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Conserved domains on  [gi|2327921558|ref|NP_001400917|]
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collagen alpha-3(IV) chain precursor [Rattus norvegicus]

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 ...
1557-1668 1.89e-61

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: 205.14  E-value: 1.89e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1557 MAIAVHSQTTAIPPCPQGWVSLWKGFSFVMFTSAGsEGAGQALASPGSCLEEFRASPFIECHGRGTCNYYSNSYSFWLAS 1636
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYASNDYSYWLST 79
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2327921558 1637 lnPERMFRKPIPSTVKAGD-LEKIISRCQVCMK 1668
Cdd:pfam01413   80 --VEEQFRKPMSQTPKAGNeLRSYISRCVVCEA 110
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
1447-1553 1.20e-58

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: 197.05  E-value: 1.20e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1447 FIFTRHSQTTANPSCPEGTQPLYSGFSLLFVQGNEHAHGQDLGTLGSCLQRFTTMPFLFCNVDNVCNFASrNDYSYWLST 1526
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 2327921558 1527 PA---PMPMDMAPITGRALEPYVSRCTVCE 1553
Cdd:pfam01413   80 VEeqfRKPMSQTPKAGNELRSYISRCVVCE 109
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
950-1205 2.15e-25

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 111.54  E-value: 2.15e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  950 LKGDKGEPGLKGFVGNPGEKGNRGNPGLPGPKGLEGVpglPGSPGPRGDTGSSGDPGRPGPQGLPGSMGNMGVPGPKGRK 1029
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGP---PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1030 GTSGFPGVAGRPGLPGIPGPQGDKGEPGysegaspgpPGPKGDPGLPGDKGKKGERGLPGPPGHSGPAGPDGAPGSPGSP 1109
Cdd:NF038329   192 GPQGPRGETGPAGEQGPAGPAGPDGEAG---------PAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1110 GHPGRPGPDGDSGLKGQKGFPGPPGSTgppgppglpglpgpmgmrGDQGQDGIPGPPGEKGETGLLGAhPGQKGSPGVPG 1189
Cdd:NF038329   263 GDRGEAGPDGPDGKDGERGPVGPAGKD------------------GQNGKDGLPGKDGKDGQNGKDGL-PGKDGKDGQPG 323
                          250
                   ....*....|....*.
gi 2327921558 1190 VKGDRGVPGLSGLPGR 1205
Cdd:NF038329   324 KDGLPGKDGKDGQPGK 339
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
750-1030 4.67e-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: 92.28  E-value: 4.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  750 GEPGKPGFPGERGNSGENGDIGLPGLPGPPGTPGKDGFDGPPGDPGQsgppgakgppgrciPGPRGTQGLPGLNGLKGQP 829
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGP--------------AGPQGEAGPQGPAGKDGEA 182
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  830 GRRGDTGPKGDPGipgmdrsgvpgergppgtpglpgemgppgqkgypgppgfpglpgEKGEVGIMGYPGTTGLPGLPGKP 909
Cdd:NF038329   183 GAKGPAGEKGPQG--------------------------------------------PRGETGPAGEQGPAGPAGPDGEA 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  910 GSQGQRGNLGIPGvKGERGRPGVKGERGEKGKPGPPHAPHLKGDKGEPGLKGFVGNPGEKGNRGNPGLPGPKGLEGVPGL 989
Cdd:NF038329   219 GPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2327921558  990 PGSPGPRGDTGSSGDPGRPGPQGLPGSMGNMGVPGPKGRKG 1030
Cdd:NF038329   298 PGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
495-755 2.56e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 86.88  E-value: 2.56e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  495 LDGVKGIPGGRGAPGVKGNPGSPGNAGLPGFAGFPGDQGHPGLKGDKGDTplpwgqvGDPGDPGHRGLPGRKGFDGSPGG 574
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA-------GPQGEAGPQGPAGKDGEAGAKGP 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  575 PGAKGPRGPRGEPALSGRKGDQGPPGAPGSPGPPGPAGPAGPPGYGPQGEPGPKGAQGVPGALGPPGEAGLKGESsasip 654
Cdd:NF038329   188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR----- 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  655 vlgppgppgppgqagprGLPGLPGPvgtcdPGHPGPDGEPGipEVGFPGARGPKGDQGFPGTIGLPGYPGETGRPGYPGE 734
Cdd:NF038329   263 -----------------GDRGEAGP-----DGPDGKDGERG--PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGK 318
                          250       260
                   ....*....|....*....|..
gi 2327921558  735 MGVPGAKGEPSV-GRPGEPGKP 755
Cdd:NF038329   319 DGQPGKDGLPGKdGKDGQPGKP 340
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
390-594 3.01e-14

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 77.25  E-value: 3.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  390 GLRGPVGWPGLKGSKGERGPPGidTVGPPGSLGCPGSPGPPGPPGPPGRPGDTVFQpGPPGDHGAPGDIGPPGVPGVDGP 469
Cdd:NF038329   120 GEPGPAGPAGPAGEQGPRGDRG--ETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ-GPAGKDGEAGAKGPAGEKGPQGP 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  470 KGEPGQPCTECHCIPGPPGVPGVPGLDGVKGIPGGRGAPGVKGNPGSPGNAGLPGFAGFPGDQGHPGLKGDKGdtplPWG 549
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG----PDG 272
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2327921558  550 QVGDPGDPGHRGLPGRKGFDGSPGGPGAKGPRGPRGEPALSGRKG 594
Cdd:NF038329   273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1080-1336 2.12e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 74.56  E-value: 2.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1080 GKKGERGLPGPPGHSGPAGPDGAPGSPGSPGHPGRPGPDGDSGLKGQKgfpgppgstgppgppglpglpgpmgmrGDQGQ 1159
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA---------------------------GPQGE 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1160 DGIPGPPGEKGETGLLGAhPGQKGSPGVPGVKGDRGVPGLSGLPGRKGTMGDVGPQGPPGTTGLPGPPGLPGTIVPGPKG 1239
Cdd:NF038329   170 AGPQGPAGKDGEAGAKGP-AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDG 248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1240 NRGLPGLRGNPGEPGPPGPPGPVGEgiKGDKGFMGLPGSRGLPGMVGDTGAPGQPGAPGIPGLPGVRGDPGFPGFPGVKG 1319
Cdd:NF038329   249 PQGPDGPAGKDGPRGDRGEAGPDGP--DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326
                          250
                   ....*....|....*..
gi 2327921558 1320 EKGNPGFLGSIGHPGPV 1336
Cdd:NF038329   327 LPGKDGKDGQPGKPAPK 343
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
62-342 1.28e-11

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: 68.78  E-value: 1.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558   62 QKGFPGPEGLPGPQGPKGSPGLPgltGPKGIRGITGLPGFAGPPGLPGIPGYPGPPGLAGLPGCNGSKGEQGFPGIPGTP 141
Cdd:NF038329   112 QLKGDGEKGEPGPAGPAGPAGEQ---GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA 188
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  142 GYAGLPGPDGLKGQKGKpaQGEDGEfngkgdpgppgapgfqglpgppgfpgpagppgppgfFGFPGAMGPRGPKGRMGDS 221
Cdd:NF038329   189 GEKGPQGPRGETGPAGE--QGPAGP------------------------------------AGPDGEAGPAGEDGPAGPA 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  222 TIGQEGEKGVKGLTGPPGLPGPViftlrhpyRKSDFQGQKGDegergepgPPGPSGPPGDSYGSEKGAPGEPGPRGKPGK 301
Cdd:NF038329   231 GDGQQGPDGDPGPTGEDGPQGPD--------GPAGKDGPRGD--------RGEAGPDGPDGKDGERGPVGPAGKDGQNGK 294
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2327921558  302 DGAPGFPGTEGAKGTRGFPGLRGEAGIKGWKGDIGPPGFPG 342
Cdd:NF038329   295 DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
 
Name Accession Description Interval E-value
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
1557-1668 1.89e-61

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: 205.14  E-value: 1.89e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1557 MAIAVHSQTTAIPPCPQGWVSLWKGFSFVMFTSAGsEGAGQALASPGSCLEEFRASPFIECHGRGTCNYYSNSYSFWLAS 1636
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYASNDYSYWLST 79
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2327921558 1637 lnPERMFRKPIPSTVKAGD-LEKIISRCQVCMK 1668
Cdd:pfam01413   80 --VEEQFRKPMSQTPKAGNeLRSYISRCVVCEA 110
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
1447-1553 1.20e-58

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: 197.05  E-value: 1.20e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1447 FIFTRHSQTTANPSCPEGTQPLYSGFSLLFVQGNEHAHGQDLGTLGSCLQRFTTMPFLFCNVDNVCNFASrNDYSYWLST 1526
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 2327921558 1527 PA---PMPMDMAPITGRALEPYVSRCTVCE 1553
Cdd:pfam01413   80 VEeqfRKPMSQTPKAGNELRSYISRCVVCE 109
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
1556-1668 4.90e-57

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 128421  Cd Length: 114  Bit Score: 192.60  E-value: 4.90e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  1556 AMAIAVHSQTTAIPPCPQGWVSLWKGFSFVMFTsAGSEGAGQALASPGSCLEEFRASPFIECHGRGTCNYYS-NSYSFWL 1634
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASrNDYSFWL 79
                            90       100       110
                    ....*....|....*....|....*....|....
gi 2327921558  1635 ASLNPERMFRKPIPSTVKAGDLEKIISRCQVCMK 1668
Cdd:smart00111   80 STIEPSDQFTAPRPMTPKAGDLRPYISRCQVCEK 113
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
1446-1555 8.63e-56

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: 189.14  E-value: 8.63e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  1446 GFIFTRHSQTTANPSCPEGTQPLYSGFSLLFVQGNEHAHGQDLGTLGSCLQRFTTMPFLFCNVDNVCNFASRNDYSYWLS 1525
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 2327921558  1526 TPAP-----MPMDMAPITGrALEPYVSRCTVCEGP 1555
Cdd:smart00111   81 TIEPsdqftAPRPMTPKAG-DLRPYISRCQVCEKP 114
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
950-1205 2.15e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 111.54  E-value: 2.15e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  950 LKGDKGEPGLKGFVGNPGEKGNRGNPGLPGPKGLEGVpglPGSPGPRGDTGSSGDPGRPGPQGLPGSMGNMGVPGPKGRK 1029
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGP---PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1030 GTSGFPGVAGRPGLPGIPGPQGDKGEPGysegaspgpPGPKGDPGLPGDKGKKGERGLPGPPGHSGPAGPDGAPGSPGSP 1109
Cdd:NF038329   192 GPQGPRGETGPAGEQGPAGPAGPDGEAG---------PAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1110 GHPGRPGPDGDSGLKGQKGFPGPPGSTgppgppglpglpgpmgmrGDQGQDGIPGPPGEKGETGLLGAhPGQKGSPGVPG 1189
Cdd:NF038329   263 GDRGEAGPDGPDGKDGERGPVGPAGKD------------------GQNGKDGLPGKDGKDGQNGKDGL-PGKDGKDGQPG 323
                          250
                   ....*....|....*.
gi 2327921558 1190 VKGDRGVPGLSGLPGR 1205
Cdd:NF038329   324 KDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
934-1197 4.99e-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: 4.99e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  934 GERGEKGKPGPPHAPHLKGDKGEPGLKGFVGNPGEKGNRGNPGLPGPKGLEGVPGLPGSPGPRGDTGSSGDPGRPGPQGL 1013
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1014 PGSMGNMGVPGPKGRKGTSGFPGVAGRPGLPGIPG--PQGDKGEPGysegaspgppgPKGDPGLPGDKGKKGERGLPGPP 1091
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPG-----------PTGEDGPQGPDGPAGKDGPRGDR 265
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1092 GHSGPAGPDGAPGSPGSPGHPGRPGPDGDSGLKGQKgfpgppgstgppgppglpglpgpmgmrGDQGQDGIPGPPGEKGE 1171
Cdd:NF038329   266 GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD---------------------------GKDGQNGKDGLPGKDGK 318
                          250       260
                   ....*....|....*....|....*.
gi 2327921558 1172 TGLlgahPGQKGSPGVPGVKGDRGVP 1197
Cdd:NF038329   319 DGQ----PGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
750-1030 4.67e-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: 4.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  750 GEPGKPGFPGERGNSGENGDIGLPGLPGPPGTPGKDGFDGPPGDPGQsgppgakgppgrciPGPRGTQGLPGLNGLKGQP 829
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGP--------------AGPQGEAGPQGPAGKDGEA 182
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  830 GRRGDTGPKGDPGipgmdrsgvpgergppgtpglpgemgppgqkgypgppgfpglpgEKGEVGIMGYPGTTGLPGLPGKP 909
Cdd:NF038329   183 GAKGPAGEKGPQG--------------------------------------------PRGETGPAGEQGPAGPAGPDGEA 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  910 GSQGQRGNLGIPGvKGERGRPGVKGERGEKGKPGPPHAPHLKGDKGEPGLKGFVGNPGEKGNRGNPGLPGPKGLEGVPGL 989
Cdd:NF038329   219 GPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2327921558  990 PGSPGPRGDTGSSGDPGRPGPQGLPGSMGNMGVPGPKGRKG 1030
Cdd:NF038329   298 PGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
495-755 2.56e-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: 86.88  E-value: 2.56e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  495 LDGVKGIPGGRGAPGVKGNPGSPGNAGLPGFAGFPGDQGHPGLKGDKGDTplpwgqvGDPGDPGHRGLPGRKGFDGSPGG 574
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA-------GPQGEAGPQGPAGKDGEAGAKGP 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  575 PGAKGPRGPRGEPALSGRKGDQGPPGAPGSPGPPGPAGPAGPPGYGPQGEPGPKGAQGVPGALGPPGEAGLKGESsasip 654
Cdd:NF038329   188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR----- 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  655 vlgppgppgppgqagprGLPGLPGPvgtcdPGHPGPDGEPGipEVGFPGARGPKGDQGFPGTIGLPGYPGETGRPGYPGE 734
Cdd:NF038329   263 -----------------GDRGEAGP-----DGPDGKDGERG--PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGK 318
                          250       260
                   ....*....|....*....|..
gi 2327921558  735 MGVPGAKGEPSV-GRPGEPGKP 755
Cdd:NF038329   319 DGQPGKDGLPGKdGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
629-845 8.79e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 81.88  E-value: 8.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  629 GAQGVPGALGPPGEAGLKGESSASiPVLGPPGPPGPPGQAGPRGLPGLPGPVGTCDP-GHPGPDGEPGIP----EVGFPG 703
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDR-GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPqGPAGKDGEAGAKgpagEKGPQG 195
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  704 ARGPKGDQGFPGTIGLPGYPGETGRPGYPGEMGVPGAKGEPSVGRPGEPGKPGFPGERGNSGENGDIGLPGLPGPPGTPG 783
Cdd:NF038329   196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2327921558  784 KDGFDGPPGDPGQSGPPGAKGPPGRCIP-GPRGTQGLPGLNGLKGQPGRRGDTGPKGDPGIPG 845
Cdd:NF038329   276 KDGERGPVGPAGKDGQNGKDGLPGKDGKdGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
390-594 3.01e-14

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 77.25  E-value: 3.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  390 GLRGPVGWPGLKGSKGERGPPGidTVGPPGSLGCPGSPGPPGPPGPPGRPGDTVFQpGPPGDHGAPGDIGPPGVPGVDGP 469
Cdd:NF038329   120 GEPGPAGPAGPAGEQGPRGDRG--ETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ-GPAGKDGEAGAKGPAGEKGPQGP 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  470 KGEPGQPCTECHCIPGPPGVPGVPGLDGVKGIPGGRGAPGVKGNPGSPGNAGLPGFAGFPGDQGHPGLKGDKGdtplPWG 549
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG----PDG 272
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2327921558  550 QVGDPGDPGHRGLPGRKGFDGSPGGPGAKGPRGPRGEPALSGRKG 594
Cdd:NF038329   273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1080-1336 2.12e-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: 74.56  E-value: 2.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1080 GKKGERGLPGPPGHSGPAGPDGAPGSPGSPGHPGRPGPDGDSGLKGQKgfpgppgstgppgppglpglpgpmgmrGDQGQ 1159
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA---------------------------GPQGE 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1160 DGIPGPPGEKGETGLLGAhPGQKGSPGVPGVKGDRGVPGLSGLPGRKGTMGDVGPQGPPGTTGLPGPPGLPGTIVPGPKG 1239
Cdd:NF038329   170 AGPQGPAGKDGEAGAKGP-AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDG 248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1240 NRGLPGLRGNPGEPGPPGPPGPVGEgiKGDKGFMGLPGSRGLPGMVGDTGAPGQPGAPGIPGLPGVRGDPGFPGFPGVKG 1319
Cdd:NF038329   249 PQGPDGPAGKDGPRGDRGEAGPDGP--DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326
                          250
                   ....*....|....*..
gi 2327921558 1320 EKGNPGFLGSIGHPGPV 1336
Cdd:NF038329   327 LPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
62-342 1.28e-11

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: 68.78  E-value: 1.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558   62 QKGFPGPEGLPGPQGPKGSPGLPgltGPKGIRGITGLPGFAGPPGLPGIPGYPGPPGLAGLPGCNGSKGEQGFPGIPGTP 141
Cdd:NF038329   112 QLKGDGEKGEPGPAGPAGPAGEQ---GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA 188
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  142 GYAGLPGPDGLKGQKGKpaQGEDGEfngkgdpgppgapgfqglpgppgfpgpagppgppgfFGFPGAMGPRGPKGRMGDS 221
Cdd:NF038329   189 GEKGPQGPRGETGPAGE--QGPAGP------------------------------------AGPDGEAGPAGEDGPAGPA 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  222 TIGQEGEKGVKGLTGPPGLPGPViftlrhpyRKSDFQGQKGDegergepgPPGPSGPPGDSYGSEKGAPGEPGPRGKPGK 301
Cdd:NF038329   231 GDGQQGPDGDPGPTGEDGPQGPD--------GPAGKDGPRGD--------RGEAGPDGPDGKDGERGPVGPAGKDGQNGK 294
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2327921558  302 DGAPGFPGTEGAKGTRGFPGLRGEAGIKGWKGDIGPPGFPG 342
Cdd:NF038329   295 DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1274-1328 1.37e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.02  E-value: 1.37e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2327921558 1274 GLPGSRGLPGMVGDTGAPGQPGAPGIPGLPGVRGDPGFPGFPGVKGEKGNPGFLG 1328
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
982-1036 2.64e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 2.64e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2327921558  982 GLEGVPGLPGSPGPRGDTGSSGDPGRPGPQGLPGSMGNMGVPGPKGRKGTSGFPG 1036
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
43-166 2.81e-05

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 48.75  E-value: 2.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558   43 GTKGEKGEIGFPGPPGFPGQKGFPGPEGLPGPQGPKGSPGLPGLTGPKGIRGITGLPGFAGPPGLPGIPGYpgppglagl 122
Cdd:NF038329   162 GPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD--------- 232
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2327921558  123 pGCNGSKGEQGFPGIPGTPGYAGLPGPDGLKGQKGKPA-QGEDGE 166
Cdd:NF038329   233 -GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGpDGPDGK 276
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1158-1442 1.02e-04

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: 46.82  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1158 GQDGIPGPPGEKGETGLLGAHpGQKGSPGVPGVKGDRGVPGLSGLPGRKGTMGDVGPQgppgttglpgppglpgtivpGP 1237
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPR-GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ--------------------GP 175
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1238 KGNRGLPGLrgnpgepgppgppgpvgegiKGDKGFMGLPGSRGLPGMVGDTGAPGQPGAPGIPGLPGVRGDPGFPGfPGV 1317
Cdd:NF038329   176 AGKDGEAGA--------------------KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQ 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1318 KGEKGNPgflgsighpgpvgpkgppGPQGKPGTLKVISLPGSPGPPGAPGQPGVKGDPGPLGPPGIPGPCGPRGQPGKDG 1397
Cdd:NF038329   235 QGPDGDP------------------GPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG 296
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2327921558 1398 KPGAPGP---PGVKGSKGSKGEQGPPGLDGLPGLKGKPGDRGTPANGT 1442
Cdd:NF038329   297 LPGKDGKdgqNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKT 344
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
629-755 1.60e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 46.60  E-value: 1.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  629 GAQGVPGALGPPGEAGLKGESSASipvlgppgppgppGQAGPRGLPGLPGPVGTCDPGHPGPDGEPGIPEVGFPgargPK 708
Cdd:PRK14959   389 PASGGAATIPTPGTQGPQGTAPAA-------------GMTPSSAAPATPAPSAAPSPRVPWDDAPPAPPRSGIP----PR 451
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2327921558  709 GDQGFPGTIGLPGYPGETGRPGypgemGVPGAKGEPSVGRPGEPGKP 755
Cdd:PRK14959   452 PAPRMPEASPVPGAPDSVASAS-----DAPPTLGDPSDTAEHTPSGP 493
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
286-339 2.10e-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: 2.10e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2327921558  286 EKGAPGEPGPRGKPGKDGAPGFPGTEGAKGTRGFPGLRGEAGIKGWKGDIGPPG 339
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
904-958 1.34e-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: 1.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2327921558  904 GLPGKPGSQGQRGNLGIPGVKGERGRPGVKGERGEKGKPGPPHAPHLKGDKGEPG 958
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
700-755 1.64e-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: 1.64e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2327921558  700 GFPGARGPKGDQGFPGTIGLPGYPGETGRPGYPGEMGVPGAKGEPsvGRPGEPGKP 755
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP--GAPGAPGPP 57
 
Name Accession Description Interval E-value
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
1557-1668 1.89e-61

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: 205.14  E-value: 1.89e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1557 MAIAVHSQTTAIPPCPQGWVSLWKGFSFVMFTSAGsEGAGQALASPGSCLEEFRASPFIECHGRGTCNYYSNSYSFWLAS 1636
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYASNDYSYWLST 79
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2327921558 1637 lnPERMFRKPIPSTVKAGD-LEKIISRCQVCMK 1668
Cdd:pfam01413   80 --VEEQFRKPMSQTPKAGNeLRSYISRCVVCEA 110
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
1447-1553 1.20e-58

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: 197.05  E-value: 1.20e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1447 FIFTRHSQTTANPSCPEGTQPLYSGFSLLFVQGNEHAHGQDLGTLGSCLQRFTTMPFLFCNVDNVCNFASrNDYSYWLST 1526
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYAS-NDYSYWLST 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 2327921558 1527 PA---PMPMDMAPITGRALEPYVSRCTVCE 1553
Cdd:pfam01413   80 VEeqfRKPMSQTPKAGNELRSYISRCVVCE 109
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
1556-1668 4.90e-57

C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of type 4 collagens. Mutations in alpha-5 collagen IV are associated with X-linked Alport syndrome.


Pssm-ID: 128421  Cd Length: 114  Bit Score: 192.60  E-value: 4.90e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  1556 AMAIAVHSQTTAIPPCPQGWVSLWKGFSFVMFTsAGSEGAGQALASPGSCLEEFRASPFIECHGRGTCNYYS-NSYSFWL 1634
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASrNDYSFWL 79
                            90       100       110
                    ....*....|....*....|....*....|....
gi 2327921558  1635 ASLNPERMFRKPIPSTVKAGDLEKIISRCQVCMK 1668
Cdd:smart00111   80 STIEPSDQFTAPRPMTPKAGDLRPYISRCQVCEK 113
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
1446-1555 8.63e-56

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: 189.14  E-value: 8.63e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  1446 GFIFTRHSQTTANPSCPEGTQPLYSGFSLLFVQGNEHAHGQDLGTLGSCLQRFTTMPFLFCNVDNVCNFASRNDYSYWLS 1525
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 2327921558  1526 TPAP-----MPMDMAPITGrALEPYVSRCTVCEGP 1555
Cdd:smart00111   81 TIEPsdqftAPRPMTPKAG-DLRPYISRCQVCEKP 114
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
950-1205 2.15e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 111.54  E-value: 2.15e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  950 LKGDKGEPGLKGFVGNPGEKGNRGNPGLPGPKGLEGVpglPGSPGPRGDTGSSGDPGRPGPQGLPGSMGNMGVPGPKGRK 1029
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGP---PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1030 GTSGFPGVAGRPGLPGIPGPQGDKGEPGysegaspgpPGPKGDPGLPGDKGKKGERGLPGPPGHSGPAGPDGAPGSPGSP 1109
Cdd:NF038329   192 GPQGPRGETGPAGEQGPAGPAGPDGEAG---------PAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1110 GHPGRPGPDGDSGLKGQKGFPGPPGSTgppgppglpglpgpmgmrGDQGQDGIPGPPGEKGETGLLGAhPGQKGSPGVPG 1189
Cdd:NF038329   263 GDRGEAGPDGPDGKDGERGPVGPAGKD------------------GQNGKDGLPGKDGKDGQNGKDGL-PGKDGKDGQPG 323
                          250
                   ....*....|....*.
gi 2327921558 1190 VKGDRGVPGLSGLPGR 1205
Cdd:NF038329   324 KDGLPGKDGKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
934-1197 4.99e-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: 4.99e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  934 GERGEKGKPGPPHAPHLKGDKGEPGLKGFVGNPGEKGNRGNPGLPGPKGLEGVPGLPGSPGPRGDTGSSGDPGRPGPQGL 1013
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1014 PGSMGNMGVPGPKGRKGTSGFPGVAGRPGLPGIPG--PQGDKGEPGysegaspgppgPKGDPGLPGDKGKKGERGLPGPP 1091
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPG-----------PTGEDGPQGPDGPAGKDGPRGDR 265
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1092 GHSGPAGPDGAPGSPGSPGHPGRPGPDGDSGLKGQKgfpgppgstgppgppglpglpgpmgmrGDQGQDGIPGPPGEKGE 1171
Cdd:NF038329   266 GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD---------------------------GKDGQNGKDGLPGKDGK 318
                          250       260
                   ....*....|....*....|....*.
gi 2327921558 1172 TGLlgahPGQKGSPGVPGVKGDRGVP 1197
Cdd:NF038329   319 DGQ----PGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
750-1030 4.67e-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: 4.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  750 GEPGKPGFPGERGNSGENGDIGLPGLPGPPGTPGKDGFDGPPGDPGQsgppgakgppgrciPGPRGTQGLPGLNGLKGQP 829
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGP--------------AGPQGEAGPQGPAGKDGEA 182
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  830 GRRGDTGPKGDPGipgmdrsgvpgergppgtpglpgemgppgqkgypgppgfpglpgEKGEVGIMGYPGTTGLPGLPGKP 909
Cdd:NF038329   183 GAKGPAGEKGPQG--------------------------------------------PRGETGPAGEQGPAGPAGPDGEA 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  910 GSQGQRGNLGIPGvKGERGRPGVKGERGEKGKPGPPHAPHLKGDKGEPGLKGFVGNPGEKGNRGNPGLPGPKGLEGVPGL 989
Cdd:NF038329   219 GPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2327921558  990 PGSPGPRGDTGSSGDPGRPGPQGLPGSMGNMGVPGPKGRKG 1030
Cdd:NF038329   298 PGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
495-755 2.56e-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: 86.88  E-value: 2.56e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  495 LDGVKGIPGGRGAPGVKGNPGSPGNAGLPGFAGFPGDQGHPGLKGDKGDTplpwgqvGDPGDPGHRGLPGRKGFDGSPGG 574
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA-------GPQGEAGPQGPAGKDGEAGAKGP 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  575 PGAKGPRGPRGEPALSGRKGDQGPPGAPGSPGPPGPAGPAGPPGYGPQGEPGPKGAQGVPGALGPPGEAGLKGESsasip 654
Cdd:NF038329   188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR----- 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  655 vlgppgppgppgqagprGLPGLPGPvgtcdPGHPGPDGEPGipEVGFPGARGPKGDQGFPGTIGLPGYPGETGRPGYPGE 734
Cdd:NF038329   263 -----------------GDRGEAGP-----DGPDGKDGERG--PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGK 318
                          250       260
                   ....*....|....*....|..
gi 2327921558  735 MGVPGAKGEPSV-GRPGEPGKP 755
Cdd:NF038329   319 DGQPGKDGLPGKdGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
629-845 8.79e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 81.88  E-value: 8.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  629 GAQGVPGALGPPGEAGLKGESSASiPVLGPPGPPGPPGQAGPRGLPGLPGPVGTCDP-GHPGPDGEPGIP----EVGFPG 703
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDR-GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPqGPAGKDGEAGAKgpagEKGPQG 195
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  704 ARGPKGDQGFPGTIGLPGYPGETGRPGYPGEMGVPGAKGEPSVGRPGEPGKPGFPGERGNSGENGDIGLPGLPGPPGTPG 783
Cdd:NF038329   196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2327921558  784 KDGFDGPPGDPGQSGPPGAKGPPGRCIP-GPRGTQGLPGLNGLKGQPGRRGDTGPKGDPGIPG 845
Cdd:NF038329   276 KDGERGPVGPAGKDGQNGKDGLPGKDGKdGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
390-594 3.01e-14

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 77.25  E-value: 3.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  390 GLRGPVGWPGLKGSKGERGPPGidTVGPPGSLGCPGSPGPPGPPGPPGRPGDTVFQpGPPGDHGAPGDIGPPGVPGVDGP 469
Cdd:NF038329   120 GEPGPAGPAGPAGEQGPRGDRG--ETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ-GPAGKDGEAGAKGPAGEKGPQGP 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  470 KGEPGQPCTECHCIPGPPGVPGVPGLDGVKGIPGGRGAPGVKGNPGSPGNAGLPGFAGFPGDQGHPGLKGDKGdtplPWG 549
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG----PDG 272
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2327921558  550 QVGDPGDPGHRGLPGRKGFDGSPGGPGAKGPRGPRGEPALSGRKG 594
Cdd:NF038329   273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1080-1336 2.12e-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: 74.56  E-value: 2.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1080 GKKGERGLPGPPGHSGPAGPDGAPGSPGSPGHPGRPGPDGDSGLKGQKgfpgppgstgppgppglpglpgpmgmrGDQGQ 1159
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPA---------------------------GPQGE 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1160 DGIPGPPGEKGETGLLGAhPGQKGSPGVPGVKGDRGVPGLSGLPGRKGTMGDVGPQGPPGTTGLPGPPGLPGTIVPGPKG 1239
Cdd:NF038329   170 AGPQGPAGKDGEAGAKGP-AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDG 248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1240 NRGLPGLRGNPGEPGPPGPPGPVGEgiKGDKGFMGLPGSRGLPGMVGDTGAPGQPGAPGIPGLPGVRGDPGFPGFPGVKG 1319
Cdd:NF038329   249 PQGPDGPAGKDGPRGDRGEAGPDGP--DGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326
                          250
                   ....*....|....*..
gi 2327921558 1320 EKGNPGFLGSIGHPGPV 1336
Cdd:NF038329   327 LPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
62-342 1.28e-11

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: 68.78  E-value: 1.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558   62 QKGFPGPEGLPGPQGPKGSPGLPgltGPKGIRGITGLPGFAGPPGLPGIPGYPGPPGLAGLPGCNGSKGEQGFPGIPGTP 141
Cdd:NF038329   112 QLKGDGEKGEPGPAGPAGPAGEQ---GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA 188
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  142 GYAGLPGPDGLKGQKGKpaQGEDGEfngkgdpgppgapgfqglpgppgfpgpagppgppgfFGFPGAMGPRGPKGRMGDS 221
Cdd:NF038329   189 GEKGPQGPRGETGPAGE--QGPAGP------------------------------------AGPDGEAGPAGEDGPAGPA 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  222 TIGQEGEKGVKGLTGPPGLPGPViftlrhpyRKSDFQGQKGDegergepgPPGPSGPPGDSYGSEKGAPGEPGPRGKPGK 301
Cdd:NF038329   231 GDGQQGPDGDPGPTGEDGPQGPD--------GPAGKDGPRGD--------RGEAGPDGPDGKDGERGPVGPAGKDGQNGK 294
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2327921558  302 DGAPGFPGTEGAKGTRGFPGLRGEAGIKGWKGDIGPPGFPG 342
Cdd:NF038329   295 DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1274-1328 1.37e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.02  E-value: 1.37e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2327921558 1274 GLPGSRGLPGMVGDTGAPGQPGAPGIPGLPGVRGDPGFPGFPGVKGEKGNPGFLG 1328
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
982-1036 2.64e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 2.64e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2327921558  982 GLEGVPGLPGSPGPRGDTGSSGDPGRPGPQGLPGSMGNMGVPGPKGRKGTSGFPG 1036
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
43-166 2.81e-05

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 48.75  E-value: 2.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558   43 GTKGEKGEIGFPGPPGFPGQKGFPGPEGLPGPQGPKGSPGLPGLTGPKGIRGITGLPGFAGPPGLPGIPGYpgppglagl 122
Cdd:NF038329   162 GPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD--------- 232
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2327921558  123 pGCNGSKGEQGFPGIPGTPGYAGLPGPDGLKGQKGKPA-QGEDGE 166
Cdd:NF038329   233 -GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGpDGPDGK 276
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
976-1030 8.42e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 8.42e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2327921558  976 GLPGPKGLEGVPGLPGSPGPRGDTGSSGDPGRPGPQGLPGSMGNMGVPGPKGRKG 1030
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1158-1442 1.02e-04

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: 46.82  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1158 GQDGIPGPPGEKGETGLLGAHpGQKGSPGVPGVKGDRGVPGLSGLPGRKGTMGDVGPQgppgttglpgppglpgtivpGP 1237
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPR-GDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ--------------------GP 175
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1238 KGNRGLPGLrgnpgepgppgppgpvgegiKGDKGFMGLPGSRGLPGMVGDTGAPGQPGAPGIPGLPGVRGDPGFPGfPGV 1317
Cdd:NF038329   176 AGKDGEAGA--------------------KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQ 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1318 KGEKGNPgflgsighpgpvgpkgppGPQGKPGTLKVISLPGSPGPPGAPGQPGVKGDPGPLGPPGIPGPCGPRGQPGKDG 1397
Cdd:NF038329   235 QGPDGDP------------------GPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG 296
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2327921558 1398 KPGAPGP---PGVKGSKGSKGEQGPPGLDGLPGLKGKPGDRGTPANGT 1442
Cdd:NF038329   297 LPGKDGKdgqNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKT 344
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
973-1027 1.26e-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: 1.26e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2327921558  973 GNPGLPGPKGLEGVPGLPGSPGPRGDTGSSGDPGRPGPQGLPGSMGNMGVPGPKG 1027
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
629-755 1.60e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 46.60  E-value: 1.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327921558  629 GAQGVPGALGPPGEAGLKGESSASipvlgppgppgppGQAGPRGLPGLPGPVGTCDPGHPGPDGEPGIPEVGFPgargPK 708
Cdd:PRK14959   389 PASGGAATIPTPGTQGPQGTAPAA-------------GMTPSSAAPATPAPSAAPSPRVPWDDAPPAPPRSGIP----PR 451
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2327921558  709 GDQGFPGTIGLPGYPGETGRPGypgemGVPGAKGEPSVGRPGEPGKP 755
Cdd:PRK14959   452 PAPRMPEASPVPGAPDSVASAS-----DAPPTLGDPSDTAEHTPSGP 493
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
286-339 2.10e-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: 2.10e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2327921558  286 EKGAPGEPGPRGKPGKDGAPGFPGTEGAKGTRGFPGLRGEAGIKGWKGDIGPPG 339
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
970-1025 2.34e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 2.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2327921558  970 GNRGNPGLPGPKGLEGVPGLPGSPGPRGDTGSSGDPGRPGPQGLPGSMGNMGVPGP 1025
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
288-343 3.27e-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: 3.27e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2327921558  288 GAPGEPGPRGKPGKDGAPGFPGTEGAKGTRGFPGLRGEAGIKGWKGDIGPPGFPGP 343
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
952-1008 4.85e-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: 4.85e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2327921558  952 GDKGEPGLKGFVGNPGEKGNRGNPGLPGPKGLEGVPGLPGSPGPRGDTGSSGDPGRP 1008
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1080-1129 5.51e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 5.51e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2327921558 1080 GKKGERGLPGPPGHSGPAGPDGAPGSPGSPGHPGRPGPDGDSGLKGQKGF 1129
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
964-1018 8.41e-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: 8.41e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2327921558  964 GNPGEKGNRGNPGLPGPKGLEGVPGLPGSPGPRGDTGSSGDPGRPGPQGLPGSMG 1018
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
928-982 8.92e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 8.92e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2327921558  928 GRPGVKGERGEKGKPGPPHAPHLKGDKGEPGLKGFVGNPGEKGNRGNPGLPGPKG 982
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
904-958 1.34e-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: 1.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2327921558  904 GLPGKPGSQGQRGNLGIPGVKGERGRPGVKGERGEKGKPGPPHAPHLKGDKGEPG 958
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1078-1119 1.38e-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: 38.24  E-value: 1.38e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2327921558 1078 DKGKKGERGLPGPPGHSGPAGPDGAPGSPGSPGHPGRPGPDG 1119
Cdd:pfam01391   14 PPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
700-755 1.64e-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: 1.64e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2327921558  700 GFPGARGPKGDQGFPGTIGLPGYPGETGRPGYPGEMGVPGAKGEPsvGRPGEPGKP 755
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP--GAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
895-948 2.99e-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: 2.99e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2327921558  895 GYPGTTGLPGLPGKPGSQGQRGNLGIPGVKGERGRPGVKGERGEKGKPGPPHAP 948
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1006-1057 3.79e-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: 37.09  E-value: 3.79e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2327921558 1006 GRPGPQGLPGSMGNMGVPGPKGRKGTSGFPGVAGRPGLPGIPGPQGDKGEPG 1057
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1033-1109 6.85e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 6.85e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2327921558 1033 GFPGVAGRPGLPGIPGPQGDKGEPGysegaspgppgpkgdpglpgDKGKKGERGLPGPPGHSGPAGPDGAPGSPGSP 1109
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPG--------------------PPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1268-1320 7.27e-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: 7.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2327921558 1268 GDKGFMGLPGSRGLPGMVGDTGAPGQPGAPGIPGLPGVRGDPGFPGFPGVKGE 1320
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
 
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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