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Conserved domains on  [gi|1036212653|ref|NP_001315194|]
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collagen alpha-2(XI) chain isoform 2 precursor [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 ...
 1571-1801 1.00e-122

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: 1.00e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1571 GMEEIFGSLNSLRQEIESMRFPLGTKESPGRTCQDLHLSQPDLKDGEYWIDPNQGCARDSFKVYCNFTAgGETCLYPSKA 1650
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1651 VENvKMNSWIKEKPGSLFSQFAKGNK-FSY-VDSVGEAVGVVQLGFLRLLSVQARQNLTYHCQRSVAWTDQTTdGGYKRA 1728
Cdd:pfam01410   80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQAT-GNLKKA 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1036212653 1729 LRLQGANDEEISYE--TSPYIKALIDGCSYRKGL-DRTVLEVNTPQVEQLPLLDIRISDFGEDNQKFGFEVGPVCF 1801
Cdd:pfam01410  158 LLLQGSNDEEIRAEgnSRFTYTVLEDGCTKRTGQwGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 29-218 1.71e-53

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


:

Pssm-ID: 214560  Cd Length: 184  Bit Score: 185.64  E-value: 1.71e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653    29 PVDVLRVLQLPSLPEGVQKVPGFCTsrlsgtPDHAYRITKKAQISAPTKQLFSGRFPENFSIMTLVKAKAGLQAFLLSIY 108
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEP------GSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653   109 NEQGVQQLGLEL-GRSPIFLYEDQhRKPAPEDYPLFKGVNLADGKWHRIAISVQKKNITLILDCKNRITKTLPRSNNPVL 187
Cdd:smart00210   75 DAQNVRQFGLEVdGRANTLLLRYQ-GVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQPPI 153

                           170       180       190
                    ....*....|....*....|....*....|.
gi 1036212653   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 ...
 616-874 1.87e-37

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: 147.74  E-value: 1.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  616 DGERGDDGDVGPRGLPGEPGPRGllgpkgpsglpgppgVRGNDGPHGPKGNlgpqgepgppgqqgapgtQGMPGPQGATG 695
Cdd:NF038329   116 DGEKGEPGPAGPAGPAGEQGPRG---------------DRGETGPAGPAGP------------------PGPQGERGEKG 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  696 PPGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKGNQGPNGPQGSIGYPGPRGLKGAQGIRGLKGH--KGEKGEDGFPG 773
Cdd:NF038329   163 PAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPG 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  774 IKGDFGVKGERGEVGVPGPRGEDGPEGPKGRVGPPGEIGPLGLLGEKGKLGVPGLPGYPGRQGIKGSLGFPGFPGTNGEK 853
Cdd:NF038329   243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                          250       260
                   ....*....|....*....|.
gi 1036212653  854 GTRGLIGKPGPRGQRGPTGPR 874
Cdd:NF038329   323 GKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 442-726 9.06e-23

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 103.45  E-value: 9.06e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  442 GPQGQPGSVGDPGERGPTGKAGLPGADGVPGPPGtsvmlpfrfgqSAGEKGPvasaqeaqaqailsqarlalKGPSGPMG 521
Cdd:NF038329   123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG-----------ERGEKGP--------------------AGPQGEAG 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  522 FTGRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGiKGDRGFDGLPGLPGDKGYR 601
Cdd:NF038329   172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  602 GQPGGMGPPGPHGEDGERGDDGDVGPRGLPGEPGPRGLLGPKGPSglpgppgvrGNDGPHGPKGNlgpqgepgppgqqga 681
Cdd:NF038329   251 GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKD---------GLPGKDGKDGQ--------------- 306

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1036212653  682 pgtqgmPGPQGATGPPGEKGPTGKPGLPGMPGADGPPGHPGKEGP 726
Cdd:NF038329   307 ------NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1241-1496 5.21e-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: 5.21e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1241 GEPGESGPPGVGGEPGKLGPRGERGEKGESGQPGTPGPPGGKGPTGDDGPKGnpgpvgfpgDPGPPGEVGPRGQDGAKGD 1320
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------EAGPQGPAGKDGEAGAKGP 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1321 RGEDGEQGEAGSPGPTGENGPPGPPGKRGPAGTRGPEGRQGEKGsKGDSGALGPPGKTGPVGPQGQPGKPGTEGLRGlpg 1400
Cdd:NF038329   188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG--- 263

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1401 tvgeqgspgaagpkgppgplgppglagLRGDPGAKGEKGHPGMLGLIGPAGEQGEKGDRGMPGPQGSTGPKGETGISGGT 1480
Cdd:NF038329   264 ---------------------------DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKD 316

                          250
                   ....*....|....*.
gi 1036212653 1481 GPLGPAGPAGMPGPRG 1496
Cdd:NF038329   317 GKDGQPGKDGLPGKDG 332
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 782-1031 3.76e-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: 76.87  E-value: 3.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  782 GERGEVGVPGPRGEDGPEGPKGRVGPPGEIGPLGLLGEKGKlgvpglpgypgrqgikgslgfpgfpgtngekgtRGLIGK 861
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE---------------------------------RGEKGP 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  862 PGPRGQRGPTGPRGQRGPRGATGKSGAKGGSGSDGPPGPPGERGLTGPQGANGFPGPKGPPGPPGKDGLpghpGQRGEVG 941
Cdd:NF038329   164 AGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDG 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  942 FQGKVGPPGPPGVVGPHGPSGETGQMGERGHPGPPGPPGEQGLSGSSGKEGTKGDPGPPGGPGKDGPPGLRGFPGERGLP 1021
Cdd:NF038329   240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD 319

                          250
                   ....*....|
gi 1036212653 1022 GTPGSGGLKG 1031
Cdd:NF038329   320 GQPGKDGLPG 329
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1571-1801 1.00e-122

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: 1.00e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1571 GMEEIFGSLNSLRQEIESMRFPLGTKESPGRTCQDLHLSQPDLKDGEYWIDPNQGCARDSFKVYCNFTAgGETCLYPSKA 1650
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1651 VENvKMNSWIKEKPGSLFSQFAKGNK-FSY-VDSVGEAVGVVQLGFLRLLSVQARQNLTYHCQRSVAWTDQTTdGGYKRA 1728
Cdd:pfam01410   80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQAT-GNLKKA 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1036212653 1729 LRLQGANDEEISYE--TSPYIKALIDGCSYRKGL-DRTVLEVNTPQVEQLPLLDIRISDFGEDNQKFGFEVGPVCF 1801
Cdd:pfam01410  158 LLLQGSNDEEIRAEgnSRFTYTVLEDGCTKRTGQwGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1572-1802 5.36e-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: 315.18  E-value: 5.36e-98
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  1572 MEEIFGSLNSLRQEIESMRFPLGTKESPGRTCQDLHLSQPDLKDGEYWIDPNQGCARDSFKVYCNFTAgGETCLYPSKAV 1651
Cdd:smart00038    1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFET-GETCVSPSPSS 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  1652 ENVKmNSWIKEKPGSLFSQFAK-GNKFSYVDSVGEAVGVVQLGFLRLLSVQARQNLTYHCQRSVAWTDQTTdGGYKRALR 1730
Cdd:smart00038   80 IPRK-TWYSGKSKHVWFGETMNgGFKFSYGDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEAT-GNLKKALR 157

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1036212653  1731 LQGANDEEISYE--TSPYIKALIDGCSYRKG-LDRTVLEVNTPQVEQLPLLDIRISDFGEDNQKFGFEVGPVCFL 1802
Cdd:smart00038  158 LRGSNDVELSAEgnSKFTYEVLEDGCQKRTGkWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 29-218 1.71e-53

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 185.64  E-value: 1.71e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653    29 PVDVLRVLQLPSLPEGVQKVPGFCTsrlsgtPDHAYRITKKAQISAPTKQLFSGRFPENFSIMTLVKAKAGLQAFLLSIY 108
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEP------GSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653   109 NEQGVQQLGLEL-GRSPIFLYEDQhRKPAPEDYPLFKGVNLADGKWHRIAISVQKKNITLILDCKNRITKTLPRSNNPVL 187
Cdd:smart00210   75 DAQNVRQFGLEVdGRANTLLLRYQ-GVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQPPI 153

                           170       180       190
                    ....*....|....*....|....*....|.
gi 1036212653   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 ...
 616-874 1.87e-37

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: 147.74  E-value: 1.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  616 DGERGDDGDVGPRGLPGEPGPRGllgpkgpsglpgppgVRGNDGPHGPKGNlgpqgepgppgqqgapgtQGMPGPQGATG 695
Cdd:NF038329   116 DGEKGEPGPAGPAGPAGEQGPRG---------------DRGETGPAGPAGP------------------PGPQGERGEKG 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  696 PPGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKGNQGPNGPQGSIGYPGPRGLKGAQGIRGLKGH--KGEKGEDGFPG 773
Cdd:NF038329   163 PAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPG 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  774 IKGDFGVKGERGEVGVPGPRGEDGPEGPKGRVGPPGEIGPLGLLGEKGKLGVPGLPGYPGRQGIKGSLGFPGFPGTNGEK 853
Cdd:NF038329   243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                          250       260
                   ....*....|....*....|.
gi 1036212653  854 GTRGLIGKPGPRGQRGPTGPR 874
Cdd:NF038329   323 GKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 537-802 4.71e-33

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: 134.65  E-value: 4.71e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  537 FKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDRGFDGLPGLPGDKGYRGQPGGMGPPGPHGED 616
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  617 GERGDDGDVGPRGLPGEPGPRGLlgpkgpsglpgppgvRGNDGPHGPKGnlgpqgepgppgqqgaPGTQGMPGPQGATGP 696
Cdd:NF038329   195 GPRGETGPAGEQGPAGPAGPDGE---------------AGPAGEDGPAG----------------PAGDGQQGPDGDPGP 243

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  697 PGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKGNQGPNGPQGSIGYPGPRGLKGAQGIRGLKGHKGEKGEDGFPGIKG 776
Cdd:NF038329   244 TGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                          250       260
                   ....*....|....*....|....*.
gi 1036212653  777 DFGVKGERGEVGVPGPRGEDGPEGPK 802
Cdd:NF038329   324 KDGLPGKDGKDGQPGKPAPKTPEVPQ 349
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 513-739 7.69e-28

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: 118.85  E-value: 7.69e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  513 LKGPSGPMGFTGRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDRGFDGLP 592
Cdd:NF038329   133 EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPA 212

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  593 GLPGDKGYRGQPGGMGPPGPHG-----EDGERGDDGDVGPRGLPGEPGPRGllgpkgPSGLPGPPGVRGNDGPHGPKGnl 667
Cdd:NF038329   213 GPDGEAGPAGEDGPAGPAGDGQqgpdgDPGPTGEDGPQGPDGPAGKDGPRG------DRGEAGPDGPDGKDGERGPVG-- 284

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1036212653  668 gpqgepgppgqqgAPGTQGMPGPQGATGPPGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKGNQGPNGPQ 739
Cdd:NF038329   285 -------------PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 442-726 9.06e-23

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 103.45  E-value: 9.06e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  442 GPQGQPGSVGDPGERGPTGKAGLPGADGVPGPPGtsvmlpfrfgqSAGEKGPvasaqeaqaqailsqarlalKGPSGPMG 521
Cdd:NF038329   123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG-----------ERGEKGP--------------------AGPQGEAG 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  522 FTGRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGiKGDRGFDGLPGLPGDKGYR 601
Cdd:NF038329   172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  602 GQPGGMGPPGPHGEDGERGDDGDVGPRGLPGEPGPRGLLGPKGPSglpgppgvrGNDGPHGPKGNlgpqgepgppgqqga 681
Cdd:NF038329   251 GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKD---------GLPGKDGKDGQ--------------- 306

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1036212653  682 pgtqgmPGPQGATGPPGEKGPTGKPGLPGMPGADGPPGHPGKEGP 726
Cdd:NF038329   307 ------NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1241-1496 5.21e-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: 5.21e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1241 GEPGESGPPGVGGEPGKLGPRGERGEKGESGQPGTPGPPGGKGPTGDDGPKGnpgpvgfpgDPGPPGEVGPRGQDGAKGD 1320
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------EAGPQGPAGKDGEAGAKGP 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1321 RGEDGEQGEAGSPGPTGENGPPGPPGKRGPAGTRGPEGRQGEKGsKGDSGALGPPGKTGPVGPQGQPGKPGTEGLRGlpg 1400
Cdd:NF038329   188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG--- 263

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1401 tvgeqgspgaagpkgppgplgppglagLRGDPGAKGEKGHPGMLGLIGPAGEQGEKGDRGMPGPQGSTGPKGETGISGGT 1480
Cdd:NF038329   264 ---------------------------DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKD 316

                          250
                   ....*....|....*.
gi 1036212653 1481 GPLGPAGPAGMPGPRG 1496
Cdd:NF038329   317 GKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1364-1514 2.07e-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: 84.19  E-value: 2.07e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1364 GSKGDSGALGPPGKTGPVGPQGQPGKPGTEGLRGLPGTVGEQGSPGAAGPKGPPGPLGPPGLAGLRGDPGAKGEKGHPGM 1443
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1444 LGLIGPAGEQGEKG------------DRGMPGPQGS--TGPKGETGISGGTGPLGPAGPAGMPGPRGVKGAKGASGGAGP 1509
Cdd:NF038329   197 RGETGPAGEQGPAGpagpdgeagpagEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276


                   ....*
gi 1036212653 1510 KGEKG 1514
Cdd:NF038329   277 DGERG 281
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 782-1031 3.76e-14

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 76.87  E-value: 3.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  782 GERGEVGVPGPRGEDGPEGPKGRVGPPGEIGPLGLLGEKGKlgvpglpgypgrqgikgslgfpgfpgtngekgtRGLIGK 861
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE---------------------------------RGEKGP 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  862 PGPRGQRGPTGPRGQRGPRGATGKSGAKGGSGSDGPPGPPGERGLTGPQGANGFPGPKGPPGPPGKDGLpghpGQRGEVG 941
Cdd:NF038329   164 AGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDG 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  942 FQGKVGPPGPPGVVGPHGPSGETGQMGERGHPGPPGPPGEQGLSGSSGKEGTKGDPGPPGGPGKDGPPGLRGFPGERGLP 1021
Cdd:NF038329   240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD 319

                          250
                   ....*....|
gi 1036212653 1022 GTPGSGGLKG 1031
Cdd:NF038329   320 GQPGKDGLPG 329
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
656-881 1.14e-11

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 69.29  E-value: 1.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  656 GNDGPHGPKGNLGPQGEPGPPGQQGAPGTQGMPGPQGATGPPGEKGPTGKPGLPGmpgADGPPGHPGKEGPGGTKGNQGP 735
Cdd:COG5164     25 GSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQG---GTTPAQNQGGTRPAGNTGGTTP 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  736 NGPQGSIGYPGPRGLKGAQGIRGLKGHK------------GEKGEDGFPGIKGDFGVKGERGEVGVPGPRGEDGPEGPKG 803
Cdd:COG5164    102 AGDGGATGPPDDGGATGPPDDGGSTTPPsggsttppgdggSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGG 181

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1036212653  804 RVGPPgeigplgllgEKGKLGVPGLPGYPGRQGIKGSLGFPGFPGTNGEKGTRGliGKPGPRGQRGPTGPRGQRGPRG 881
Cdd:COG5164    182 STTPP----------NKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGPKDQRPKTNPIERRGPER 247
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1153-1457 1.16e-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: 69.16  E-value: 1.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1153 DGETGPRGQQGQFGAKGDEGTRGFPGPPGPIGLQGLPGPGGEKGETGDVGPLGPPGPPgprgpagpngadgpqgppgglg 1232
Cdd:NF038329   116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------------- 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1233 npgpiGEKGEPGESGPPGVGGEPGKLGPRGERGEKGESGQPGTPGPPGGKGPTGDDGPKGnpgpvgfpgdpgppgeVGPR 1312
Cdd:NF038329   174 -----GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG----------------PAGD 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1313 GQDGAKGDRGEDGEQGEAGSpgptgengppgppgkrgpagtRGPEGRQGEKGSKGDSGALGPPGKTGPVGPQGQPGKPGT 1392
Cdd:NF038329   233 GQQGPDGDPGPTGEDGPQGP---------------------DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1036212653 1393 EGLRGLPGTVGEQGSPGAAgpkgppgplgppglaglrGDPGAKGEKGHPGMLGLIGPAGEQGEKG 1457
Cdd:NF038329   292 NGKDGLPGKDGKDGQNGKD------------------GLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1393-1514 9.22e-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: 66.08  E-value: 9.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1393 EGLRGLPGTVGEQGspgaagpkgPPGPLGPPGLAGLRGDPGAKGEKGHPGMLGLIGPAGEQGEKGDRGMPGPQGSTGPKG 1472
Cdd:NF038329   116 DGEKGEPGPAGPAG---------PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1036212653 1473 ETGISGGTGPLGPAGPAGMPGPRGVKGAKGASGGAGPKGEKG 1514
Cdd:NF038329   187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG 228
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
441-755 2.64e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 61.97  E-value: 2.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  441 SGPQGqPGSVGDPGERGPTGKAGLPGADGVPGPPGTSvmlpfRFGQSAGEKGPVASAqeaqaqailsqarlalkGPSGPM 520
Cdd:COG5164      1 TGLYG-PGKTGPSDPGGVTTPAGSQGSTKPAQNQGST-----RPAGNTGGTRPAQNQ-----------------GSTTPA 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  521 GFTGRPGPlgtPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDRGFDGLPGLPGDKGY 600
Cdd:COG5164     58 GNTGGTRP---AGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGST 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  601 RGQPGGMGPPGPHGEDGERGDDGDVGPRGLPGEPGPRGllgpkgpsglpgPPGVRGNDGPHGPkgnlgpqgepgppgqqG 680
Cdd:COG5164    135 TPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGG------------STTPPDDGGSTTP----------------P 186

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1036212653  681 APGTQGMPGPQGATGPPGEKGPTGKPGlpGMPGADGPPGHPGKEGPGGTKGNQGPNGPQGSIGYPGPRGLKGAQG 755
Cdd:COG5164    187 NKGETGTDIPTGGTPRQGPDGPVKKDD--KNGKGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTA 259
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 683-738 6.22e-09

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: 53.65  E-value: 6.22e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1036212653  683 GTQGMPGPQGATGPPGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKGNQGPNGP 738
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 863-1123 1.58e-08

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 59.15  E-value: 1.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  863 GPRGQRGPTGPRGQRGPRGATGKSGAKGGSGSDGPPGPPGERGLTGPQGANGFPGPKGPpgppgkdglpghPGQRGEVGF 942
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP------------AGKDGEAGA 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  943 QgkvgppgppgvvgphgpsGETGQMGERGHPGPPGPPGEQGLSGSSGKEGTKGDPGPPGGPGKDGppglRGFPGERGLPG 1022
Cdd:NF038329   185 K------------------GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPG 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1023 TPGSGGLKGNEGPAGPPGPAGSSGERGGAGTAGPVGPPGRPGPQGPPGTSGEKGVPGEKGPVGPAGRDGIQGPVGLPGPA 1102
Cdd:NF038329   243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                          250       260
                   ....*....|....*....|.
gi 1036212653 1103 GPPGISGEDGDKGEVGEPGQK 1123
Cdd:NF038329   323 GKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1076-1390 4.62e-07

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: 54.53  E-value: 4.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1076 GVPGEKGPVGPAGRDGIQgpvglpgpagppgisGEDGDKGEVGEPGQKGAKGSKGEHGPPGppgpmgpvgqpgAAGADGE 1155
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQ---------------GPRGDRGETGPAGPAGPPGPQGERGEKG------------PAGPQGE 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1156 TGPRGQQGQFGAKGDEGTRGFPGPPGPIGLQGLPGPGGEKGEtgdvgplgppgppgprGPAGPNGADGPQGPPGGLGNPG 1235
Cdd:NF038329   170 AGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP----------------AGPDGEAGPAGEDGPAGPAGDG 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1236 PIGEKGEPGESGPPGVGGEPGKLGPRGERGEKGESGQPGTPGPPGGKGPTGDDGPKGnpgpvgfpgdpgppgevgprgQD 1315
Cdd:NF038329   234 QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG---------------------QN 292

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1036212653 1316 GAKGDRGEDGEQGEAGspgptgengPPgppgkrgpagtrgpegrqGEKGSKGDSGALGPPGKTGPVGPQGQPGKP 1390
Cdd:NF038329   293 GKDGLPGKDGKDGQNG---------KD------------------GLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 524-579 1.14e-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: 47.10  E-value: 1.14e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1036212653  524 GRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGE 579
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 63-214 3.51e-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: 48.57  E-value: 3.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653   63 AYRITKKAQISAPTKQLFSGRFPENFSIMTLVKakaglQAFLLSIYNEQGVQQLGLEL--GRsPIFLYEDqhrkpAPEDY 140
Cdd:cd00110      1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSP-----NGLLLYAGSQNGGDFLALELedGR-LVLRYDL-----GSGSL 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  141 PLFKGVNLADGKWHRIAISVQKKNITLILDCKNRITKTLPRSnNPVLDTKGITVFGARLLDEEV--------FQGEIQQL 212
Cdd:cd00110     70 VLSSKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGG-SALLNLDGPLYLGGLPEDLKSpglpvspgFVGCIRDL 148


                   ..
gi 1036212653  213 LI 214
Cdd:cd00110    149 KV 150
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 1602-1641 9.82e-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: 41.39  E-value: 9.82e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1036212653 1602 TCQDLHLSQPDLKDGEYWIDPNQGCARDSFKVYCNFTAGG 1641
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 2.52e-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: 42.79  E-value: 2.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  142 LFKGVNLADGKWHRIAISVQKKNITLILDCKNRITKTLPrSNNPVLDTKGITVFGARLLDEEV--------FQGEIQQLL 213
Cdd:pfam02210   44 LSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP-GESLLLNLNGPLYLGGLPPLLLLpalpvragFVGCIRDVR 122


                   .
gi 1036212653  214 I 214
Cdd:pfam02210  123 V 123
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1451-1496 4.26e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 4.26e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1036212653 1451 GEQGEKGDRGMPGPQGSTGPKGETGISGGTGPLGPAGPAGMPGPRG 1496
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 ...
 1571-1801 1.00e-122

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: 1.00e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1571 GMEEIFGSLNSLRQEIESMRFPLGTKESPGRTCQDLHLSQPDLKDGEYWIDPNQGCARDSFKVYCNFTAgGETCLYPSKA 1650
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1651 VENvKMNSWIKEKPGSLFSQFAKGNK-FSY-VDSVGEAVGVVQLGFLRLLSVQARQNLTYHCQRSVAWTDQTTdGGYKRA 1728
Cdd:pfam01410   80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQAT-GNLKKA 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1036212653 1729 LRLQGANDEEISYE--TSPYIKALIDGCSYRKGL-DRTVLEVNTPQVEQLPLLDIRISDFGEDNQKFGFEVGPVCF 1801
Cdd:pfam01410  158 LLLQGSNDEEIRAEgnSRFTYTVLEDGCTKRTGQwGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1572-1802 5.36e-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: 315.18  E-value: 5.36e-98
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  1572 MEEIFGSLNSLRQEIESMRFPLGTKESPGRTCQDLHLSQPDLKDGEYWIDPNQGCARDSFKVYCNFTAgGETCLYPSKAV 1651
Cdd:smart00038    1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFET-GETCVSPSPSS 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  1652 ENVKmNSWIKEKPGSLFSQFAK-GNKFSYVDSVGEAVGVVQLGFLRLLSVQARQNLTYHCQRSVAWTDQTTdGGYKRALR 1730
Cdd:smart00038   80 IPRK-TWYSGKSKHVWFGETMNgGFKFSYGDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEAT-GNLKKALR 157

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1036212653  1731 LQGANDEEISYE--TSPYIKALIDGCSYRKG-LDRTVLEVNTPQVEQLPLLDIRISDFGEDNQKFGFEVGPVCFL 1802
Cdd:smart00038  158 LRGSNDVELSAEgnSKFTYEVLEDGCQKRTGkWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 29-218 1.71e-53

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 185.64  E-value: 1.71e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653    29 PVDVLRVLQLPSLPEGVQKVPGFCTsrlsgtPDHAYRITKKAQISAPTKQLFSGRFPENFSIMTLVKAKAGLQAFLLSIY 108
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEP------GSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653   109 NEQGVQQLGLEL-GRSPIFLYEDQhRKPAPEDYPLFKGVNLADGKWHRIAISVQKKNITLILDCKNRITKTLPRSNNPVL 187
Cdd:smart00210   75 DAQNVRQFGLEVdGRANTLLLRYQ-GVDGKQHTVSFRNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQPPI 153

                           170       180       190
                    ....*....|....*....|....*....|.
gi 1036212653   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 ...
 616-874 1.87e-37

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: 147.74  E-value: 1.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  616 DGERGDDGDVGPRGLPGEPGPRGllgpkgpsglpgppgVRGNDGPHGPKGNlgpqgepgppgqqgapgtQGMPGPQGATG 695
Cdd:NF038329   116 DGEKGEPGPAGPAGPAGEQGPRG---------------DRGETGPAGPAGP------------------PGPQGERGEKG 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  696 PPGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKGNQGPNGPQGSIGYPGPRGLKGAQGIRGLKGH--KGEKGEDGFPG 773
Cdd:NF038329   163 PAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPG 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  774 IKGDFGVKGERGEVGVPGPRGEDGPEGPKGRVGPPGEIGPLGLLGEKGKLGVPGLPGYPGRQGIKGSLGFPGFPGTNGEK 853
Cdd:NF038329   243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                          250       260
                   ....*....|....*....|.
gi 1036212653  854 GTRGLIGKPGPRGQRGPTGPR 874
Cdd:NF038329   323 GKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 537-802 4.71e-33

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: 134.65  E-value: 4.71e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  537 FKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDRGFDGLPGLPGDKGYRGQPGGMGPPGPHGED 616
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  617 GERGDDGDVGPRGLPGEPGPRGLlgpkgpsglpgppgvRGNDGPHGPKGnlgpqgepgppgqqgaPGTQGMPGPQGATGP 696
Cdd:NF038329   195 GPRGETGPAGEQGPAGPAGPDGE---------------AGPAGEDGPAG----------------PAGDGQQGPDGDPGP 243

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  697 PGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKGNQGPNGPQGSIGYPGPRGLKGAQGIRGLKGHKGEKGEDGFPGIKG 776
Cdd:NF038329   244 TGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                          250       260
                   ....*....|....*....|....*.
gi 1036212653  777 DFGVKGERGEVGVPGPRGEDGPEGPK 802
Cdd:NF038329   324 KDGLPGKDGKDGQPGKPAPKTPEVPQ 349
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 513-739 7.69e-28

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: 118.85  E-value: 7.69e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  513 LKGPSGPMGFTGRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDRGFDGLP 592
Cdd:NF038329   133 EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPA 212

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  593 GLPGDKGYRGQPGGMGPPGPHG-----EDGERGDDGDVGPRGLPGEPGPRGllgpkgPSGLPGPPGVRGNDGPHGPKGnl 667
Cdd:NF038329   213 GPDGEAGPAGEDGPAGPAGDGQqgpdgDPGPTGEDGPQGPDGPAGKDGPRG------DRGEAGPDGPDGKDGERGPVG-- 284

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1036212653  668 gpqgepgppgqqgAPGTQGMPGPQGATGPPGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKGNQGPNGPQ 739
Cdd:NF038329   285 -------------PAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 442-726 9.06e-23

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 103.45  E-value: 9.06e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  442 GPQGQPGSVGDPGERGPTGKAGLPGADGVPGPPGtsvmlpfrfgqSAGEKGPvasaqeaqaqailsqarlalKGPSGPMG 521
Cdd:NF038329   123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG-----------ERGEKGP--------------------AGPQGEAG 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  522 FTGRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGiKGDRGFDGLPGLPGDKGYR 601
Cdd:NF038329   172 PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  602 GQPGGMGPPGPHGEDGERGDDGDVGPRGLPGEPGPRGLLGPKGPSglpgppgvrGNDGPHGPKGNlgpqgepgppgqqga 681
Cdd:NF038329   251 GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKD---------GLPGKDGKDGQ--------------- 306

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1036212653  682 pgtqgmPGPQGATGPPGEKGPTGKPGLPGMPGADGPPGHPGKEGP 726
Cdd:NF038329   307 ------NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1241-1496 5.21e-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: 5.21e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1241 GEPGESGPPGVGGEPGKLGPRGERGEKGESGQPGTPGPPGGKGPTGDDGPKGnpgpvgfpgDPGPPGEVGPRGQDGAKGD 1320
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------EAGPQGPAGKDGEAGAKGP 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1321 RGEDGEQGEAGSPGPTGENGPPGPPGKRGPAGTRGPEGRQGEKGsKGDSGALGPPGKTGPVGPQGQPGKPGTEGLRGlpg 1400
Cdd:NF038329   188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG--- 263

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1401 tvgeqgspgaagpkgppgplgppglagLRGDPGAKGEKGHPGMLGLIGPAGEQGEKGDRGMPGPQGSTGPKGETGISGGT 1480
Cdd:NF038329   264 ---------------------------DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKD 316

                          250
                   ....*....|....*.
gi 1036212653 1481 GPLGPAGPAGMPGPRG 1496
Cdd:NF038329   317 GKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1364-1514 2.07e-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: 84.19  E-value: 2.07e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1364 GSKGDSGALGPPGKTGPVGPQGQPGKPGTEGLRGLPGTVGEQGSPGAAGPKGPPGPLGPPGLAGLRGDPGAKGEKGHPGM 1443
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1444 LGLIGPAGEQGEKG------------DRGMPGPQGS--TGPKGETGISGGTGPLGPAGPAGMPGPRGVKGAKGASGGAGP 1509
Cdd:NF038329   197 RGETGPAGEQGPAGpagpdgeagpagEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276


                   ....*
gi 1036212653 1510 KGEKG 1514
Cdd:NF038329   277 DGERG 281
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 782-1031 3.76e-14

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 76.87  E-value: 3.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  782 GERGEVGVPGPRGEDGPEGPKGRVGPPGEIGPLGLLGEKGKlgvpglpgypgrqgikgslgfpgfpgtngekgtRGLIGK 861
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGE---------------------------------RGEKGP 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  862 PGPRGQRGPTGPRGQRGPRGATGKSGAKGGSGSDGPPGPPGERGLTGPQGANGFPGPKGPPGPPGKDGLpghpGQRGEVG 941
Cdd:NF038329   164 AGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDG 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  942 FQGKVGPPGPPGVVGPHGPSGETGQMGERGHPGPPGPPGEQGLSGSSGKEGTKGDPGPPGGPGKDGPPGLRGFPGERGLP 1021
Cdd:NF038329   240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD 319

                          250
                   ....*....|
gi 1036212653 1022 GTPGSGGLKG 1031
Cdd:NF038329   320 GQPGKDGLPG 329
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
656-881 1.14e-11

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 69.29  E-value: 1.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  656 GNDGPHGPKGNLGPQGEPGPPGQQGAPGTQGMPGPQGATGPPGEKGPTGKPGLPGmpgADGPPGHPGKEGPGGTKGNQGP 735
Cdd:COG5164     25 GSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQG---GTTPAQNQGGTRPAGNTGGTTP 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  736 NGPQGSIGYPGPRGLKGAQGIRGLKGHK------------GEKGEDGFPGIKGDFGVKGERGEVGVPGPRGEDGPEGPKG 803
Cdd:COG5164    102 AGDGGATGPPDDGGATGPPDDGGSTTPPsggsttppgdggSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGG 181

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1036212653  804 RVGPPgeigplgllgEKGKLGVPGLPGYPGRQGIKGSLGFPGFPGTNGEKGTRGliGKPGPRGQRGPTGPRGQRGPRG 881
Cdd:COG5164    182 STTPP----------NKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGPKDQRPKTNPIERRGPER 247
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1153-1457 1.16e-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: 69.16  E-value: 1.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1153 DGETGPRGQQGQFGAKGDEGTRGFPGPPGPIGLQGLPGPGGEKGETGDVGPLGPPGPPgprgpagpngadgpqgppgglg 1232
Cdd:NF038329   116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------------- 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1233 npgpiGEKGEPGESGPPGVGGEPGKLGPRGERGEKGESGQPGTPGPPGGKGPTGDDGPKGnpgpvgfpgdpgppgeVGPR 1312
Cdd:NF038329   174 -----GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG----------------PAGD 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1313 GQDGAKGDRGEDGEQGEAGSpgptgengppgppgkrgpagtRGPEGRQGEKGSKGDSGALGPPGKTGPVGPQGQPGKPGT 1392
Cdd:NF038329   233 GQQGPDGDPGPTGEDGPQGP---------------------DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ 291

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1036212653 1393 EGLRGLPGTVGEQGSPGAAgpkgppgplgppglaglrGDPGAKGEKGHPGMLGLIGPAGEQGEKG 1457
Cdd:NF038329   292 NGKDGLPGKDGKDGQNGKD------------------GLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1393-1514 9.22e-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: 66.08  E-value: 9.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1393 EGLRGLPGTVGEQGspgaagpkgPPGPLGPPGLAGLRGDPGAKGEKGHPGMLGLIGPAGEQGEKGDRGMPGPQGSTGPKG 1472
Cdd:NF038329   116 DGEKGEPGPAGPAG---------PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1036212653 1473 ETGISGGTGPLGPAGPAGMPGPRGVKGAKGASGGAGPKGEKG 1514
Cdd:NF038329   187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG 228
LamG smart00282
Laminin G domain;
88-214 1.53e-09

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 57.73  E-value: 1.53e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653    88 FSIMTLVKakaglQAFLLSIYNEQGVQQLGLEL--GRsPIFLYEDQHRKPAPEdyplFKGVNLADGKWHRIAISVQKKNI 165
Cdd:smart00282    4 FSFRTTSP-----NGLLLYAGSKGGGDYLALELrdGR-LVLRYDLGSGPARLT----SDPTPLNDGQWHRVAVERNGRSV 73

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1036212653   166 TLILDCKNRITKTLPRSnNPVLDTKGITVFGA--------RLLDEEVFQGEIQQLLI 214
Cdd:smart00282   74 TLSVDGGNRVSGESPGG-LTILNLDGPLYLGGlpedlklpPLPVTPGFRGCIRNLKV 129
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
441-755 2.64e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 61.97  E-value: 2.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  441 SGPQGqPGSVGDPGERGPTGKAGLPGADGVPGPPGTSvmlpfRFGQSAGEKGPVASAqeaqaqailsqarlalkGPSGPM 520
Cdd:COG5164      1 TGLYG-PGKTGPSDPGGVTTPAGSQGSTKPAQNQGST-----RPAGNTGGTRPAQNQ-----------------GSTTPA 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  521 GFTGRPGPlgtPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDRGFDGLPGLPGDKGY 600
Cdd:COG5164     58 GNTGGTRP---AGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGST 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  601 RGQPGGMGPPGPHGEDGERGDDGDVGPRGLPGEPGPRGllgpkgpsglpgPPGVRGNDGPHGPkgnlgpqgepgppgqqG 680
Cdd:COG5164    135 TPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGG------------STTPPDDGGSTTP----------------P 186

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1036212653  681 APGTQGMPGPQGATGPPGEKGPTGKPGlpGMPGADGPPGHPGKEGPGGTKGNQGPNGPQGSIGYPGPRGLKGAQG 755
Cdd:COG5164    187 NKGETGTDIPTGGTPRQGPDGPVKKDD--KNGKGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTA 259
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 683-738 6.22e-09

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: 53.65  E-value: 6.22e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1036212653  683 GTQGMPGPQGATGPPGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKGNQGPNGP 738
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 863-1123 1.58e-08

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 59.15  E-value: 1.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  863 GPRGQRGPTGPRGQRGPRGATGKSGAKGGSGSDGPPGPPGERGLTGPQGANGFPGPKGPpgppgkdglpghPGQRGEVGF 942
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP------------AGKDGEAGA 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  943 QgkvgppgppgvvgphgpsGETGQMGERGHPGPPGPPGEQGLSGSSGKEGTKGDPGPPGGPGKDGppglRGFPGERGLPG 1022
Cdd:NF038329   185 K------------------GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPG 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1023 TPGSGGLKGNEGPAGPPGPAGSSGERGGAGTAGPVGPPGRPGPQGPPGTSGEKGVPGEKGPVGPAGRDGIQGPVGLPGPA 1102
Cdd:NF038329   243 PTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                          250       260
                   ....*....|....*....|.
gi 1036212653 1103 GPPGISGEDGDKGEVGEPGQK 1123
Cdd:NF038329   323 GKDGLPGKDGKDGQPGKPAPK 343
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 692-748 2.52e-07

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: 49.03  E-value: 2.52e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1036212653  692 GATGPPGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKGNQGPNGPQGSIGYPGPR 748
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1076-1390 4.62e-07

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: 54.53  E-value: 4.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1076 GVPGEKGPVGPAGRDGIQgpvglpgpagppgisGEDGDKGEVGEPGQKGAKGSKGEHGPPGppgpmgpvgqpgAAGADGE 1155
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQ---------------GPRGDRGETGPAGPAGPPGPQGERGEKG------------PAGPQGE 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1156 TGPRGQQGQFGAKGDEGTRGFPGPPGPIGLQGLPGPGGEKGEtgdvgplgppgppgprGPAGPNGADGPQGPPGGLGNPG 1235
Cdd:NF038329   170 AGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP----------------AGPDGEAGPAGEDGPAGPAGDG 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653 1236 PIGEKGEPGESGPPGVGGEPGKLGPRGERGEKGESGQPGTPGPPGGKGPTGDDGPKGnpgpvgfpgdpgppgevgprgQD 1315
Cdd:NF038329   234 QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDG---------------------QN 292

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1036212653 1316 GAKGDRGEDGEQGEAGspgptgengPPgppgkrgpagtrgpegrqGEKGSKGDSGALGPPGKTGPVGPQGQPGKP 1390
Cdd:NF038329   293 GKDGLPGKDGKDGQNG---------KD------------------GLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 524-579 1.14e-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: 47.10  E-value: 1.14e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1036212653  524 GRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGE 579
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 681-731 1.58e-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: 1.58e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1036212653  681 APGTQGMPGPQGATGPPGEKGPTGKPGLPGMPGADGPPGHPGKEGPGGTKG 731
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 530-586 2.24e-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: 46.33  E-value: 2.24e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1036212653  530 GTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDR 586
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 515-566 2.65e-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: 45.95  E-value: 2.65e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1036212653  515 GPSGPMGFTGRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRG 566
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 518-574 2.81e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.95  E-value: 2.81e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1036212653  518 GPMGFTGRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGAR 574
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 63-214 3.51e-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: 48.57  E-value: 3.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653   63 AYRITKKAQISAPTKQLFSGRFPENFSIMTLVKakaglQAFLLSIYNEQGVQQLGLEL--GRsPIFLYEDqhrkpAPEDY 140
Cdd:cd00110      1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSP-----NGLLLYAGSQNGGDFLALELedGR-LVLRYDL-----GSGSL 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  141 PLFKGVNLADGKWHRIAISVQKKNITLILDCKNRITKTLPRSnNPVLDTKGITVFGARLLDEEV--------FQGEIQQL 212
Cdd:cd00110     70 VLSSKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGG-SALLNLDGPLYLGGLPEDLKSpglpvspgFVGCIRDL 148


                   ..
gi 1036212653  213 LI 214
Cdd:cd00110    149 KV 150
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 515-570 4.08e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.56  E-value: 4.08e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1036212653  515 GPSGPMGFTGRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGA 570
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 521-577 5.27e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.18  E-value: 5.27e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1036212653  521 GFTGRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMP 577
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 701-758 7.96e-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: 7.96e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1036212653  701 GPTGKPGLPGMPGADGPPGHPGKEGPggtKGNQGPNGPQGSIGYPGPRGLKGAQGIRG 758
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGP---PGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 737-793 2.71e-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: 2.71e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1036212653  737 GPQGSIGYPGPRGLKGAQGIRGLKGHKGEKGEDGFPGIKGDFGVKGERGEVGVPGPR 793
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 710-765 3.27e-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: 3.27e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1036212653  710 GMPGADGPPGHPGKEGPGGTKGNQGPNGPQGSIGYPGPRGLKGAQGIRGLKGHKGE 765
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 536-592 5.29e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 5.29e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1036212653  536 GFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDRGFDGLP 592
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 533-587 7.40e-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: 42.10  E-value: 7.40e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1036212653  533 GSPGFKGERGDPGAQGPRGPQGVSGPPGKAGRRGRAGADGARGMPGESGIKGDRG 587
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 514-563 8.91e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 8.91e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1036212653  514 KGPSGPMGFTGRPGPLGTPGSPGFKGERGDPGAQGPRGPQGVSGPPGKAG 563
Cdd:pfam01391    6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 1602-1641 9.82e-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: 41.39  E-value: 9.82e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1036212653 1602 TCQDLHLSQPDLKDGEYWIDPNQGCARDSFKVYCNFTAGG 1641
Cdd:NF040941     1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTTDG 40
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 764-819 1.12e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 1.12e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1036212653  764 GEKGEDGFPGIKGDFGVKGERGEVGVPGPRGEDGPEGPKGRVGPPGEIGPLGLLGE 819
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 743-810 2.25e-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: 2.25e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1036212653  743 GYPGPRGLKGAQGIRGLKGHKGEKGEdgfpgikgdfgvKGERGEVGVPGPRGEDGPEGPKGRVGPPGE 810
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGP------------PGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 785-839 2.34e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 2.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1036212653  785 GEVGVPGPRGEDGPEGPKGRVGPPGEIGPLGLLGEKGKLGVPGLPGYPGRQGIKG 839
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 142-214 2.52e-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: 42.79  E-value: 2.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036212653  142 LFKGVNLADGKWHRIAISVQKKNITLILDCKNRITKTLPrSNNPVLDTKGITVFGARLLDEEV--------FQGEIQQLL 213
Cdd:pfam02210   44 LSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP-GESLLLNLNGPLYLGGLPPLLLLpalpvragFVGCIRDVR 122


                   .
gi 1036212653  214 I 214
Cdd:pfam02210  123 V 123
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1451-1496 4.26e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 4.26e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1036212653 1451 GEQGEKGDRGMPGPQGSTGPKGETGISGGTGPLGPAGPAGMPGPRG 1496
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 779-833 4.47e-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: 4.47e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1036212653  779 GVKGERGEVGVPGPRGEDGPEGPKGRVGPPGEIGPLGLLGEKGKLGVPGLPGYPG 833
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 679-726 4.74e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 4.74e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1036212653  679 QGAPGTQGMPGPQGATGPPGEKGPTGKPGLPGMPGADGPPGHPGKEGP 726
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 800-854 5.13e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 5.13e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1036212653  800 GPKGRVGPPGEIGPLGLLGEKGKLGVPGLPGYPGRQGIKGSLGFPGFPGTNGEKG 854
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 788-842 7.03e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 7.03e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1036212653  788 GVPGPRGEDGPEGPKGRVGPPGEIGPLGLLGEKGKLGVPGLPGYPGRQGIKGSLG 842
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 821-877 7.83e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 7.83e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1036212653  821 GKLGVPGLPGYPGRQGIKGSLGFPGFPGTNGEKGTRGLIGKPGPRGQRGPTGPRGQR 877
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Laminin_G_1 pfam00054
Laminin G domain;
142-191 2.25e-03

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 39.99  E-value: 2.25e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1036212653  142 LFKGVNLADGKWHRIAISVQKKNITLILDCKNRITKTLPRSNNPVLDTKG 191
Cdd:pfam00054   44 VRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGESPLGATTDLDVDG 93
 
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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