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Conserved domains on  [gi|1802828103|ref|XP_032049632|]
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collagen alpha-4(IV) chain-like [Aythya fuligula]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1457-1562 1.77e-55

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: 188.19  E-value: 1.77e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1457 FLLVLHSQSDREPPCPQGMPKLWTGYSLLYLEGQEKAHNQDLGLAGSCLPVFNTMPFAYCNINQVCYYASrNDKSYWLSS 1536
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1802828103 1537 AA-----PLPMTPLSEEEIEPYISRCAVCEA 1562
Cdd:pfam01413   80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1565-1679 1.21e-51

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: 177.02  E-value: 1.21e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1565 QAVAVHSQDQSIPPCPMNWRSLWIGYSFLMHTgSGDQGGGQSLMSPGSCLEDFRSAPFIECQGqRGTCQFFANEYSFWLT 1644
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNG-NGTCNYASNDYSYWLS 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1802828103 1645 TVmpELQFaSAPLSGTLKEGQEQRKKISRCQVCLK 1679
Cdd:pfam01413   79 TV--EEQF-RKPMSQTPKAGNELRSYISRCVVCEA 110
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1217-1448 7.13e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 109.99  E-value: 7.13e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1217 GAPGERGFPGFPGIRGPVGPAGPMGRSPSSAPPGLPGDQGPPGLDGirgqpgnpgppgetifVQGDPGDTGIQGAPGISG 1296
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKG----------------PAGPQGEAGPQGPAGKDG 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1297 QRGQQGARGPPGNQGREGPKGPMGIHGPQGPPGAVGHPGDQGFQGKPGP--KGPTGFIGDPGEPGRRDDSCPTipGPPGE 1374
Cdd:NF038329   181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDGPQGPD--GPAGK 258

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1802828103 1375 AGQRGDDGSIGLSGPIGHPGPQGRKGEEGSCGLPGQDGLPGAPGPPGDQGHVGEQGYTGPQGPPGQTGIPGPPG 1448
Cdd:NF038329   259 DGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 54-289 3.28e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 107.68  E-value: 3.28e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103   54 EKGSRGQPGELGAQGPIGSLGSAGPAGLPGEKGQRGENGQPGPAGEKGDKGPTGVPGFPGLDGVPGLPGSEGPRGKRGVD 133
Cdd:NF038329   121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  134 GCNGSRGDPGFPGENGYIGPRGPSGNPGQKgekgnsvfvshfGKGPPGERGDPGPPGIPGPRGSRGTTGPRGYPGQPGLP 213
Cdd:NF038329   201 GPAGEQGPAGPAGPDGEAGPAGEDGPAGPA------------GDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1802828103  214 GIPGYPGLPGEQGNPGIgvDGQKGEPGDVGLPGPPGSPLLVGPPGAqlfKGEKGQKGLPGITGYRGPRGPKGIPGR 289
Cdd:NF038329   269 GPDGPDGKDGERGPVGP--AGKDGQNGKDGLPGKDGKDGQNGKDGL---PGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 966-1194 6.86e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 106.91  E-value: 6.86e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  966 GQKGEPGFPGENGFRGERGEKGNIGFRGAPGFPGKNGVPGLPGDHGDTGLMGFPGLRGFPGPKGFKGMTGFQGQPGDQGD 1045
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1046 VGLPGMPGNPGLTGPKGSKGKRGDPtlllGIRGQKGPPGDpGLTGFCGLPGEKGSAGIQGQPGRLGSKGESGYPGIPGFP 1125
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPA----GEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD 271

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1802828103 1126 GAPGPPGLPGEPGEKGKQGLSGPPGLQGLAGSQGRKGLPGLPGLDGLDGLKGQKGSAGAPGQSetGRPG 1194
Cdd:NF038329   272 GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD--GQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 813-1061 1.19e-23

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 106.14  E-value: 1.19e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  813 GCPGFPGPLCDMGLPGPPGLRGVIGLPGPQGLPGFKGQKGDRGLAGPPGIKGlkgspgsrgppgppgSRGLPGLPGNNGP 892
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------------EAGPQGPAGKDGE 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  893 PGFPGQTGSKGIQGPQGFLGLPGTQGPMGISGVKGEEGKMGPSGPSGECGDiGMKGERGRPGDSGsinirlEKGQKGEPG 972
Cdd:NF038329   182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTG------EDGPQGPDG 254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  973 FPGENGFRGERGEKGNIGFRGAPGFPGKNGVPGLPGDHGDTGLMGFPGLRGFPGPKGFKGMTGFQGQPGDQGDVGLPGMP 1052
Cdd:NF038329   255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD 334


                   ....*....
gi 1802828103 1053 GNPGLTGPK 1061
Cdd:NF038329   335 GQPGKPAPK 343
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 491-728 1.40e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 96.90  E-value: 1.40e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  491 AGPPGPRGIQGPPGTQGKKGQMGYPGRHGEKGDPGLSGAMGSPGLPGTPGSAGQHGEKGEKGDLGRVRIKGIKGERGPTG 570
Cdd:NF038329   122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  571 VPGFPGQRGNDGRDGDLGLPGEKGAEGDSGIPVPGDKGIPGVPGLPGVKGPiglpglgipgppgvRGSPGDFGDTGSVGP 650
Cdd:NF038329   202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGP--------------DGPAGKDGPRGDRGE 267

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  651 PGLKGQKGEtvcivspspgnPGPPGFKGVQGPKGLKGLPGRPGPNGFDGQKGQQGRPG----AGIPGPEGFRGKAGDPGE 726
Cdd:NF038329   268 AGPDGPDGK-----------DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGkdgkDGQPGKDGLPGKDGKDGQ 336


                   ..
gi 1802828103  727 EG 728
Cdd:NF038329   337 PG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 174-419 3.22e-19

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 92.66  E-value: 3.22e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  174 HFGKGPPGERGDPGPPGIPGPRGSRG---TTGPRGYPGQPGLPGIPGYPGLPGEQGNPG-IGVDGQKGEPGDVGLPGPPG 249
Cdd:NF038329   113 LKGDGEKGEPGPAGPAGPAGEQGPRGdrgETGPAGPAGPPGPQGERGEKGPAGPQGEAGpQGPAGKDGEAGAKGPAGEKG 192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  250 SPLLVGPPGAQLFKGEKGQKGLPGITGYRGPRGPKGIPGRGEKGEKGIAGFPGLRGSPGSYGPAGFPGIKGETGTAGFPG 329
Cdd:NF038329   193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  330 QPGYPGIKGDPgekgppgppgavgtpllpmkGPQGDPGFPGPAGDVGSVGPSGPAGALGRPGDDGASlpGLPGLSGAPGP 409
Cdd:NF038329   273 PDGKDGERGPV--------------------GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD--GQPGKDGLPGK 330

                          250
                   ....*....|
gi 1802828103  410 QGFHGDPGLP 419
Cdd:NF038329   331 DGKDGQPGKP 340
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 759-813 5.69e-06

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


:

Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.18  E-value: 5.69e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1802828103  759 GPPGIPGNRGLPGPPGAQGARGDPGIPGLQGQPGTPGFPGAKGFRGPEGNIGAPG 813
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
 
Name Accession Description Interval E-value
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1457-1562 1.77e-55

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: 188.19  E-value: 1.77e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1457 FLLVLHSQSDREPPCPQGMPKLWTGYSLLYLEGQEKAHNQDLGLAGSCLPVFNTMPFAYCNINQVCYYASrNDKSYWLSS 1536
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1802828103 1537 AA-----PLPMTPLSEEEIEPYISRCAVCEA 1562
Cdd:pfam01413   80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1565-1679 1.21e-51

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: 177.02  E-value: 1.21e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1565 QAVAVHSQDQSIPPCPMNWRSLWIGYSFLMHTgSGDQGGGQSLMSPGSCLEDFRSAPFIECQGqRGTCQFFANEYSFWLT 1644
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNG-NGTCNYASNDYSYWLS 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1802828103 1645 TVmpELQFaSAPLSGTLKEGQEQRKKISRCQVCLK 1679
Cdd:pfam01413   79 TV--EEQF-RKPMSQTPKAGNELRSYISRCVVCEA 110
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1456-1563 1.76e-46

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: 162.56  E-value: 1.76e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  1456 GFLLVLHSQSDREPPCPQGMPKLWTGYSLLYLEGQEKAHNQDLGLAGSCLPVFNTMPFAYCNINQVCYYASRNDKSYWLS 1535
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 1802828103  1536 S-------AAPLPMTPLSeEEIEPYISRCAVCEAP 1563
Cdd:smart00111   81 TiepsdqfTAPRPMTPKA-GDLRPYISRCQVCEKP 114
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1564-1679 8.03e-43

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: 152.16  E-value: 8.03e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  1564 AQAVAVHSQDQSIPPCPMNWRSLWIGYSFLMHTgSGDQGGGQSLMSPGSCLEDFRSAPFIECQGqRGTCQFFA-NEYSFW 1642
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASrNDYSFW 78

                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 1802828103  1643 LTTVMPELQFAsAPLSGTLKEGqEQRKKISRCQVCLK 1679
Cdd:smart00111   79 LSTIEPSDQFT-APRPMTPKAG-DLRPYISRCQVCEK 113
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1217-1448 7.13e-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: 109.99  E-value: 7.13e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1217 GAPGERGFPGFPGIRGPVGPAGPMGRSPSSAPPGLPGDQGPPGLDGirgqpgnpgppgetifVQGDPGDTGIQGAPGISG 1296
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKG----------------PAGPQGEAGPQGPAGKDG 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1297 QRGQQGARGPPGNQGREGPKGPMGIHGPQGPPGAVGHPGDQGFQGKPGP--KGPTGFIGDPGEPGRRDDSCPTipGPPGE 1374
Cdd:NF038329   181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDGPQGPD--GPAGK 258

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1802828103 1375 AGQRGDDGSIGLSGPIGHPGPQGRKGEEGSCGLPGQDGLPGAPGPPGDQGHVGEQGYTGPQGPPGQTGIPGPPG 1448
Cdd:NF038329   259 DGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1172-1451 8.63e-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: 109.61  E-value: 8.63e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1172 LDGLKGQKGSAGAPGQSetgrpgysGELGPKGDRGKPGWPGISIP-GAPGERGFPGFPGIRGPVGPAGPMGrspssaPPG 1250
Cdd:NF038329   115 GDGEKGEPGPAGPAGPA--------GEQGPRGDRGETGPAGPAGPpGPQGERGEKGPAGPQGEAGPQGPAG------KDG 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1251 LPGDQGPPGLDGirgqpgnpgppgetifvqgDPGDTGIQGAPGISGQRGQQGARGPPGNQGREGPKGPMGI--HGPQGPP 1328
Cdd:NF038329   181 EAGAKGPAGEKG-------------------PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDP 241

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1329 GAVGHPGDQGFQGKPGPKGPTGFIGDPGEPGRRDDSCPTipGPPGEAGQRGDDGSIGLsgpighPGPQGRKGEEGSCGLP 1408
Cdd:NF038329   242 GPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER--GPVGPAGKDGQNGKDGL------PGKDGKDGQNGKDGLP 313

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1802828103 1409 GQDglpgapgppGDQGHVGEQGYTGPQGPPGQTGIPGPPGPHV 1451
Cdd:NF038329   314 GKD---------GKDGQPGKDGLPGKDGKDGQPGKPAPKTPEV 347
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1139-1375 1.33e-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: 1.33e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1139 EKGKQGLSGPPGLQGLAGSQGRKGLPGLPGLDGLDGLKGQKGSAGAPGqsETGRPGYSGELGPKGDRGKPGWPGISipGA 1218
Cdd:NF038329   118 EKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG--PQGEAGPQGPAGKDGEAGAKGPAGEK--GP 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1219 PGERGFPGFPGIRGPVGPAGPMGRSPSSAPPGLPG-----DQGPPGLDGIRGQPGNPGPPGETiFVQGDPGDTGIQGAPG 1293
Cdd:NF038329   194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPGPTGEDGPQGPDGPA-GKDGPRGDRGEAGPDG 272

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1294 ISGQRGQQGARGPPGNQGREGPKGPMGIHGPQGPPGAVGHPGDQGFQGKPGPKGPTGFIGDPGEPGRRDDSCPTIPGPPG 1373
Cdd:NF038329   273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPD 352


                   ..
gi 1802828103 1374 EA 1375
Cdd:NF038329   353 TA 354
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 54-289 3.28e-24

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 107.68  E-value: 3.28e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103   54 EKGSRGQPGELGAQGPIGSLGSAGPAGLPGEKGQRGENGQPGPAGEKGDKGPTGVPGFPGLDGVPGLPGSEGPRGKRGVD 133
Cdd:NF038329   121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  134 GCNGSRGDPGFPGENGYIGPRGPSGNPGQKgekgnsvfvshfGKGPPGERGDPGPPGIPGPRGSRGTTGPRGYPGQPGLP 213
Cdd:NF038329   201 GPAGEQGPAGPAGPDGEAGPAGEDGPAGPA------------GDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1802828103  214 GIPGYPGLPGEQGNPGIgvDGQKGEPGDVGLPGPPGSPLLVGPPGAqlfKGEKGQKGLPGITGYRGPRGPKGIPGR 289
Cdd:NF038329   269 GPDGPDGKDGERGPVGP--AGKDGQNGKDGLPGKDGKDGQNGKDGL---PGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 966-1194 6.86e-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: 106.91  E-value: 6.86e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  966 GQKGEPGFPGENGFRGERGEKGNIGFRGAPGFPGKNGVPGLPGDHGDTGLMGFPGLRGFPGPKGFKGMTGFQGQPGDQGD 1045
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1046 VGLPGMPGNPGLTGPKGSKGKRGDPtlllGIRGQKGPPGDpGLTGFCGLPGEKGSAGIQGQPGRLGSKGESGYPGIPGFP 1125
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPA----GEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD 271

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1802828103 1126 GAPGPPGLPGEPGEKGKQGLSGPPGLQGLAGSQGRKGLPGLPGLDGLDGLKGQKGSAGAPGQSetGRPG 1194
Cdd:NF038329   272 GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD--GQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 813-1061 1.19e-23

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 106.14  E-value: 1.19e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  813 GCPGFPGPLCDMGLPGPPGLRGVIGLPGPQGLPGFKGQKGDRGLAGPPGIKGlkgspgsrgppgppgSRGLPGLPGNNGP 892
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------------EAGPQGPAGKDGE 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  893 PGFPGQTGSKGIQGPQGFLGLPGTQGPMGISGVKGEEGKMGPSGPSGECGDiGMKGERGRPGDSGsinirlEKGQKGEPG 972
Cdd:NF038329   182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTG------EDGPQGPDG 254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  973 FPGENGFRGERGEKGNIGFRGAPGFPGKNGVPGLPGDHGDTGLMGFPGLRGFPGPKGFKGMTGFQGQPGDQGDVGLPGMP 1052
Cdd:NF038329   255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD 334


                   ....*....
gi 1802828103 1053 GNPGLTGPK 1061
Cdd:NF038329   335 GQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 847-1086 1.27e-23

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 106.14  E-value: 1.27e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  847 FKGQKGDRGLAGPPGIKGLKGSPGSRGPPGPpgsrglpglPGNNGPPGFPGQTGSKGIQGPQGFLGLPGTQGPMGISGVK 926
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGP---------AGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  927 GEEGKMGPSGPSGECGDIGMKGERGRPGDSGSINIRLEKGQKGEPGfPGENGFRGERGEKGNIGFRGAPGFPGKNGVPGL 1006
Cdd:NF038329   186 GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1007 PGDHGDTGLMGFPGLRGFPGPKGFKGMTGFQGQPGDQGDVGLPGMPGNPGLTGPKGSKGKRGDPtlllGIRGQKGPPGDP 1086
Cdd:NF038329   265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP----GKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 68-317 1.31e-23

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 106.14  E-value: 1.31e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103   68 GPIGSLGSAGPAGLPGEKGQRGENGQPGPAGEKGDKGPTGVPGFPGLDGVPGLPGSEGPRGKRGVDGCNGSRGDPGFPGE 147
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  148 NGYIGPRGPSGNPGQKGEKGNSvfvshfgkGPPGERGDPGPPGipgprgsRGTTGPRGYPGQPGLPGIPGYPGLPGEQGN 227
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEA--------GPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGP 261

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  228 pgigvDGQKGEPGDVGLPGPPGSPLLVGPPGAQlfkGEKGQKGLPGITGYRGPRGPKGIPGRgekgeKGIAGFPGLRGSP 307
Cdd:NF038329   262 -----RGDRGEAGPDGPDGKDGERGPVGPAGKD---GQNGKDGLPGKDGKDGQNGKDGLPGK-----DGKDGQPGKDGLP 328

                          250
                   ....*....|
gi 1802828103  308 GSYGPAGFPG 317
Cdd:NF038329   329 GKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 900-1117 1.62e-23

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 105.76  E-value: 1.62e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  900 GSKGIQGPQGFLGLPGTQGPMGISGVKGEEGKMGPSGPSGECGDIGMKGERGRPGDSGSINIRLEKGQKGEPGFPGENGF 979
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  980 RGERGEKGNIGFRGAPGFPGKNGVPGLPGDHGDTGlmgfpglRGFPGPKGFKGMTGFQGQPGDQGDVGLPGMPGNPGLTG 1059
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1802828103 1060 PKGSKGKRGDptlllgiRGQKGPPGDPGLTGFCGLPGEKGSAGIQGQPGRLGSKGESG 1117
Cdd:NF038329   270 PDGPDGKDGE-------RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDG 320
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 796-1028 3.41e-23

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 104.60  E-value: 3.41e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  796 FPGAKGFRGPEGNIGAPGCPGFPGPlcdmglPGPPGLRGVIGLPGPQGLPGFKGQKGDRGLAGPPGIKGLKGSPGSRGPP 875
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGD------RGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  876 GPPGSRGLPGLPGNNGPPGFPGQTGSKGIQGPQGFLGLPGTQG--PMGISGVKGEEGKMGPSGPSGECGDIGMKGERGRP 953
Cdd:NF038329   189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1802828103  954 GDSGSINIRLEKGQKGEPGFPGENGFRGERGEKGNIGFRGAPGFPGKNGVPGLPGDHGDTGLMGFPGLRGFPGPK 1028
Cdd:NF038329   269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 677-953 1.06e-21

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 100.36  E-value: 1.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  677 KGVQGPKGLKGLPGRPGPNGFDGQKGQQGRpgAGIPGPEGFRGKAGDPGEEGERGSTingkngapgppgpdgqkgvpgdt 756
Cdd:NF038329   119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGP--AGPPGPQGERGEKGPAGPQGEAGPQ----------------------- 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  757 tyGPPGIPGNRGLPGPPGAQGARGDPGIPGLQGQPGTPGFPGAKGFRGPEGNIGAPGCPGFPgplcDMGLPGPPGLRGVI 836
Cdd:NF038329   174 --GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG----QQGPDGDPGPTGED 247

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  837 GLPGPQGLPGFKGQKGDRGLAGPPGIKglkgspgsrgppgppgsrglpglpGNNGPPGFPGQTGSKGIQGPQGFLGLPGT 916
Cdd:NF038329   248 GPQGPDGPAGKDGPRGDRGEAGPDGPD------------------------GKDGERGPVGPAGKDGQNGKDGLPGKDGK 303

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1802828103  917 QGPMGISGVKGEEGKMGPSGPSGECGDIGMKGERGRP 953
Cdd:NF038329   304 DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 491-728 1.40e-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: 1.40e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  491 AGPPGPRGIQGPPGTQGKKGQMGYPGRHGEKGDPGLSGAMGSPGLPGTPGSAGQHGEKGEKGDLGRVRIKGIKGERGPTG 570
Cdd:NF038329   122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  571 VPGFPGQRGNDGRDGDLGLPGEKGAEGDSGIPVPGDKGIPGVPGLPGVKGPiglpglgipgppgvRGSPGDFGDTGSVGP 650
Cdd:NF038329   202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGP--------------DGPAGKDGPRGDRGE 267

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  651 PGLKGQKGEtvcivspspgnPGPPGFKGVQGPKGLKGLPGRPGPNGFDGQKGQQGRPG----AGIPGPEGFRGKAGDPGE 726
Cdd:NF038329   268 AGPDGPDGK-----------DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGkdgkDGQPGKDGLPGKDGKDGQ 336


                   ..
gi 1802828103  727 EG 728
Cdd:NF038329   337 PG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 174-419 3.22e-19

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 92.66  E-value: 3.22e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  174 HFGKGPPGERGDPGPPGIPGPRGSRG---TTGPRGYPGQPGLPGIPGYPGLPGEQGNPG-IGVDGQKGEPGDVGLPGPPG 249
Cdd:NF038329   113 LKGDGEKGEPGPAGPAGPAGEQGPRGdrgETGPAGPAGPPGPQGERGEKGPAGPQGEAGpQGPAGKDGEAGAKGPAGEKG 192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  250 SPLLVGPPGAQLFKGEKGQKGLPGITGYRGPRGPKGIPGRGEKGEKGIAGFPGLRGSPGSYGPAGFPGIKGETGTAGFPG 329
Cdd:NF038329   193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  330 QPGYPGIKGDPgekgppgppgavgtpllpmkGPQGDPGFPGPAGDVGSVGPSGPAGALGRPGDDGASlpGLPGLSGAPGP 409
Cdd:NF038329   273 PDGKDGERGPV--------------------GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD--GQPGKDGLPGK 330

                          250
                   ....*....|
gi 1802828103  410 QGFHGDPGLP 419
Cdd:NF038329   331 DGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 636-864 6.44e-19

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 91.51  E-value: 6.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  636 RGSPGDFGDTGSVGPPGLKGQKGETvcivspspGNPGPPGFKGVQGPKGLKGLPGRPGPNGFDGQKGQQGRPGA-GIPGP 714
Cdd:NF038329   119 KGEPGPAGPAGPAGEQGPRGDRGET--------GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAkGPAGE 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  715 EGFRGKAGDPGEEGERGstingKNGAPGPPGPDGQKGVPGDTTYGPPGIPGNRGLPGPPGAQGARGDPGIPGLQGQPGTP 794
Cdd:NF038329   191 KGPQGPRGETGPAGEQG-----PAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  795 GFPGAKGFRGPEGNIGAPGCPGFPGPLCDMGLPGPPGLRGVIGLPGPQGLPGFKGQKGDRGLAGPPGIKG 864
Cdd:NF038329   266 GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 268-551 4.71e-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: 4.71e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  268 QKGLPGITGYRGPRGPKGIPG----RGEKGEKGIAGFPGLRGSPGSYGPAGFPGIKGETGTAGFPGQPGYPGIKGDPGEk 343
Cdd:NF038329   112 QLKGDGEKGEPGPAGPAGPAGeqgpRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE- 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  344 gppgppgavgtpllpmKGPQGDPGFPGPAGDVGSVGPSGPAGALGRPGDDGASLPGLPGLSGAPGPQGFHGDPGLPGtge 423
Cdd:NF038329   191 ----------------KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG--- 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  424 plpgrpgypgppglpgqpgrqglpglpsvictDRGIPGEPGAKGQIGLPGRKGEKGEKGNQGLcscsAGPPGPRGIQGPP 503
Cdd:NF038329   252 --------------------------------PDGPAGKDGPRGDRGEAGPDGPDGKDGERGP----VGPAGKDGQNGKD 295

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1802828103  504 GTQGKKGQMGYPGRHGEKGDPGLSGAMGSPGLPGTPGSAGQHGEKGEK 551
Cdd:NF038329   296 GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 220-504 4.84e-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: 4.84e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  220 GLPGEQGNPGIGVDGQKGEPGDVGLPGPPGSPLLVGPPGAQLFKGEKGQKGLPGITGYRGPRGPKGIPG-RGEKGEKGIA 298
Cdd:NF038329   109 GLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGkDGEAGAKGPA 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  299 GFPGLRGSPGSYGPAGFPGIKGETGTAGFPGQPGYPGIKGDpgekgppgppgavgtpllPMKGPQGDPGFPGPAGDVGSV 378
Cdd:NF038329   189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP------------------AGDGQQGPDGDPGPTGEDGPQ 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  379 GPSGPAGALGRPGDDGasLPGLPGLSGAPGPQGFHGDPGLPGtgeplpgrpgypgppglpgQPGRQGLPGLpsvictdrg 458
Cdd:NF038329   251 GPDGPAGKDGPRGDRG--EAGPDGPDGKDGERGPVGPAGKDG-------------------QNGKDGLPGK--------- 300

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1802828103  459 iPGEPGAKGQIGLPGRKGEKGEKGNQGLcscsagpPGPRGIQGPPG 504
Cdd:NF038329   301 -DGKDGQNGKDGLPGKDGKDGQPGKDGL-------PGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 40-166 6.48e-14

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: 76.10  E-value: 6.48e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103   40 PCGGQDCSVCRCFPEKGSRGQPGELGAQGPIGSLGSAGPAGLPGE---KGQRGENGQPGPAGEKGDKGPTGVPGFPGLDG 116
Cdd:NF038329   214 PDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKdgpRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1802828103  117 VPGLPGSEGPRGKRGVDGCNGSRGDPGFPGENGYIGPRGPSGNPGQKGEK 166
Cdd:NF038329   294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1332-1474 7.40e-09

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 59.92  E-value: 7.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1332 GHPGDQGFQGKPGPKGPTGFIGDPGEPGRRDDScptipGPPGEAGQRGDDGSIGLSGPIGHPGPQGRKGEEGSCGLPGQD 1411
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPA-----GPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1802828103 1412 glpgapgppgdqGHVGEQGYTGPQGPPGQTGIPGPPGPHVRSSSGFLLVLHSQSDREPPCPQG 1474
Cdd:NF038329   192 ------------GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG 242
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
56-287 4.69e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 54.27  E-value: 4.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103   56 GSRGQPGELGAQGPIGSLGSAGPAGLPGEKGQRGENGQPGPAGEKGDKGPtgvPGFPGLDGVPGLPGSEGPRGKRGVDGC 135
Cdd:COG5164     16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRP---AGNQGATGPAQNQGGTTPAQNQGGTRP 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  136 NGSRGDPGFPGENGYIGPRGPSGNPGQKGEKGNSVFVSHFGKGPPGERGDPGPPGipgprgsrGTTGPRGYPGQPGLPGI 215
Cdd:COG5164     93 AGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGP--------GSTGPGGSTTPPGDGGS 164

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1802828103  216 PGYPGLPGEQGNPGIGVDGQKGEPGDVGLPGPPGSPLLVGPPGAQLFKGEKGQKGLPGITGYRGPRGPKGIP 287
Cdd:COG5164    165 TTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPK 236
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 759-813 5.69e-06

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.18  E-value: 5.69e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1802828103  759 GPPGIPGNRGLPGPPGAQGARGDPGIPGLQGQPGTPGFPGAKGFRGPEGNIGAPG 813
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1280-1449 1.56e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 49.64  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1280 QGDPGDTGIQGAPGISGQRGQQGARGPPGNQGREGPKGPMGIHGPQGPPGAVGHPGDQGFQGKPGPKGPTGFIGDPGEPG 1359
Cdd:COG5164     21 AGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTT 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1360 RRDDSCPTIPGPPGEAGQRGDDGSIGLSGPIGHPGPQGRKGEEGSCglPGQDGLPGAPGPPGDQGHVGEQGYTGPQGPPG 1439
Cdd:COG5164    101 PAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPG--PGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPD 178

                          170
                   ....*....|
gi 1802828103 1440 QTGIPGPPGP 1449
Cdd:COG5164    179 DGGSTTPPNK 188
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 77-131 2.12e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 2.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1802828103   77 GPAGLPGEKGQRGENGQPGPAGEKGDKGPTGVPGFPGLDGVPGLPGSEGPRGKRG 131
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1296-1350 1.81e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 1.81e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1802828103 1296 GQRGQQGARGPPGNQGREGPKGPMGIHGPQGPPGAVGHPGDQGFQGKPGPKGPTG 1350
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 492-547 4.92e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 4.92e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1802828103  492 GPPGPRGIQGPPGTQGKKGQMGYPGRHGEKGDPGLSGAMGSPGLPGTPGSAGQHGE 547
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1038-1348 5.85e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 44.64  E-value: 5.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1038 GQPGDQGDVGLPGMPGNPGLTGPKGSKGKRGDPtlllGIRGQKGPPGDPGLTGFCGLPGEKGSAGIQGQPGRLGSKGESG 1117
Cdd:COG5164      7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPA----GNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTT 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1118 ypgipgfpgapgppglpgepgEKGKQGLSGPPGLQGLAGSQGRKGLPGLPGLDGLDGLKGQKGSAGAPGQSETGRPGysg 1197
Cdd:COG5164     83 ---------------------PAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPG--- 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1198 elgpkgdrgkpgwPGISIPGAPGERGFPGFPGIRGPVGPAGPMGRSPSSAPPGLPGDQGPPGLDGIRGQpgnpgppgeti 1277
Cdd:COG5164    139 -------------DGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTD----------- 194

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1802828103 1278 fvqGDPGDTGIQGAPGISGQRGQQGARGPPGNQ-GREGPKGPMGIHGPQGPPGAVGHPGDQGFQGKPGPKGP 1348
Cdd:COG5164    195 ---IPTGGTPRQGPDGPVKKDDKNGKGNPPDDRgGKTGPKDQRPKTNPIERRGPERPEAAALPAELTALEAE 263
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1014-1070 2.13e-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: 2.13e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1802828103 1014 GLMGFPGLRGFPGPKGFKGMTGFQGQPGDQGDVGLPGMPGNPGLTGPKGSKGKRGDP 1070
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 795-850 6.43e-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: 6.43e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1802828103  795 GFPGAKGFRGPEGNIGAPGCPGFPGPLCDMGLPGPPGLRGVIGLPGPQGLPGFKGQ 850
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
 
Name Accession Description Interval E-value
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1457-1562 1.77e-55

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: 188.19  E-value: 1.77e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1457 FLLVLHSQSDREPPCPQGMPKLWTGYSLLYLEGQEKAHNQDLGLAGSCLPVFNTMPFAYCNINQVCYYASrNDKSYWLSS 1536
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1802828103 1537 AA-----PLPMTPLSEEEIEPYISRCAVCEA 1562
Cdd:pfam01413   80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1565-1679 1.21e-51

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: 177.02  E-value: 1.21e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1565 QAVAVHSQDQSIPPCPMNWRSLWIGYSFLMHTgSGDQGGGQSLMSPGSCLEDFRSAPFIECQGqRGTCQFFANEYSFWLT 1644
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNG-NGTCNYASNDYSYWLS 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1802828103 1645 TVmpELQFaSAPLSGTLKEGQEQRKKISRCQVCLK 1679
Cdd:pfam01413   79 TV--EEQF-RKPMSQTPKAGNELRSYISRCVVCEA 110
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1456-1563 1.76e-46

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: 162.56  E-value: 1.76e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  1456 GFLLVLHSQSDREPPCPQGMPKLWTGYSLLYLEGQEKAHNQDLGLAGSCLPVFNTMPFAYCNINQVCYYASRNDKSYWLS 1535
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 1802828103  1536 S-------AAPLPMTPLSeEEIEPYISRCAVCEAP 1563
Cdd:smart00111   81 TiepsdqfTAPRPMTPKA-GDLRPYISRCQVCEKP 114
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1564-1679 8.03e-43

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: 152.16  E-value: 8.03e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  1564 AQAVAVHSQDQSIPPCPMNWRSLWIGYSFLMHTgSGDQGGGQSLMSPGSCLEDFRSAPFIECQGqRGTCQFFA-NEYSFW 1642
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASrNDYSFW 78

                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 1802828103  1643 LTTVMPELQFAsAPLSGTLKEGqEQRKKISRCQVCLK 1679
Cdd:smart00111   79 LSTIEPSDQFT-APRPMTPKAG-DLRPYISRCQVCEK 113
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1217-1448 7.13e-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: 109.99  E-value: 7.13e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1217 GAPGERGFPGFPGIRGPVGPAGPMGRSPSSAPPGLPGDQGPPGLDGirgqpgnpgppgetifVQGDPGDTGIQGAPGISG 1296
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKG----------------PAGPQGEAGPQGPAGKDG 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1297 QRGQQGARGPPGNQGREGPKGPMGIHGPQGPPGAVGHPGDQGFQGKPGP--KGPTGFIGDPGEPGRRDDSCPTipGPPGE 1374
Cdd:NF038329   181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDGPQGPD--GPAGK 258

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1802828103 1375 AGQRGDDGSIGLSGPIGHPGPQGRKGEEGSCGLPGQDGLPGAPGPPGDQGHVGEQGYTGPQGPPGQTGIPGPPG 1448
Cdd:NF038329   259 DGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1172-1451 8.63e-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: 109.61  E-value: 8.63e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1172 LDGLKGQKGSAGAPGQSetgrpgysGELGPKGDRGKPGWPGISIP-GAPGERGFPGFPGIRGPVGPAGPMGrspssaPPG 1250
Cdd:NF038329   115 GDGEKGEPGPAGPAGPA--------GEQGPRGDRGETGPAGPAGPpGPQGERGEKGPAGPQGEAGPQGPAG------KDG 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1251 LPGDQGPPGLDGirgqpgnpgppgetifvqgDPGDTGIQGAPGISGQRGQQGARGPPGNQGREGPKGPMGI--HGPQGPP 1328
Cdd:NF038329   181 EAGAKGPAGEKG-------------------PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDP 241

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1329 GAVGHPGDQGFQGKPGPKGPTGFIGDPGEPGRRDDSCPTipGPPGEAGQRGDDGSIGLsgpighPGPQGRKGEEGSCGLP 1408
Cdd:NF038329   242 GPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER--GPVGPAGKDGQNGKDGL------PGKDGKDGQNGKDGLP 313

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1802828103 1409 GQDglpgapgppGDQGHVGEQGYTGPQGPPGQTGIPGPPGPHV 1451
Cdd:NF038329   314 GKD---------GKDGQPGKDGLPGKDGKDGQPGKPAPKTPEV 347
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1139-1375 1.33e-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: 1.33e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1139 EKGKQGLSGPPGLQGLAGSQGRKGLPGLPGLDGLDGLKGQKGSAGAPGqsETGRPGYSGELGPKGDRGKPGWPGISipGA 1218
Cdd:NF038329   118 EKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG--PQGEAGPQGPAGKDGEAGAKGPAGEK--GP 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1219 PGERGFPGFPGIRGPVGPAGPMGRSPSSAPPGLPG-----DQGPPGLDGIRGQPGNPGPPGETiFVQGDPGDTGIQGAPG 1293
Cdd:NF038329   194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPGPTGEDGPQGPDGPA-GKDGPRGDRGEAGPDG 272

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1294 ISGQRGQQGARGPPGNQGREGPKGPMGIHGPQGPPGAVGHPGDQGFQGKPGPKGPTGFIGDPGEPGRRDDSCPTIPGPPG 1373
Cdd:NF038329   273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPD 352


                   ..
gi 1802828103 1374 EA 1375
Cdd:NF038329   353 TA 354
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 54-289 3.28e-24

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 107.68  E-value: 3.28e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103   54 EKGSRGQPGELGAQGPIGSLGSAGPAGLPGEKGQRGENGQPGPAGEKGDKGPTGVPGFPGLDGVPGLPGSEGPRGKRGVD 133
Cdd:NF038329   121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  134 GCNGSRGDPGFPGENGYIGPRGPSGNPGQKgekgnsvfvshfGKGPPGERGDPGPPGIPGPRGSRGTTGPRGYPGQPGLP 213
Cdd:NF038329   201 GPAGEQGPAGPAGPDGEAGPAGEDGPAGPA------------GDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1802828103  214 GIPGYPGLPGEQGNPGIgvDGQKGEPGDVGLPGPPGSPLLVGPPGAqlfKGEKGQKGLPGITGYRGPRGPKGIPGR 289
Cdd:NF038329   269 GPDGPDGKDGERGPVGP--AGKDGQNGKDGLPGKDGKDGQNGKDGL---PGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 966-1194 6.86e-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: 106.91  E-value: 6.86e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  966 GQKGEPGFPGENGFRGERGEKGNIGFRGAPGFPGKNGVPGLPGDHGDTGLMGFPGLRGFPGPKGFKGMTGFQGQPGDQGD 1045
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1046 VGLPGMPGNPGLTGPKGSKGKRGDPtlllGIRGQKGPPGDpGLTGFCGLPGEKGSAGIQGQPGRLGSKGESGYPGIPGFP 1125
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPA----GEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD 271

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1802828103 1126 GAPGPPGLPGEPGEKGKQGLSGPPGLQGLAGSQGRKGLPGLPGLDGLDGLKGQKGSAGAPGQSetGRPG 1194
Cdd:NF038329   272 GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD--GQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 813-1061 1.19e-23

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 106.14  E-value: 1.19e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  813 GCPGFPGPLCDMGLPGPPGLRGVIGLPGPQGLPGFKGQKGDRGLAGPPGIKGlkgspgsrgppgppgSRGLPGLPGNNGP 892
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------------EAGPQGPAGKDGE 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  893 PGFPGQTGSKGIQGPQGFLGLPGTQGPMGISGVKGEEGKMGPSGPSGECGDiGMKGERGRPGDSGsinirlEKGQKGEPG 972
Cdd:NF038329   182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTG------EDGPQGPDG 254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  973 FPGENGFRGERGEKGNIGFRGAPGFPGKNGVPGLPGDHGDTGLMGFPGLRGFPGPKGFKGMTGFQGQPGDQGDVGLPGMP 1052
Cdd:NF038329   255 PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD 334


                   ....*....
gi 1802828103 1053 GNPGLTGPK 1061
Cdd:NF038329   335 GQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 847-1086 1.27e-23

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 106.14  E-value: 1.27e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  847 FKGQKGDRGLAGPPGIKGLKGSPGSRGPPGPpgsrglpglPGNNGPPGFPGQTGSKGIQGPQGFLGLPGTQGPMGISGVK 926
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGP---------AGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  927 GEEGKMGPSGPSGECGDIGMKGERGRPGDSGSINIRLEKGQKGEPGfPGENGFRGERGEKGNIGFRGAPGFPGKNGVPGL 1006
Cdd:NF038329   186 GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1007 PGDHGDTGLMGFPGLRGFPGPKGFKGMTGFQGQPGDQGDVGLPGMPGNPGLTGPKGSKGKRGDPtlllGIRGQKGPPGDP 1086
Cdd:NF038329   265 RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP----GKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 68-317 1.31e-23

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 106.14  E-value: 1.31e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103   68 GPIGSLGSAGPAGLPGEKGQRGENGQPGPAGEKGDKGPTGVPGFPGLDGVPGLPGSEGPRGKRGVDGCNGSRGDPGFPGE 147
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  148 NGYIGPRGPSGNPGQKGEKGNSvfvshfgkGPPGERGDPGPPGipgprgsRGTTGPRGYPGQPGLPGIPGYPGLPGEQGN 227
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEA--------GPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGP 261

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  228 pgigvDGQKGEPGDVGLPGPPGSPLLVGPPGAQlfkGEKGQKGLPGITGYRGPRGPKGIPGRgekgeKGIAGFPGLRGSP 307
Cdd:NF038329   262 -----RGDRGEAGPDGPDGKDGERGPVGPAGKD---GQNGKDGLPGKDGKDGQNGKDGLPGK-----DGKDGQPGKDGLP 328

                          250
                   ....*....|
gi 1802828103  308 GSYGPAGFPG 317
Cdd:NF038329   329 GKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 900-1117 1.62e-23

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 105.76  E-value: 1.62e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  900 GSKGIQGPQGFLGLPGTQGPMGISGVKGEEGKMGPSGPSGECGDIGMKGERGRPGDSGSINIRLEKGQKGEPGFPGENGF 979
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  980 RGERGEKGNIGFRGAPGFPGKNGVPGLPGDHGDTGlmgfpglRGFPGPKGFKGMTGFQGQPGDQGDVGLPGMPGNPGLTG 1059
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1802828103 1060 PKGSKGKRGDptlllgiRGQKGPPGDPGLTGFCGLPGEKGSAGIQGQPGRLGSKGESG 1117
Cdd:NF038329   270 PDGPDGKDGE-------RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDG 320
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 796-1028 3.41e-23

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 104.60  E-value: 3.41e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  796 FPGAKGFRGPEGNIGAPGCPGFPGPlcdmglPGPPGLRGVIGLPGPQGLPGFKGQKGDRGLAGPPGIKGLKGSPGSRGPP 875
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGD------RGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  876 GPPGSRGLPGLPGNNGPPGFPGQTGSKGIQGPQGFLGLPGTQG--PMGISGVKGEEGKMGPSGPSGECGDIGMKGERGRP 953
Cdd:NF038329   189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1802828103  954 GDSGSINIRLEKGQKGEPGFPGENGFRGERGEKGNIGFRGAPGFPGKNGVPGLPGDHGDTGLMGFPGLRGFPGPK 1028
Cdd:NF038329   269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 677-953 1.06e-21

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 100.36  E-value: 1.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  677 KGVQGPKGLKGLPGRPGPNGFDGQKGQQGRpgAGIPGPEGFRGKAGDPGEEGERGSTingkngapgppgpdgqkgvpgdt 756
Cdd:NF038329   119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGP--AGPPGPQGERGEKGPAGPQGEAGPQ----------------------- 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  757 tyGPPGIPGNRGLPGPPGAQGARGDPGIPGLQGQPGTPGFPGAKGFRGPEGNIGAPGCPGFPgplcDMGLPGPPGLRGVI 836
Cdd:NF038329   174 --GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG----QQGPDGDPGPTGED 247

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  837 GLPGPQGLPGFKGQKGDRGLAGPPGIKglkgspgsrgppgppgsrglpglpGNNGPPGFPGQTGSKGIQGPQGFLGLPGT 916
Cdd:NF038329   248 GPQGPDGPAGKDGPRGDRGEAGPDGPD------------------------GKDGERGPVGPAGKDGQNGKDGLPGKDGK 303

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1802828103  917 QGPMGISGVKGEEGKMGPSGPSGECGDIGMKGERGRP 953
Cdd:NF038329   304 DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 491-728 1.40e-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: 1.40e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  491 AGPPGPRGIQGPPGTQGKKGQMGYPGRHGEKGDPGLSGAMGSPGLPGTPGSAGQHGEKGEKGDLGRVRIKGIKGERGPTG 570
Cdd:NF038329   122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  571 VPGFPGQRGNDGRDGDLGLPGEKGAEGDSGIPVPGDKGIPGVPGLPGVKGPiglpglgipgppgvRGSPGDFGDTGSVGP 650
Cdd:NF038329   202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGP--------------DGPAGKDGPRGDRGE 267

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  651 PGLKGQKGEtvcivspspgnPGPPGFKGVQGPKGLKGLPGRPGPNGFDGQKGQQGRPG----AGIPGPEGFRGKAGDPGE 726
Cdd:NF038329   268 AGPDGPDGK-----------DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGkdgkDGQPGKDGLPGKDGKDGQ 336


                   ..
gi 1802828103  727 EG 728
Cdd:NF038329   337 PG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 174-419 3.22e-19

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 92.66  E-value: 3.22e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  174 HFGKGPPGERGDPGPPGIPGPRGSRG---TTGPRGYPGQPGLPGIPGYPGLPGEQGNPG-IGVDGQKGEPGDVGLPGPPG 249
Cdd:NF038329   113 LKGDGEKGEPGPAGPAGPAGEQGPRGdrgETGPAGPAGPPGPQGERGEKGPAGPQGEAGpQGPAGKDGEAGAKGPAGEKG 192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  250 SPLLVGPPGAQLFKGEKGQKGLPGITGYRGPRGPKGIPGRGEKGEKGIAGFPGLRGSPGSYGPAGFPGIKGETGTAGFPG 329
Cdd:NF038329   193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  330 QPGYPGIKGDPgekgppgppgavgtpllpmkGPQGDPGFPGPAGDVGSVGPSGPAGALGRPGDDGASlpGLPGLSGAPGP 409
Cdd:NF038329   273 PDGKDGERGPV--------------------GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD--GQPGKDGLPGK 330

                          250
                   ....*....|
gi 1802828103  410 QGFHGDPGLP 419
Cdd:NF038329   331 DGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 636-864 6.44e-19

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 91.51  E-value: 6.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  636 RGSPGDFGDTGSVGPPGLKGQKGETvcivspspGNPGPPGFKGVQGPKGLKGLPGRPGPNGFDGQKGQQGRPGA-GIPGP 714
Cdd:NF038329   119 KGEPGPAGPAGPAGEQGPRGDRGET--------GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAkGPAGE 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  715 EGFRGKAGDPGEEGERGstingKNGAPGPPGPDGQKGVPGDTTYGPPGIPGNRGLPGPPGAQGARGDPGIPGLQGQPGTP 794
Cdd:NF038329   191 KGPQGPRGETGPAGEQG-----PAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  795 GFPGAKGFRGPEGNIGAPGCPGFPGPLCDMGLPGPPGLRGVIGLPGPQGLPGFKGQKGDRGLAGPPGIKG 864
Cdd:NF038329   266 GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 268-551 4.71e-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: 4.71e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  268 QKGLPGITGYRGPRGPKGIPG----RGEKGEKGIAGFPGLRGSPGSYGPAGFPGIKGETGTAGFPGQPGYPGIKGDPGEk 343
Cdd:NF038329   112 QLKGDGEKGEPGPAGPAGPAGeqgpRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE- 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  344 gppgppgavgtpllpmKGPQGDPGFPGPAGDVGSVGPSGPAGALGRPGDDGASLPGLPGLSGAPGPQGFHGDPGLPGtge 423
Cdd:NF038329   191 ----------------KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG--- 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  424 plpgrpgypgppglpgqpgrqglpglpsvictDRGIPGEPGAKGQIGLPGRKGEKGEKGNQGLcscsAGPPGPRGIQGPP 503
Cdd:NF038329   252 --------------------------------PDGPAGKDGPRGDRGEAGPDGPDGKDGERGP----VGPAGKDGQNGKD 295

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1802828103  504 GTQGKKGQMGYPGRHGEKGDPGLSGAMGSPGLPGTPGSAGQHGEKGEK 551
Cdd:NF038329   296 GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 220-504 4.84e-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: 4.84e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  220 GLPGEQGNPGIGVDGQKGEPGDVGLPGPPGSPLLVGPPGAQLFKGEKGQKGLPGITGYRGPRGPKGIPG-RGEKGEKGIA 298
Cdd:NF038329   109 GLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGkDGEAGAKGPA 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  299 GFPGLRGSPGSYGPAGFPGIKGETGTAGFPGQPGYPGIKGDpgekgppgppgavgtpllPMKGPQGDPGFPGPAGDVGSV 378
Cdd:NF038329   189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP------------------AGDGQQGPDGDPGPTGEDGPQ 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  379 GPSGPAGALGRPGDDGasLPGLPGLSGAPGPQGFHGDPGLPGtgeplpgrpgypgppglpgQPGRQGLPGLpsvictdrg 458
Cdd:NF038329   251 GPDGPAGKDGPRGDRG--EAGPDGPDGKDGERGPVGPAGKDG-------------------QNGKDGLPGK--------- 300

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1802828103  459 iPGEPGAKGQIGLPGRKGEKGEKGNQGLcscsagpPGPRGIQGPPG 504
Cdd:NF038329   301 -DGKDGQNGKDGLPGKDGKDGQPGKDGL-------PGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 40-166 6.48e-14

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: 76.10  E-value: 6.48e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103   40 PCGGQDCSVCRCFPEKGSRGQPGELGAQGPIGSLGSAGPAGLPGE---KGQRGENGQPGPAGEKGDKGPTGVPGFPGLDG 116
Cdd:NF038329   214 PDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKdgpRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG 293

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1802828103  117 VPGLPGSEGPRGKRGVDGCNGSRGDPGFPGENGYIGPRGPSGNPGQKGEK 166
Cdd:NF038329   294 KDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1332-1474 7.40e-09

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 59.92  E-value: 7.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1332 GHPGDQGFQGKPGPKGPTGFIGDPGEPGRRDDScptipGPPGEAGQRGDDGSIGLSGPIGHPGPQGRKGEEGSCGLPGQD 1411
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPA-----GPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1802828103 1412 glpgapgppgdqGHVGEQGYTGPQGPPGQTGIPGPPGPHVRSSSGFLLVLHSQSDREPPCPQG 1474
Cdd:NF038329   192 ------------GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG 242
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
56-287 4.69e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 54.27  E-value: 4.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103   56 GSRGQPGELGAQGPIGSLGSAGPAGLPGEKGQRGENGQPGPAGEKGDKGPtgvPGFPGLDGVPGLPGSEGPRGKRGVDGC 135
Cdd:COG5164     16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRP---AGNQGATGPAQNQGGTTPAQNQGGTRP 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103  136 NGSRGDPGFPGENGYIGPRGPSGNPGQKGEKGNSVFVSHFGKGPPGERGDPGPPGipgprgsrGTTGPRGYPGQPGLPGI 215
Cdd:COG5164     93 AGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGP--------GSTGPGGSTTPPGDGGS 164

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1802828103  216 PGYPGLPGEQGNPGIGVDGQKGEPGDVGLPGPPGSPLLVGPPGAQLFKGEKGQKGLPGITGYRGPRGPKGIP 287
Cdd:COG5164    165 TTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPK 236
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 759-813 5.69e-06

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.18  E-value: 5.69e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1802828103  759 GPPGIPGNRGLPGPPGAQGARGDPGIPGLQGQPGTPGFPGAKGFRGPEGNIGAPG 813
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1280-1449 1.56e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 49.64  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1280 QGDPGDTGIQGAPGISGQRGQQGARGPPGNQGREGPKGPMGIHGPQGPPGAVGHPGDQGFQGKPGPKGPTGFIGDPGEPG 1359
Cdd:COG5164     21 AGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTT 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1360 RRDDSCPTIPGPPGEAGQRGDDGSIGLSGPIGHPGPQGRKGEEGSCglPGQDGLPGAPGPPGDQGHVGEQGYTGPQGPPG 1439
Cdd:COG5164    101 PAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPG--PGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPD 178

                          170
                   ....*....|
gi 1802828103 1440 QTGIPGPPGP 1449
Cdd:COG5164    179 DGGSTTPPNK 188
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 77-131 2.12e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 2.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1802828103   77 GPAGLPGEKGQRGENGQPGPAGEKGDKGPTGVPGFPGLDGVPGLPGSEGPRGKRG 131
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 74-130 2.53e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 2.53e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1802828103   74 GSAGPAGLPGEKGQRGENGQPGPAGEKGDKGPTGVPGFPGLDGVPGLPGSEGPRGKR 130
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 59-113 3.78e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 3.78e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1802828103   59 GQPGELGAQGPIGSLGSAGPAGLPGEKGQRGENGQPGPAGEKGDKGPTGVPGFPG 113
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 768-820 5.72e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 5.72e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1802828103  768 GLPGPPGAQGARGDPGIPGLQGQPGTPGFPGAKGFRGPEGNIGAPGCPGFPGP 820
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 68-122 5.83e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 5.83e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1802828103   68 GPIGSLGSAGPAGLPGEKGQRGENGQPGPAGEKGDKGPTGVPGFPGLDGVPGLPG 122
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 762-816 6.96e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 6.96e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1802828103  762 GIPGNRGLPGPPGAQGARGDPGIPGLQGQPGTPGFPGAKGFRGPEGNIGAPGCPG 816
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 71-127 1.03e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 1.03e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1802828103   71 GSLGSAGPAGLPGEKGQRGENGQPGPAGEKGDKGPTGVPGFPGLDGVPGLPGSEGPR 127
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1296-1350 1.81e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 1.81e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1802828103 1296 GQRGQQGARGPPGNQGREGPKGPMGIHGPQGPPGAVGHPGDQGFQGKPGPKGPTG 1350
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 89-143 3.01e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 3.01e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1802828103   89 GENGQPGPAGEKGDKGPTGVPGFPGLDGVPGLPGSEGPRGKRGVDGCNGSRGDPG 143
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 765-820 3.74e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 3.74e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1802828103  765 GNRGLPGPPGAQGARGDPGIPGLQGQPGTPGFPGAKGFRGPEGNIGAPGCPGFPGP 820
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 492-547 4.92e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 4.92e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1802828103  492 GPPGPRGIQGPPGTQGKKGQMGYPGRHGEKGDPGLSGAMGSPGLPGTPGSAGQHGE 547
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1290-1348 4.97e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 4.97e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1802828103 1290 GAPGISGQRGQQGARGPPGNQGREGPKGPmgiHGPQGPPGAVGHPGDQGFQGKPGPKGP 1348
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGP---PGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 759-805 5.54e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 5.54e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1802828103  759 GPPGIPGNRGLPGPPGAQGARGDPGIPGLQGQPGTPGFPGAKGFRGP 805
Cdd:pfam01391   10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1038-1348 5.85e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 44.64  E-value: 5.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1038 GQPGDQGDVGLPGMPGNPGLTGPKGSKGKRGDPtlllGIRGQKGPPGDPGLTGFCGLPGEKGSAGIQGQPGRLGSKGESG 1117
Cdd:COG5164      7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPA----GNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTT 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1118 ypgipgfpgapgppglpgepgEKGKQGLSGPPGLQGLAGSQGRKGLPGLPGLDGLDGLKGQKGSAGAPGQSETGRPGysg 1197
Cdd:COG5164     83 ---------------------PAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPG--- 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1198 elgpkgdrgkpgwPGISIPGAPGERGFPGFPGIRGPVGPAGPMGRSPSSAPPGLPGDQGPPGLDGIRGQpgnpgppgeti 1277
Cdd:COG5164    139 -------------DGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTD----------- 194

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1802828103 1278 fvqGDPGDTGIQGAPGISGQRGQQGARGPPGNQ-GREGPKGPMGIHGPQGPPGAVGHPGDQGFQGKPGPKGP 1348
Cdd:COG5164    195 ---IPTGGTPRQGPDGPVKKDDKNGKGNPPDDRgGKTGPKDQRPKTNPIERRGPERPEAAALPAELTALEAE 263
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1281-1335 6.30e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 6.30e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1802828103 1281 GDPGDTGIQGAPGISGQRGQQGARGPPGNQGREGPKGPMGIHGPQGPPGAVGHPG 1335
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 54-105 7.16e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 7.16e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1802828103   54 EKGSRGQPGELGAQGPIGSLGSAGPAGLPGEKGQRGENGQPGPAGEKGDKGP 105
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 116-167 1.22e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 1.22e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1802828103  116 GVPGLPGSEGPRGKRGVDGCNGSRGDPGFPGENGYIGPRGPSGNPGQKGEKG 167
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 54-109 1.22e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 1.22e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1802828103   54 EKGSRGQPGELGAQGPIGSLGSAGPAGLPGEKGQRGENGQPGPAGEKGDKGPTGVP 109
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1280-1334 1.88e-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: 1.88e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1802828103 1280 QGDPGDTGIQGAPGISGQRGQQGARGPPGNQGREGPKGPMGIHGPQGPPGAVGHP 1334
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1014-1070 2.13e-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: 2.13e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1802828103 1014 GLMGFPGLRGFPGPKGFKGMTGFQGQPGDQGDVGLPGMPGNPGLTGPKGSKGKRGDP 1070
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 490-544 2.22e-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: 2.22e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1802828103  490 SAGPPGPRGIQGPPGTQGKKGQMGYPgrhGEKGDPGLSGAMGSPGLPGTPGSAGQ 544
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPP---GEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 780-841 2.47e-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: 2.47e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1802828103  780 GDPGIPGLQGQPGTPGFPGAKGFRGPEGNigaPGCPGFPGPlcdMGLPGPPGLRGVIGLPGP 841
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGP---PGEPGPPGP---PGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1305-1359 2.57e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.47  E-value: 2.57e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1802828103 1305 GPPGNQGREGPKGPMGIHGPQGPPGAVGHPGDQGFQGKPGPKGPTGFIGDPGEPG 1359
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 56-110 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: 37.47  E-value: 2.62e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1802828103   56 GSRGQPGELGAQGPIGSLGSAGPAGLPGEKGQRGENGQPGPAGEKGDKGPTGVPG 110
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 113-167 5.66e-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: 36.70  E-value: 5.66e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1802828103  113 GLDGVPGLPGSEGPRGKRGVDGCNGSRGDPGFPGENGYIGPRGPSGNPGQKGEKG 167
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 964-1014 6.18e-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: 6.18e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1802828103  964 EKGQKGEPGFPGENGFRGERGEKGNIGFRGAPGFPGKNGVPGLPGDHGDTG 1014
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 795-850 6.43e-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: 6.43e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1802828103  795 GFPGAKGFRGPEGNIGAPGCPGFPGPLCDMGLPGPPGLRGVIGLPGPQGLPGFKGQ 850
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 1149-1450 6.46e-03

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: 41.15  E-value: 6.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1149 PGLQGLAGSQGRKGLPGLPGLDGLDGLKG--QKGSAGAPGQSETGRPGYSGELGPKGDR----GKPGWPGISIPGAPGER 1222
Cdd:pfam09606  142 QMSRVGRMQPGGQAGGMMQPSSGQPGSGTpnQMGPNGGPGQGQAGGMNGGQQGPMGGQMppqmGVPGMPGPADAGAQMGQ 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1223 GFPGFPGIRGPVGPAGPMGRSPSSAPPGLPGDQGPPGL---------DGIRGQPGNPGPPGETIFVQGDPGDTGIQGAPG 1293
Cdd:pfam09606  222 QAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMginqmqqmpQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIG 301

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1294 ISGQRGQQGARGPPGNQGREGP-KGPMGIHGPQGPPGAVGHPGDQGFQGKPGPKGPTGFIGDPGEPGRRDDSCPTIPGPP 1372
Cdd:pfam09606  302 DQNNYQQQQTRQQQQQQGGNHPaAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPVPG 381

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802828103 1373 GEAGQRGDDGSIGLSGPIGHPGPQGRKGEEGSCGLPG--------QDGLPGAPGPPGDQGHVGEQGYTGPQGPPGQTGIP 1444
Cdd:pfam09606  382 QQVRQVTPNQFMRQSPQPSVPSPQGPGSQPPQSHPGGmipspaliPSPSPQMSQQPAQQRTIGQDSPGGSLNTPGQSAVN 461


                   ....*.
gi 1802828103 1445 GPPGPH 1450
Cdd:pfam09606  462 SPLNPQ 467
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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