlenlrdrsfYRGFTGDQGLQ 1196
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG-------------------------------KDGQNGKDGLP 313
|
250 260
....*....|....*....|....*
gi 442626069 1197 GERGEQGDMGPIGFIGPPGAKGERG 1221
Cdd:NF038329 314 GKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
398-682 |
1.21e-24 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 109.22 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 398 DPGLNGSRGPPGRSERGEAGDYGFIGPPGPQGPPGEAGLPGRYGLHGEPGQNvvGPKGEPGLNGQPGLEGYRGDRGEVGL 477
Cdd:NF038329 107 DEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGER--GEKGPAGPQGEAGPQGPAGKDGEAGA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 478 PGDkglpgegynivgppgsqgppgfrglPGDDGYNGLRGLPGEKGLRGDDcpvcnaGPRGPRGQEGDTGYPGSHGNRGAi 557
Cdd:NF038329 185 KGP-------------------------AGEKGPQGPRGETGPAGEQGPA------GPAGPDGEAGPAGEDGPAGPAGD- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 558 GLTGPRGVQGLQGNPGRAGHKGLPGPAGIPGEPGKVGAAGPDGKAievgslrkGEIGDTGDSGHRGDTGDDGEKGRDGSD 637
Cdd:NF038329 233 GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD--------GERGPVGPAGKDGQNGKDGLPGKDGKD 304
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 442626069 638 GSKGERGETGQRgdyGDAGYQGRDGEPGRDGRDGAPGRNA-TTPKV 682
Cdd:NF038329 305 GQNGKDGLPGKD---GKDGQPGKDGLPGKDGKDGQPGKPApKTPEV 347
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
256-485 |
2.32e-22 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 102.29 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 256 GYVGLQGDEGPQGPTGEQGAVGRNGLPGARGEIGGPGERGKPGKDGEPGRFGDKGMKGAPGWTGADGLDGSPGERGEDGF 335
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 336 TGMPGVQGGAGPPGIYDPSLTKSLPGPIGSQGdigppgeqgppglPGKPGRRGPIGLAGQSGDPGLNGSRGPPGRSerGE 415
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG-------------PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKD--GP 261
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 416 AGDYGFIGPPGPQGPPGEAGLPGRYGLHGEPGQNvvGPKGEPGLNGQPGLEGYRGDRGEVGLPGDKGLPG 485
Cdd:NF038329 262 RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKD--GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
290-578 |
1.64e-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: 96.90 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 290 GPGERGKPGKDGEPGRFGDKGMKGAPGWTGADGLDGSPGERGEDGFTGMPGVQGGAGPPGiydpsltksLPGPIGSQGDi 369
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQG---------PAGKDGEAGA- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 370 gppgeQGPPGLPGKPGRRGPIGLAGQSGDPGLNGSRGppgrsergeagdygfigppgpqgppgEAGLPGRYGLHGEPGQN 449
Cdd:NF038329 185 -----KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDG--------------------------EAGPAGEDGPAGPAGDG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 450 VVGPKGEPGLNGQPGLEGYRGDRGEVGLPGDKGLPGEgynivgppgsqgppgfRGLPGDDGYNGLRGLPGEKGLRGDDCP 529
Cdd:NF038329 234 QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP----------------DGPDGKDGERGPVGPAGKDGQNGKDGL 297
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 442626069 530 vcnAGPRGPRGQEGDTGYPGSHGNRGAIGLTGPRGVQGLQGNPGRAGHK 578
Cdd:NF038329 298 ---PGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
41-238 |
6.64e-18 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 88.81 E-value: 6.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 41 KGIKGRMGAPGPIGVPGLEGPAGDIGPPGRAGPLGEKGDVGEYGEQGEKGHRGDIGPKGEMGYPGIMGKSGEpGTPGPRG 120
Cdd:NF038329 161 KGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDG 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 121 IDGCDGRPGMQGPSGAPGQNGVRGPPGKPGQQGPPGEAgegginskGTKGNRGETGQPGGVGPPGFDGDRGSKGDTGYAG 200
Cdd:NF038329 240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD--------GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
|
170 180 190
....*....|....*....|....*....|....*...
gi 442626069 201 LTGEKGDPGLPGPKGdtgavselpysLIGPPGAKGEPG 238
Cdd:NF038329 312 LPGKDGKDGQPGKDG-----------LPGKDGKDGQPG 338
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
609-769 |
2.72e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 51.90 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 609 RKGEIGDTGDSGHRGDTGDDGEKGRDGSDGSKGERGETGQRGDYGDAGyqgrDGEPGRDGRDGAPGrnattpkvyligEP 688
Cdd:PHA03169 86 ERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPAS----HSPPPSPPSHPGPH------------EP 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 689 GYDGIKGERGDDGDTGFKGVKGEPNPGQIYDNTGEPGEDGYTGPKGVKGAKGEQGAIGLRGEIGDRGPAGEVIPGPVGAK 768
Cdd:PHA03169 150 APPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQ 229
|
.
gi 442626069 769 G 769
Cdd:PHA03169 230 A 230
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
1188-1418 |
1.96e-05 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 49.26 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1188 GFTGDQGLQGERGEQGDMGPIGFIGPPGAKGERGDIGYAGQLGFDGAEGLKGFQGDQGPRGPP----GITLPAEKGDEGV 1263
Cdd:COG5164 13 DPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAqnqgGTTPAQNQGGTRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 1264 AGLDGRAGRPGHFGQKGAPGPPGENGPNGAIGHRGPQIQGPPGPQGDVG-FPGAPGHNGRHGLIGPKGELGDMGRQGERG 1342
Cdd:COG5164 93 AGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGsTPPGPGSTGPGGSTTPPGDGGSTTPPGPGG 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626069 1343 ESGYAIVGRQGDIGDIGFQGEPGWDGAKGEQGYPGLPGKNGRVGAPGPrgPTGDAGWGGIDGMDGLVGPKGQPGVT 1418
Cdd:COG5164 173 STTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNP--PDDRGGKTGPKDQRPKTNPIERRGPE 246
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
41-119 |
4.15e-05 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 48.36 E-value: 4.15e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626069 41 KGIKGRMGAPGPIGVPGLEGPAGDIGPPGRAGPLGEKGDVGEYGEQGEKGHRGDIGPKGEMGYPGIMGKSGEPGTPGPR 119
Cdd:NF038329 265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
618-810 |
1.75e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 46.12 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 618 DSGHRgDTGDDGEKGRDGSDGSKGERGETGQRGDyGDAGYQGRDGEPGRDGRDGAPGrnattpkvyliGEPGYDGIKGER 697
Cdd:PHA03169 63 EQGHR-QTESDTETAEESRHGEKEERGQGGPSGS-GSESVGSPTPSPSGSAEELASG-----------LSPENTSGSSPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 698 GDDGDTGFKGVKGEPNPGqiydntgEPGEDGYTGPKGVKGAKGEQGAIGLRGEIGDRGPAGEVIPGPVGAKGYPGPTGDY 777
Cdd:PHA03169 130 SPASHSPPPSPPSHPGPH-------EPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSP 202
|
170 180 190
....*....|....*....|....*....|...
gi 442626069 778 GQQGAPGLPGRDGEPGLDGGIGYKGQRGVPGQE 810
Cdd:PHA03169 203 PPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHED 235
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
764-1151 |
3.85e-04 |
|
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.
Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 45.38 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 764 PVGAKGYPGP-----TGDYGQQGAPGLPGRDGEPGldggigyKGQRGVPGQEVIQGEIGPPGRSGIKGFPGDVGAPGQYG 838
Cdd:pfam09606 133 PMGGAGFPSQmsrvgRMQPGGQAGGMMQPSSGQPG-------SGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 839 LAGRPGPkGVKGEQGPDGAVGQTGLPGNKGQRGdflvgppgpkgQPGRNGRQAPHGAKGQKGEVGSLGQNGQNGAKGSig 918
Cdd:pfam09606 206 VPGMPGP-ADAGAQMGQQAQANGGMNPQQMGGA-----------PNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGV-- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 919 fsgrrgllGNAGLQGLPGSPGIPglpgmigeigergeigYNGRQGDIGPRGPNGEFGPKGLSGDDGPDGYPGANGLPGRK 998
Cdd:pfam09606 272 --------GGGAGQGGPGQPMGP----------------PGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 999 GETGNPGFPGrpgakgvaaysgikgddgesGLTGPIGYPGAPGAKGQRGPVGDSQPAldgvAGRKGEVGSPGPNGLPGRH 1078
Cdd:pfam09606 328 QQMNQSVGQG--------------------GQVVALGGLNHLETWNPGNFGGLGANP----MQRGQPGMMSSPSPVPGQQ 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626069 1079 gLKGQRGDRGLPgQQGRPGEPGAKGLGGYPGRNGINGLKGATGF---PGPQGPKGPQGESgVVGLDGRNGQIGDQG 1151
Cdd:pfam09606 384 -VRQVTPNQFMR-QSPQPSVPSPQGPGSQPPQSHPGGMIPSPALipsPSPQMSQQPAQQR-TIGQDSPGGSLNTPG 456
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
960-1014 |
4.28e-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: 4.28e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 442626069 960 GRQGDIGPRGPNGEFGPKGLSGDDGPDGYPGANGLPGRKGETGNPGFPGRPGAKG 1014
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
561-702 |
9.21e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 44.12 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 561 GPRGVQGLQGNPGRAGHKGLPGPAGIPGEPGKVGAAGPDGKAIEVGSLRK----------GEIGDTGDSGHRGDTGDDGE 630
Cdd:PRK12678 125 AQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRrgdredrqaeAERGERGRREERGRDGDDRD 204
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626069 631 KGRDGSDGSKGERGETGQRGDYGDAGYQGRDGEPGRDGRDGAPGRNATTpkvyliGEPGYDGIKGERGDDGD 702
Cdd:PRK12678 205 RRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGD------DGEGRGGRRGRRFRDRD 270
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1079-1134 |
9.68e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.01 E-value: 9.68e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 442626069 1079 GLKGQRGDRGLPGQQGRPGEPGAKGLGGYPGRNGINGLKGATGFPGPQGPKGPQGE 1134
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
87-361 |
1.42e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 43.48 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 87 GEKGHRGDIGPKGEMGYPGIMGKSGEPGTPGPRGIDGCDGRPGMQGPSGAPGQNGVRGPPGKPGqqgppgeagegginSK 166
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQG--------------AT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 167 GTKGNRGETGQPGGVGPPGFDGDRGSKGDTGYAGLTGEKGDPGLPGPKGDTGAVSELPYSLIGPPGAKGEPgdslsgvlK 246
Cdd:COG5164 73 GPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGST--------P 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 247 PDDTLKGYKGYVGLQGDEGPQGPTGEQGAVGRNGLPGARGEiGGPGERGKPGKDGEPGRFGDKGMKGAPGWTGA-DGLDG 325
Cdd:COG5164 145 PGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTP-PNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKgNPPDD 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 442626069 326 SPGERGEDGFTGMPGVQGGAGPPGIYDPSLTKSLPG 361
Cdd:COG5164 224 RGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTA 259
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1064-1119 |
1.55e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 38.24 E-value: 1.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 442626069 1064 GEVGSPGPNGLPGRHGLKGQRGDRGLPGQQGRPGEPGAKGLGGYPGRNGINGLKGA 1119
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
534-590 |
2.04e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 38.24 E-value: 2.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 442626069 534 GPRGPRGQEGDTGYPGSHGNRGAIGLTGPRGVQGLQGNPGRAGHKGLPGPAGIPGEP 590
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
280-334 |
2.39e-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: 2.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 442626069 280 GLPGARGEIGGPGERGKPGKDGEPGRFGDKGMKGAPGWTGADGLDGSPGERGEDG 334
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1082-1136 |
2.62e-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: 2.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 442626069 1082 GQRGDRGLPGQQGRPGEPGAKGLGGYPGRNGINGLKGATGFPGPQGPKGPQGESG 1136
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
66-120 |
2.75e-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: 2.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 442626069 66 GPPGRAGPLGEKGDVGEYGEQGEKGHRGDIGPKGEMGYPGIMGKSGEPGTPGPRG 120
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
314-599 |
2.96e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 42.32 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 314 APGWTGADGLDGSPGERGEDGFTGMPGVQGGAGPPGiydpslTKSLPGPIGSQGDIGPPGEQGPPGLPGKPGRRGPIGLA 393
Cdd:COG5164 5 GPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAG------NTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 394 GQSGDPGLNGSRGPPGRSerGEAGDYGFIGPPGPQGPPGEAGLPGRYGLHGEPGQNVVGPKGEPGLN-GQPGLEGYRGDR 472
Cdd:COG5164 79 GGTTPAQNQGGTRPAGNT--GGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTpPGPGSTGPGGST 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 473 GEVGLPGDKGLPGEGYNIVgppgsqgppgfrglPGDDGYNGLRGLPGEKGLRGDDCPVCNAGPRGPRGQEGDTGYPGSHG 552
Cdd:COG5164 157 TPPGDGGSTTPPGPGGSTT--------------PPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPD 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 442626069 553 NRGAI-GLTGPRGVQGLQGNPGRAGHKGLPGPAGIPGEPGKVGAAGPD 599
Cdd:COG5164 223 DRGGKtGPKDQRPKTNPIERRGPERPEAAALPAELTALEAENRAANPE 270
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
817-871 |
3.12e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.47 E-value: 3.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 442626069 817 GPPGRSGIKGFPGDVGAPGQYGLAGRPGPKGVKGEQGPDGAVGQTGLPGNKGQRG 871
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
45-100 |
3.66e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.47 E-value: 3.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 442626069 45 GRMGAPGPIGVPGLEGPAGDIGPPGRAGPLGEKGDVGEYGEQGEKGHRGDIGPKGE 100
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
954-1010 |
4.20e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 37.09 E-value: 4.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 442626069 954 GEIGYNGRQGDIGPRGPNGEFGPKGLSGDDGPDGYPGANGLPGRKGETGNPGFPGRP 1010
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
569-744 |
4.55e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 41.49 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 569 QGNPGRAGHKGLPGPAGIPGEPGKVGAAGPDGKAievgslrKGEIGDTGDSGHRGDTGDDGekgrDGSDGSKGERGETGQ 648
Cdd:PHA03169 89 QGGPSGSGSESVGSPTPSPSGSAEELASGLSPEN-------TSGSSPESPASHSPPPSPPS----HPGPHEPAPPESHNP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 649 RGDYGDAGYQGRDGEPGRDGRDGAPgrnattpkvyliGEPGYDGIKGERGDDGDTGfkgvkgePNPGQIYDNTGEPGEDg 728
Cdd:PHA03169 158 SPNQQPSSFLQPSHEDSPEEPEPPT------------SEPEPDSPGPPQSETPTSS-------PPPQSPPDEPGEPQSP- 217
|
170
....*....|....*.
gi 442626069 729 ytGPKGVKGAKGEQGA 744
Cdd:PHA03169 218 --TPQQAPSPNTQQAV 231
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
546-602 |
4.91e-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: 37.09 E-value: 4.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 442626069 546 GYPGSHGNRGAIGLTGPRGVQGLQGNPGRAGHKGLPGPAGIPGEPGKVGAAGPDGKA 602
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
520-676 |
6.16e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 41.11 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 520 EKGLRGDDCPVCNAGPRGPRGQEGDTGYPGSHGNRGAIGLTGPRGVQGLQGNPGRAGHKGLPGPAGIPG--EPGKVGAAG 597
Cdd:PHA03169 77 EESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGphEPAPPESHN 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626069 598 PDGKaievgslrKGEIGDTGDSGHRGDTGDDGEKGRDGSDGSKGERGETGQRGDYGDAGYQgRDGEPGRDGRDGAPGRN 676
Cdd:PHA03169 157 PSPN--------QQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPD-EPGEPQSPTPQQAPSPN 226
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
265-320 |
6.28e-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: 36.70 E-value: 6.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 442626069 265 GPQGPTGEQGAVGRNGLPGARGEIGGPGERGKPGKDGEPGRFGDKGMKGAPGWTGA 320
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
533-742 |
7.57e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 41.04 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 533 AGPRGPRGQEGDTGYPGSHGNRGAIGLTGPRGVQGLQGNPGRAGHKGLPGPAGIPGEPGKVGAAGPDGKAIEVGSLRKGE 612
Cdd:PRK12678 71 AAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626069 613 IGDTGDSGHRGDTGDDGEKGRDGSDGSKGERGETGQRGDYGDAGYQGRDGEPGRDGRDGAPGRNATtpkvyligepgyDG 692
Cdd:PRK12678 151 QPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRRE------------ER 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442626069 693 IKGERGDDGDTGFKGVKGEPNPGQIYDNTGEPGEDGYTGPKGVKGAKGEQ 742
Cdd:PRK12678 219 GRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRD 268
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
99-150 |
9.14e-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: 9.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 442626069 99 GEMGYPGIMGKSGEPGTPGPRGIDGCDGRPGMQGPSGAPGQNGVRGPPGKPG 150
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
1058-1112 |
9.32e-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: 9.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 442626069 1058 GVAGRKGEVGSPGPNGLPGRHGLKGQRGDRGLPGQQGRPGEPGAKGLGGYPGRNG 1112
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| |
