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Conserved domains on  [gi|2158835932|ref|NP_001155862|]
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collagen alpha-2(IV) chain precursor [Gallus gallus]

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 ...
 1604-1713 2.02e-63

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: 210.91  E-value: 2.02e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1604 IAVHSQEASIPRCPEGWRSLWIGYSFLMHTAAGdEGGGQSLVSPGSCLEDFRATPFIECNGArGTCHYFANKYSFWLTTI 1683
Cdd:pfam01413    3 IAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLSTV 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2158835932 1684 DQPFQsKPSADTLKAGL-IRSHISRCQVCMK 1713
Cdd:pfam01413   81 EEQFR-KPMSQTPKAGNeLRSYISRCVVCEA 110
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1494-1599 1.58e-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: 1.58e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1494 YLLVKHSQSDQEPMCPIGMNKLWSGYSLLYFEGQEKAHNQDLGLAGSCLARFSTMPFLYCNPGDICYYANrNDKSYWLST 1573
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2158835932 1574 TA-----PLPMMPVAEEEIRPYISRCSVCEA 1599
Cdd:pfam01413   80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 705-944 1.17e-29

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 124.25  E-value: 1.17e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  705 GARGFPGDPGPVGFPGLNGTRGDPGREGYPGPPGFIGPRGDRGPNGLPGLQGHPGLMGKSGAPGLAGQKGAPGdvlgaaa 784
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG------- 189

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  785 gPRGDDGLPGFPGLKGAPGDQGIPGIRGADGNPGLPGPKGDPGlQGLPGLMGLPGTPGTHGFPGPPGNRGPDGGPGSQGP 864
Cdd:NF038329   190 -EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  865 LGPPGARGEDGEQGFPGPVGMKGLSGDkgetgfpglQGIPGVTGPPGISGMDGFPGDKGSRGSPGIDGFKGMPGLKGRPG 944
Cdd:NF038329   268 AGPDGPDGKDGERGPVGPAGKDGQNGK---------DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1133-1350 1.26e-26

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 115.39  E-value: 1.26e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1133 DPGLPGIEGLKGIQGVPGSLGQKGLPGLVGPPGQQGSPGTPGFQGEKGAPGWPGLPGQAGLPGLRGISGLHGLPGTKGLP 1212
Cdd:NF038329   121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1213 GSPGPDG----YGSAGFPGPVGDKGEAGEPSRveGSQGPPGQKGDRGVPGVQGPFGIPGQDGLPGPPGISNISGYPGDTG 1288
Cdd:NF038329   201 GPAGEQGpagpAGPDGEAGPAGEDGPAGPAGD--GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932 1289 SPGLDGVPGYPGLHGQPGIPAPPGSKGESGRAGVSGQ---AGPKGTRGDPGLPGRPGIPGYPGPK 1350
Cdd:NF038329   279 ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKdgkDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 844-1079 1.14e-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: 109.22  E-value: 1.14e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  844 HGFPGPPGNRGPDGGPGSQGPLGPPGARGEDGEQgfpGPVGMKGLSGDKGETGFPGLQGIPGVTGPPGISGMDGFPGDKG 923
Cdd:NF038329   113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPA---GPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG 189

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  924 SRGSPGIDGFKGMPGLKGRPGIKGIKGEFGLLGTRGDKGAQGaRGFKGDRGEQGPPGEPPKLKPSMMMEVKGEKGDAGET 1003
Cdd:NF038329   190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2158835932 1004 GTKGFFGIKGSKGMPGLPGKTGIPGSPGhpsyVPGVKGDIGAKGLTGLKGYPGPTGSPGIRGFPGSTGGRGDKGAP 1079
Cdd:NF038329   269 GPDGPDGKDGERGPVGPAGKDGQNGKDG----LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1242-1487 1.48e-22

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 102.68  E-value: 1.48e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1242 EGSQGPPGQKGDRGVPGVQGPFGIPGQDGLPGPPGISNISGYPGDTGSPGLDGVPGYPGLHGQPGIPAPPGSKGESGRAG 1321
Cdd:NF038329   116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1322 VSGQAGPKGTRGDPGLPGRPGIPGYPGPKGRKGEQGViGFIGTIGFPGDLGPIGPKGDRGLTGFQGppgspglppipprl 1401
Cdd:NF038329   196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDG-------------- 260

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1402 vaEQGSPGPRGNAGPRGSPGDAGPQgppgepglrGLPGEPGLQGRGGIPAPPGSRGEQGAMGFQGPVGFEGQPGRPGSPG 1481
Cdd:NF038329   261 --PRGDRGEAGPDGPDGKDGERGPV---------GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329


                   ....*.
gi 2158835932 1482 LPGMPG 1487
Cdd:NF038329   330 KDGKDG 335
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 69-360 3.09e-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: 95.74  E-value: 3.09e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932   69 GSQGFPGPPGLMGIPGLQGPKGHKGERGHPGISGPKGETGQRGVTGFPGADGVPGHPGQPGSRGKPGHDGCNGTVGDPGD 148
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  149 PGTPGHSGFPGTIGVQGPKGQKGE--PYVLPPDIASRHRGDPGDPGFTGFPGAPGTLGIQGPIgprgvpgrpgppgspgp 226
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPagEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKD----------------- 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  227 qgpqgnrglgfyGEKGEqgspgppgppglptreligvptdkhKGERGEPGQKGEAGFPGvllfapEKGEEGVMGFPGQRG 306
Cdd:NF038329   260 ------------GPRGD-------------------------RGEAGPDGPDGKDGERG------PVGPAGKDGQNGKDG 296

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2158835932  307 LPGNDGFPGLSGERGFPGFDGQPGQYGPRGGKGEQGEMGPPGPPAYVPYRIPRK 360
Cdd:NF038329   297 LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQK 350
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 287-580 2.74e-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: 2.74e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  287 LLFAPEKGEEGVMGFPGQRGLPGNDGFPGLSGERGFPGFDGQPGQYGPRGGKGEQGEMGPPGPPayvpyriprkgvrGDP 366
Cdd:NF038329   113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA-------------GKD 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  367 GSPGASGLRGEQGEQGDRGLPGipgfsdgdadKPGLPGEIGPKGEKGEEGsPAYQAGPPGFPGKhgepgirgppgppgtp 446
Cdd:NF038329   180 GEAGAKGPAGEKGPQGPRGETG----------PAGEQGPAGPAGPDGEAG-PAGEDGPAGPAGD---------------- 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  447 gslfGLKGQEGTPGRPGVQGFPGPRGQRGPKGEEGDcskcllsdelrrgstgprgppgfpgtPGQPGRKGEPGDQGPHGI 526
Cdd:NF038329   233 ----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD--------------------------RGEAGPDGPDGKDGERGP 282

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2158835932  527 PGYAGAKGQSGQEGLPGPKGEKGDSiyittkgtkgirGDPGLPGIRGEDGFPGR 580
Cdd:NF038329   283 VGPAGKDGQNGKDGLPGKDGKDGQN------------GKDGLPGKDGKDGQPGK 324
 
Name Accession Description Interval E-value
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1604-1713 2.02e-63

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: 210.91  E-value: 2.02e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1604 IAVHSQEASIPRCPEGWRSLWIGYSFLMHTAAGdEGGGQSLVSPGSCLEDFRATPFIECNGArGTCHYFANKYSFWLTTI 1683
Cdd:pfam01413    3 IAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLSTV 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2158835932 1684 DQPFQsKPSADTLKAGL-IRSHISRCQVCMK 1713
Cdd:pfam01413   81 EEQFR-KPMSQTPKAGNeLRSYISRCVVCEA 110
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1494-1599 1.58e-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: 1.58e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1494 YLLVKHSQSDQEPMCPIGMNKLWSGYSLLYFEGQEKAHNQDLGLAGSCLARFSTMPFLYCNPGDICYYANrNDKSYWLST 1573
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2158835932 1574 TA-----PLPMMPVAEEEIRPYISRCSVCEA 1599
Cdd:pfam01413   80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1604-1714 2.77e-54

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: 184.90  E-value: 2.77e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  1604 IAVHSQEASIPRCPEGWRSLWIGYSFLMHTaAGDEGGGQSLVSPGSCLEDFRATPFIECNGaRGTCHYFANK-YSFWLTT 1682
Cdd:smart00111    4 IAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASRNdYSFWLST 81

                            90       100       110
                    ....*....|....*....|....*....|...
gi 2158835932  1683 IDQPFQ-SKPSADTLKAGLIRSHISRCQVCMKN 1714
Cdd:smart00111   82 IEPSDQfTAPRPMTPKAGDLRPYISRCQVCEKP 114
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1493-1600 1.01e-45

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: 160.63  E-value: 1.01e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  1493 GYLLVKHSQSDQEPMCPIGMNKLWSGYSLLYFEGQEKAHNQDLGLAGSCLARFSTMPFLYCNPGDICYYANRNDKSYWLS 1572
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 2158835932  1573 T-------TAPLPMMPVAeEEIRPYISRCSVCEAP 1600
Cdd:smart00111   81 TiepsdqfTAPRPMTPKA-GDLRPYISRCQVCEKP 114
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 705-944 1.17e-29

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 124.25  E-value: 1.17e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  705 GARGFPGDPGPVGFPGLNGTRGDPGREGYPGPPGFIGPRGDRGPNGLPGLQGHPGLMGKSGAPGLAGQKGAPGdvlgaaa 784
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG------- 189

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  785 gPRGDDGLPGFPGLKGAPGDQGIPGIRGADGNPGLPGPKGDPGlQGLPGLMGLPGTPGTHGFPGPPGNRGPDGGPGSQGP 864
Cdd:NF038329   190 -EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  865 LGPPGARGEDGEQGFPGPVGMKGLSGDkgetgfpglQGIPGVTGPPGISGMDGFPGDKGSRGSPGIDGFKGMPGLKGRPG 944
Cdd:NF038329   268 AGPDGPDGKDGERGPVGPAGKDGQNGK---------DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 790-1023 1.78e-27

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 117.70  E-value: 1.78e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  790 DGLPGFPGLKGAPGDQGIPGIRGADGNPGLPGPKGDPGLQGLPGLMGLPGTPGTHGFPGPPGNRGPDGGPGSQGPLGPPG 869
Cdd:NF038329   116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  870 ARGEDGEQGFPGPVGMKGLSGDKGETGFPGLQGIPGV--TGPPGISGMDGFPGDKGSRGSPGIDGFKGMPGLKGRPGIKG 947
Cdd:NF038329   196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2158835932  948 IKGEFGLLGTRGDKGAQGARGFKGDRGEQGPPGEPpklkpsmmmevkGEKGDAGETGTKGFFGIKGSKGMPGLPGK 1023
Cdd:NF038329   276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD------------GLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 689-910 2.72e-27

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 117.31  E-value: 2.72e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  689 KGSQGNPGLPGATGTKGARGFPGDPGPVGFPGLNGTRGDPGREGYPGPPGFIGPRGDRGPNGLPGLQGHPGLMGKSGAPG 768
Cdd:NF038329   119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  769 LAGQKGAPGDVlgAAAGPRGDDGLPGFPGLKGAPGD--QGIPGIRGADGNPGLPGPKGDPGLQGLPGLMGLPGTPGTHGF 846
Cdd:NF038329   199 ETGPAGEQGPA--GPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2158835932  847 PGPPGNRGPDGGPGSQGPLGPPGARGEDGEQGFPGPVGMKGLSGDKGETGFPGLQGIPGVTGPP 910
Cdd:NF038329   277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1133-1350 1.26e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 115.39  E-value: 1.26e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1133 DPGLPGIEGLKGIQGVPGSLGQKGLPGLVGPPGQQGSPGTPGFQGEKGAPGWPGLPGQAGLPGLRGISGLHGLPGTKGLP 1212
Cdd:NF038329   121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1213 GSPGPDG----YGSAGFPGPVGDKGEAGEPSRveGSQGPPGQKGDRGVPGVQGPFGIPGQDGLPGPPGISNISGYPGDTG 1288
Cdd:NF038329   201 GPAGEQGpagpAGPDGEAGPAGEDGPAGPAGD--GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932 1289 SPGLDGVPGYPGLHGQPGIPAPPGSKGESGRAGVSGQ---AGPKGTRGDPGLPGRPGIPGYPGPK 1350
Cdd:NF038329   279 ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKdgkDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 664-890 2.44e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 114.23  E-value: 2.44e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  664 QVIEDFSRGEATDPVWSGGGCVRPPKGSQGNPGLPGATGTKGARGFPGDPGPVGFPGLNGTRGDPGREGYPGPPGFIGPR 743
Cdd:NF038329   112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  744 GDRGPNGLPGLQGHPGLMGKSGAPGLAGQKGAPGDVLGAAAGPRGDDGLPGFPGLKGAPGDQGIPGIRGADGNPGLPGPK 823
Cdd:NF038329   192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD 271

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2158835932  824 GDPGLQGLPGLMGLPGTPGTHGFPGPPGNRGPDGGPGSQGPLGPPGARGEDGEQGFPGPVGMKGLSG 890
Cdd:NF038329   272 GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 844-1079 1.14e-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: 1.14e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  844 HGFPGPPGNRGPDGGPGSQGPLGPPGARGEDGEQgfpGPVGMKGLSGDKGETGFPGLQGIPGVTGPPGISGMDGFPGDKG 923
Cdd:NF038329   113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPA---GPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG 189

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  924 SRGSPGIDGFKGMPGLKGRPGIKGIKGEFGLLGTRGDKGAQGaRGFKGDRGEQGPPGEPPKLKPSMMMEVKGEKGDAGET 1003
Cdd:NF038329   190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2158835932 1004 GTKGFFGIKGSKGMPGLPGKTGIPGSPGhpsyVPGVKGDIGAKGLTGLKGYPGPTGSPGIRGFPGSTGGRGDKGAP 1079
Cdd:NF038329   269 GPDGPDGKDGERGPVGPAGKDGQNGKDG----LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 969-1217 4.50e-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: 107.30  E-value: 4.50e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  969 FKGDRGEQGPPGEPPKLKPsmmmevKGEKGDAGETGTKGFFGIKGSKGMPGLPGKTGIPGSPGHpsyvpgvKGDIGAKGL 1048
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGE------QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGP-------QGPAGKDGE 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1049 TGLKGYPGPTGSPGIRGFPGSTGGRGDKGAPGISGHFGTPGSHGEIGEPGDtinlpgmpGLKGEVGVPGLTGLRGGPGQK 1128
Cdd:NF038329   182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD--------GQQGPDGDPGPTGEDGPQGPD 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1129 GEGGDPGLPGIEGLKGIQGVPGSLGQKGLPGLVGPPGQQGSPGTPGFQGEKGAPGWPGLPGQAGLPGLRGISGLHGLPGT 1208
Cdd:NF038329   254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333


                   ....*....
gi 2158835932 1209 KGLPGSPGP 1217
Cdd:NF038329   334 DGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1242-1487 1.48e-22

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 102.68  E-value: 1.48e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1242 EGSQGPPGQKGDRGVPGVQGPFGIPGQDGLPGPPGISNISGYPGDTGSPGLDGVPGYPGLHGQPGIPAPPGSKGESGRAG 1321
Cdd:NF038329   116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1322 VSGQAGPKGTRGDPGLPGRPGIPGYPGPKGRKGEQGViGFIGTIGFPGDLGPIGPKGDRGLTGFQGppgspglppipprl 1401
Cdd:NF038329   196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDG-------------- 260

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1402 vaEQGSPGPRGNAGPRGSPGDAGPQgppgepglrGLPGEPGLQGRGGIPAPPGSRGEQGAMGFQGPVGFEGQPGRPGSPG 1481
Cdd:NF038329   261 --PRGDRGEAGPDGPDGKDGERGPV---------GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329


                   ....*.
gi 2158835932 1482 LPGMPG 1487
Cdd:NF038329   330 KDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 69-360 3.09e-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: 95.74  E-value: 3.09e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932   69 GSQGFPGPPGLMGIPGLQGPKGHKGERGHPGISGPKGETGQRGVTGFPGADGVPGHPGQPGSRGKPGHDGCNGTVGDPGD 148
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  149 PGTPGHSGFPGTIGVQGPKGQKGE--PYVLPPDIASRHRGDPGDPGFTGFPGAPGTLGIQGPIgprgvpgrpgppgspgp 226
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPagEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKD----------------- 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  227 qgpqgnrglgfyGEKGEqgspgppgppglptreligvptdkhKGERGEPGQKGEAGFPGvllfapEKGEEGVMGFPGQRG 306
Cdd:NF038329   260 ------------GPRGD-------------------------RGEAGPDGPDGKDGERG------PVGPAGKDGQNGKDG 296

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2158835932  307 LPGNDGFPGLSGERGFPGFDGQPGQYGPRGGKGEQGEMGPPGPPAYVPYRIPRK 360
Cdd:NF038329   297 LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQK 350
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 287-580 2.74e-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: 2.74e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  287 LLFAPEKGEEGVMGFPGQRGLPGNDGFPGLSGERGFPGFDGQPGQYGPRGGKGEQGEMGPPGPPayvpyriprkgvrGDP 366
Cdd:NF038329   113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA-------------GKD 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  367 GSPGASGLRGEQGEQGDRGLPGipgfsdgdadKPGLPGEIGPKGEKGEEGsPAYQAGPPGFPGKhgepgirgppgppgtp 446
Cdd:NF038329   180 GEAGAKGPAGEKGPQGPRGETG----------PAGEQGPAGPAGPDGEAG-PAGEDGPAGPAGD---------------- 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  447 gslfGLKGQEGTPGRPGVQGFPGPRGQRGPKGEEGDcskcllsdelrrgstgprgppgfpgtPGQPGRKGEPGDQGPHGI 526
Cdd:NF038329   233 ----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD--------------------------RGEAGPDGPDGKDGERGP 282

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2158835932  527 PGYAGAKGQSGQEGLPGPKGEKGDSiyittkgtkgirGDPGLPGIRGEDGFPGR 580
Cdd:NF038329   283 VGPAGKDGQNGKDGLPGKDGKDGQN------------GKDGLPGKDGKDGQPGK 324
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1267-1488 3.68e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 92.28  E-value: 3.68e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1267 GQDGLPGPPGISNISGYPGDTGSPGLDGVPGYPGLHGQPGIPAPPGSKGESGRAGVSGQAGPKGTRGDPGLPGRPGIPGY 1346
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1347 PGPKGRKGEQGVIGFIGTIGFPGDLGPIGPKGDRGltgfqgppgspglppipprlvaeQGSPGPRGNAGPRGSPGDAGPQ 1426
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-----------------------DGQQGPDGDPGPTGEDGPQGPD 253

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2158835932 1427 GPPGEPGLRGLPGEPGLQGRGGIPAPPGSRGEQGAMGFQGPVGFEGQPGRPGSPGLPGMPGR 1488
Cdd:NF038329   254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK 315
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 235-481 6.56e-17

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 85.34  E-value: 6.56e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  235 LGFYGEKGEQGSPGPPGPPGLPTReligvptdkhKGERGEPGQKGEAGFPGVLLFAPEKGEEGVMGFPGQRGLPGNDGFP 314
Cdd:NF038329   113 LKGDGEKGEPGPAGPAGPAGEQGP----------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  315 GLSGERGFPGFDGQPGQYGPRGGKGEQGEMGPPG-PPAYVPYRIPRKGVRGDPGSPGASGLRGEQGEQGDRGLPGIPGfS 393
Cdd:NF038329   183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGeAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG-P 261

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  394 DGDADKPGLPGEIGPKGEKGEEGSPAY--QAGPPGFPGKHGEPgirgppgppgtpgslfGLKGQEGTPGRPGVQGFPGPR 471
Cdd:NF038329   262 RGDRGEAGPDGPDGKDGERGPVGPAGKdgQNGKDGLPGKDGKD----------------GQNGKDGLPGKDGKDGQPGKD 325

                          250
                   ....*....|
gi 2158835932  472 GQRGPKGEEG 481
Cdd:NF038329   326 GLPGKDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 494-777 2.90e-15

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 80.33  E-value: 2.90e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  494 RGSTGPRGPPGFPGTPGQPGRKGEPGDQGPHGIPGYAGAKGQSGQEGLPGPKGEKGDsiyittKGTKGIRGDPGLPGIRG 573
Cdd:NF038329   122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK------DGEAGAKGPAGEKGPQG 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  574 EDGFPGRdgldglpglpglpgdgiRGLPGDPGYPGELGPKGFPGEIGLPGEGYPGPKGYRGLPGDRGtdghpgppglpgp 653
Cdd:NF038329   196 PRGETGP-----------------AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTG------------- 245

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  654 pgepgqldcgqviedfsrgeatdpvwsgggcvrpPKGSQGNPGLPGATGTKGARGFPGDPGPVGFPGLNGTRGDPGREGY 733
Cdd:NF038329   246 ----------------------------------EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2158835932  734 PGP---PGFIGPRGDRGPNGLPGLQGHPGLMGKSGAPGLAGQKGAPG 777
Cdd:NF038329   292 NGKdglPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 35-208 3.10e-13

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: 74.17  E-value: 3.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932   35 AGGKSYTGPCGGRDCSGGCQCFPEKGARGQPGILGSQGFPGPPGLMGIPGLQGPKGHKGERGHPGISGPKGETGQRGVtg 114
Cdd:NF038329   134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP-- 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  115 fPGADGVPGHPGQPGSRGKPGhDGCNGTVGDPGDPGTPGHSGFPGTIGVQGPKGQKGEPYVLPPDIASRHRGDPGDPGFT 194
Cdd:NF038329   212 -AGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKD 289

                          170
                   ....*....|....
gi 2158835932  195 GFPGAPGTLGIQGP 208
Cdd:NF038329   290 GQNGKDGLPGKDGK 303
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 196-430 4.41e-13

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: 73.40  E-value: 4.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  196 FPGAPGTLGIQGPIGPRGVPGRPGPPGSPGPQGPQGNRG-LGFYGEKGEQGSPGPPGPpglptreligvptdkhKGERGE 274
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGpQGERGEKGPAGPQGEAGP----------------QGPAGK 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  275 PGQKGEAGFPGVLLFAPEKGEEGVMGFPGQRGLPGNDGFPGLSGERGFPGFDGQpGQYGPRGGKGEQGEMGPPGPPAyvp 354
Cdd:NF038329   179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDG--- 254

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2158835932  355 yRIPRKGVRGDPGSPGASGLRGEQGEQGDRGLPGipgfSDGDADKPGLPGEIGPKGEKGEEGSPAyQAGPPGFPGK 430
Cdd:NF038329   255 -PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG----KDGQNGKDGLPGKDGKDGQNGKDGLPG-KDGKDGQPGK 324
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 58-153 1.39e-08

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 59.15  E-value: 1.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932   58 EKGARGQPGILGSQGFPGPPGLMGIPGLQGPKGHKGERGHPGISGPKGETGQRGVTGFPGADGVPGHPGQPGSRGKPGHD 137
Cdd:NF038329   243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                           90
                   ....*....|....*.
gi 2158835932  138 GCNGTVGDPGDPGTPG 153
Cdd:NF038329   323 GKDGLPGKDGKDGQPG 338
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
762-1010 2.97e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 51.95  E-value: 2.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  762 GKSGAPGLAGQKGAPGDvlGAAAGPRGDDGLPGFPGLKGAPGDQGIPGIRGADGNPGLPGPKGDPGLQGLPGLMGLPGTP 841
Cdd:COG5164      7 GKTGPSDPGGVTTPAGS--QGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPA 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  842 GTHGFPGPPGNRGPDGGPGSQGPLGPPGARGEDGEQGFPGPV-----GMKGLSGDKGET-GFPGLQGIPGVTGPPGISGM 915
Cdd:COG5164     85 QNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTtppsgGSTTPPGDGGSTpPGPGSTGPGGSTTPPGDGGS 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  916 DGFPGDKGSRGSPGIDGFKGMP--GLKGRPGIKGIKGEFGLLGTRGDKGAQGARGFKGDRGEQGPPGEP-PKLKPSMMME 992
Cdd:COG5164    165 TTPPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQrPKTNPIERRG 244

                          250
                   ....*....|....*...
gi 2158835932  993 VKGEKGDAGETGTKGFFG 1010
Cdd:COG5164    245 PERPEAAALPAELTALEA 262
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1405-1511 9.05e-06

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 50.29  E-value: 9.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1405 QGSPGPRGNAGPRGSPGDAGPQGPPGEPGLRGLPGEPGLQGRGGIPAPPGSRGEQGAMGFQGPVGFEGQPGRPGSPGLPG 1484
Cdd:NF038329   125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204

                           90       100
                   ....*....|....*....|....*..
gi 2158835932 1485 MPGRSVSIGYLLVKHSQSDQEPMCPIG 1511
Cdd:NF038329   205 EQGPAGPAGPDGEAGPAGEDGPAGPAG 231
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 797-853 1.15e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.41  E-value: 1.15e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2158835932  797 GLKGAPGDQGIPGIRGADGNPGLPGPKGDPGLQGLPGLMGLPGTPGTHGFPGPPGNR 853
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1137-1342 2.29e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 48.87  E-value: 2.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1137 PGIEGLKGIQGVPGSLGQKGLPGLVGPPGQQGSPGTPGFQGEKGAPGWPGLPGQAGLPGLRGISGLHGLPGTKGLPGSPG 1216
Cdd:COG5164     48 AQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1217 PDGYGSAGFPGPVGDKGEAGEPSRVEGSQGPPGQKGDRGVPGVQGPFGIPGQDGLPGPPGISNISGYPGDTGSPGLDGVP 1296
Cdd:COG5164    128 PPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDG 207

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2158835932 1297 GYPGLHGQPGIPAPPGSKGESGRAGVSGQAGPKGTRGDPGLPGRPG 1342
Cdd:COG5164    208 PVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAAL 253
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1159-1215 1.14e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 1.14e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2158835932 1159 GLVGPPGQQGSPGTPGFQGEKGAPGWPGLPGQAGLPGLRGISGLHGLPGTKGLPGSP 1215
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 72-128 1.21e-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: 41.33  E-value: 1.21e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2158835932   72 GFPGPPGLMGIPGLQGPKGHKGERGHPGISGPKGETGQRGVTGFPGADGVPGHPGQP 128
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 1222-1357 2.74e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 45.83  E-value: 2.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1222 SAGFPGPVGDKGEAGEPSRVEGSQGPPGQKGDRGVPGVQgpfGIPGQDGLPGPPGisnisgyPGDTGSPGL--DGVPGYP 1299
Cdd:PRK14959   374 SGGGASAPSGSAAEGPASGGAATIPTPGTQGPQGTAPAA---GMTPSSAAPATPA-------PSAAPSPRVpwDDAPPAP 443

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2158835932 1300 GLHGQPGIPAP--PGSKGESGR-AGVSGQAGPKGTRGDPGLPGrPGIPGYPGP--------KGRKGEQG 1357
Cdd:PRK14959   444 PRSGIPPRPAPrmPEASPVPGApDSVASASDAPPTLGDPSDTA-EHTPSGPRTwdgflefcQGRNGQGG 511
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1415-1511 1.26e-03

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: 43.36  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1415 GPRGSPGDAGPQGPPGEPGLRGLPGEPGLQGRGGIPAPPGSRGEQGAMGFQGPVGFEGQPGRPGSPGLPGMPGRSVSIGY 1494
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90
                   ....*....|....*..
gi 2158835932 1495 LLVKHSQSDQEPMCPIG 1511
Cdd:NF038329   197 RGETGPAGEQGPAGPAG 213
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1044-1098 7.46e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 7.46e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932 1044 GAKGLTGLKGYPGPTGSPGIRGFPGSTGGRGDKGAPGISGHFGTPGSHGEIGEPG 1098
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 ...
 1604-1713 2.02e-63

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: 210.91  E-value: 2.02e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1604 IAVHSQEASIPRCPEGWRSLWIGYSFLMHTAAGdEGGGQSLVSPGSCLEDFRATPFIECNGArGTCHYFANKYSFWLTTI 1683
Cdd:pfam01413    3 IAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLSTV 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2158835932 1684 DQPFQsKPSADTLKAGL-IRSHISRCQVCMK 1713
Cdd:pfam01413   81 EEQFR-KPMSQTPKAGNeLRSYISRCVVCEA 110
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1494-1599 1.58e-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: 1.58e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1494 YLLVKHSQSDQEPMCPIGMNKLWSGYSLLYFEGQEKAHNQDLGLAGSCLARFSTMPFLYCNPGDICYYANrNDKSYWLST 1573
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2158835932 1574 TA-----PLPMMPVAEEEIRPYISRCSVCEA 1599
Cdd:pfam01413   80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1604-1714 2.77e-54

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: 184.90  E-value: 2.77e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  1604 IAVHSQEASIPRCPEGWRSLWIGYSFLMHTaAGDEGGGQSLVSPGSCLEDFRATPFIECNGaRGTCHYFANK-YSFWLTT 1682
Cdd:smart00111    4 IAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASRNdYSFWLST 81

                            90       100       110
                    ....*....|....*....|....*....|...
gi 2158835932  1683 IDQPFQ-SKPSADTLKAGLIRSHISRCQVCMKN 1714
Cdd:smart00111   82 IEPSDQfTAPRPMTPKAGDLRPYISRCQVCEKP 114
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1493-1600 1.01e-45

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: 160.63  E-value: 1.01e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  1493 GYLLVKHSQSDQEPMCPIGMNKLWSGYSLLYFEGQEKAHNQDLGLAGSCLARFSTMPFLYCNPGDICYYANRNDKSYWLS 1572
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 2158835932  1573 T-------TAPLPMMPVAeEEIRPYISRCSVCEAP 1600
Cdd:smart00111   81 TiepsdqfTAPRPMTPKA-GDLRPYISRCQVCEKP 114
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 705-944 1.17e-29

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 124.25  E-value: 1.17e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  705 GARGFPGDPGPVGFPGLNGTRGDPGREGYPGPPGFIGPRGDRGPNGLPGLQGHPGLMGKSGAPGLAGQKGAPGdvlgaaa 784
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG------- 189

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  785 gPRGDDGLPGFPGLKGAPGDQGIPGIRGADGNPGLPGPKGDPGlQGLPGLMGLPGTPGTHGFPGPPGNRGPDGGPGSQGP 864
Cdd:NF038329   190 -EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  865 LGPPGARGEDGEQGFPGPVGMKGLSGDkgetgfpglQGIPGVTGPPGISGMDGFPGDKGSRGSPGIDGFKGMPGLKGRPG 944
Cdd:NF038329   268 AGPDGPDGKDGERGPVGPAGKDGQNGK---------DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 790-1023 1.78e-27

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 117.70  E-value: 1.78e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  790 DGLPGFPGLKGAPGDQGIPGIRGADGNPGLPGPKGDPGLQGLPGLMGLPGTPGTHGFPGPPGNRGPDGGPGSQGPLGPPG 869
Cdd:NF038329   116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  870 ARGEDGEQGFPGPVGMKGLSGDKGETGFPGLQGIPGV--TGPPGISGMDGFPGDKGSRGSPGIDGFKGMPGLKGRPGIKG 947
Cdd:NF038329   196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2158835932  948 IKGEFGLLGTRGDKGAQGARGFKGDRGEQGPPGEPpklkpsmmmevkGEKGDAGETGTKGFFGIKGSKGMPGLPGK 1023
Cdd:NF038329   276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD------------GLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 689-910 2.72e-27

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 117.31  E-value: 2.72e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  689 KGSQGNPGLPGATGTKGARGFPGDPGPVGFPGLNGTRGDPGREGYPGPPGFIGPRGDRGPNGLPGLQGHPGLMGKSGAPG 768
Cdd:NF038329   119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  769 LAGQKGAPGDVlgAAAGPRGDDGLPGFPGLKGAPGD--QGIPGIRGADGNPGLPGPKGDPGLQGLPGLMGLPGTPGTHGF 846
Cdd:NF038329   199 ETGPAGEQGPA--GPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2158835932  847 PGPPGNRGPDGGPGSQGPLGPPGARGEDGEQGFPGPVGMKGLSGDKGETGFPGLQGIPGVTGPP 910
Cdd:NF038329   277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1133-1350 1.26e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 115.39  E-value: 1.26e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1133 DPGLPGIEGLKGIQGVPGSLGQKGLPGLVGPPGQQGSPGTPGFQGEKGAPGWPGLPGQAGLPGLRGISGLHGLPGTKGLP 1212
Cdd:NF038329   121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1213 GSPGPDG----YGSAGFPGPVGDKGEAGEPSRveGSQGPPGQKGDRGVPGVQGPFGIPGQDGLPGPPGISNISGYPGDTG 1288
Cdd:NF038329   201 GPAGEQGpagpAGPDGEAGPAGEDGPAGPAGD--GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932 1289 SPGLDGVPGYPGLHGQPGIPAPPGSKGESGRAGVSGQ---AGPKGTRGDPGLPGRPGIPGYPGPK 1350
Cdd:NF038329   279 ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKdgkDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 664-890 2.44e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 114.23  E-value: 2.44e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  664 QVIEDFSRGEATDPVWSGGGCVRPPKGSQGNPGLPGATGTKGARGFPGDPGPVGFPGLNGTRGDPGREGYPGPPGFIGPR 743
Cdd:NF038329   112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  744 GDRGPNGLPGLQGHPGLMGKSGAPGLAGQKGAPGDVLGAAAGPRGDDGLPGFPGLKGAPGDQGIPGIRGADGNPGLPGPK 823
Cdd:NF038329   192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD 271

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2158835932  824 GDPGLQGLPGLMGLPGTPGTHGFPGPPGNRGPDGGPGSQGPLGPPGARGEDGEQGFPGPVGMKGLSG 890
Cdd:NF038329   272 GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 844-1079 1.14e-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: 1.14e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  844 HGFPGPPGNRGPDGGPGSQGPLGPPGARGEDGEQgfpGPVGMKGLSGDKGETGFPGLQGIPGVTGPPGISGMDGFPGDKG 923
Cdd:NF038329   113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPA---GPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG 189

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  924 SRGSPGIDGFKGMPGLKGRPGIKGIKGEFGLLGTRGDKGAQGaRGFKGDRGEQGPPGEPPKLKPSMMMEVKGEKGDAGET 1003
Cdd:NF038329   190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2158835932 1004 GTKGFFGIKGSKGMPGLPGKTGIPGSPGhpsyVPGVKGDIGAKGLTGLKGYPGPTGSPGIRGFPGSTGGRGDKGAP 1079
Cdd:NF038329   269 GPDGPDGKDGERGPVGPAGKDGQNGKDG----LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 969-1217 4.50e-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: 107.30  E-value: 4.50e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  969 FKGDRGEQGPPGEPPKLKPsmmmevKGEKGDAGETGTKGFFGIKGSKGMPGLPGKTGIPGSPGHpsyvpgvKGDIGAKGL 1048
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGE------QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGP-------QGPAGKDGE 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1049 TGLKGYPGPTGSPGIRGFPGSTGGRGDKGAPGISGHFGTPGSHGEIGEPGDtinlpgmpGLKGEVGVPGLTGLRGGPGQK 1128
Cdd:NF038329   182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD--------GQQGPDGDPGPTGEDGPQGPD 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1129 GEGGDPGLPGIEGLKGIQGVPGSLGQKGLPGLVGPPGQQGSPGTPGFQGEKGAPGWPGLPGQAGLPGLRGISGLHGLPGT 1208
Cdd:NF038329   254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333


                   ....*....
gi 2158835932 1209 KGLPGSPGP 1217
Cdd:NF038329   334 DGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1242-1487 1.48e-22

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 102.68  E-value: 1.48e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1242 EGSQGPPGQKGDRGVPGVQGPFGIPGQDGLPGPPGISNISGYPGDTGSPGLDGVPGYPGLHGQPGIPAPPGSKGESGRAG 1321
Cdd:NF038329   116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1322 VSGQAGPKGTRGDPGLPGRPGIPGYPGPKGRKGEQGViGFIGTIGFPGDLGPIGPKGDRGLTGFQGppgspglppipprl 1401
Cdd:NF038329   196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDG-------------- 260

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1402 vaEQGSPGPRGNAGPRGSPGDAGPQgppgepglrGLPGEPGLQGRGGIPAPPGSRGEQGAMGFQGPVGFEGQPGRPGSPG 1481
Cdd:NF038329   261 --PRGDRGEAGPDGPDGKDGERGPV---------GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329


                   ....*.
gi 2158835932 1482 LPGMPG 1487
Cdd:NF038329   330 KDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 69-360 3.09e-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: 95.74  E-value: 3.09e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932   69 GSQGFPGPPGLMGIPGLQGPKGHKGERGHPGISGPKGETGQRGVTGFPGADGVPGHPGQPGSRGKPGHDGCNGTVGDPGD 148
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  149 PGTPGHSGFPGTIGVQGPKGQKGE--PYVLPPDIASRHRGDPGDPGFTGFPGAPGTLGIQGPIgprgvpgrpgppgspgp 226
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPagEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKD----------------- 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  227 qgpqgnrglgfyGEKGEqgspgppgppglptreligvptdkhKGERGEPGQKGEAGFPGvllfapEKGEEGVMGFPGQRG 306
Cdd:NF038329   260 ------------GPRGD-------------------------RGEAGPDGPDGKDGERG------PVGPAGKDGQNGKDG 296

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2158835932  307 LPGNDGFPGLSGERGFPGFDGQPGQYGPRGGKGEQGEMGPPGPPAYVPYRIPRK 360
Cdd:NF038329   297 LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQK 350
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 287-580 2.74e-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: 2.74e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  287 LLFAPEKGEEGVMGFPGQRGLPGNDGFPGLSGERGFPGFDGQPGQYGPRGGKGEQGEMGPPGPPayvpyriprkgvrGDP 366
Cdd:NF038329   113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA-------------GKD 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  367 GSPGASGLRGEQGEQGDRGLPGipgfsdgdadKPGLPGEIGPKGEKGEEGsPAYQAGPPGFPGKhgepgirgppgppgtp 446
Cdd:NF038329   180 GEAGAKGPAGEKGPQGPRGETG----------PAGEQGPAGPAGPDGEAG-PAGEDGPAGPAGD---------------- 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  447 gslfGLKGQEGTPGRPGVQGFPGPRGQRGPKGEEGDcskcllsdelrrgstgprgppgfpgtPGQPGRKGEPGDQGPHGI 526
Cdd:NF038329   233 ----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGD--------------------------RGEAGPDGPDGKDGERGP 282

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2158835932  527 PGYAGAKGQSGQEGLPGPKGEKGDSiyittkgtkgirGDPGLPGIRGEDGFPGR 580
Cdd:NF038329   283 VGPAGKDGQNGKDGLPGKDGKDGQN------------GKDGLPGKDGKDGQPGK 324
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1267-1488 3.68e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 92.28  E-value: 3.68e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1267 GQDGLPGPPGISNISGYPGDTGSPGLDGVPGYPGLHGQPGIPAPPGSKGESGRAGVSGQAGPKGTRGDPGLPGRPGIPGY 1346
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1347 PGPKGRKGEQGVIGFIGTIGFPGDLGPIGPKGDRGltgfqgppgspglppipprlvaeQGSPGPRGNAGPRGSPGDAGPQ 1426
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-----------------------DGQQGPDGDPGPTGEDGPQGPD 253

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2158835932 1427 GPPGEPGLRGLPGEPGLQGRGGIPAPPGSRGEQGAMGFQGPVGFEGQPGRPGSPGLPGMPGR 1488
Cdd:NF038329   254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK 315
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 235-481 6.56e-17

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 85.34  E-value: 6.56e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  235 LGFYGEKGEQGSPGPPGPPGLPTReligvptdkhKGERGEPGQKGEAGFPGVLLFAPEKGEEGVMGFPGQRGLPGNDGFP 314
Cdd:NF038329   113 LKGDGEKGEPGPAGPAGPAGEQGP----------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  315 GLSGERGFPGFDGQPGQYGPRGGKGEQGEMGPPG-PPAYVPYRIPRKGVRGDPGSPGASGLRGEQGEQGDRGLPGIPGfS 393
Cdd:NF038329   183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGeAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG-P 261

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  394 DGDADKPGLPGEIGPKGEKGEEGSPAY--QAGPPGFPGKHGEPgirgppgppgtpgslfGLKGQEGTPGRPGVQGFPGPR 471
Cdd:NF038329   262 RGDRGEAGPDGPDGKDGERGPVGPAGKdgQNGKDGLPGKDGKD----------------GQNGKDGLPGKDGKDGQPGKD 325

                          250
                   ....*....|
gi 2158835932  472 GQRGPKGEEG 481
Cdd:NF038329   326 GLPGKDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 494-777 2.90e-15

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 80.33  E-value: 2.90e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  494 RGSTGPRGPPGFPGTPGQPGRKGEPGDQGPHGIPGYAGAKGQSGQEGLPGPKGEKGDsiyittKGTKGIRGDPGLPGIRG 573
Cdd:NF038329   122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK------DGEAGAKGPAGEKGPQG 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  574 EDGFPGRdgldglpglpglpgdgiRGLPGDPGYPGELGPKGFPGEIGLPGEGYPGPKGYRGLPGDRGtdghpgppglpgp 653
Cdd:NF038329   196 PRGETGP-----------------AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTG------------- 245

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  654 pgepgqldcgqviedfsrgeatdpvwsgggcvrpPKGSQGNPGLPGATGTKGARGFPGDPGPVGFPGLNGTRGDPGREGY 733
Cdd:NF038329   246 ----------------------------------EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2158835932  734 PGP---PGFIGPRGDRGPNGLPGLQGHPGLMGKSGAPGLAGQKGAPG 777
Cdd:NF038329   292 NGKdglPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 35-208 3.10e-13

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: 74.17  E-value: 3.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932   35 AGGKSYTGPCGGRDCSGGCQCFPEKGARGQPGILGSQGFPGPPGLMGIPGLQGPKGHKGERGHPGISGPKGETGQRGVtg 114
Cdd:NF038329   134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP-- 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  115 fPGADGVPGHPGQPGSRGKPGhDGCNGTVGDPGDPGTPGHSGFPGTIGVQGPKGQKGEPYVLPPDIASRHRGDPGDPGFT 194
Cdd:NF038329   212 -AGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKD 289

                          170
                   ....*....|....
gi 2158835932  195 GFPGAPGTLGIQGP 208
Cdd:NF038329   290 GQNGKDGLPGKDGK 303
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 196-430 4.41e-13

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: 73.40  E-value: 4.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  196 FPGAPGTLGIQGPIGPRGVPGRPGPPGSPGPQGPQGNRG-LGFYGEKGEQGSPGPPGPpglptreligvptdkhKGERGE 274
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGpQGERGEKGPAGPQGEAGP----------------QGPAGK 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  275 PGQKGEAGFPGVLLFAPEKGEEGVMGFPGQRGLPGNDGFPGLSGERGFPGFDGQpGQYGPRGGKGEQGEMGPPGPPAyvp 354
Cdd:NF038329   179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDG--- 254

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2158835932  355 yRIPRKGVRGDPGSPGASGLRGEQGEQGDRGLPGipgfSDGDADKPGLPGEIGPKGEKGEEGSPAyQAGPPGFPGK 430
Cdd:NF038329   255 -PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG----KDGQNGKDGLPGKDGKDGQNGKDGLPG-KDGKDGQPGK 324
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 58-153 1.39e-08

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 59.15  E-value: 1.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932   58 EKGARGQPGILGSQGFPGPPGLMGIPGLQGPKGHKGERGHPGISGPKGETGQRGVTGFPGADGVPGHPGQPGSRGKPGHD 137
Cdd:NF038329   243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                           90
                   ....*....|....*.
gi 2158835932  138 GCNGTVGDPGDPGTPG 153
Cdd:NF038329   323 GKDGLPGKDGKDGQPG 338
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
762-1010 2.97e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 51.95  E-value: 2.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  762 GKSGAPGLAGQKGAPGDvlGAAAGPRGDDGLPGFPGLKGAPGDQGIPGIRGADGNPGLPGPKGDPGLQGLPGLMGLPGTP 841
Cdd:COG5164      7 GKTGPSDPGGVTTPAGS--QGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPA 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  842 GTHGFPGPPGNRGPDGGPGSQGPLGPPGARGEDGEQGFPGPV-----GMKGLSGDKGET-GFPGLQGIPGVTGPPGISGM 915
Cdd:COG5164     85 QNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTtppsgGSTTPPGDGGSTpPGPGSTGPGGSTTPPGDGGS 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  916 DGFPGDKGSRGSPGIDGFKGMP--GLKGRPGIKGIKGEFGLLGTRGDKGAQGARGFKGDRGEQGPPGEP-PKLKPSMMME 992
Cdd:COG5164    165 TTPPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQrPKTNPIERRG 244

                          250
                   ....*....|....*...
gi 2158835932  993 VKGEKGDAGETGTKGFFG 1010
Cdd:COG5164    245 PERPEAAALPAELTALEA 262
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
817-1059 7.18e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 50.80  E-value: 7.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  817 PGLPGPKGDPGLQGLPGLMGLPGTPGTHGFPGPPGNRGPDGGPGSQGPLGPPGARGEDGEQGFPGPVGMKGLSGDKGETG 896
Cdd:COG5164      6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  897 FPGLQGIPGVTG---PPGISGMDGFPGDKGSRGSPGIDGFKGMPGLKGRPGIKGIKGEFGLLGTRGDKGAQGARGFKGDR 973
Cdd:COG5164     86 NQGGTRPAGNTGgttPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGST 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  974 GEQGPPGE--PPKLKPSMMMEVKGEKGDAGETGTKGFFGIKGSKGMPGLPGKTGIPGSPGHPSYVPGVKGDIGAKGLTGL 1051
Cdd:COG5164    166 TPPGPGGSttPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERRGP 245


                   ....*...
gi 2158835932 1052 KGYPGPTG 1059
Cdd:COG5164    246 ERPEAAAL 253
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
800-1055 8.82e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 50.41  E-value: 8.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  800 GAPGDQGIPGIRGADGNPGLPGPKGDPGLQGLPGLMGLPGTPGTHGFPGPPGNRGPDGGPGSQGPLGPP---GARGEDGE 876
Cdd:COG5164      7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAqnqGGTTPAQN 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  877 QGFPGPVGMKGLSGDKGETGFPGLQGIPGVTGPPGISGMDGfPGDKGSRGSPGIDGfkGMPGLKGRPGIKGIKGEFGLLG 956
Cdd:COG5164     87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-PPSGGSTTPPGDGG--STPPGPGSTGPGGSTTPPGDGG 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  957 TRGDKGAQGARGFKGDRGEQGPP--GEPPKLKPSMMMEVKGEKGDAGETGTKGFFGIKGSKGMPGLPGKTGIPGSPGHPS 1034
Cdd:COG5164    164 STTPPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERR 243

                          250       260
                   ....*....|....*....|.
gi 2158835932 1035 YVPGVKGDIGAKGLTGLKGYP 1055
Cdd:COG5164    244 GPERPEAAALPAELTALEAEN 264
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1405-1511 9.05e-06

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 50.29  E-value: 9.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1405 QGSPGPRGNAGPRGSPGDAGPQGPPGEPGLRGLPGEPGLQGRGGIPAPPGSRGEQGAMGFQGPVGFEGQPGRPGSPGLPG 1484
Cdd:NF038329   125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204

                           90       100
                   ....*....|....*....|....*..
gi 2158835932 1485 MPGRSVSIGYLLVKHSQSDQEPMCPIG 1511
Cdd:NF038329   205 EQGPAGPAGPDGEAGPAGEDGPAGPAG 231
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 797-853 1.15e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.41  E-value: 1.15e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2158835932  797 GLKGAPGDQGIPGIRGADGNPGLPGPKGDPGLQGLPGLMGLPGTPGTHGFPGPPGNR 853
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1137-1342 2.29e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 48.87  E-value: 2.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1137 PGIEGLKGIQGVPGSLGQKGLPGLVGPPGQQGSPGTPGFQGEKGAPGWPGLPGQAGLPGLRGISGLHGLPGTKGLPGSPG 1216
Cdd:COG5164     48 AQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1217 PDGYGSAGFPGPVGDKGEAGEPSRVEGSQGPPGQKGDRGVPGVQGPFGIPGQDGLPGPPGISNISGYPGDTGSPGLDGVP 1296
Cdd:COG5164    128 PPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDG 207

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2158835932 1297 GYPGLHGQPGIPAPPGSKGESGRAGVSGQAGPKGTRGDPGLPGRPG 1342
Cdd:COG5164    208 PVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAAL 253
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1213-1486 4.62e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 48.10  E-value: 4.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1213 GSPGPDGYGSAGFPGPVGDKGEAGE--PSRVEGSQGPPGQKGDRGVPGVQGPFGIPGQDGLPGPPGISNISGYPGDTGSP 1290
Cdd:COG5164      2 GLYGPGKTGPSDPGGVTTPAGSQGStkPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1291 GLDGVPGYPGLHGQPGIPAPPGSKGESGRAGVSGQAGPKGTRGDPGLPGRPGIPGYPGPKGRKGEQGVIGFIGTIGFPGD 1370
Cdd:COG5164     82 TPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGD 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1371 LGPIGPKGDRGLTGFQGPPGSPGLPPIpprlvAEQGSPGPRGNAGPRGSPGDAGPQGppgepglrGLPGEPGLQGRGGIP 1450
Cdd:COG5164    162 GGSTTPPGPGGSTTPPDDGGSTTPPNK-----GETGTDIPTGGTPRQGPDGPVKKDD--------KNGKGNPPDDRGGKT 228

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2158835932 1451 APPGSRGEQGAMGFQGPVGFEGQPGRPGSPGLPGMP 1486
Cdd:COG5164    229 GPKDQRPKTNPIERRGPERPEAAALPAELTALEAEN 264
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 827-883 4.84e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 4.84e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2158835932  827 GLQGLPGLMGLPGTPGTHGFPGPPGNRGPDGGPGSQGPLGPPGARGEDGEQGFPGPV 883
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 785-841 7.68e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 7.68e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2158835932  785 GPRGDDGLPGFPGLKGAPGDQGIPGIRGADGNPGLPGPKGDPGLQGLPGLMGLPGTP 841
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1159-1215 1.14e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 1.14e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2158835932 1159 GLVGPPGQQGSPGTPGFQGEKGAPGWPGLPGQAGLPGLRGISGLHGLPGTKGLPGSP 1215
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 72-128 1.21e-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: 41.33  E-value: 1.21e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2158835932   72 GFPGPPGLMGIPGLQGPKGHKGERGHPGISGPKGETGQRGVTGFPGADGVPGHPGQP 128
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 848-902 1.22e-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: 41.33  E-value: 1.22e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932  848 GPPGNRGPDGGPGSQGPLGPPGARGEDGEQGFPGPVGMKGLSGDKGETGFPGLQG 902
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1303-1357 1.50e-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: 1.50e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932 1303 GQPGIPAPPGSKGESGRAGVSGQAGPKGTRGDPGLPGRPGIPGYPGPKGRKGEQG 1357
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 833-887 1.64e-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: 1.64e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932  833 GLMGLPGTPGTHGFPGPPGNRGPDGGPGSQGPLGPPGARGEDGEQGFPGPVGMKG 887
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1153-1207 1.79e-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: 1.79e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932 1153 GQKGLPGLVGPPGQQGSPGTPGFQGEKGAPGWPGLPGQAGLPGLRGISGLHGLPG 1207
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 791-845 1.88e-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: 1.88e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932  791 GLPGFPGLKGAPGDQGIPGIRGADGNPGLPGPKGDPGLQGLPGLMGLPGTPGTHG 845
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 836-890 2.24e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 2.24e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932  836 GLPGTPGTHGFPGPPGNRGPDGGPGSQGPLGPPGARGEDGEQGFPGPVGMKGLSG 890
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 696-752 2.31e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 2.31e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2158835932  696 GLPGATGTKGARGFPGDPGPVGFPGLNGTRGDPGREGYPGPPGFIGPRGDRGPNGLP 752
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 1222-1357 2.74e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 45.83  E-value: 2.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1222 SAGFPGPVGDKGEAGEPSRVEGSQGPPGQKGDRGVPGVQgpfGIPGQDGLPGPPGisnisgyPGDTGSPGL--DGVPGYP 1299
Cdd:PRK14959   374 SGGGASAPSGSAAEGPASGGAATIPTPGTQGPQGTAPAA---GMTPSSAAPATPA-------PSAAPSPRVpwDDAPPAP 443

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2158835932 1300 GLHGQPGIPAP--PGSKGESGR-AGVSGQAGPKGTRGDPGLPGrPGIPGYPGP--------KGRKGEQG 1357
Cdd:PRK14959   444 PRSGIPPRPAPrmPEASPVPGApDSVASASDAPPTLGDPSDTA-EHTPSGPRTwdgflefcQGRNGQGG 511
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1294-1349 2.84e-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: 2.84e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2158835932 1294 GVPGYPGLHGQPGIPAPPGSKGESGRAGVSGQAGPKGTRGDPGLPGRPGIPGYPGP 1349
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 81-135 3.23e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 3.23e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932   81 GIPGLQGPKGHKGERGHPGISGPKGETGQRGVTGFPGADGVPGHPGQPGSRGKPG 135
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1147-1201 3.67e-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: 3.67e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932 1147 GVPGSLGQKGLPGLVGPPGQQGSPGTPGFQGEKGAPGWPGLPGQAGLPGLRGISG 1201
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 292-347 3.85e-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: 3.85e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2158835932  292 EKGEEGVMGFPGQRGLPGNDGFPGLSGERGFPGFDGQPGQYGPRGGKGEQGEMGPP 347
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 708-763 5.07e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 5.07e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2158835932  708 GFPGDPGPVGFPGLNGTRGDPGREGYPGPPGFIGPRGDRGPNGLPGLQGHPGLMGK 763
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1300-1355 6.24e-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: 6.24e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2158835932 1300 GLHGQPGIPAPPGSKGESGRAGVSGQAGPKGTRGDPGLPGRPGIPGYPGPKGRKGE 1355
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 705-759 8.14e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 8.14e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932  705 GARGFPGDPGPVGFPGLNGTRGDPGREGYPGPPGFIGPRGDRGPNGLPGLQGHPG 759
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 857-911 8.22e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 8.22e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932  857 GGPGSQGPLGPPGARGEDGEQGFPGPVGMKGLSGDKGETGFPGLQGIPGVTGPPG 911
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 784-838 8.98e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 8.98e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932  784 AGPRGDDGLPGFPGLKGAPGDQGIPGIRGADGNPGLPGPKGDPGLQGLPGLMGLP 838
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 723-777 1.01e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 1.01e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932  723 GTRGDPGREGYPGPPGFIGPRGDRGPNGLPGLQGHPGLMGKSGAPGLAGQKGAPG 777
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 99-153 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 2158835932   99 GISGPKGETGQRGVTGFPGADGVPGHPGQPGSRGKPGHDGCNGTVGDPGDPGTPG 153
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 783-833 1.25e-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: 1.25e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2158835932  783 AAGPRGDDGLPGFPGLKGAPGDQGIPGIRGADGNPGLPGPKGDPGLQGLPG 833
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1415-1511 1.26e-03

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: 43.36  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1415 GPRGSPGDAGPQGPPGEPGLRGLPGEPGLQGRGGIPAPPGSRGEQGAMGFQGPVGFEGQPGRPGSPGLPGMPGRSVSIGY 1494
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90
                   ....*....|....*..
gi 2158835932 1495 LLVKHSQSDQEPMCPIG 1511
Cdd:NF038329   197 RGETGPAGEQGPAGPAG 213
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 688-738 1.54e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 1.54e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2158835932  688 PKGSQGNPGLPGATGTKGARGFPGDPGPVGFPGLNGTRGDPGREGYPGPPG 738
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1255-1311 1.74e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 1.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2158835932 1255 GVPGVQGPFGIPGQDGLPGPPGISNISGYPGDTGSPGLDGVPGYPGLHGQPGIPAPP 1311
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 688-743 2.16e-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: 2.16e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2158835932  688 PKGSQGNPGLPGATGTKGARGFPGDPGPVGFPGLNGTRGDPGREGYPGPPGFIGPR 743
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 714-768 2.24e-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: 2.24e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932  714 GPVGFPGLNGTRGDPGREGYPGPPGFIGPRGDRGPNGLPGLQGHPGLMGKSGAPG 768
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1134-1183 2.76e-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: 2.76e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1134 PGLPGIEGLKGIQGVPGSLGQKGLPGLVGPPGQQGSPGTPGFQGEKGAPG 1183
Cdd:pfam01391    6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 93-149 2.79e-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: 2.79e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2158835932   93 GERGHPGISGPKGETGQRGVTGFPGADGVPGHPGQPGSRGKPGHDGCNGTVGDPGDP 149
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PPE COG5651
PPE-repeat protein [Function unknown];
708-884 2.92e-03

PPE-repeat protein [Function unknown];


Pssm-ID: 444372 [Multi-domain]  Cd Length: 385  Bit Score: 42.19  E-value: 2.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  708 GFPGDpGPVGFPGLNGTRGDPGREGYPGPPGFIGPRGDRGPNGLPGLQGHPG--LMGKSGAPGLAGQKGAPGDVLGAAAG 785
Cdd:COG5651    201 GLTGL-NQVGIGGLNSGSGPIGLNSGPGNTGFAGTGAAAGAAAAAAAAAAAAgaGASAALASLAATLLNASSLGLAATAA 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932  786 PRGDDGLPG-FPGLKGAPGDQGIPGIRGADGNPGLP-GPKGDPGLQGLPGLMGLPGTPGthGFPGPPGNRGPDGGPGSQG 863
Cdd:COG5651    280 SSAATNLGLaGSPLGLAGGGAGAAAATGLGLGAGGAaGAAGATGAGAALGAGAAAAAAG--AAAGAGAAAAAAAGGAGGG 357

                          170       180
                   ....*....|....*....|.
gi 2158835932  864 PLGPPGARGEDGEQGFPGPVG 884
Cdd:COG5651    358 GGGALGAGGGGGSAGAAAGAA 378
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 96-152 3.17e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.47  E-value: 3.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2158835932   96 GHPGISGPKGETGQRGVTGFPGADGVPGHPGQPGSRGKPGHDGCNGTVGDPGDPGTP 152
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1144-1198 3.29e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.47  E-value: 3.29e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932 1144 GIQGVPGSLGQKGLPGLVGPPGQQGSPGTPGFQGEKGAPGWPGLPGQAGLPGLRG 1198
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1141-1195 3.60e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 3.60e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932 1141 GLKGIQGVPGSLGQKGLPGLVGPPGQQGSPGTPGFQGEKGAPGWPGLPGQAGLPG 1195
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1282-1338 4.38e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 4.38e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2158835932 1282 GYPGDTGSPGLDGVPGYPGLHGQPGIPAPPGSKGESGRAGVSGQAGPKGTRGDPGLP 1338
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 105-159 4.47e-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: 37.09  E-value: 4.47e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932  105 GETGQRGVTGFPGADGVPGHPGQPGSRGKPGHDGCNGTVGDPGDPGTPGHSGFPG 159
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1285-1341 4.51e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 4.51e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2158835932 1285 GDTGSPGLDGVPGYPGLHGQPGIPAPPGSKGESGRAGVSGQAGPKGTRGDPGLPGRP 1341
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 875-929 4.74e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 4.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932  875 GEQGFPGPVGMKGLSGDKGETGFPGLQGIPGVTGPPGISGMDGFPGDKGSRGSPG 929
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1267-1321 7.24e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 7.24e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932 1267 GQDGLPGPPGISNISGYPGDTGSPGLDGVPGYPGLHGQPGIPAPPGSKGESGRAG 1321
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1044-1098 7.46e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 7.46e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932 1044 GAKGLTGLKGYPGPTGSPGIRGFPGSTGGRGDKGAPGISGHFGTPGSHGEIGEPG 1098
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 893-947 7.68e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 7.68e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932  893 GETGFPGLQGIPGVTGPPGISGMDGFPGDKGSRGSPGIDGFKGMPGLKGRPGIKG 947
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 1231-1381 8.21e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.72  E-value: 8.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158835932 1231 DKGEAGEPSRVEGSQGPPGQKGDRGVPGVQGPFGIPGQDGLPGPPGISNISGYPGDTGSPGLDGVPGYPGLHGQPGIPAP 1310
Cdd:PHA03169    72 DTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAP 151

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2158835932 1311 PGSKGESGRAGVSGQAGPKGTRGDPGLPGRPGIPGYPGPKGRKGEQGVIGFIGTIGFPGDLGPIGPKGDRG 1381
Cdd:PHA03169   152 PESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQA 222
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1258-1312 8.40e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 8.40e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2158835932 1258 GVQGPFGIPGQDGLPGPPGISNISGYPGDTGSPGLDGVPGYPGLHGQPGIPAPPG 1312
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1180-1238 8.48e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 8.48e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2158835932 1180 GAPGWPGLPGQAGLPGLRGISGLHGLPGTKGLPGSPGPDgyGSAGFPGPVGDKGEAGEP 1238
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPP--GPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 117-173 8.73e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 8.73e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2158835932  117 GADGVPGHPGQPGSRGKPGHDGCNGTVGDPGDPGTPGHSGFPGTIGVQGPKGQKGEP 173
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 783-832 9.73e-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: 35.93  E-value: 9.73e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2158835932  783 AAGPRGDDGLPGFPGLKGAPGDQGIPGIRGADGNPGLPGPKGDPGLQGLP 832
Cdd:pfam01391    8 PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
 
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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