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Conserved domains on  [gi|688598960|ref|XP_009292324|]
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collagen alpha-2(XI) chain isoform X8 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1463-1693 4.56e-123

Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


:

Pssm-ID: 460199  Cd Length: 233  Bit Score: 385.16  E-value: 4.56e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  1463 GMEEIFGSLNSLRQEIESMRFPLGTKESPGRTCQDLHLSQPDLKDGEYWIDPNQGCARDSFKVYCNFTAgGETCLYPSKA 1542
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  1543 VENvKMNSWIKEKPGSLFSQFAKGNK-FSY-VDSVGEAVGVVQLGFLRLLSVQARQNLTYHCQRSVAWTDQTTdGGYKRA 1620
Cdd:pfam01410   80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQAT-GNLKKA 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688598960  1621 LRLQGANDEEISYE--TSPYIKALIDGCSYRKGL-DRTVLEVNTPQVEQLPLLDIRISDFGEDNQKFGFEVGPVCF 1693
Cdd:pfam01410  158 LLLQGSNDEEIRAEgnSRFTYTVLEDGCTKRTGQwGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 29-218 5.10e-53

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


:

Pssm-ID: 214560  Cd Length: 184  Bit Score: 184.10  E-value: 5.10e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960     29 PVDVLRVLQLPSLPEGVQKVPGFCTsrlsgtPDHAYRITKKAQISAPTKQLFSGRFPENFSIMTLVKAKAGLQAFLLSIY 108
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEP------GSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960    109 NEQGVQQLGLEL-GRSPIFLYEDQhRKPAPEDYPLFKGVNLADGKWHRIAISVQKKNITLILDCKNRITKTLPRSNNPVL 187
Cdd:smart00210   75 DAQNVRQFGLEVdGRANTLLLRYQ-GVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQPPI 153

                           170       180       190
                    ....*....|....*....|....*....|.
gi 688598960    188 DTKGITVFGARLLDEEVFQGEIQQLLIASNP 218
Cdd:smart00210  154 DTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 508-766 3.03e-36

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: 143.89  E-value: 3.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  508 DGERGDDGDVGPRGLPGEPGPRGllgpkgpsglpgppgVRGNDGPHGPKGNlgpqgepgppgqqgapgtQGMPGPQGATG 587
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRG---------------DRGETGPAGPAGP------------------PGPQGERGEKG 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  588 PPGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKGNQGPNGPQGSIGYPGPRGLKGAQGIRGLKGH--KGEKGEDGFPG 665
Cdd:NF038329  163 PAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPG 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  666 IKGDFGVKGERGEVGVPGPRGEDGPEGPKGRVGPPGEIGPLGLLGEKGKLGVPGLPGYPGRQGIKGSLGFPGFPGTNGEK 745
Cdd:NF038329  243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                         250       260
                  ....*....|....*....|.
gi 688598960  746 GTRGLIGKPGPRGQRGPTGPR 766
Cdd:NF038329  323 GKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 334-531 5.38e-20

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 94.97  E-value: 5.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  334 GPQGQPGSVGDPGERGPTGKAGLPGADGVPGPPGtsvmlpfrfgqSAGEKGPvasaqeaqaqailsQARLALKGPSGPMG 413
Cdd:NF038329  153 GPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG-----------PAGEKGP--------------QGPRGETGPAGEQG 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  414 FTGRPGPLGTPGSPGFKGERGDPGA--QGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDRGFDGLPGLPGDKG 491
Cdd:NF038329  208 PAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 688598960  492 YRGQPGGMGPPGPHGEDGERGDDGDVGPRGLPGEPGPRGL 531
Cdd:NF038329  288 KDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1133-1388 2.34e-19

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 93.05  E-value: 2.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1133 GEPGESGPPGVGGEPGKLGPRGERGEKGESGQPGTPGPPGGKGPTGDDGPKGnpgpvgfpgDPGPPGEVGPRGQDGAKGD 1212
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------EAGPQGPAGKDGEAGAKGP 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1213 RGEDGEQGEAGSPGPTGENGPPGPPGKRGPAGTRGPEGRQGEKGsKGDSGALGPPGKTGPVGPQGQPGKPGTEGLRGlpg 1292
Cdd:NF038329  188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG--- 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1293 tvgeqgspgaagpkgppgplgppglagLRGDPGAKGEKGHPGMLGLIGPAGEQGEKGDRGMPGPQGSTGPKGETGISGGT 1372
Cdd:NF038329  264 ---------------------------DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKD 316

                         250
                  ....*....|....*.
gi 688598960 1373 GPLGPAGPAGMPGPRG 1388
Cdd:NF038329  317 GKDGQPGKDGLPGKDG 332
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 707-923 9.07e-14

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 75.71  E-value: 9.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  707 GLLGEKGKLGVPGLPGYPGRQGIKGSLGFPGFPGTNGEKGTRGLIGKPGPRGQRGPTGPRGQRGPRGATGKSGAKGGSGS 786
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  787 DGPPGPPGERGLTGPQGANGFPGPKGPPGPPGKDGLpghpGQRGEVGFQGKVGPPGPPGVVGPHGPSGETGQMGERGHPG 866
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 688598960  867 PPGPPGEQGLSGSSGKEGTKGDPGPPGGPGKDGPPGLRGFPGERGLPGTPGSGGLKG 923
Cdd:NF038329  273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1463-1693 4.56e-123

Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 460199  Cd Length: 233  Bit Score: 385.16  E-value: 4.56e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  1463 GMEEIFGSLNSLRQEIESMRFPLGTKESPGRTCQDLHLSQPDLKDGEYWIDPNQGCARDSFKVYCNFTAgGETCLYPSKA 1542
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  1543 VENvKMNSWIKEKPGSLFSQFAKGNK-FSY-VDSVGEAVGVVQLGFLRLLSVQARQNLTYHCQRSVAWTDQTTdGGYKRA 1620
Cdd:pfam01410   80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQAT-GNLKKA 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688598960  1621 LRLQGANDEEISYE--TSPYIKALIDGCSYRKGL-DRTVLEVNTPQVEQLPLLDIRISDFGEDNQKFGFEVGPVCF 1693
Cdd:pfam01410  158 LLLQGSNDEEIRAEgnSRFTYTVLEDGCTKRTGQwGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1464-1694 2.62e-98

Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 197483  Cd Length: 232  Bit Score: 315.95  E-value: 2.62e-98
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960   1464 MEEIFGSLNSLRQEIESMRFPLGTKESPGRTCQDLHLSQPDLKDGEYWIDPNQGCARDSFKVYCNFTAgGETCLYPSKAV 1543
Cdd:smart00038    1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFET-GETCVSPSPSS 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960   1544 ENVKmNSWIKEKPGSLFSQFAK-GNKFSYVDSVGEAVGVVQLGFLRLLSVQARQNLTYHCQRSVAWTDQTTdGGYKRALR 1622
Cdd:smart00038   80 IPRK-TWYSGKSKHVWFGETMNgGFKFSYGDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEAT-GNLKKALR 157

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688598960   1623 LQGANDEEISYE--TSPYIKALIDGCSYRKG-LDRTVLEVNTPQVEQLPLLDIRISDFGEDNQKFGFEVGPVCFL 1694
Cdd:smart00038  158 LRGSNDVELSAEgnSKFTYEVLEDGCQKRTGkWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 29-218 5.10e-53

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


Pssm-ID: 214560  Cd Length: 184  Bit Score: 184.10  E-value: 5.10e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960     29 PVDVLRVLQLPSLPEGVQKVPGFCTsrlsgtPDHAYRITKKAQISAPTKQLFSGRFPENFSIMTLVKAKAGLQAFLLSIY 108
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEP------GSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960    109 NEQGVQQLGLEL-GRSPIFLYEDQhRKPAPEDYPLFKGVNLADGKWHRIAISVQKKNITLILDCKNRITKTLPRSNNPVL 187
Cdd:smart00210   75 DAQNVRQFGLEVdGRANTLLLRYQ-GVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQPPI 153

                           170       180       190
                    ....*....|....*....|....*....|.
gi 688598960    188 DTKGITVFGARLLDEEVFQGEIQQLLIASNP 218
Cdd:smart00210  154 DTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 508-766 3.03e-36

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: 143.89  E-value: 3.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  508 DGERGDDGDVGPRGLPGEPGPRGllgpkgpsglpgppgVRGNDGPHGPKGNlgpqgepgppgqqgapgtQGMPGPQGATG 587
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRG---------------DRGETGPAGPAGP------------------PGPQGERGEKG 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  588 PPGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKGNQGPNGPQGSIGYPGPRGLKGAQGIRGLKGH--KGEKGEDGFPG 665
Cdd:NF038329  163 PAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPG 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  666 IKGDFGVKGERGEVGVPGPRGEDGPEGPKGRVGPPGEIGPLGLLGEKGKLGVPGLPGYPGRQGIKGSLGFPGFPGTNGEK 745
Cdd:NF038329  243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                         250       260
                  ....*....|....*....|.
gi 688598960  746 GTRGLIGKPGPRGQRGPTGPR 766
Cdd:NF038329  323 GKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 429-694 5.16e-32

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: 131.18  E-value: 5.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  429 FKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDRGFDGLPGLPGDKGYRGQPGGMGPPGPHGED 508
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  509 GERGDDGDVGPRGLPGEPGPRGLlgpkgpsglpgppgvRGNDGPHGPKGnlgpqgepgppgqqgaPGTQGMPGPQGATGP 588
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGE---------------AGPAGEDGPAG----------------PAGDGQQGPDGDPGP 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  589 PGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKGNQGPNGPQGSIGYPGPRGLKGAQGIRGLKGHKGEKGEDGFPGIKG 668
Cdd:NF038329  244 TGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                         250       260
                  ....*....|....*....|....*.
gi 688598960  669 DFGVKGERGEVGVPGPRGEDGPEGPK 694
Cdd:NF038329  324 KDGLPGKDGKDGQPGKPAPKTPEVPQ 349
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 405-631 6.36e-27

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 116.16  E-value: 6.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  405 LKGPSGPMGFTGRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDRGFDGLP 484
Cdd:NF038329  133 EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPA 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  485 GLPGDKGYRGQPGGMGPPGPHG-----EDGERGDDGDVGPRGLPGEPGPRGllgpkgPSGLPGPPGVRGNDGPHGPKGnl 559
Cdd:NF038329  213 GPDGEAGPAGEDGPAGPAGDGQqgpdgDPGPTGEDGPQGPDGPAGKDGPRG------DRGEAGPDGPDGKDGERGPVG-- 284

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688598960  560 gpqgepgppgqqgAPGTQGMPGPQGATGPPGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKGNQGPNGPQ 631
Cdd:NF038329  285 -------------PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 334-531 5.38e-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: 94.97  E-value: 5.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  334 GPQGQPGSVGDPGERGPTGKAGLPGADGVPGPPGtsvmlpfrfgqSAGEKGPvasaqeaqaqailsQARLALKGPSGPMG 413
Cdd:NF038329  153 GPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG-----------PAGEKGP--------------QGPRGETGPAGEQG 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  414 FTGRPGPLGTPGSPGFKGERGDPGA--QGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDRGFDGLPGLPGDKG 491
Cdd:NF038329  208 PAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 688598960  492 YRGQPGGMGPPGPHGEDGERGDDGDVGPRGLPGEPGPRGL 531
Cdd:NF038329  288 KDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1133-1388 2.34e-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: 93.05  E-value: 2.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1133 GEPGESGPPGVGGEPGKLGPRGERGEKGESGQPGTPGPPGGKGPTGDDGPKGnpgpvgfpgDPGPPGEVGPRGQDGAKGD 1212
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------EAGPQGPAGKDGEAGAKGP 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1213 RGEDGEQGEAGSPGPTGENGPPGPPGKRGPAGTRGPEGRQGEKGsKGDSGALGPPGKTGPVGPQGQPGKPGTEGLRGlpg 1292
Cdd:NF038329  188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG--- 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1293 tvgeqgspgaagpkgppgplgppglagLRGDPGAKGEKGHPGMLGLIGPAGEQGEKGDRGMPGPQGSTGPKGETGISGGT 1372
Cdd:NF038329  264 ---------------------------DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKD 316

                         250
                  ....*....|....*.
gi 688598960 1373 GPLGPAGPAGMPGPRG 1388
Cdd:NF038329  317 GKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1256-1406 7.69e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 82.26  E-value: 7.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1256 GSKGDSGALGPPGKTGPVGPQGQPGKPGTEGLRGLPGTVGEQGSPGAAGPKGPPGPLGPPGLAGLRGDPGAKGEKGHPGM 1335
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1336 LGLIGPAGEQGEKG------------DRGMPGPQGS--TGPKGETGISGGTGPLGPAGPAGMPGPRGVKGAKGASGGAGP 1401
Cdd:NF038329  197 RGETGPAGEQGPAGpagpdgeagpagEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276


                  ....*
gi 688598960 1402 KGEKG 1406
Cdd:NF038329  277 DGERG 281
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 707-923 9.07e-14

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 75.71  E-value: 9.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  707 GLLGEKGKLGVPGLPGYPGRQGIKGSLGFPGFPGTNGEKGTRGLIGKPGPRGQRGPTGPRGQRGPRGATGKSGAKGGSGS 786
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  787 DGPPGPPGERGLTGPQGANGFPGPKGPPGPPGKDGLpghpGQRGEVGFQGKVGPPGPPGVVGPHGPSGETGQMGERGHPG 866
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 688598960  867 PPGPPGEQGLSGSSGKEGTKGDPGPPGGPGKDGPPGLRGFPGERGLPGTPGSGGLKG 923
Cdd:NF038329  273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
548-773 1.75e-11

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 68.52  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  548 GNDGPHGPKGNLGPQGEPGPPGQQGAPGTQGMPGPQGATGPPGEKGPTGKPGLPGmpgADGPPGHPGKEGPGGTKGNQGP 627
Cdd:COG5164    25 GSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQG---GTTPAQNQGGTRPAGNTGGTTP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  628 NGPQGSIGYPGPRGLKGAQGIRGLKGHK------------GEKGEDGFPGIKGDFGVKGERGEVGVPGPRGEDGPEGPKG 695
Cdd:COG5164   102 AGDGGATGPPDDGGATGPPDDGGSTTPPsggsttppgdggSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGG 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688598960  696 RVGPPgeigplgllgEKGKLGVPGLPGYPGRQGIKGSLGFPGFPGTNGEKGTRGliGKPGPRGQRGPTGPRGQRGPRG 773
Cdd:COG5164   182 STTPP----------NKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGPKDQRPKTNPIERRGPER 247
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1131-1298 3.84e-11

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 67.24  E-value: 3.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1131 EKGEPGESGPPGVGGEPGKLGPRGERGEKGESGQPGTPGPPGGKGPTGDDGPKGNPGPVGFPGDPGPPGEVGPRGQ--DG 1208
Cdd:NF038329  160 EKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQgpDG 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1209 AKGDRGEDGEQGEAGSPGPTGENGPPGPPGKRGPAGTRGPEGRQGEKGSKGDSGALGPPGKTGPVGPQGQPGKPGTEGLR 1288
Cdd:NF038329  240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD 319

                         170
                  ....*....|
gi 688598960 1289 GLPGTVGEQG 1298
Cdd:NF038329  320 GQPGKDGLPG 329
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1045-1349 4.99e-11

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 66.85  E-value: 4.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1045 DGETGPRGQQGQFGAKGDEGTRGFPGPPGPIGLQGLPGPGGEKGETGDVGPLGPPGPPgprgpagpngadgpqgppgglg 1124
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------------- 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1125 npgpiGEKGEPGESGPPGVGGEPGKLGPRGERGEKGESGQPGTPGPPGGKGPTGDDGPKGnpgpvgfpgdpgppgeVGPR 1204
Cdd:NF038329  174 -----GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG----------------PAGD 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1205 GQDGAKGDRGEDGEQGEAGSpgptgengppgppgkrgpagtRGPEGRQGEKGSKGDSGALGPPGKTGPVGPQGQPGKPGT 1284
Cdd:NF038329  233 GQQGPDGDPGPTGEDGPQGP---------------------DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688598960 1285 EGLRGLPGTVGEQGSPGAAgpkgppgplgppglaglrGDPGAKGEKGHPGMLGLIGPAGEQGEKG 1349
Cdd:NF038329  292 NGKDGLPGKDGKDGQNGKD------------------GLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1285-1406 2.44e-10

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: 64.93  E-value: 2.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1285 EGLRGLPGTVGEQGspgaagpkgPPGPLGPPGLAGLRGDPGAKGEKGHPGMLGLIGPAGEQGEKGDRGMPGPQGSTGPKG 1364
Cdd:NF038329  116 DGEKGEPGPAGPAG---------PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 688598960 1365 ETGISGGTGPLGPAGPAGMPGPRGVKGAKGASGGAGPKGEKG 1406
Cdd:NF038329  187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG 228
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
333-647 4.16e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 61.20  E-value: 4.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  333 SGPQGqPGSVGDPGERGPTGKAGLPGADGVPGPPGTSvmlpfRFGQSAGEKGPVASAqeaqaqailsqarlalkGPSGPM 412
Cdd:COG5164     1 TGLYG-PGKTGPSDPGGVTTPAGSQGSTKPAQNQGST-----RPAGNTGGTRPAQNQ-----------------GSTTPA 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  413 GFTGRPGPlgtPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDRGFDGLPGLPGDKGY 492
Cdd:COG5164    58 GNTGGTRP---AGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGST 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  493 RGQPGGMGPPGPHGEDGERGDDGDVGPRGLPGEPGPRGLLGPKgpsglpgppgvrGNDGPHGPkgnlgpqgepgppgqqG 572
Cdd:COG5164   135 TPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPP------------DDGGSTTP----------------P 186

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688598960  573 APGTQGMPGPQGATGPPGEKGPTGKPGlpGMPGADGPPGHPGKEGPGGTKGNQGPNGPQGSIGYPGPRGLKGAQG 647
Cdd:COG5164   187 NKGETGTDIPTGGTPRQGPDGPVKKDD--KNGKGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTA 259
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 755-1015 3.13e-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: 57.99  E-value: 3.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  755 GPRGQRGPTGPRGQRGPRGATGKSGAKGGSGSDGPPGPPGERGLTGPQGANGFPGPKGPpgppgkdglpghPGQRGEVGF 834
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP------------AGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  835 QgkvgppgppgvvgphgpsGETGQMGERGHPGPPGPPGEQGLSGSSGKEGTKGDPGPPGGPGKDGppglRGFPGERGLPG 914
Cdd:NF038329  185 K------------------GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPG 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  915 TPGSGGLKGNEGPAGPPGPAGSSGERGGAGTAGPVGPPGRPGPQGPPGTSGEKGVPGEKGPVGPAGRDGIQGPVGLPGPA 994
Cdd:NF038329  243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                         250       260
                  ....*....|....*....|.
gi 688598960  995 GPPGISGEDGDKGEVGEPGQK 1015
Cdd:NF038329  323 GKDGLPGKDGKDGQPGKPAPK 343
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 575-630 5.24e-08

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: 50.96  E-value: 5.24e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 688598960   575 GTQGMPGPQGATGPPGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKGNQGPNGP 630
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 968-1282 1.69e-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: 52.60  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  968 GVPGEKGPVGPAGRDGIQgpvglpgpagppgisGEDGDKGEVGEPGQKGAKGSKGEHGPPGppgpmgpvgqpgAAGADGE 1047
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQ---------------GPRGDRGETGPAGPAGPPGPQGERGEKG------------PAGPQGE 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1048 TGPRGQQGQFGAKGDEGTRGFPGPPGPIGLQGLPGPGGEKGEtgdvgplgppgppgprGPAGPNGADGPQGPPGGLGNPG 1127
Cdd:NF038329  170 AGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP----------------AGPDGEAGPAGEDGPAGPAGDG 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1128 PIGEKGEPGESGPPGVGGEPGKLGPRGERGEKGESGQPGTPGPPGGKGPTGDDGPKGnpgpvgfpgdpgppgevgprgQD 1207
Cdd:NF038329  234 QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG---------------------QN 292

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688598960 1208 GAKGDRGEDGEQGEAGspgptgengPPgppgkrgpagtrgpegrqGEKGSKGDSGALGPPGKTGPVGPQGQPGKP 1282
Cdd:NF038329  293 GKDGLPGKDGKDGQNG---------KD------------------GLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 63-214 4.18e-06

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 48.18  E-value: 4.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960   63 AYRITKKAQISAPTKQLFSGRFPENFSIMTLVKakaglQAFLLSIYNEQGVQQLGLEL--GRsPIFLYEDqhrkpAPEDY 140
Cdd:cd00110     1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSP-----NGLLLYAGSQNGGDFLALELedGR-LVLRYDL-----GSGSL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  141 PLFKGVNLADGKWHRIAISVQKKNITLILDCKNRITKTLPRSnNPVLDTKGITVFGARLLDEEV--------FQGEIQQL 212
Cdd:cd00110    70 VLSSKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGG-SALLNLDGPLYLGGLPEDLKSpglpvspgFVGCIRDL 148


                  ..
gi 688598960  213 LI 214
Cdd:cd00110   149 KV 150
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 416-471 7.78e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.79  E-value: 7.78e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 688598960   416 GRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGE 471
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 1494-1533 6.67e-05

fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.


Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 41.78  E-value: 6.67e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 688598960 1494 TCQDLHLSQPDLKDGEYWIDPNQGCARDSFKVYCNFTAGG 1533
Cdd:NF040941    1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTTDG 40
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 142-214 2.76e-04

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 42.41  E-value: 2.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960   142 LFKGVNLADGKWHRIAISVQKKNITLILDCKNRITKTLPrSNNPVLDTKGITVFGARLLDEEV--------FQGEIQQLL 213
Cdd:pfam02210   44 LSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP-GESLLLNLNGPLYLGGLPPLLLLpalpvragFVGCIRDVR 122


                   .
gi 688598960   214 I 214
Cdd:pfam02210  123 V 123
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1343-1388 2.01e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 2.01e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 688598960  1343 GEQGEKGDRGMPGPQGSTGPKGETGISGGTGPLGPAGPAGMPGPRG 1388
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1463-1693 4.56e-123

Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 460199  Cd Length: 233  Bit Score: 385.16  E-value: 4.56e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  1463 GMEEIFGSLNSLRQEIESMRFPLGTKESPGRTCQDLHLSQPDLKDGEYWIDPNQGCARDSFKVYCNFTAgGETCLYPSKA 1542
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  1543 VENvKMNSWIKEKPGSLFSQFAKGNK-FSY-VDSVGEAVGVVQLGFLRLLSVQARQNLTYHCQRSVAWTDQTTdGGYKRA 1620
Cdd:pfam01410   80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQAT-GNLKKA 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688598960  1621 LRLQGANDEEISYE--TSPYIKALIDGCSYRKGL-DRTVLEVNTPQVEQLPLLDIRISDFGEDNQKFGFEVGPVCF 1693
Cdd:pfam01410  158 LLLQGSNDEEIRAEgnSRFTYTVLEDGCTKRTGQwGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1464-1694 2.62e-98

Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 197483  Cd Length: 232  Bit Score: 315.95  E-value: 2.62e-98
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960   1464 MEEIFGSLNSLRQEIESMRFPLGTKESPGRTCQDLHLSQPDLKDGEYWIDPNQGCARDSFKVYCNFTAgGETCLYPSKAV 1543
Cdd:smart00038    1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFET-GETCVSPSPSS 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960   1544 ENVKmNSWIKEKPGSLFSQFAK-GNKFSYVDSVGEAVGVVQLGFLRLLSVQARQNLTYHCQRSVAWTDQTTdGGYKRALR 1622
Cdd:smart00038   80 IPRK-TWYSGKSKHVWFGETMNgGFKFSYGDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEAT-GNLKKALR 157

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688598960   1623 LQGANDEEISYE--TSPYIKALIDGCSYRKG-LDRTVLEVNTPQVEQLPLLDIRISDFGEDNQKFGFEVGPVCFL 1694
Cdd:smart00038  158 LRGSNDVELSAEgnSKFTYEVLEDGCQKRTGkWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 29-218 5.10e-53

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


Pssm-ID: 214560  Cd Length: 184  Bit Score: 184.10  E-value: 5.10e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960     29 PVDVLRVLQLPSLPEGVQKVPGFCTsrlsgtPDHAYRITKKAQISAPTKQLFSGRFPENFSIMTLVKAKAGLQAFLLSIY 108
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEP------GSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960    109 NEQGVQQLGLEL-GRSPIFLYEDQhRKPAPEDYPLFKGVNLADGKWHRIAISVQKKNITLILDCKNRITKTLPRSNNPVL 187
Cdd:smart00210   75 DAQNVRQFGLEVdGRANTLLLRYQ-GVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQPPI 153

                           170       180       190
                    ....*....|....*....|....*....|.
gi 688598960    188 DTKGITVFGARLLDEEVFQGEIQQLLIASNP 218
Cdd:smart00210  154 DTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 508-766 3.03e-36

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: 143.89  E-value: 3.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  508 DGERGDDGDVGPRGLPGEPGPRGllgpkgpsglpgppgVRGNDGPHGPKGNlgpqgepgppgqqgapgtQGMPGPQGATG 587
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRG---------------DRGETGPAGPAGP------------------PGPQGERGEKG 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  588 PPGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKGNQGPNGPQGSIGYPGPRGLKGAQGIRGLKGH--KGEKGEDGFPG 665
Cdd:NF038329  163 PAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPG 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  666 IKGDFGVKGERGEVGVPGPRGEDGPEGPKGRVGPPGEIGPLGLLGEKGKLGVPGLPGYPGRQGIKGSLGFPGFPGTNGEK 745
Cdd:NF038329  243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                         250       260
                  ....*....|....*....|.
gi 688598960  746 GTRGLIGKPGPRGQRGPTGPR 766
Cdd:NF038329  323 GKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 429-694 5.16e-32

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: 131.18  E-value: 5.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  429 FKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDRGFDGLPGLPGDKGYRGQPGGMGPPGPHGED 508
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  509 GERGDDGDVGPRGLPGEPGPRGLlgpkgpsglpgppgvRGNDGPHGPKGnlgpqgepgppgqqgaPGTQGMPGPQGATGP 588
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGE---------------AGPAGEDGPAG----------------PAGDGQQGPDGDPGP 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  589 PGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKGNQGPNGPQGSIGYPGPRGLKGAQGIRGLKGHKGEKGEDGFPGIKG 668
Cdd:NF038329  244 TGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                         250       260
                  ....*....|....*....|....*.
gi 688598960  669 DFGVKGERGEVGVPGPRGEDGPEGPK 694
Cdd:NF038329  324 KDGLPGKDGKDGQPGKPAPKTPEVPQ 349
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 405-631 6.36e-27

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 116.16  E-value: 6.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  405 LKGPSGPMGFTGRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDRGFDGLP 484
Cdd:NF038329  133 EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPA 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  485 GLPGDKGYRGQPGGMGPPGPHG-----EDGERGDDGDVGPRGLPGEPGPRGllgpkgPSGLPGPPGVRGNDGPHGPKGnl 559
Cdd:NF038329  213 GPDGEAGPAGEDGPAGPAGDGQqgpdgDPGPTGEDGPQGPDGPAGKDGPRG------DRGEAGPDGPDGKDGERGPVG-- 284

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688598960  560 gpqgepgppgqqgAPGTQGMPGPQGATGPPGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKGNQGPNGPQ 631
Cdd:NF038329  285 -------------PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 334-531 5.38e-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: 94.97  E-value: 5.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  334 GPQGQPGSVGDPGERGPTGKAGLPGADGVPGPPGtsvmlpfrfgqSAGEKGPvasaqeaqaqailsQARLALKGPSGPMG 413
Cdd:NF038329  153 GPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG-----------PAGEKGP--------------QGPRGETGPAGEQG 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  414 FTGRPGPLGTPGSPGFKGERGDPGA--QGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDRGFDGLPGLPGDKG 491
Cdd:NF038329  208 PAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 688598960  492 YRGQPGGMGPPGPHGEDGERGDDGDVGPRGLPGEPGPRGL 531
Cdd:NF038329  288 KDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1133-1388 2.34e-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: 93.05  E-value: 2.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1133 GEPGESGPPGVGGEPGKLGPRGERGEKGESGQPGTPGPPGGKGPTGDDGPKGnpgpvgfpgDPGPPGEVGPRGQDGAKGD 1212
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------EAGPQGPAGKDGEAGAKGP 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1213 RGEDGEQGEAGSPGPTGENGPPGPPGKRGPAGTRGPEGRQGEKGsKGDSGALGPPGKTGPVGPQGQPGKPGTEGLRGlpg 1292
Cdd:NF038329  188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG--- 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1293 tvgeqgspgaagpkgppgplgppglagLRGDPGAKGEKGHPGMLGLIGPAGEQGEKGDRGMPGPQGSTGPKGETGISGGT 1372
Cdd:NF038329  264 ---------------------------DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKD 316

                         250
                  ....*....|....*.
gi 688598960 1373 GPLGPAGPAGMPGPRG 1388
Cdd:NF038329  317 GKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1256-1406 7.69e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 82.26  E-value: 7.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1256 GSKGDSGALGPPGKTGPVGPQGQPGKPGTEGLRGLPGTVGEQGSPGAAGPKGPPGPLGPPGLAGLRGDPGAKGEKGHPGM 1335
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1336 LGLIGPAGEQGEKG------------DRGMPGPQGS--TGPKGETGISGGTGPLGPAGPAGMPGPRGVKGAKGASGGAGP 1401
Cdd:NF038329  197 RGETGPAGEQGPAGpagpdgeagpagEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276


                  ....*
gi 688598960 1402 KGEKG 1406
Cdd:NF038329  277 DGERG 281
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 707-923 9.07e-14

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 75.71  E-value: 9.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  707 GLLGEKGKLGVPGLPGYPGRQGIKGSLGFPGFPGTNGEKGTRGLIGKPGPRGQRGPTGPRGQRGPRGATGKSGAKGGSGS 786
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  787 DGPPGPPGERGLTGPQGANGFPGPKGPPGPPGKDGLpghpGQRGEVGFQGKVGPPGPPGVVGPHGPSGETGQMGERGHPG 866
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 688598960  867 PPGPPGEQGLSGSSGKEGTKGDPGPPGGPGKDGPPGLRGFPGERGLPGTPGSGGLKG 923
Cdd:NF038329  273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
548-773 1.75e-11

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 68.52  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  548 GNDGPHGPKGNLGPQGEPGPPGQQGAPGTQGMPGPQGATGPPGEKGPTGKPGLPGmpgADGPPGHPGKEGPGGTKGNQGP 627
Cdd:COG5164    25 GSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQG---GTTPAQNQGGTRPAGNTGGTTP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  628 NGPQGSIGYPGPRGLKGAQGIRGLKGHK------------GEKGEDGFPGIKGDFGVKGERGEVGVPGPRGEDGPEGPKG 695
Cdd:COG5164   102 AGDGGATGPPDDGGATGPPDDGGSTTPPsggsttppgdggSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGG 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688598960  696 RVGPPgeigplgllgEKGKLGVPGLPGYPGRQGIKGSLGFPGFPGTNGEKGTRGliGKPGPRGQRGPTGPRGQRGPRG 773
Cdd:COG5164   182 STTPP----------NKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGPKDQRPKTNPIERRGPER 247
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1131-1298 3.84e-11

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 67.24  E-value: 3.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1131 EKGEPGESGPPGVGGEPGKLGPRGERGEKGESGQPGTPGPPGGKGPTGDDGPKGNPGPVGFPGDPGPPGEVGPRGQ--DG 1208
Cdd:NF038329  160 EKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQgpDG 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1209 AKGDRGEDGEQGEAGSPGPTGENGPPGPPGKRGPAGTRGPEGRQGEKGSKGDSGALGPPGKTGPVGPQGQPGKPGTEGLR 1288
Cdd:NF038329  240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD 319

                         170
                  ....*....|
gi 688598960 1289 GLPGTVGEQG 1298
Cdd:NF038329  320 GQPGKDGLPG 329
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1045-1349 4.99e-11

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 66.85  E-value: 4.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1045 DGETGPRGQQGQFGAKGDEGTRGFPGPPGPIGLQGLPGPGGEKGETGDVGPLGPPGPPgprgpagpngadgpqgppgglg 1124
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------------- 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1125 npgpiGEKGEPGESGPPGVGGEPGKLGPRGERGEKGESGQPGTPGPPGGKGPTGDDGPKGnpgpvgfpgdpgppgeVGPR 1204
Cdd:NF038329  174 -----GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG----------------PAGD 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1205 GQDGAKGDRGEDGEQGEAGSpgptgengppgppgkrgpagtRGPEGRQGEKGSKGDSGALGPPGKTGPVGPQGQPGKPGT 1284
Cdd:NF038329  233 GQQGPDGDPGPTGEDGPQGP---------------------DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688598960 1285 EGLRGLPGTVGEQGSPGAAgpkgppgplgppglaglrGDPGAKGEKGHPGMLGLIGPAGEQGEKG 1349
Cdd:NF038329  292 NGKDGLPGKDGKDGQNGKD------------------GLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1285-1406 2.44e-10

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: 64.93  E-value: 2.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1285 EGLRGLPGTVGEQGspgaagpkgPPGPLGPPGLAGLRGDPGAKGEKGHPGMLGLIGPAGEQGEKGDRGMPGPQGSTGPKG 1364
Cdd:NF038329  116 DGEKGEPGPAGPAG---------PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 688598960 1365 ETGISGGTGPLGPAGPAGMPGPRGVKGAKGASGGAGPKGEKG 1406
Cdd:NF038329  187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG 228
LamG smart00282
Laminin G domain;
88-214 1.82e-09

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 57.35  E-value: 1.82e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960     88 FSIMTLVKakaglQAFLLSIYNEQGVQQLGLEL--GRsPIFLYEDQHRKPAPEdyplFKGVNLADGKWHRIAISVQKKNI 165
Cdd:smart00282    4 FSFRTTSP-----NGLLLYAGSKGGGDYLALELrdGR-LVLRYDLGSGPARLT----SDPTPLNDGQWHRVAVERNGRSV 73

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 688598960    166 TLILDCKNRITKTLPRSnNPVLDTKGITVFGA--------RLLDEEVFQGEIQQLLI 214
Cdd:smart00282   74 TLSVDGGNRVSGESPGG-LTILNLDGPLYLGGlpedlklpPLPVTPGFRGCIRNLKV 129
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
333-647 4.16e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 61.20  E-value: 4.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  333 SGPQGqPGSVGDPGERGPTGKAGLPGADGVPGPPGTSvmlpfRFGQSAGEKGPVASAqeaqaqailsqarlalkGPSGPM 412
Cdd:COG5164     1 TGLYG-PGKTGPSDPGGVTTPAGSQGSTKPAQNQGST-----RPAGNTGGTRPAQNQ-----------------GSTTPA 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  413 GFTGRPGPlgtPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDRGFDGLPGLPGDKGY 492
Cdd:COG5164    58 GNTGGTRP---AGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGST 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  493 RGQPGGMGPPGPHGEDGERGDDGDVGPRGLPGEPGPRGLLGPKgpsglpgppgvrGNDGPHGPkgnlgpqgepgppgqqG 572
Cdd:COG5164   135 TPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPP------------DDGGSTTP----------------P 186

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688598960  573 APGTQGMPGPQGATGPPGEKGPTGKPGlpGMPGADGPPGHPGKEGPGGTKGNQGPNGPQGSIGYPGPRGLKGAQG 647
Cdd:COG5164   187 NKGETGTDIPTGGTPRQGPDGPVKKDD--KNGKGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTA 259
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 755-1015 3.13e-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: 57.99  E-value: 3.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  755 GPRGQRGPTGPRGQRGPRGATGKSGAKGGSGSDGPPGPPGERGLTGPQGANGFPGPKGPpgppgkdglpghPGQRGEVGF 834
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP------------AGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  835 QgkvgppgppgvvgphgpsGETGQMGERGHPGPPGPPGEQGLSGSSGKEGTKGDPGPPGGPGKDGppglRGFPGERGLPG 914
Cdd:NF038329  185 K------------------GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPG 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  915 TPGSGGLKGNEGPAGPPGPAGSSGERGGAGTAGPVGPPGRPGPQGPPGTSGEKGVPGEKGPVGPAGRDGIQGPVGLPGPA 994
Cdd:NF038329  243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                         250       260
                  ....*....|....*....|.
gi 688598960  995 GPPGISGEDGDKGEVGEPGQK 1015
Cdd:NF038329  323 GKDGLPGKDGKDGQPGKPAPK 343
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 575-630 5.24e-08

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: 50.96  E-value: 5.24e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 688598960   575 GTQGMPGPQGATGPPGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKGNQGPNGP 630
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 968-1282 1.69e-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: 52.60  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  968 GVPGEKGPVGPAGRDGIQgpvglpgpagppgisGEDGDKGEVGEPGQKGAKGSKGEHGPPGppgpmgpvgqpgAAGADGE 1047
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQ---------------GPRGDRGETGPAGPAGPPGPQGERGEKG------------PAGPQGE 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1048 TGPRGQQGQFGAKGDEGTRGFPGPPGPIGLQGLPGPGGEKGEtgdvgplgppgppgprGPAGPNGADGPQGPPGGLGNPG 1127
Cdd:NF038329  170 AGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP----------------AGPDGEAGPAGEDGPAGPAGDG 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960 1128 PIGEKGEPGESGPPGVGGEPGKLGPRGERGEKGESGQPGTPGPPGGKGPTGDDGPKGnpgpvgfpgdpgppgevgprgQD 1207
Cdd:NF038329  234 QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG---------------------QN 292

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688598960 1208 GAKGDRGEDGEQGEAGspgptgengPPgppgkrgpagtrgpegrqGEKGSKGDSGALGPPGKTGPVGPQGQPGKP 1282
Cdd:NF038329  293 GKDGLPGKDGKDGQNG---------KD------------------GLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 584-640 1.75e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.72  E-value: 1.75e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 688598960   584 GATGPPGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKGNQGPNGPQGSIGYPGPR 640
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 63-214 4.18e-06

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 48.18  E-value: 4.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960   63 AYRITKKAQISAPTKQLFSGRFPENFSIMTLVKakaglQAFLLSIYNEQGVQQLGLEL--GRsPIFLYEDqhrkpAPEDY 140
Cdd:cd00110     1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSP-----NGLLLYAGSQNGGDFLALELedGR-LVLRYDL-----GSGSL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960  141 PLFKGVNLADGKWHRIAISVQKKNITLILDCKNRITKTLPRSnNPVLDTKGITVFGARLLDEEV--------FQGEIQQL 212
Cdd:cd00110    70 VLSSKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGG-SALLNLDGPLYLGGLPEDLKSpglpvspgFVGCIRDL 148


                  ..
gi 688598960  213 LI 214
Cdd:cd00110   149 KV 150
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 416-471 7.78e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.79  E-value: 7.78e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 688598960   416 GRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGE 471
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 573-623 9.65e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.41  E-value: 9.65e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 688598960   573 APGTQGMPGPQGATGPPGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKG 623
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 422-478 1.40e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.02  E-value: 1.40e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 688598960   422 GTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDR 478
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 407-458 1.62e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.02  E-value: 1.62e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 688598960   407 GPSGPMGFTGRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRG 458
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 410-466 1.72e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 1.72e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 688598960   410 GPMGFTGRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGAR 466
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 407-462 2.43e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 2.43e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 688598960   407 GPSGPMGFTGRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGA 462
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 413-469 3.20e-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: 3.20e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 688598960   413 GFTGRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMP 469
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 593-650 5.77e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 5.77e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 688598960   593 GPTGKPGLPGMPGADGPPGHPGKEGPggtKGNQGPNGPQGSIGYPGPRGLKGAQGIRG 650
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGP---PGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 1494-1533 6.67e-05

fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.


Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 41.78  E-value: 6.67e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 688598960 1494 TCQDLHLSQPDLKDGEYWIDPNQGCARDSFKVYCNFTAGG 1533
Cdd:NF040941    1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTTDG 40
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 629-685 1.50e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 1.50e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 688598960   629 GPQGSIGYPGPRGLKGAQGIRGLKGHKGEKGEDGFPGIKGDFGVKGERGEVGVPGPR 685
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 602-657 1.84e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 1.84e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 688598960   602 GMPGADGPPGHPGKEGPGGTKGNQGPNGPQGSIGYPGPRGLKGAQGIRGLKGHKGE 657
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 428-484 2.75e-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: 2.75e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 688598960   428 GFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDRGFDGLP 484
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 142-214 2.76e-04

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 42.41  E-value: 2.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598960   142 LFKGVNLADGKWHRIAISVQKKNITLILDCKNRITKTLPrSNNPVLDTKGITVFGARLLDEEV--------FQGEIQQLL 213
Cdd:pfam02210   44 LSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP-GESLLLNLNGPLYLGGLPPLLLLpalpvragFVGCIRDVR 122


                   .
gi 688598960   214 I 214
Cdd:pfam02210  123 V 123
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 425-479 3.77e-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: 3.77e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 688598960   425 GSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDRG 479
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 406-455 4.46e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 4.46e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 688598960   406 KGPSGPMGFTGRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAG 455
Cdd:pfam01391    6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 656-711 5.75e-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: 5.75e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 688598960   656 GEKGEDGFPGIKGDFGVKGERGEVGVPGPRGEDGPEGPKGRVGPPGEIGPLGLLGE 711
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 677-731 1.19e-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: 1.19e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 688598960   677 GEVGVPGPRGEDGPEGPKGRVGPPGEIGPLGLLGEKGKLGVPGLPGYPGRQGIKG 731
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 635-702 1.63e-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: 1.63e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688598960   635 GYPGPRGLKGAQGIRGLKGHKGEKGEdgfpgikgdfgvKGERGEVGVPGPRGEDGPEGPKGRVGPPGE 702
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGP------------PGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1343-1388 2.01e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 2.01e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 688598960  1343 GEQGEKGDRGMPGPQGSTGPKGETGISGGTGPLGPAGPAGMPGPRG 1388
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 671-725 2.11e-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: 2.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 688598960   671 GVKGERGEVGVPGPRGEDGPEGPKGRVGPPGEIGPLGLLGEKGKLGVPGLPGYPG 725
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 571-618 2.15e-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: 2.15e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 688598960   571 QGAPGTQGMPGPQGATGPPGEKGPTGKPGLPGMPGADGPPGHPGKEGP 618
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Laminin_G_1 pfam00054
Laminin G domain;
142-191 2.48e-03

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 39.99  E-value: 2.48e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 688598960   142 LFKGVNLADGKWHRIAISVQKKNITLILDCKNRITKTLPRSNNPVLDTKG 191
Cdd:pfam00054   44 VRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGESPLGATTDLDVDG 93
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 692-746 2.65e-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: 2.65e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 688598960   692 GPKGRVGPPGEIGPLGLLGEKGKLGVPGLPGYPGRQGIKGSLGFPGFPGTNGEKG 746
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 680-734 3.32e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.47  E-value: 3.32e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 688598960   680 GVPGPRGEDGPEGPKGRVGPPGEIGPLGLLGEKGKLGVPGLPGYPGRQGIKGSLG 734
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 713-769 3.59e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 3.59e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 688598960   713 GKLGVPGLPGYPGRQGIKGSLGFPGFPGTNGEKGTRGLIGKPGPRGQRGPTGPRGQR 769
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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