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Conserved domains on  [gi|1418319177|ref|XP_025287253|]
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collagen alpha-6(IV) chain isoform X4 [Canis lupus dingo]

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 ...
 1556-1669 1.35e-62

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: 208.60  E-value: 1.35e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1556 QAIAVHSQDITIPQCPLGWHSLWIGYSFLMHTAAGaEGGGQSLVSPGSCLEDFRATPFIECSGArGTCHYFANKYSFWLT 1635
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1418319177 1636 TVEErqQFReEPVSETLKAG-QLHTRVSRCQVCMR 1669
Cdd:pfam01413   79 TVEE--QFR-KPMSQTPKAGnELRSYISRCVVCEA 110
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1448-1553 8.38e-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: 186.26  E-value: 8.38e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1448 YTLVKHSQSEQLPLCPAGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYArRNDKSYWLST 1527
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYA-SNDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1418319177 1528 TA-----PIPMMPVGQAQIPQYISRCSVCEA 1553
Cdd:pfam01413   80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1227-1442 5.60e-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: 113.08  E-value: 5.60e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1227 GGRGFPGLQGPAGLPGAPGLSLPSIIVGQPGDPGRPGLDGEQGDPGDPGFPGVPGPQGPKGVQGIPGFSGLPGELGLKGM 1306
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1307 RGEPGFMGIPGKVGPPGDPGLPGMKGKAGPQGFS-----GPQGAPGQTtiaeAVQVPPGPMGLPGIDGIPGLTGDPGVQG 1381
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPT----GEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1418319177 1382 PVGLQGSKGLPGVPGKDGLN---GIPGPPGALGDPGLPGLQGPPGFEGAPGKKGPFGRAGVPGQ 1442
Cdd:NF038329   273 PDGKDGERGPVGPAGKDGQNgkdGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 507-748 8.55e-24

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 106.53  E-value: 8.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  507 GLKGTRGDPGSGGAQGPSGAPGLFGPPGPAGSKGDKGEPT---FSSASGVPGEQGDPGPQGLPGEMGAPGKdgipglpgl 583
Cdd:NF038329   132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGpqgPAGKDGEAGAKGPAGEKGPQGPRGETGP--------- 202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  584 pglpgdggQGFPGEKGLPGLPGERGHSGPTGPPGIGLPGSPGPRGLPGDQGIDGLPGQQGLPGLPGitlpciipeTYGLS 663
Cdd:NF038329   203 --------AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG---------PRGDR 265

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  664 GLPGAPGFPGPKGARGLPGTPGQPGLRGNKGepgspglvhlpeLPGFPGPRGEKGLPGFPGLPGKDGLPGKLGSPGLPGP 743
Cdd:NF038329   266 GEAGPDGPDGKDGERGPVGPAGKDGQNGKDG------------LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333


                   ....*
gi 1418319177  744 KGAPG 748
Cdd:NF038329   334 DGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 667-909 9.54e-23

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 103.45  E-value: 9.54e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  667 GAPGFPGPKGARGLPGTPGQPGLRGNKGEPGSPGLVHLPELPGFPGPRGEKGLPGFPGLPGKDGLPGKLGSPGLPGPKGA 746
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  747 PGdifgaENGSPGEQGLQGLPGDRGLPGDSGLPGPKGLLGKSgllgPKGERGSPGTPGHMGEPGPpgpdglygsiKGKPG 826
Cdd:NF038329   197 RG-----ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG----QQGPDGDPGPTGEDGPQGP----------DGPAG 257

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  827 LPGVPGFPGPSGHPGKKGLRGETGSPASAGKRGLPGLKGLPGSPGLIGFLGSSGLPGNTGLPGLPGPKGEKGSVGLVGFP 906
Cdd:NF038329   258 KDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337


                   ...
gi 1418319177  907 GMP 909
Cdd:NF038329   338 GKP 340
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 904-1158 2.05e-21

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 99.21  E-value: 2.05e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  904 GFPGMPGLPGIPGTSGIKGISGSAGRVGPSGKAGHAGEKGDRGDPGPAGVPSPRPPmlnlqfKGDKGSRGSAGLDGFPGP 983
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGP------QGPAGKDGEAGAKGPAGE 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  984 RGDKGEAgplgppglpgapgfpstikgliGRAGLPGSIGLRGLPGLKGSPGITGFPGIAGESGsQGLNGAPGLPGASGLP 1063
Cdd:NF038329   191 KGPQGPR----------------------GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGED 247

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1064 GSKGDQGQTlgisGSPGLKGQPGESGFKGVQGTNGLVGDVGLPGSKGEDGKVGISGDLGLPGSPGLPGIAGMRGNPGLPG 1143
Cdd:NF038329   248 GPQGPDGPA----GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                          250
                   ....*....|....*
gi 1418319177 1144 SPGHPGATGTLGPPG 1158
Cdd:NF038329   324 KDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 254-477 3.76e-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: 86.11  E-value: 3.76e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  254 PKGKKGSKGEPGLPGFPGISGPPGLPG-LGTAGEKGEKGIPGLPGPRGPMGLERLQGPPGIQGKKGSSGFPGLNGLPGIK 332
Cdd:NF038329   130 PAGEQGPRGDRGETGPAGPAGPPGPQGeRGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA 209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  333 GEKGGIGLPGPDVFIDTDGAVISGYPGDPGMPGLPGLKGDEGIQGLPGPSGIPGLPALPGVPGALGPQGVPGLkgdqgsp 412
Cdd:NF038329   210 GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP------- 282

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1418319177  413 grttVGTAGTPGRDGLPGLPGLRGPPGpafetetlQNTEPGFPGLRGERGPKGNPGLKGIKGDLG 477
Cdd:NF038329   283 ----VGPAGKDGQNGKDGLPGKDGKDG--------QNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 50-323 1.64e-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: 74.94  E-value: 1.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177   50 GQPGPIGIQGPTGPQGFAGPSGLAGLKGERGSPGPLGPYGPKGDKGPMGVPGFLGINGIPGHPGQPGPRGPPGLDGCNGT 129
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  130 QGAVGYPGPNGYPGLLGPPGLPGQKGSKGEPVLAQGTFKGMKGEPGLPGLDGiigppgapgspgavgpmgppglqgppgp 209
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDG---------------------------- 248

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  210 pgfpgpdGNMGLGFQGEKGVKGDVGLPGPAGpppstgelefmgfPKGKKGSKGEPGLPGFPGISGPPGLPglGTAGEKGE 289
Cdd:NF038329   249 -------PQGPDGPAGKDGPRGDRGEAGPDG-------------PDGKDGERGPVGPAGKDGQNGKDGLP--GKDGKDGQ 306

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1418319177  290 KGIPGLPGPRGPMGLERLQGPPGIQGKKGSSGFP 323
Cdd:NF038329   307 NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1134-1189 6.51e-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: 6.51e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1418319177 1134 GMRGNPGLPGSPGHPGATGTLGPPGLIGTKGFPGLPGLHGLNGLPGTKGTHGTPGP 1189
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
 
Name Accession Description Interval E-value
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1556-1669 1.35e-62

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: 208.60  E-value: 1.35e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1556 QAIAVHSQDITIPQCPLGWHSLWIGYSFLMHTAAGaEGGGQSLVSPGSCLEDFRATPFIECSGArGTCHYFANKYSFWLT 1635
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1418319177 1636 TVEErqQFReEPVSETLKAG-QLHTRVSRCQVCMR 1669
Cdd:pfam01413   79 TVEE--QFR-KPMSQTPKAGnELRSYISRCVVCEA 110
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1555-1669 2.35e-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: 190.68  E-value: 2.35e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  1555 SQAIAVHSQDITIPQCPLGWHSLWIGYSFLMHTaAGAEGGGQSLVSPGSCLEDFRATPFIECSGaRGTCHYFANK-YSFW 1633
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASRNdYSFW 78

                            90       100       110
                    ....*....|....*....|....*....|....*.
gi 1418319177  1634 LTTVEERQQFReEPVSETLKAGQLHTRVSRCQVCMR 1669
Cdd:smart00111   79 LSTIEPSDQFT-APRPMTPKAGDLRPYISRCQVCEK 113
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1448-1553 8.38e-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: 186.26  E-value: 8.38e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1448 YTLVKHSQSEQLPLCPAGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYArRNDKSYWLST 1527
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYA-SNDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1418319177 1528 TA-----PIPMMPVGQAQIPQYISRCSVCEA 1553
Cdd:pfam01413   80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1447-1554 2.12e-50

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: 173.73  E-value: 2.12e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  1447 GYTLVKHSQSEQLPLCPAGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYARRNDKSYWLS 1526
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 1418319177  1527 T-------TAPIPMMPVgQAQIPQYISRCSVCEAP 1554
Cdd:smart00111   81 TiepsdqfTAPRPMTPK-AGDLRPYISRCQVCEKP 114
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1227-1442 5.60e-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: 113.08  E-value: 5.60e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1227 GGRGFPGLQGPAGLPGAPGLSLPSIIVGQPGDPGRPGLDGEQGDPGDPGFPGVPGPQGPKGVQGIPGFSGLPGELGLKGM 1306
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1307 RGEPGFMGIPGKVGPPGDPGLPGMKGKAGPQGFS-----GPQGAPGQTtiaeAVQVPPGPMGLPGIDGIPGLTGDPGVQG 1381
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPT----GEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1418319177 1382 PVGLQGSKGLPGVPGKDGLN---GIPGPPGALGDPGLPGLQGPPGFEGAPGKKGPFGRAGVPGQ 1442
Cdd:NF038329   273 PDGKDGERGPVGPAGKDGQNgkdGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1181-1433 3.53e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 107.68  E-value: 3.53e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1181 KGTHGTPGPSISGVPGPAGLPGPKGEKGspgtgigAPGRPGSRGQKGGRGFPGLQGPAGLPGAPGLSlpsiivGQPGDPG 1260
Cdd:NF038329   108 EGLQQLKGDGEKGEPGPAGPAGPAGEQG-------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ------GEAGPQG 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1261 RPGLDGEQGDPGDPGFPGVPGPQGPKGVQGIPGFSGLPGELGLKGMRGEPGFMGIPGKvgppGDPGLPGMKGKAGPQGFS 1340
Cdd:NF038329   175 PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQ 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1341 GPQGAPGQttiaEAVQVPPGPMGLPGIDGIPGLTGDPGVQGPVGLQGSKGLPGVPGKDGLNGIPGPPGALGDPGLPG--- 1417
Cdd:NF038329   251 GPDGPAGK----DGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGkdg 326

                          250
                   ....*....|....*.
gi 1418319177 1418 LQGPPGFEGAPGKKGP 1433
Cdd:NF038329   327 LPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 507-748 8.55e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 106.53  E-value: 8.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  507 GLKGTRGDPGSGGAQGPSGAPGLFGPPGPAGSKGDKGEPT---FSSASGVPGEQGDPGPQGLPGEMGAPGKdgipglpgl 583
Cdd:NF038329   132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGpqgPAGKDGEAGAKGPAGEKGPQGPRGETGP--------- 202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  584 pglpgdggQGFPGEKGLPGLPGERGHSGPTGPPGIGLPGSPGPRGLPGDQGIDGLPGQQGLPGLPGitlpciipeTYGLS 663
Cdd:NF038329   203 --------AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG---------PRGDR 265

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  664 GLPGAPGFPGPKGARGLPGTPGQPGLRGNKGepgspglvhlpeLPGFPGPRGEKGLPGFPGLPGKDGLPGKLGSPGLPGP 743
Cdd:NF038329   266 GEAGPDGPDGKDGERGPVGPAGKDGQNGKDG------------LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333


                   ....*
gi 1418319177  744 KGAPG 748
Cdd:NF038329   334 DGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 667-909 9.54e-23

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 103.45  E-value: 9.54e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  667 GAPGFPGPKGARGLPGTPGQPGLRGNKGEPGSPGLVHLPELPGFPGPRGEKGLPGFPGLPGKDGLPGKLGSPGLPGPKGA 746
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  747 PGdifgaENGSPGEQGLQGLPGDRGLPGDSGLPGPKGLLGKSgllgPKGERGSPGTPGHMGEPGPpgpdglygsiKGKPG 826
Cdd:NF038329   197 RG-----ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG----QQGPDGDPGPTGEDGPQGP----------DGPAG 257

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  827 LPGVPGFPGPSGHPGKKGLRGETGSPASAGKRGLPGLKGLPGSPGLIGFLGSSGLPGNTGLPGLPGPKGEKGSVGLVGFP 906
Cdd:NF038329   258 KDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337


                   ...
gi 1418319177  907 GMP 909
Cdd:NF038329   338 GKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 904-1158 2.05e-21

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 99.21  E-value: 2.05e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  904 GFPGMPGLPGIPGTSGIKGISGSAGRVGPSGKAGHAGEKGDRGDPGPAGVPSPRPPmlnlqfKGDKGSRGSAGLDGFPGP 983
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGP------QGPAGKDGEAGAKGPAGE 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  984 RGDKGEAgplgppglpgapgfpstikgliGRAGLPGSIGLRGLPGLKGSPGITGFPGIAGESGsQGLNGAPGLPGASGLP 1063
Cdd:NF038329   191 KGPQGPR----------------------GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGED 247

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1064 GSKGDQGQTlgisGSPGLKGQPGESGFKGVQGTNGLVGDVGLPGSKGEDGKVGISGDLGLPGSPGLPGIAGMRGNPGLPG 1143
Cdd:NF038329   248 GPQGPDGPA----GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                          250
                   ....*....|....*
gi 1418319177 1144 SPGHPGATGTLGPPG 1158
Cdd:NF038329   324 KDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 508-800 2.08e-21

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 99.21  E-value: 2.08e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  508 LKGTRGDPGSGGAQGPSGAPGLFGPPGPAGSKGDKGEPtfsSASGVPGEQGDPGPQGLPGEMGAPGKDgipglpglpglp 587
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPP---GPQGERGEKGPAGPQGEAGPQGPAGKD------------ 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  588 gdggqGFPGEKGLPGLPGERGHSGPTGPPGiglpgSPGPRGLPGDQGIDGLPGQQGLPGLPGitlpciiPETYGLSGLPG 667
Cdd:NF038329   180 -----GEAGAKGPAGEKGPQGPRGETGPAG-----EQGPAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPG 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  668 APGFPGPKGARGLPGTPGQPGLRGnkgepgspglvhlpeLPGFPGPRGEKGLPGFPGLPGKDGLPGKLGSPGLPGPKGAP 747
Cdd:NF038329   243 PTGEDGPQGPDGPAGKDGPRGDRG---------------EAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN 307

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1418319177  748 GdifgaENGSPGEQGLQGLPGDRGLPGdsglpgpkgllgksgllgPKGERGSP 800
Cdd:NF038329   308 G-----KDGLPGKDGKDGQPGKDGLPG------------------KDGKDGQP 337
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 877-1131 3.00e-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: 3.00e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  877 GSSGLPGNTGLPGLPGPKGEKGSVGLVGFPGMPGLPGIPGTSGIKGISGSAGRVGPSGKAGHAGEKGDRGDPGPAGVpsp 956
Cdd:NF038329   120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP--- 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  957 rppmlnlqfKGDKGSRGSAGLDGFPGPRGDKGEAgplgppglpgapgfpstikgliGRAGLPGSIGlRGLPGLKGSPGIT 1036
Cdd:NF038329   197 ---------RGETGPAGEQGPAGPAGPDGEAGPA----------------------GEDGPAGPAG-DGQQGPDGDPGPT 244

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1037 GFPGIAGESGSQGLNGAPGLPGASGLPGSKGDQGQTlGISGSPGLKGQPGESGFKGVQGTNGLVGDVGLPGSKGEDGKVG 1116
Cdd:NF038329   245 GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER-GPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                          250
                   ....*....|....*
gi 1418319177 1117 ISGDLGLPGSPGLPG 1131
Cdd:NF038329   324 KDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 895-1166 3.40e-20

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 95.74  E-value: 3.40e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  895 GEKGSVGLVGFPGMPGLPGIPGTSGIKGISGSAGRVGPSGKAGHAGEKGDRGDPGPAGVPSPrppmlnlqfKGDKGSRGS 974
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK---------DGEAGAKGP 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  975 AGLDGFPGPRGDKGEAgplgppglpgapgfpstikgligraglpGSIGLRGLPGLKGSPGITGFPGIAGESGsQGLNGAP 1054
Cdd:NF038329   188 AGEKGPQGPRGETGPA----------------------------GEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPD 238

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1055 GLPGASGLPGSKGDQGQTlgisGSPGLKGQPGESGFKGVQGTNGLVGDVGLPGSKGEDGKVGisgdlgLPGSPGLPGIAG 1134
Cdd:NF038329   239 GDPGPTGEDGPQGPDGPA----GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG------LPGKDGKDGQNG 308

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1418319177 1135 MRGNPGLPGSPGHPGATGTLGPPGLIGTKGFP 1166
Cdd:NF038329   309 KDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1264-1447 1.08e-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: 94.20  E-value: 1.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1264 LDGEQGDPGDPGFPGVPGPQGPKGVQGIPGFSGLPGELGLKGMRGEPGFMGIPGKVGPPGDPGLPGMKGKAGPQGFSGPQ 1343
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1344 GAPGQTTIAEavqvPPGPMGLPGIDGIPGLTGDPGVQGPVGL--QGSKGLPGVPGKDGLNGIPGPPGALGDPGLPGLQGP 1421
Cdd:NF038329   195 GPRGETGPAG----EQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP 270

                          170       180
                   ....*....|....*....|....*.
gi 1418319177 1422 PGFEGAPGKKGPFGRAGVPGQSVRVG 1447
Cdd:NF038329   271 DGPDGKDGERGPVGPAGKDGQNGKDG 296
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1101-1348 5.11e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 91.89  E-value: 5.11e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1101 GDVGLPGSKGEDGKVGISGDLGLPGSPGLPGIAGMRGNPGLPGSPGHPGATGTLGPPGLIGTKGFPGLPGLHGLNGLPGT 1180
Cdd:NF038329   120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1181 KGTHGTPGPSisGVPGPAGLPGPKGEKGSPGtgigapgrPGSRGQKGGRGFPGLQGPAGlpgapglslpsiivgqpgDPG 1260
Cdd:NF038329   200 TGPAGEQGPA--GPAGPDGEAGPAGEDGPAG--------PAGDGQQGPDGDPGPTGEDG------------------PQG 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1261 RPGLDGEQGDPGDPGFPGVPGPQGPKGVQGIPGFSGLPGELGLKGMRGEPGFMGIPGKVGPPGDPGLPGMKGKAGPQGFS 1340
Cdd:NF038329   252 PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKD 331


                   ....*...
gi 1418319177 1341 GPQGAPGQ 1348
Cdd:NF038329   332 GKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 605-853 9.84e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 91.12  E-value: 9.84e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  605 GERGHSGPTGPPGI-GLPGSPGPRGLPGDQGIDGLPGQQGLPGLPGitlpciipetyglsglpgAPGFPGPKGARGLPGT 683
Cdd:NF038329   117 GEKGEPGPAGPAGPaGEQGPRGDRGETGPAGPAGPPGPQGERGEKG------------------PAGPQGEAGPQGPAGK 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  684 PGQPGLRGNKGEPGSPGLVHLPELPGFPGPRGEKGLPGFPGLPGKDGLPGKLGSpGLPGPKGAPGdifgaENGSPGEQGL 763
Cdd:NF038329   179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPG-----PTGEDGPQGP 252

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  764 QGLPGDRGLPGDSGLPGPKGLLGKSGLLGPKGERGSPGTPGHMGEPGPPGPDGLYGSiKGKPGLPGVPGFPGPSGHPGKK 843
Cdd:NF038329   253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK-DGLPGKDGKDGQPGKDGLPGKD 331

                          250
                   ....*....|
gi 1418319177  844 GLRGETGSPA 853
Cdd:NF038329   332 GKDGQPGKPA 341
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 751-989 1.22e-17

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 87.65  E-value: 1.22e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  751 FGAENGSPGEQGLQGLPGDRGLPGDSGLPGPKGLLGKSGLLGPKGERGSPGTPGHMGEPGPpgpdglygsikgkPGLPGV 830
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP-------------AGKDGE 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  831 PGFPGPSGHPGKKGLRGETGSPASAGKRGLPGLKGLPGSPGLIGFLGSSGlPGNTGLPGLPGPKGEKGSVGLVGFPGMPG 910
Cdd:NF038329   182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1418319177  911 LPGIPGTSGIKGISGSAGRVGPSGKAGHAGEKGDRGDPGPAGvpsPRPPMLNLQFKGDKGSRGSAGLDGFPGPRGDKGE 989
Cdd:NF038329   261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG---KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 254-477 3.76e-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: 86.11  E-value: 3.76e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  254 PKGKKGSKGEPGLPGFPGISGPPGLPG-LGTAGEKGEKGIPGLPGPRGPMGLERLQGPPGIQGKKGSSGFPGLNGLPGIK 332
Cdd:NF038329   130 PAGEQGPRGDRGETGPAGPAGPPGPQGeRGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA 209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  333 GEKGGIGLPGPDVFIDTDGAVISGYPGDPGMPGLPGLKGDEGIQGLPGPSGIPGLPALPGVPGALGPQGVPGLkgdqgsp 412
Cdd:NF038329   210 GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP------- 282

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1418319177  413 grttVGTAGTPGRDGLPGLPGLRGPPGpafetetlQNTEPGFPGLRGERGPKGNPGLKGIKGDLG 477
Cdd:NF038329   283 ----VGPAGKDGQNGKDGLPGKDGKDG--------QNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 278-545 7.12e-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: 79.18  E-value: 7.12e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  278 LPGLGTAGEKGEKGIPGLPGPRGPMGLERLQGPPGIQGKKGSSGFPGLNGLPGIKGEKGGIGLPGPDvfidtdgavisgy 357
Cdd:NF038329   113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD------------- 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  358 pGDPGMPGLPGLKGDEGIQGLPGPSGIPGLPALPGVPGALGPQGVPGLkgdQGSPGRTTVGTAGTPGRDGLPGLPGLRGP 437
Cdd:NF038329   180 -GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGP---AGPAGDGQQGPDGDPGPTGEDGPQGPDGP 255

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  438 PGPafETETLQNTEPGFPGLRGERGPKGNPGLkgikgdlgfcacdggvpntgppgePGMPGPPGLIGLPGLKGTRGDPGS 517
Cdd:NF038329   256 AGK--DGPRGDRGEAGPDGPDGKDGERGPVGP------------------------AGKDGQNGKDGLPGKDGKDGQNGK 309

                          250       260
                   ....*....|....*....|....*...
gi 1418319177  518 GGAQGPSGAPGLFGPPGPAGSKGDKGEP 545
Cdd:NF038329   310 DGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 50-323 1.64e-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: 74.94  E-value: 1.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177   50 GQPGPIGIQGPTGPQGFAGPSGLAGLKGERGSPGPLGPYGPKGDKGPMGVPGFLGINGIPGHPGQPGPRGPPGLDGCNGT 129
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  130 QGAVGYPGPNGYPGLLGPPGLPGQKGSKGEPVLAQGTFKGMKGEPGLPGLDGiigppgapgspgavgpmgppglqgppgp 209
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDG---------------------------- 248

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  210 pgfpgpdGNMGLGFQGEKGVKGDVGLPGPAGpppstgelefmgfPKGKKGSKGEPGLPGFPGISGPPGLPglGTAGEKGE 289
Cdd:NF038329   249 -------PQGPDGPAGKDGPRGDRGEAGPDG-------------PDGKDGERGPVGPAGKDGQNGKDGLP--GKDGKDGQ 306

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1418319177  290 KGIPGLPGPRGPMGLERLQGPPGIQGKKGSSGFP 323
Cdd:NF038329   307 NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 21-181 1.66e-09

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 62.23  E-value: 1.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177   21 AGEKKSYGKPcGGQDCRGGCKCFPEKGARGQPGPIGIQGPTGPQGFAGPSGLAGLKGERGSPGPLGPYGPKGDKGPMGVP 100
Cdd:NF038329   131 AGEQGPRGDR-GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA 209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  101 GFLGINGIPGHPGQPGPRGPPGlDGCNGTQGAVGYPGPNGYPGLLGPPGLPGQKGSKGEPVLAQGTFK-GMKGEPGLPGL 179
Cdd:NF038329   210 GPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKdGERGPVGPAGK 288


                   ..
gi 1418319177  180 DG 181
Cdd:NF038329   289 DG 290
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1358-1468 5.94e-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: 57.22  E-value: 5.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1358 PPGPMGLPGIDGIPGLTGDPGVQGP---VGLQGSKGLPGVPGKDGLNGIPGPPGALGDPGLPGLQGPPGFEGAPGKKGPF 1434
Cdd:NF038329   121 EPGPAGPAGPAGEQGPRGDRGETGPagpAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1418319177 1435 GRAGVPGQSVRVGYTLVKHSQSEQLPLCPAGMSQ 1468
Cdd:NF038329   201 GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ 234
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 33-140 2.25e-06

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 52.21  E-value: 2.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177   33 GQDCRGGCKCFPEKGARGQPGPIGIQGPTGPQGFAGPSGLAGLKGERGSPGPLGPYGPKGDKGPMGVPGFLGINGIPGHP 112
Cdd:NF038329   219 GPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLP 298

                           90       100
                   ....*....|....*....|....*...
gi 1418319177  113 GQPGPRGPPGLDGCNGTQGAVGYPGPNG 140
Cdd:NF038329   299 GKDGKDGQNGKDGLPGKDGKDGQPGKDG 326
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 664-720 3.44e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 3.44e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1418319177  664 GLPGAPGFPGPKGARGLPGTPGQPGLRGNKGEPGSPGLVHLPELPGFPGPRGEKGLP 720
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1378-1433 6.09e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 6.09e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1418319177 1378 GVQGPVGLQGSKGLPGVPGKDGLNGIPGPPGALGDPGLPGLQGPPGFEGAPGKKGP 1433
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 45-100 3.37e-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: 3.37e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1418319177   45 EKGARGQPGPIGIQGPTGPQGFAGPSGLAGLKGERGSPGPLGPYGPKGDKGPMGVP 100
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1010-1064 5.79e-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: 39.40  E-value: 5.79e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1418319177 1010 GLIGRAGLPGSIGLRGLPGLKGSPGITGFPGIAGESGSQGLNGAPGLPGASGLPG 1064
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1134-1189 6.51e-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: 6.51e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1418319177 1134 GMRGNPGLPGSPGHPGATGTLGPPGLIGTKGFPGLPGLHGLNGLPGTKGTHGTPGP 1189
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 865-919 8.49e-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: 8.49e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1418319177  865 GLPGSPGLIGFLGSSGLPGNTGLPGLPGPKGEKGSVGLVGFPGMPGLPGIPGTSG 919
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PPE COG5651
PPE-repeat protein [Function unknown];
1015-1203 9.97e-04

PPE-repeat protein [Function unknown];


Pssm-ID: 444372 [Multi-domain]  Cd Length: 385  Bit Score: 43.34  E-value: 9.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1015 AGLPGSIGLRGLPGLKGSPGITGFPGIAGESGSQGLNGAPGLPGASGLPGSKGDQGQTLGISGSPGLKGQPGESGFKGVQ 1094
Cdd:COG5651    208 VGIGGLNSGSGPIGLNSGPGNTGFAGTGAAAGAAAAAAAAAAAAGAGASAALASLAATLLNASSLGLAATAASSAATNLG 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1095 GTNGLVGDVglpgskgedgkVGISGDLGLPGSPGLPGIAGMRGNPGLPGSPGHPGATGTLGPPGLIGTKGFPGLPGLHGL 1174
Cdd:COG5651    288 LAGSPLGLA-----------GGGAGAAAATGLGLGAGGAAGAAGATGAGAALGAGAAAAAAGAAAGAGAAAAAAAGGAGG 356

                          170       180
                   ....*....|....*....|....*....
gi 1418319177 1175 NGLPGTKGTHGTPGPSISGVPGPAGLPGP 1203
Cdd:COG5651    357 GGGGALGAGGGGGSAGAAAGAASGGGAAA 385
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 1131-1228 1.24e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 43.52  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1131 GIAGMRGNPGLPGspGHPGATGTLGPPGLIGTKGFPGLPGLHGLNGLPGTKGTHGTPGPSI-----SGVPGPAGLPgPKG 1205
Cdd:PRK14959   376 GGASAPSGSAAEG--PASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPAPSAAPSPRVpwddaPPAPPRSGIP-PRP 452

                           90       100
                   ....*....|....*....|...
gi 1418319177 1206 EKGSPGTGiGAPGRPGSRGQKGG 1228
Cdd:PRK14959   453 APRMPEAS-PVPGAPDSVASASD 474
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 359-413 1.81e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 1.81e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1418319177  359 GDPGMPGLPGLKGDEGIQGLPGPSGIPGLPALPGVPGALGPQGVPGLKGDQGSPG 413
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 ...
 1556-1669 1.35e-62

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: 208.60  E-value: 1.35e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1556 QAIAVHSQDITIPQCPLGWHSLWIGYSFLMHTAAGaEGGGQSLVSPGSCLEDFRATPFIECSGArGTCHYFANKYSFWLT 1635
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNG-EGHGQDLGSPGSCLERFRTMPFIECNGN-GTCNYASNDYSYWLS 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1418319177 1636 TVEErqQFReEPVSETLKAG-QLHTRVSRCQVCMR 1669
Cdd:pfam01413   79 TVEE--QFR-KPMSQTPKAGnELRSYISRCVVCEA 110
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1555-1669 2.35e-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: 190.68  E-value: 2.35e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  1555 SQAIAVHSQDITIPQCPLGWHSLWIGYSFLMHTaAGAEGGGQSLVSPGSCLEDFRATPFIECSGaRGTCHYFANK-YSFW 1633
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHT-GNGEGHGQDLGSPGSCLERFRTMPFIECNG-RGVCNYASRNdYSFW 78

                            90       100       110
                    ....*....|....*....|....*....|....*.
gi 1418319177  1634 LTTVEERQQFReEPVSETLKAGQLHTRVSRCQVCMR 1669
Cdd:smart00111   79 LSTIEPSDQFT-APRPMTPKAGDLRPYISRCQVCEK 113
C4 pfam01413
C-terminal tandem repeated domain in type 4 procollagen; Duplicated domain in C-terminus of ...
 1448-1553 8.38e-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: 186.26  E-value: 8.38e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1448 YTLVKHSQSEQLPLCPAGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYArRNDKSYWLST 1527
Cdd:pfam01413    1 FLIAVHSQTTQIPDCPPGWTSLWTGYSLLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGNGTCNYA-SNDYSYWLST 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1418319177 1528 TA-----PIPMMPVGQAQIPQYISRCSVCEA 1553
Cdd:pfam01413   80 VEeqfrkPMSQTPKAGNELRSYISRCVVCEA 110
C4 smart00111
C-terminal tandem repeated domain in type 4 procollagens; Duplicated domain in C-terminus of ...
 1447-1554 2.12e-50

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: 173.73  E-value: 2.12e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  1447 GYTLVKHSQSEQLPLCPAGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYARRNDKSYWLS 1526
Cdd:smart00111    1 GFVIAVHSQTTNVPQCPAGWVELWTGYSFLMHTGNGEGHGQDLGSPGSCLERFRTMPFIECNGRGVCNYASRNDYSFWLS 80

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 1418319177  1527 T-------TAPIPMMPVgQAQIPQYISRCSVCEAP 1554
Cdd:smart00111   81 TiepsdqfTAPRPMTPK-AGDLRPYISRCQVCEKP 114
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1227-1442 5.60e-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: 113.08  E-value: 5.60e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1227 GGRGFPGLQGPAGLPGAPGLSLPSIIVGQPGDPGRPGLDGEQGDPGDPGFPGVPGPQGPKGVQGIPGFSGLPGELGLKGM 1306
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1307 RGEPGFMGIPGKVGPPGDPGLPGMKGKAGPQGFS-----GPQGAPGQTtiaeAVQVPPGPMGLPGIDGIPGLTGDPGVQG 1381
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPT----GEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1418319177 1382 PVGLQGSKGLPGVPGKDGLN---GIPGPPGALGDPGLPGLQGPPGFEGAPGKKGPFGRAGVPGQ 1442
Cdd:NF038329   273 PDGKDGERGPVGPAGKDGQNgkdGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1181-1433 3.53e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 107.68  E-value: 3.53e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1181 KGTHGTPGPSISGVPGPAGLPGPKGEKGspgtgigAPGRPGSRGQKGGRGFPGLQGPAGLPGAPGLSlpsiivGQPGDPG 1260
Cdd:NF038329   108 EGLQQLKGDGEKGEPGPAGPAGPAGEQG-------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQ------GEAGPQG 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1261 RPGLDGEQGDPGDPGFPGVPGPQGPKGVQGIPGFSGLPGELGLKGMRGEPGFMGIPGKvgppGDPGLPGMKGKAGPQGFS 1340
Cdd:NF038329   175 PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQ 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1341 GPQGAPGQttiaEAVQVPPGPMGLPGIDGIPGLTGDPGVQGPVGLQGSKGLPGVPGKDGLNGIPGPPGALGDPGLPG--- 1417
Cdd:NF038329   251 GPDGPAGK----DGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGkdg 326

                          250
                   ....*....|....*.
gi 1418319177 1418 LQGPPGFEGAPGKKGP 1433
Cdd:NF038329   327 LPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 507-748 8.55e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 106.53  E-value: 8.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  507 GLKGTRGDPGSGGAQGPSGAPGLFGPPGPAGSKGDKGEPT---FSSASGVPGEQGDPGPQGLPGEMGAPGKdgipglpgl 583
Cdd:NF038329   132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGpqgPAGKDGEAGAKGPAGEKGPQGPRGETGP--------- 202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  584 pglpgdggQGFPGEKGLPGLPGERGHSGPTGPPGIGLPGSPGPRGLPGDQGIDGLPGQQGLPGLPGitlpciipeTYGLS 663
Cdd:NF038329   203 --------AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG---------PRGDR 265

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  664 GLPGAPGFPGPKGARGLPGTPGQPGLRGNKGepgspglvhlpeLPGFPGPRGEKGLPGFPGLPGKDGLPGKLGSPGLPGP 743
Cdd:NF038329   266 GEAGPDGPDGKDGERGPVGPAGKDGQNGKDG------------LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333


                   ....*
gi 1418319177  744 KGAPG 748
Cdd:NF038329   334 DGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 667-909 9.54e-23

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 103.45  E-value: 9.54e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  667 GAPGFPGPKGARGLPGTPGQPGLRGNKGEPGSPGLVHLPELPGFPGPRGEKGLPGFPGLPGKDGLPGKLGSPGLPGPKGA 746
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  747 PGdifgaENGSPGEQGLQGLPGDRGLPGDSGLPGPKGLLGKSgllgPKGERGSPGTPGHMGEPGPpgpdglygsiKGKPG 826
Cdd:NF038329   197 RG-----ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG----QQGPDGDPGPTGEDGPQGP----------DGPAG 257

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  827 LPGVPGFPGPSGHPGKKGLRGETGSPASAGKRGLPGLKGLPGSPGLIGFLGSSGLPGNTGLPGLPGPKGEKGSVGLVGFP 906
Cdd:NF038329   258 KDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337


                   ...
gi 1418319177  907 GMP 909
Cdd:NF038329   338 GKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 904-1158 2.05e-21

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 99.21  E-value: 2.05e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  904 GFPGMPGLPGIPGTSGIKGISGSAGRVGPSGKAGHAGEKGDRGDPGPAGVPSPRPPmlnlqfKGDKGSRGSAGLDGFPGP 983
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGP------QGPAGKDGEAGAKGPAGE 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  984 RGDKGEAgplgppglpgapgfpstikgliGRAGLPGSIGLRGLPGLKGSPGITGFPGIAGESGsQGLNGAPGLPGASGLP 1063
Cdd:NF038329   191 KGPQGPR----------------------GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGED 247

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1064 GSKGDQGQTlgisGSPGLKGQPGESGFKGVQGTNGLVGDVGLPGSKGEDGKVGISGDLGLPGSPGLPGIAGMRGNPGLPG 1143
Cdd:NF038329   248 GPQGPDGPA----GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                          250
                   ....*....|....*
gi 1418319177 1144 SPGHPGATGTLGPPG 1158
Cdd:NF038329   324 KDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 508-800 2.08e-21

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 99.21  E-value: 2.08e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  508 LKGTRGDPGSGGAQGPSGAPGLFGPPGPAGSKGDKGEPtfsSASGVPGEQGDPGPQGLPGEMGAPGKDgipglpglpglp 587
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPP---GPQGERGEKGPAGPQGEAGPQGPAGKD------------ 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  588 gdggqGFPGEKGLPGLPGERGHSGPTGPPGiglpgSPGPRGLPGDQGIDGLPGQQGLPGLPGitlpciiPETYGLSGLPG 667
Cdd:NF038329   180 -----GEAGAKGPAGEKGPQGPRGETGPAG-----EQGPAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDPG 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  668 APGFPGPKGARGLPGTPGQPGLRGnkgepgspglvhlpeLPGFPGPRGEKGLPGFPGLPGKDGLPGKLGSPGLPGPKGAP 747
Cdd:NF038329   243 PTGEDGPQGPDGPAGKDGPRGDRG---------------EAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN 307

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1418319177  748 GdifgaENGSPGEQGLQGLPGDRGLPGdsglpgpkgllgksgllgPKGERGSP 800
Cdd:NF038329   308 G-----KDGLPGKDGKDGQPGKDGLPG------------------KDGKDGQP 337
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 877-1131 3.00e-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: 3.00e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  877 GSSGLPGNTGLPGLPGPKGEKGSVGLVGFPGMPGLPGIPGTSGIKGISGSAGRVGPSGKAGHAGEKGDRGDPGPAGVpsp 956
Cdd:NF038329   120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP--- 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  957 rppmlnlqfKGDKGSRGSAGLDGFPGPRGDKGEAgplgppglpgapgfpstikgliGRAGLPGSIGlRGLPGLKGSPGIT 1036
Cdd:NF038329   197 ---------RGETGPAGEQGPAGPAGPDGEAGPA----------------------GEDGPAGPAG-DGQQGPDGDPGPT 244

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1037 GFPGIAGESGSQGLNGAPGLPGASGLPGSKGDQGQTlGISGSPGLKGQPGESGFKGVQGTNGLVGDVGLPGSKGEDGKVG 1116
Cdd:NF038329   245 GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER-GPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                          250
                   ....*....|....*
gi 1418319177 1117 ISGDLGLPGSPGLPG 1131
Cdd:NF038329   324 KDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 895-1166 3.40e-20

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 95.74  E-value: 3.40e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  895 GEKGSVGLVGFPGMPGLPGIPGTSGIKGISGSAGRVGPSGKAGHAGEKGDRGDPGPAGVPSPrppmlnlqfKGDKGSRGS 974
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK---------DGEAGAKGP 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  975 AGLDGFPGPRGDKGEAgplgppglpgapgfpstikgligraglpGSIGLRGLPGLKGSPGITGFPGIAGESGsQGLNGAP 1054
Cdd:NF038329   188 AGEKGPQGPRGETGPA----------------------------GEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPD 238

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1055 GLPGASGLPGSKGDQGQTlgisGSPGLKGQPGESGFKGVQGTNGLVGDVGLPGSKGEDGKVGisgdlgLPGSPGLPGIAG 1134
Cdd:NF038329   239 GDPGPTGEDGPQGPDGPA----GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG------LPGKDGKDGQNG 308

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1418319177 1135 MRGNPGLPGSPGHPGATGTLGPPGLIGTKGFP 1166
Cdd:NF038329   309 KDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1264-1447 1.08e-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: 94.20  E-value: 1.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1264 LDGEQGDPGDPGFPGVPGPQGPKGVQGIPGFSGLPGELGLKGMRGEPGFMGIPGKVGPPGDPGLPGMKGKAGPQGFSGPQ 1343
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1344 GAPGQTTIAEavqvPPGPMGLPGIDGIPGLTGDPGVQGPVGL--QGSKGLPGVPGKDGLNGIPGPPGALGDPGLPGLQGP 1421
Cdd:NF038329   195 GPRGETGPAG----EQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP 270

                          170       180
                   ....*....|....*....|....*.
gi 1418319177 1422 PGFEGAPGKKGPFGRAGVPGQSVRVG 1447
Cdd:NF038329   271 DGPDGKDGERGPVGPAGKDGQNGKDG 296
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1101-1348 5.11e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 91.89  E-value: 5.11e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1101 GDVGLPGSKGEDGKVGISGDLGLPGSPGLPGIAGMRGNPGLPGSPGHPGATGTLGPPGLIGTKGFPGLPGLHGLNGLPGT 1180
Cdd:NF038329   120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1181 KGTHGTPGPSisGVPGPAGLPGPKGEKGSPGtgigapgrPGSRGQKGGRGFPGLQGPAGlpgapglslpsiivgqpgDPG 1260
Cdd:NF038329   200 TGPAGEQGPA--GPAGPDGEAGPAGEDGPAG--------PAGDGQQGPDGDPGPTGEDG------------------PQG 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1261 RPGLDGEQGDPGDPGFPGVPGPQGPKGVQGIPGFSGLPGELGLKGMRGEPGFMGIPGKVGPPGDPGLPGMKGKAGPQGFS 1340
Cdd:NF038329   252 PDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKD 331


                   ....*...
gi 1418319177 1341 GPQGAPGQ 1348
Cdd:NF038329   332 GKDGQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 605-853 9.84e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 91.12  E-value: 9.84e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  605 GERGHSGPTGPPGI-GLPGSPGPRGLPGDQGIDGLPGQQGLPGLPGitlpciipetyglsglpgAPGFPGPKGARGLPGT 683
Cdd:NF038329   117 GEKGEPGPAGPAGPaGEQGPRGDRGETGPAGPAGPPGPQGERGEKG------------------PAGPQGEAGPQGPAGK 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  684 PGQPGLRGNKGEPGSPGLVHLPELPGFPGPRGEKGLPGFPGLPGKDGLPGKLGSpGLPGPKGAPGdifgaENGSPGEQGL 763
Cdd:NF038329   179 DGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPG-----PTGEDGPQGP 252

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  764 QGLPGDRGLPGDSGLPGPKGLLGKSGLLGPKGERGSPGTPGHMGEPGPPGPDGLYGSiKGKPGLPGVPGFPGPSGHPGKK 843
Cdd:NF038329   253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK-DGLPGKDGKDGQPGKDGLPGKD 331

                          250
                   ....*....|
gi 1418319177  844 GLRGETGSPA 853
Cdd:NF038329   332 GKDGQPGKPA 341
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 751-989 1.22e-17

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 87.65  E-value: 1.22e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  751 FGAENGSPGEQGLQGLPGDRGLPGDSGLPGPKGLLGKSGLLGPKGERGSPGTPGHMGEPGPpgpdglygsikgkPGLPGV 830
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP-------------AGKDGE 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  831 PGFPGPSGHPGKKGLRGETGSPASAGKRGLPGLKGLPGSPGLIGFLGSSGlPGNTGLPGLPGPKGEKGSVGLVGFPGMPG 910
Cdd:NF038329   182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1418319177  911 LPGIPGTSGIKGISGSAGRVGPSGKAGHAGEKGDRGDPGPAGvpsPRPPMLNLQFKGDKGSRGSAGLDGFPGPRGDKGE 989
Cdd:NF038329   261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG---KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 254-477 3.76e-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: 86.11  E-value: 3.76e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  254 PKGKKGSKGEPGLPGFPGISGPPGLPG-LGTAGEKGEKGIPGLPGPRGPMGLERLQGPPGIQGKKGSSGFPGLNGLPGIK 332
Cdd:NF038329   130 PAGEQGPRGDRGETGPAGPAGPPGPQGeRGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA 209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  333 GEKGGIGLPGPDVFIDTDGAVISGYPGDPGMPGLPGLKGDEGIQGLPGPSGIPGLPALPGVPGALGPQGVPGLkgdqgsp 412
Cdd:NF038329   210 GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP------- 282

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1418319177  413 grttVGTAGTPGRDGLPGLPGLRGPPGpafetetlQNTEPGFPGLRGERGPKGNPGLKGIKGDLG 477
Cdd:NF038329   283 ----VGPAGKDGQNGKDGLPGKDGKDG--------QNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 278-545 7.12e-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: 79.18  E-value: 7.12e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  278 LPGLGTAGEKGEKGIPGLPGPRGPMGLERLQGPPGIQGKKGSSGFPGLNGLPGIKGEKGGIGLPGPDvfidtdgavisgy 357
Cdd:NF038329   113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD------------- 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  358 pGDPGMPGLPGLKGDEGIQGLPGPSGIPGLPALPGVPGALGPQGVPGLkgdQGSPGRTTVGTAGTPGRDGLPGLPGLRGP 437
Cdd:NF038329   180 -GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGP---AGPAGDGQQGPDGDPGPTGEDGPQGPDGP 255

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  438 PGPafETETLQNTEPGFPGLRGERGPKGNPGLkgikgdlgfcacdggvpntgppgePGMPGPPGLIGLPGLKGTRGDPGS 517
Cdd:NF038329   256 AGK--DGPRGDRGEAGPDGPDGKDGERGPVGP------------------------AGKDGQNGKDGLPGKDGKDGQNGK 309

                          250       260
                   ....*....|....*....|....*...
gi 1418319177  518 GGAQGPSGAPGLFGPPGPAGSKGDKGEP 545
Cdd:NF038329   310 DGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 50-323 1.64e-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: 74.94  E-value: 1.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177   50 GQPGPIGIQGPTGPQGFAGPSGLAGLKGERGSPGPLGPYGPKGDKGPMGVPGFLGINGIPGHPGQPGPRGPPGLDGCNGT 129
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  130 QGAVGYPGPNGYPGLLGPPGLPGQKGSKGEPVLAQGTFKGMKGEPGLPGLDGiigppgapgspgavgpmgppglqgppgp 209
Cdd:NF038329   197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDG---------------------------- 248

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  210 pgfpgpdGNMGLGFQGEKGVKGDVGLPGPAGpppstgelefmgfPKGKKGSKGEPGLPGFPGISGPPGLPglGTAGEKGE 289
Cdd:NF038329   249 -------PQGPDGPAGKDGPRGDRGEAGPDG-------------PDGKDGERGPVGPAGKDGQNGKDGLP--GKDGKDGQ 306

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1418319177  290 KGIPGLPGPRGPMGLERLQGPPGIQGKKGSSGFP 323
Cdd:NF038329   307 NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 21-181 1.66e-09

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 62.23  E-value: 1.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177   21 AGEKKSYGKPcGGQDCRGGCKCFPEKGARGQPGPIGIQGPTGPQGFAGPSGLAGLKGERGSPGPLGPYGPKGDKGPMGVP 100
Cdd:NF038329   131 AGEQGPRGDR-GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPA 209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177  101 GFLGINGIPGHPGQPGPRGPPGlDGCNGTQGAVGYPGPNGYPGLLGPPGLPGQKGSKGEPVLAQGTFK-GMKGEPGLPGL 179
Cdd:NF038329   210 GPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKdGERGPVGPAGK 288


                   ..
gi 1418319177  180 DG 181
Cdd:NF038329   289 DG 290
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1358-1468 5.94e-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: 57.22  E-value: 5.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1358 PPGPMGLPGIDGIPGLTGDPGVQGP---VGLQGSKGLPGVPGKDGLNGIPGPPGALGDPGLPGLQGPPGFEGAPGKKGPF 1434
Cdd:NF038329   121 EPGPAGPAGPAGEQGPRGDRGETGPagpAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1418319177 1435 GRAGVPGQSVRVGYTLVKHSQSEQLPLCPAGMSQ 1468
Cdd:NF038329   201 GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ 234
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 33-140 2.25e-06

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 52.21  E-value: 2.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177   33 GQDCRGGCKCFPEKGARGQPGPIGIQGPTGPQGFAGPSGLAGLKGERGSPGPLGPYGPKGDKGPMGVPGFLGINGIPGHP 112
Cdd:NF038329   219 GPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLP 298

                           90       100
                   ....*....|....*....|....*...
gi 1418319177  113 GQPGPRGPPGLDGCNGTQGAVGYPGPNG 140
Cdd:NF038329   299 GKDGKDGQNGKDGLPGKDGKDGQPGKDG 326
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 664-720 3.44e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 3.44e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1418319177  664 GLPGAPGFPGPKGARGLPGTPGQPGLRGNKGEPGSPGLVHLPELPGFPGPRGEKGLP 720
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1378-1433 6.09e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 6.09e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1418319177 1378 GVQGPVGLQGSKGLPGVPGKDGLNGIPGPPGALGDPGLPGLQGPPGFEGAPGKKGP 1433
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1239-1300 9.38e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 9.38e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1418319177 1239 GLPGAPGLSlpsiivGQPGDPGRPGLDGEQGDPGDPGFPGVPGPQGPKGVQGIPGFSGLPGE 1300
Cdd:pfam01391    1 GPPGPPGPP------GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1358-1413 1.43e-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: 1.43e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1418319177 1358 PPGPMGLPGIDGIPGLTGDPGVQGPVGLQGSKGLPGVPGKDGLNGIPGPPGALGDP 1413
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1260-1314 2.14e-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: 40.55  E-value: 2.14e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1418319177 1260 GRPGLDGEQGDPGDPGFPGVPGPQGPKGVQGIPGFSGLPGELGLKGMRGEPGFMG 1314
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 679-743 2.41e-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: 40.55  E-value: 2.41e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1418319177  679 GLPGTPGQPGLRGNKGEPGSPGlvhlpelpgFPGPRGEKGLPGFPGLPGKDGLPGKLGSPGLPGP 743
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPG---------PPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1254-1310 3.30e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 3.30e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1418319177 1254 GQPGDPGRPGLDGEQGDPGDPGFPGVPGPQGPKGVQGIPGFSGLPGELGLKGMRGEP 1310
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 45-100 3.37e-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: 3.37e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1418319177   45 EKGARGQPGPIGIQGPTGPQGFAGPSGLAGLKGERGSPGPLGPYGPKGDKGPMGVP 100
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1372-1428 3.57e-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: 3.57e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1418319177 1372 GLTGDPGVQGPVGLQGSKGLPGVPGKDGLNGIPGPPGALGDPGLPGLQGPPGFEGAP 1428
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1384-1440 5.67e-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: 39.40  E-value: 5.67e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1418319177 1384 GLQGSKGLPGVPGKDGLNGIPGPPGALGDPGLPGLQGPPGFEGAPGKKGPFGRAGVP 1440
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1010-1064 5.79e-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: 39.40  E-value: 5.79e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1418319177 1010 GLIGRAGLPGSIGLRGLPGLKGSPGITGFPGIAGESGSQGLNGAPGLPGASGLPG 1064
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1134-1189 6.51e-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: 6.51e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1418319177 1134 GMRGNPGLPGSPGHPGATGTLGPPGLIGTKGFPGLPGLHGLNGLPGTKGTHGTPGP 1189
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 661-721 7.33e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 7.33e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1418319177  661 GLSGLPGAPGFPGPKGARGLPGTPGQPGLRGNKGEPGSPGlvhlpeLPGFPGPRGEKGLPG 721
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPG------PPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 865-919 8.49e-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: 8.49e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1418319177  865 GLPGSPGLIGFLGSSGLPGNTGLPGLPGPKGEKGSVGLVGFPGMPGLPGIPGTSG 919
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 47-101 9.37e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 9.37e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1418319177   47 GARGQPGPIGIQGPTGPQGFAGPSGLAGLKGERGSPGPLGPYGPKGDKGPMGVPG 101
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PPE COG5651
PPE-repeat protein [Function unknown];
1015-1203 9.97e-04

PPE-repeat protein [Function unknown];


Pssm-ID: 444372 [Multi-domain]  Cd Length: 385  Bit Score: 43.34  E-value: 9.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1015 AGLPGSIGLRGLPGLKGSPGITGFPGIAGESGSQGLNGAPGLPGASGLPGSKGDQGQTLGISGSPGLKGQPGESGFKGVQ 1094
Cdd:COG5651    208 VGIGGLNSGSGPIGLNSGPGNTGFAGTGAAAGAAAAAAAAAAAAGAGASAALASLAATLLNASSLGLAATAASSAATNLG 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1095 GTNGLVGDVglpgskgedgkVGISGDLGLPGSPGLPGIAGMRGNPGLPGSPGHPGATGTLGPPGLIGTKGFPGLPGLHGL 1174
Cdd:COG5651    288 LAGSPLGLA-----------GGGAGAAAATGLGLGAGGAAGAAGATGAGAALGAGAAAAAAGAAAGAGAAAAAAAGGAGG 356

                          170       180
                   ....*....|....*....|....*....
gi 1418319177 1175 NGLPGTKGTHGTPGPSISGVPGPAGLPGP 1203
Cdd:COG5651    357 GGGGALGAGGGGGSAGAAAGAASGGGAAA 385
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 516-572 1.06e-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: 1.06e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1418319177  516 GSGGAQGPSGAPGLFGPPGPAGSKGDKGEPTFSSASGVPGEQGDPGPQGLPGEMGAP 572
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 1131-1228 1.24e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 43.52  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1131 GIAGMRGNPGLPGspGHPGATGTLGPPGLIGTKGFPGLPGLHGLNGLPGTKGTHGTPGPSI-----SGVPGPAGLPgPKG 1205
Cdd:PRK14959   376 GGASAPSGSAAEG--PASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPAPSAAPSPRVpwddaPPAPPRSGIP-PRP 452

                           90       100
                   ....*....|....*....|...
gi 1418319177 1206 EKGSPGTGiGAPGRPGSRGQKGG 1228
Cdd:PRK14959   453 APRMPEAS-PVPGAPDSVASASD 474
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1375-1430 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 1418319177 1375 GDPGVQGPVGLQGSKGLPGVPGKDGLNGIPGPPGALGDPGLPGLQGPPGFEGAPGK 1430
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 822-871 1.40e-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: 38.24  E-value: 1.40e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1418319177  822 KGKPGLPGVPGFPGPSGHPGKKGLRGETGSPASAGKRGLPGLKGLPGSPG 871
Cdd:pfam01391    6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 359-413 1.81e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 1.81e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1418319177  359 GDPGMPGLPGLKGDEGIQGLPGPSGIPGLPALPGVPGALGPQGVPGLKGDQGSPG 413
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1016-1071 2.21e-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: 2.21e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1418319177 1016 GLPGSIGLRGLPGLKGSPGITGFPGIAGESGSQGLNGAPGLPGASGLPGSKGDQGQ 1071
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 356-407 2.58e-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: 2.58e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1418319177  356 GYPGDPGMPGLPGLKGDEGIQGLPGPSGIPGLPALPGVPGALGPQGVPGLKG 407
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1193-1262 4.76e-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: 36.70  E-value: 4.76e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418319177 1193 GVPGPAGLPGPKGEKGspgtgigAPGRPGSRGQKGGRGFPGLQGPAGLPGAPGLSlpsiivGQPGDPGRP 1262
Cdd:pfam01391    1 GPPGPPGPPGPPGPPG-------PPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP------GAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1393-1443 5.05e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.70  E-value: 5.05e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1418319177 1393 GVPGKDGLNGIPGPPGALGDPGLPGLQGPPGFEGAPGKKGPFGRAGVPGQS 1443
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 895-951 6.72e-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: 6.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1418319177  895 GEKGSVGLVGFPGMPGLPGIPGTSGIKGISGSAGRVGPSGKAGHAGEKGDRGDPGPA 951
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1113-1169 7.79e-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: 36.32  E-value: 7.79e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1418319177 1113 GKVGISGDLGLPGSPGLPGIAGMRGNPGLPGSPGHPGATGTLGPPGLIGTKGFPGLP 1169
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 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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