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Conserved domains on  [gi|959092927|ref|NP_001304317|]
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collagen alpha-3(V) chain isoform 2 precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COLFI super family cl02436
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1506-1736 1.57e-109

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.


The actual alignment was detected with superfamily member pfam01410:

Pssm-ID: 470578  Cd Length: 233  Bit Score: 347.79  E-value: 1.57e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  1506 GLEEVMASLNSLSLELQQLQRPLGTAESPGLMCRELHRDHPHLPDGEYWIDPNQGCARDAFKVFCNFTAgGETCLYPDKK 1585
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  1586 FETvKLASWSREKPGGWYSTFRRGKK-FSY-VDADGSPVNVVQLTFLKLLSAAAHQRFTYICQNSVAWLDEAAGDHRHSI 1663
Cdd:pfam01410   80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 959092927  1664 RFQGTNWEELSFNQTTAATIKVSHDGCRVRKGQ-AKTLFEFSSS-VGFLPLWDVAASDFGQTNQKFGFELGSICF 1736
Cdd:pfam01410  159 LLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQwGKTVIEYRTQkVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 901-1161 3.73e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 134.65  E-value: 3.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  901 ELGFQGLTGPPGPAGVLGPQGKVGDvgplgergppgppgppgeqglpgiEGREGAKGELGPLGSVGkegppgprgfpgpq 980
Cdd:NF038329  112 QLKGDGEKGEPGPAGPAGPAGEQGP------------------------RGDRGETGPAGPAGPPG-------------- 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  981 gAPGDPGPIGLKGDKGPPGPVGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGTPGPTGKDGIPGPPGL 1060
Cdd:NF038329  154 -PQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1061 --QGPSGAAGPSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGIRGPAGHSGLPGADGAQGRRGPP---GLFGQKGDDGV 1135
Cdd:NF038329  233 gqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPgkdGKDGQNGKDGL 312

                         250       260
                  ....*....|....*....|....*.
gi 959092927 1136 RGFVGVIGPPGLQGLPGPPGEKGEVG 1161
Cdd:NF038329  313 PGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 678-922 1.01e-31

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: 130.41  E-value: 1.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  678 GPPGHPGHEGPTGEKGAQGPPGSAGPRGYPGLRGVKGTSGNRGLQGEKGERGEDGFPGFKGDEGPKgdrgnpgppgprGE 757
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK------------GP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  758 DGPEGQKGPGGLPGDEGPPGAAGEKGKLGVPGLPGYPGRpGPKGSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRG 837
Cdd:NF038329  194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  838 DRGQPGATGQPGPKGDVGQNGSPGPPGEKGlpglqgppgfpgpkgppgPQGKDGISGHPGQRGELGFQGLTGPPGPAGVL 917
Cdd:NF038329  273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDG------------------KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD 334


                  ....*
gi 959092927  918 GPQGK 922
Cdd:NF038329  335 GQPGK 339
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 31-210 2.47e-28

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.


The actual alignment was detected with superfamily member smart00210:

Pssm-ID: 473984  Cd Length: 184  Bit Score: 113.22  E-value: 2.47e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927     31 PVDVLEAWGVHRDQAGVAEGPGFCPlripqGDRAFRVGKSSLLSVPTWQLFPDGhFPENFSVLLTLRAQPANQSVLLSIY 110
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEP-----GSPAYRLGDPALVPQPTRDLFPSG-LPEDFSLLTTFRQTPKSRGVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927    111 DEKGVRQLG------------LALGPALGLLGDSFRPLPkqvnIMDGRWHRVAVSISGNKVTLVVDCEP------QPPtf 172
Cdd:smart00210   75 DAQNVRQFGlevdgrantlllRYQGVDGKQHTVSFRNLP----LADGQWHKLALSVSGSSATLYVDCNEidsrplDRP-- 148

                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 959092927    173 gqGPRFISTAGLTVMGTQDTREESFEGDIQELLLIPDP 210
Cdd:smart00210  149 --GQPPIDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 476-743 4.26e-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: 104.60  E-value: 4.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  476 KGPPGPVGLTGRPGPVGLPGYPGLKGELGEVGPQGPRglqgppgppgregktgraGADGARGLPGDTGPKGDRGFDGLPG 555
Cdd:NF038329  134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA------------------GPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  556 LPGEKGQRGDFGRVGQPGPPGEDGVKGLQGPPGPTGQaGEPGPRGLIGPRGLPGPLGRPGVTGSDGAPGAKGNvgppgep 635
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE------- 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  636 gppgqqgnhgsqgiPGPQGPIGTPGEKgppgnpgipgvpgseGPPGHPGHEgptGEKGAQGPPGSAGPRGYPGLRGVKGT 715
Cdd:NF038329  268 --------------AGPDGPDGKDGER---------------GPVGPAGKD---GQNGKDGLPGKDGKDGQNGKDGLPGK 315

                         250       260
                  ....*....|....*....|....*...
gi 959092927  716 SGNRGLQGEKGERGEDGFPGFKGDEGPK 743
Cdd:NF038329  316 DGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1227-1466 9.86e-22

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 100.36  E-value: 9.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1227 GEKGDSGPSGAAGPPGKKGPPGEDGSKGNMGPTGLPGDLGPPGDPGVPGIDGIPGEKGNAGDiggpgppgasgepgaRGL 1306
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK---------------DGE 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1307 PGKRGSPGRMGPEGREGEKGAKGDAGPDGPPGRTGPIGARGPPGRIGPDGlPGIPGPVGEPGLLGPPGLIGPPGPLGPPG 1386
Cdd:NF038329  182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1387 LPGLKGDAGPKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPGLQGDPGLPGPVGSLGHPGPPGVVGPLGQKGSKGSP 1466
Cdd:NF038329  261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1506-1736 1.57e-109

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: 347.79  E-value: 1.57e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  1506 GLEEVMASLNSLSLELQQLQRPLGTAESPGLMCRELHRDHPHLPDGEYWIDPNQGCARDAFKVFCNFTAgGETCLYPDKK 1585
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  1586 FETvKLASWSREKPGGWYSTFRRGKK-FSY-VDADGSPVNVVQLTFLKLLSAAAHQRFTYICQNSVAWLDEAAGDHRHSI 1663
Cdd:pfam01410   80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 959092927  1664 RFQGTNWEELSFNQTTAATIKVSHDGCRVRKGQ-AKTLFEFSSS-VGFLPLWDVAASDFGQTNQKFGFELGSICF 1736
Cdd:pfam01410  159 LLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQwGKTVIEYRTQkVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1507-1737 7.71e-86

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: 280.12  E-value: 7.71e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927   1507 LEEVMASLNSLSLELQQLQRPLGTAESPGLMCRELHRDHPHLPDGEYWIDPNQGCARDAFKVFCNFTAGgETCLYPDKKf 1586
Cdd:smart00038    1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETG-ETCVSPSPS- 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927   1587 eTVKLASWSREKPGG-WYS-TFRRGKKFSYVDADGSPVNVVQLTFLKLLSAAAHQRFTYICQNSVAWLDEAAGDHRHSIR 1664
Cdd:smart00038   79 -SIPRKTWYSGKSKHvWFGeTMNGGFKFSYGDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALR 157

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 959092927   1665 FQGTNWEELSFNQTTAATIKVSHDGCRVRKGQ-AKTLFEFSSS-VGFLPLWDVAASDFGQTNQKFGFELGSICFS 1737
Cdd:smart00038  158 LRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKwGKTVIEYRTKkTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 901-1161 3.73e-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: 3.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  901 ELGFQGLTGPPGPAGVLGPQGKVGDvgplgergppgppgppgeqglpgiEGREGAKGELGPLGSVGkegppgprgfpgpq 980
Cdd:NF038329  112 QLKGDGEKGEPGPAGPAGPAGEQGP------------------------RGDRGETGPAGPAGPPG-------------- 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  981 gAPGDPGPIGLKGDKGPPGPVGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGTPGPTGKDGIPGPPGL 1060
Cdd:NF038329  154 -PQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1061 --QGPSGAAGPSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGIRGPAGHSGLPGADGAQGRRGPP---GLFGQKGDDGV 1135
Cdd:NF038329  233 gqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPgkdGKDGQNGKDGL 312

                         250       260
                  ....*....|....*....|....*.
gi 959092927 1136 RGFVGVIGPPGLQGLPGPPGEKGEVG 1161
Cdd:NF038329  313 PGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 678-922 1.01e-31

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: 130.41  E-value: 1.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  678 GPPGHPGHEGPTGEKGAQGPPGSAGPRGYPGLRGVKGTSGNRGLQGEKGERGEDGFPGFKGDEGPKgdrgnpgppgprGE 757
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK------------GP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  758 DGPEGQKGPGGLPGDEGPPGAAGEKGKLGVPGLPGYPGRpGPKGSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRG 837
Cdd:NF038329  194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  838 DRGQPGATGQPGPKGDVGQNGSPGPPGEKGlpglqgppgfpgpkgppgPQGKDGISGHPGQRGELGFQGLTGPPGPAGVL 917
Cdd:NF038329  273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDG------------------KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD 334


                  ....*
gi 959092927  918 GPQGK 922
Cdd:NF038329  335 GQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 953-1164 5.36e-31

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: 128.48  E-value: 5.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  953 EGAKGELGPLGSVGKEGPPGPRGFPGPQGAPGDPGPIGLKGDKGPPGPVGANGSPGERGPVGPSGGIGLPGQSGGQGPIG 1032
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1033 PAGEKGSPGERGTPGPTGKDGIPGPPGLQGPSGAAGpSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGIRGPAGHSGLP 1112
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 959092927 1113 GADGAQGRRGPPGLFGQKGDDGVRGFVGVIGPPGLQGLPGPPGEKGEVGDVG 1164
Cdd:NF038329  275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 499-800 1.09e-29

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 124.63  E-value: 1.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  499 LKGELGEVGPQGPRglqgppgppgreGKTGRAGADGARGLPGDTGPKGDRGFDGLPGLPGEKGQRGDFGRVGQPGPPGED 578
Cdd:NF038329  115 GDGEKGEPGPAGPA------------GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  579 GVKGLQGPPGPTGQAGEPGPRGLIGPRGLPGPLGRPGVTGSDGAPGAKGNvgppgepgppgqqgnhGSQGIPGPQGPIGT 658
Cdd:NF038329  183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------------GQQGPDGDPGPTGE 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  659 PGEKGPpgnpgipgvpgsEGPPGHPGHEGPTGEKGAQGPPGSAGPRGYPGLRGVKGTSGNRGLQGEKGERGEDGFPgfkg 738
Cdd:NF038329  247 DGPQGP------------DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD---- 310

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 959092927  739 degpkgdrgnpgppgprgedgpegqkgpgGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPK 800
Cdd:NF038329  311 -----------------------------GLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 643-867 6.16e-29

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 122.32  E-value: 6.16e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  643 NHGSQGIPGPQGPIGTPGEKGPPGNPGIPGVPGSEGPPGHPGHEGPTGEKGAQGPPGSAGPRGYPGLRGVKGTSGNRGLQ 722
Cdd:NF038329  112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  723 GEKGERGEDGFPGFKGDEGPKGDRGNPGPPGPRGEDGPEGQkgpgGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGS 802
Cdd:NF038329  192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 959092927  803 IGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGPKGDVGQNGSPGPPGEKG 867
Cdd:NF038329  268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 31-210 2.47e-28

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 113.22  E-value: 2.47e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927     31 PVDVLEAWGVHRDQAGVAEGPGFCPlripqGDRAFRVGKSSLLSVPTWQLFPDGhFPENFSVLLTLRAQPANQSVLLSIY 110
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEP-----GSPAYRLGDPALVPQPTRDLFPSG-LPEDFSLLTTFRQTPKSRGVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927    111 DEKGVRQLG------------LALGPALGLLGDSFRPLPkqvnIMDGRWHRVAVSISGNKVTLVVDCEP------QPPtf 172
Cdd:smart00210   75 DAQNVRQFGlevdgrantlllRYQGVDGKQHTVSFRNLP----LADGQWHKLALSVSGSSATLYVDCNEidsrplDRP-- 148

                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 959092927    173 gqGPRFISTAGLTVMGTQDTREESFEGDIQELLLIPDP 210
Cdd:smart00210  149 --GQPPIDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 884-1157 5.09e-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: 119.62  E-value: 5.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  884 PgpqgkdgisGHPGQRGELGFQGLTGPPGPAGVLGPQGKVGDVgplgergppgppgppgeqglpgieGREGAKGELGPLG 963
Cdd:NF038329  128 A---------GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEK------------------------GPAGPQGEAGPQG 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  964 SvgkegppgprgfpgpqgapgdPGPIGLKGDKGPPGPVGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGEr 1043
Cdd:NF038329  175 P---------------------AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD- 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1044 gtpGPTGKDGIPGPPGLQGPSGAAGPSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGIRGPAGHSGLPGADGAQGRRGP 1123
Cdd:NF038329  233 ---GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK 309

                         250       260       270
                  ....*....|....*....|....*....|....
gi 959092927 1124 PGLFGQKGDDGVRGFVGVIGPPGLQGLPGPPGEK 1157
Cdd:NF038329  310 DGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 816-1076 6.27e-27

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 116.16  E-value: 6.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  816 GKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGPKGDVGQNGSPGPPGEKGlpglqgppgFPGPKGPPGPQGKDGISGH 895
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------EAGPQGPAGKDGEAGAKGP 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  896 PGQRGELGFQGLTGPPGPAGVLGPQGKVGDVGPLGERGPPGPPGPPGeqglpgiEGREGAKGELGPLGSVGKEgppgprg 975
Cdd:NF038329  188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ-------QGPDGDPGPTGEDGPQGPD------- 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  976 fpgpqgapGDPGPIGLKGDKGPPGPVGANGSPGERGPVGPSGGiglPGQSGGQGPIGPAGEKGSPGERGTPGPTGKDGIP 1055
Cdd:NF038329  254 --------GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK---DGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                         250       260
                  ....*....|....*....|.
gi 959092927 1056 GPPGLQGPSGAAGPSGEEGDK 1076
Cdd:NF038329  323 GKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 984-1243 4.87e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 107.30  E-value: 4.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  984 GDPGPIGLKGDKGPPGPVGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGTPGPTGKDGIPGPPGLQGP 1063
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1064 SGAAGPSGEEGDKGEVGMPGHKGSKGD--KGDAGPPGPTGIRGPAGHSGLPGADGAQGRRGPPGLFGQKGDDGVRGFVGV 1141
Cdd:NF038329  206 QGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1142 IGPPGLQGLPGPPGEKGEVGDVGsmgphgapgprgppgpsgsegppglpggvgqpgavgEKGEPGDAGdagppgipgipg 1221
Cdd:NF038329  286 AGKDGQNGKDGLPGKDGKDGQNG------------------------------------KDGLPGKDG------------ 317

                         250       260
                  ....*....|....*....|..
gi 959092927 1222 pkgeigEKGDSGPSGAAGPPGK 1243
Cdd:NF038329  318 ------KDGQPGKDGLPGKDGK 333
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 762-1063 2.40e-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: 105.37  E-value: 2.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  762 GQKGPGGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRGQ 841
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  842 PGATGQPGPKGDVGQNGSPGPPGEKGlpglqgpPGFPGPKGPPgpqgkdgisghpgqrgelGFQGLTGPPGPAGVLGPQG 921
Cdd:NF038329  206 QGPAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDP------------------GPTGEDGPQGPDGPAGKDG 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  922 KVGDvgplgergppgppgppgeqglpgiegregakgelgplgsvgkegppgprgfpgpqgaPGDPGPIGLKGDKGPPGPV 1001
Cdd:NF038329  261 PRGD---------------------------------------------------------RGEAGPDGPDGKDGERGPV 283

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 959092927 1002 GANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGTPGPTGKDGIPGPPGLQGP 1063
Cdd:NF038329  284 GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 476-743 4.26e-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: 104.60  E-value: 4.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  476 KGPPGPVGLTGRPGPVGLPGYPGLKGELGEVGPQGPRglqgppgppgregktgraGADGARGLPGDTGPKGDRGFDGLPG 555
Cdd:NF038329  134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA------------------GPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  556 LPGEKGQRGDFGRVGQPGPPGEDGVKGLQGPPGPTGQaGEPGPRGLIGPRGLPGPLGRPGVTGSDGAPGAKGNvgppgep 635
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE------- 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  636 gppgqqgnhgsqgiPGPQGPIGTPGEKgppgnpgipgvpgseGPPGHPGHEgptGEKGAQGPPGSAGPRGYPGLRGVKGT 715
Cdd:NF038329  268 --------------AGPDGPDGKDGER---------------GPVGPAGKD---GQNGKDGLPGKDGKDGQNGKDGLPGK 315

                         250       260
                  ....*....|....*....|....*...
gi 959092927  716 SGNRGLQGEKGERGEDGFPGFKGDEGPK 743
Cdd:NF038329  316 DGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1227-1466 9.86e-22

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 100.36  E-value: 9.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1227 GEKGDSGPSGAAGPPGKKGPPGEDGSKGNMGPTGLPGDLGPPGDPGVPGIDGIPGEKGNAGDiggpgppgasgepgaRGL 1306
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK---------------DGE 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1307 PGKRGSPGRMGPEGREGEKGAKGDAGPDGPPGRTGPIGARGPPGRIGPDGlPGIPGPVGEPGLLGPPGLIGPPGPLGPPG 1386
Cdd:NF038329  182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1387 LPGLKGDAGPKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPGLQGDPGLPGPVGSLGHPGPPGVVGPLGQKGSKGSP 1466
Cdd:NF038329  261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 690-1015 1.48e-21

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 99.98  E-value: 1.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  690 GEKGAQGPPGSAGPRGYPGLRGVKGTSGNRGLQGEKGERGEDGFPGFKGDEGPKgdrgnpgppgprgedgpegqkGPGGL 769
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA---------------------GPQGP 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  770 PGDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGSIGFPGPLGPLGEKGKRGKAGQPGEegergtpGTRGDRGQPGATGQPG 849
Cdd:NF038329  176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------GQQGPDGDPGPTGEDG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  850 PKGDVGQNgspgppgekglpglqgppgfpgpkgppGPQGKDGISGHPGQRGELGFQGLTGPPGPAGVLGPQGKVGdvgpl 929
Cdd:NF038329  249 PQGPDGPA---------------------------GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG----- 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  930 gergppgppgppgeqglpgIEGREGAKGELGPLGsvgkegppgprgfpgpqgAPGDPGPIGLKGDKGPPGPVGANGSPGE 1009
Cdd:NF038329  297 -------------------LPGKDGKDGQNGKDG------------------LPGKDGKDGQPGKDGLPGKDGKDGQPGK 339


                  ....*.
gi 959092927 1010 RGPVGP 1015
Cdd:NF038329  340 PAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1277-1467 3.32e-21

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 98.82  E-value: 3.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1277 DGIPGEKGNAGDIGGPGPPGASGEPGARGLPGKRGSPGRMGPEGREGEKGAKGDAGPDGPPGRTGPIGARGPPGRIGPDG 1356
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1357 LPGIPGPVGEPGLLGPPGLIGPPGPLGPPGLPGLKGD-----AGPKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPG 1431
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 959092927 1432 LQGDPGLPGPVGSLGHPGPPGVVGPLGQKGSKGSPG 1467
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1068-1363 7.02e-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: 94.59  E-value: 7.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1068 GPSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGIRGPAGHSGLPGADGAQGRRGPPGLFGQKGDDGVRGFVGVIGPPGL 1147
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1148 QGLPGPPGEKGEVgdvgsmgphgapgprgppgpsgsegppGLPGGVGQPGAVGEKGEPGDAGDagppgipgipgpkGEIG 1227
Cdd:NF038329  197 RGETGPAGEQGPA---------------------------GPAGPDGEAGPAGEDGPAGPAGD-------------GQQG 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1228 EKGDSGPSGAAGPPGKKGPPGEDGSKGNMGPTGLPGDlgppgdpgvpgiDGIPGEKGnagdiggpgppgasgepgARGLP 1307
Cdd:NF038329  237 PDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP------------DGKDGERG------------------PVGPA 286

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 959092927 1308 GKRGSPGRMGPEGREGEKGAKGDAGPDGPPGRTGPIGARGPPGRIGPDGLPGIPGP 1363
Cdd:NF038329  287 GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 370-614 4.44e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 92.28  E-value: 4.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  370 AGEKGAKGEPATveqgQQFEGPAGAPGPRGISGPSGPPGPPGFPGDRGLPGPAGLPGIPGIDGARGLPGTvimmpfhfas 449
Cdd:NF038329  125 AGPAGPAGEQGP----RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE---------- 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  450 ssmKGPPvsfqqAQAQAVLQQAQLSMKGPPGPVGLTGRPGPVGLPGYP--------GLKGELGEVGPQGPRglqgppgpp 521
Cdd:NF038329  191 ---KGPQ-----GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqgpdGDPGPTGEDGPQGPD--------- 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  522 greGKTGRAGADGARGLPGDTGPKGDRGFDGLPGLPGEKGQRGDfgrVGQPGPPGEDGVKGLQGPPGPTGQAGEPGPRGL 601
Cdd:NF038329  254 ---GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGK---DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327

                         250
                  ....*....|...
gi 959092927  602 IGPRGLPGPLGRP 614
Cdd:NF038329  328 PGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1115-1451 9.11e-17

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 84.96  E-value: 9.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1115 DGAQGRRGPPGLFGQKGDDGVRGFVGVIGPPGLQGLPGPPGEKGEVGdvgsmgphgapgprgppgpsgsegppglpggvg 1194
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKG--------------------------------- 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1195 qpgAVGEKGEPGDAGDAgppgipgipgpkgeiGEKGdsgpsgaagppgkkgppgEDGSKGNMGPTGLPGDLGPPGDPGVP 1274
Cdd:NF038329  163 ---PAGPQGEAGPQGPA---------------GKDG------------------EAGAKGPAGEKGPQGPRGETGPAGEQ 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1275 GIDGIPGEKGNAGDIGGpgppgasgepgaRGLPGKRGSpGRMGPEGREGEKGAKGDAGPDGPPGRTGPIGARGPPGRIGP 1354
Cdd:NF038329  207 GPAGPAGPDGEAGPAGE------------DGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1355 DGLPGIPGPVgepgllgppgligppgplgppglpglkgdaGPKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPGLQG 1434
Cdd:NF038329  274 DGKDGERGPV------------------------------GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                         330
                  ....*....|....*..
gi 959092927 1435 DPGLPGPVGSLGHPGPP 1451
Cdd:NF038329  324 KDGLPGKDGKDGQPGKP 340
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
951-1161 5.18e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 60.81  E-value: 5.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  951 GREGAKGELGPLGSVGKEGPPGPRGFPGPQGAPGDPGPIGLKGDKGPPGPVGANGSPGERGPVGPS---GGIGLPGQSGG 1027
Cdd:COG5164    10 GPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAqnqGGTTPAQNQGG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1028 QGPIGPAGEKGSPGERGTPGPTGKDGIPGPPGLQGPSGAAGPSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGIRGPAG 1107
Cdd:COG5164    90 TRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPG 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 959092927 1108 HSGLPGADGAQGRRGPP-----GLFGQKGDDGVRGFVGVIGPPGLQGLPGPPGEKGEVG 1161
Cdd:COG5164   170 PGGSTTPPDDGGSTTPPnkgetGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKT 228
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
585-868 1.46e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 59.27  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  585 GPPGPTGQAGEPGPRGLIGPRGLPGPLGRPGVTGSDGAPGakgnvgppgepgppgqqgNHGSQGIPGPQGPIGTPGekgp 664
Cdd:COG5164    10 GPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQ------------------NQGSTTPAGNTGGTRPAG---- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  665 pgnpgipgVPGSEGPPGHPGHEGPTGEKGAQGPPGSAGPRGYPGLRGVKGTSGNRGLQGEKGERGEDGFPGFKGDEGPKG 744
Cdd:COG5164    68 --------NQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGD 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  745 DRGNPGPPGPRGEDGPEGQKGPGGLPGDEGPPGAAGEKGKLGV--PGLPGYPGRPGPKGSIGFPGPLGPLGEKGKRGKAG 822
Cdd:COG5164   140 GGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSttPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGN 219

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 959092927  823 QPGEEGergtpGTRGDRGQPGATGQPGPKGDVGQNGSPGPPGEKGL 868
Cdd:COG5164   220 PPDDRG-----GKTGPKDQRPKTNPIERRGPERPEAAALPAELTAL 260
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 136-206 1.20e-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: 50.11  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  136 LPKQVNIMDGRWHRVAVSISGNKVTLVVDCEP--QPPTFGQGPRFISTAGLTVMGTQDTRE-------ESFEGDIQELLL 206
Cdd:cd00110    71 LSSKTPLNDGQWHSVSVERNGRSVTLSVDGERvvESGSPGGSALLNLDGPLYLGGLPEDLKspglpvsPGFVGCIRDLKV 150
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1005-1059 6.12e-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: 6.12e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 959092927  1005 GSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGTPGPTGKDGIPGPPG 1059
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 807-863 2.37e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 2.37e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 959092927   807 GPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGPKGDVGQNGSPGPP 863
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 555-610 2.91e-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: 43.25  E-value: 2.91e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 959092927   555 GLPGEKGQRGDFGRVGQPGPPGEDGVKGLQGPPGPTGQAGEPGPRGLIGPRGLPGP 610
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 1538-1576 5.30e-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: 42.16  E-value: 5.30e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 959092927 1538 CRELHRDHPHLPDGEYWIDPNQGCARDAFKVFCNFTAGG 1576
Cdd:NF040941    2 CWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTTDG 40
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 996-1162 8.90e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.29  E-value: 8.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  996 GPPGPVGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGTPGPTGKDGIPGPPGLQGPSGAAGPSGEEGD 1075
Cdd:PRK07764  599 GPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAP 678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1076 KGEVGMPGhkgskgdkgDAGPPGPTGIRGPAGHSGLPGADGAQGRRGPPGLFGQKGDDGVRGFVGVIGPPGLQGLPGPPG 1155
Cdd:PRK07764  679 AAPPPAPA---------PAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749


                  ....*..
gi 959092927 1156 EKGEVGD 1162
Cdd:PRK07764  750 DPAGAPA 756
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 134-204 1.59e-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: 43.18  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927   134 RPLPKQVNimDGRWHRVAVSISGNKVTLVVD-CEPQPPTFGQGPRFISTAGLTVMG--------TQDTREESFEGDIQEL 204
Cdd:pfam02210   44 LSSGKNLN--DGQWHSVRVERNGNTLTLSVDgQTVVSSLPPGESLLLNLNGPLYLGglppllllPALPVRAGFVGCIRDV 121
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1407-1456 2.27e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 2.27e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 959092927  1407 GLIGPPGEAGEKGDQGLPGVQGPPGLQGDPGLPGPVGSLGHPGPPGVVGP 1456
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
477-693 2.49e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 42.32  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  477 GPPGPVGLTGRPGPVGL---PGYPGLKGELGEVGPQGPRGLQGPPGPPGREGKTGRAGADGARGLPGDTGPKGDRGFDGL 553
Cdd:COG5164    46 RPAQNQGSTTPAGNTGGtrpAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGS 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  554 PGLPGEKGQRGDFGRVGQPGPPGEDGVKGLQGPPGPTGQAGEPGPRGLIGPRGLPGPlGRPGVTGSDGAPGAKGNVGPPG 633
Cdd:COG5164   126 TTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGS-TTPPNKGETGTDIPTGGTPRQG 204

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  634 EPGPPGQQGNHGSQGIPGPQGpiGTPGEKGPPGNPGIPGVPGSEGPPGHPGHEGPTGEKG 693
Cdd:COG5164   205 PDGPVKKDDKNGKGNPPDDRG--GKTGPKDQRPKTNPIERRGPERPEAAALPAELTALEA 262
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1506-1736 1.57e-109

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: 347.79  E-value: 1.57e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  1506 GLEEVMASLNSLSLELQQLQRPLGTAESPGLMCRELHRDHPHLPDGEYWIDPNQGCARDAFKVFCNFTAgGETCLYPDKK 1585
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  1586 FETvKLASWSREKPGGWYSTFRRGKK-FSY-VDADGSPVNVVQLTFLKLLSAAAHQRFTYICQNSVAWLDEAAGDHRHSI 1663
Cdd:pfam01410   80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 959092927  1664 RFQGTNWEELSFNQTTAATIKVSHDGCRVRKGQ-AKTLFEFSSS-VGFLPLWDVAASDFGQTNQKFGFELGSICF 1736
Cdd:pfam01410  159 LLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQwGKTVIEYRTQkVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1507-1737 7.71e-86

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: 280.12  E-value: 7.71e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927   1507 LEEVMASLNSLSLELQQLQRPLGTAESPGLMCRELHRDHPHLPDGEYWIDPNQGCARDAFKVFCNFTAGgETCLYPDKKf 1586
Cdd:smart00038    1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETG-ETCVSPSPS- 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927   1587 eTVKLASWSREKPGG-WYS-TFRRGKKFSYVDADGSPVNVVQLTFLKLLSAAAHQRFTYICQNSVAWLDEAAGDHRHSIR 1664
Cdd:smart00038   79 -SIPRKTWYSGKSKHvWFGeTMNGGFKFSYGDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALR 157

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 959092927   1665 FQGTNWEELSFNQTTAATIKVSHDGCRVRKGQ-AKTLFEFSSS-VGFLPLWDVAASDFGQTNQKFGFELGSICFS 1737
Cdd:smart00038  158 LRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKwGKTVIEYRTKkTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 901-1161 3.73e-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: 3.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  901 ELGFQGLTGPPGPAGVLGPQGKVGDvgplgergppgppgppgeqglpgiEGREGAKGELGPLGSVGkegppgprgfpgpq 980
Cdd:NF038329  112 QLKGDGEKGEPGPAGPAGPAGEQGP------------------------RGDRGETGPAGPAGPPG-------------- 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  981 gAPGDPGPIGLKGDKGPPGPVGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGTPGPTGKDGIPGPPGL 1060
Cdd:NF038329  154 -PQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1061 --QGPSGAAGPSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGIRGPAGHSGLPGADGAQGRRGPP---GLFGQKGDDGV 1135
Cdd:NF038329  233 gqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPgkdGKDGQNGKDGL 312

                         250       260
                  ....*....|....*....|....*.
gi 959092927 1136 RGFVGVIGPPGLQGLPGPPGEKGEVG 1161
Cdd:NF038329  313 PGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 678-922 1.01e-31

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: 130.41  E-value: 1.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  678 GPPGHPGHEGPTGEKGAQGPPGSAGPRGYPGLRGVKGTSGNRGLQGEKGERGEDGFPGFKGDEGPKgdrgnpgppgprGE 757
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK------------GP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  758 DGPEGQKGPGGLPGDEGPPGAAGEKGKLGVPGLPGYPGRpGPKGSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRG 837
Cdd:NF038329  194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  838 DRGQPGATGQPGPKGDVGQNGSPGPPGEKGlpglqgppgfpgpkgppgPQGKDGISGHPGQRGELGFQGLTGPPGPAGVL 917
Cdd:NF038329  273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDG------------------KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD 334


                  ....*
gi 959092927  918 GPQGK 922
Cdd:NF038329  335 GQPGK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 953-1164 5.36e-31

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: 128.48  E-value: 5.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  953 EGAKGELGPLGSVGKEGPPGPRGFPGPQGAPGDPGPIGLKGDKGPPGPVGANGSPGERGPVGPSGGIGLPGQSGGQGPIG 1032
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1033 PAGEKGSPGERGTPGPTGKDGIPGPPGLQGPSGAAGpSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGIRGPAGHSGLP 1112
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 959092927 1113 GADGAQGRRGPPGLFGQKGDDGVRGFVGVIGPPGLQGLPGPPGEKGEVGDVG 1164
Cdd:NF038329  275 GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 499-800 1.09e-29

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 124.63  E-value: 1.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  499 LKGELGEVGPQGPRglqgppgppgreGKTGRAGADGARGLPGDTGPKGDRGFDGLPGLPGEKGQRGDFGRVGQPGPPGED 578
Cdd:NF038329  115 GDGEKGEPGPAGPA------------GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  579 GVKGLQGPPGPTGQAGEPGPRGLIGPRGLPGPLGRPGVTGSDGAPGAKGNvgppgepgppgqqgnhGSQGIPGPQGPIGT 658
Cdd:NF038329  183 GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----------------GQQGPDGDPGPTGE 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  659 PGEKGPpgnpgipgvpgsEGPPGHPGHEGPTGEKGAQGPPGSAGPRGYPGLRGVKGTSGNRGLQGEKGERGEDGFPgfkg 738
Cdd:NF038329  247 DGPQGP------------DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKD---- 310

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 959092927  739 degpkgdrgnpgppgprgedgpegqkgpgGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPK 800
Cdd:NF038329  311 -----------------------------GLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 643-867 6.16e-29

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 122.32  E-value: 6.16e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  643 NHGSQGIPGPQGPIGTPGEKGPPGNPGIPGVPGSEGPPGHPGHEGPTGEKGAQGPPGSAGPRGYPGLRGVKGTSGNRGLQ 722
Cdd:NF038329  112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  723 GEKGERGEDGFPGFKGDEGPKGDRGNPGPPGPRGEDGPEGQkgpgGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGS 802
Cdd:NF038329  192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 959092927  803 IGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGPKGDVGQNGSPGPPGEKG 867
Cdd:NF038329  268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 31-210 2.47e-28

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 113.22  E-value: 2.47e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927     31 PVDVLEAWGVHRDQAGVAEGPGFCPlripqGDRAFRVGKSSLLSVPTWQLFPDGhFPENFSVLLTLRAQPANQSVLLSIY 110
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEP-----GSPAYRLGDPALVPQPTRDLFPSG-LPEDFSLLTTFRQTPKSRGVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927    111 DEKGVRQLG------------LALGPALGLLGDSFRPLPkqvnIMDGRWHRVAVSISGNKVTLVVDCEP------QPPtf 172
Cdd:smart00210   75 DAQNVRQFGlevdgrantlllRYQGVDGKQHTVSFRNLP----LADGQWHKLALSVSGSSATLYVDCNEidsrplDRP-- 148

                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 959092927    173 gqGPRFISTAGLTVMGTQDTREESFEGDIQELLLIPDP 210
Cdd:smart00210  149 --GQPPIDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 884-1157 5.09e-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: 119.62  E-value: 5.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  884 PgpqgkdgisGHPGQRGELGFQGLTGPPGPAGVLGPQGKVGDVgplgergppgppgppgeqglpgieGREGAKGELGPLG 963
Cdd:NF038329  128 A---------GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEK------------------------GPAGPQGEAGPQG 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  964 SvgkegppgprgfpgpqgapgdPGPIGLKGDKGPPGPVGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGEr 1043
Cdd:NF038329  175 P---------------------AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD- 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1044 gtpGPTGKDGIPGPPGLQGPSGAAGPSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGIRGPAGHSGLPGADGAQGRRGP 1123
Cdd:NF038329  233 ---GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGK 309

                         250       260       270
                  ....*....|....*....|....*....|....
gi 959092927 1124 PGLFGQKGDDGVRGFVGVIGPPGLQGLPGPPGEK 1157
Cdd:NF038329  310 DGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 816-1076 6.27e-27

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 116.16  E-value: 6.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  816 GKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGPKGDVGQNGSPGPPGEKGlpglqgppgFPGPKGPPGPQGKDGISGH 895
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------EAGPQGPAGKDGEAGAKGP 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  896 PGQRGELGFQGLTGPPGPAGVLGPQGKVGDVGPLGERGPPGPPGPPGeqglpgiEGREGAKGELGPLGSVGKEgppgprg 975
Cdd:NF038329  188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQ-------QGPDGDPGPTGEDGPQGPD------- 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  976 fpgpqgapGDPGPIGLKGDKGPPGPVGANGSPGERGPVGPSGGiglPGQSGGQGPIGPAGEKGSPGERGTPGPTGKDGIP 1055
Cdd:NF038329  254 --------GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK---DGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322

                         250       260
                  ....*....|....*....|.
gi 959092927 1056 GPPGLQGPSGAAGPSGEEGDK 1076
Cdd:NF038329  323 GKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 984-1243 4.87e-24

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 107.30  E-value: 4.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  984 GDPGPIGLKGDKGPPGPVGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGTPGPTGKDGIPGPPGLQGP 1063
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1064 SGAAGPSGEEGDKGEVGMPGHKGSKGD--KGDAGPPGPTGIRGPAGHSGLPGADGAQGRRGPPGLFGQKGDDGVRGFVGV 1141
Cdd:NF038329  206 QGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1142 IGPPGLQGLPGPPGEKGEVGDVGsmgphgapgprgppgpsgsegppglpggvgqpgavgEKGEPGDAGdagppgipgipg 1221
Cdd:NF038329  286 AGKDGQNGKDGLPGKDGKDGQNG------------------------------------KDGLPGKDG------------ 317

                         250       260
                  ....*....|....*....|..
gi 959092927 1222 pkgeigEKGDSGPSGAAGPPGK 1243
Cdd:NF038329  318 ------KDGQPGKDGLPGKDGK 333
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 762-1063 2.40e-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: 105.37  E-value: 2.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  762 GQKGPGGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRGQ 841
Cdd:NF038329  126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  842 PGATGQPGPKGDVGQNGSPGPPGEKGlpglqgpPGFPGPKGPPgpqgkdgisghpgqrgelGFQGLTGPPGPAGVLGPQG 921
Cdd:NF038329  206 QGPAGPAGPDGEAGPAGEDGPAGPAG-------DGQQGPDGDP------------------GPTGEDGPQGPDGPAGKDG 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  922 KVGDvgplgergppgppgppgeqglpgiegregakgelgplgsvgkegppgprgfpgpqgaPGDPGPIGLKGDKGPPGPV 1001
Cdd:NF038329  261 PRGD---------------------------------------------------------RGEAGPDGPDGKDGERGPV 283

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 959092927 1002 GANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGTPGPTGKDGIPGPPGLQGP 1063
Cdd:NF038329  284 GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 476-743 4.26e-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: 104.60  E-value: 4.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  476 KGPPGPVGLTGRPGPVGLPGYPGLKGELGEVGPQGPRglqgppgppgregktgraGADGARGLPGDTGPKGDRGFDGLPG 555
Cdd:NF038329  134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA------------------GPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  556 LPGEKGQRGDFGRVGQPGPPGEDGVKGLQGPPGPTGQaGEPGPRGLIGPRGLPGPLGRPGVTGSDGAPGAKGNvgppgep 635
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE------- 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  636 gppgqqgnhgsqgiPGPQGPIGTPGEKgppgnpgipgvpgseGPPGHPGHEgptGEKGAQGPPGSAGPRGYPGLRGVKGT 715
Cdd:NF038329  268 --------------AGPDGPDGKDGER---------------GPVGPAGKD---GQNGKDGLPGKDGKDGQNGKDGLPGK 315

                         250       260
                  ....*....|....*....|....*...
gi 959092927  716 SGNRGLQGEKGERGEDGFPGFKGDEGPK 743
Cdd:NF038329  316 DGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1227-1466 9.86e-22

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 100.36  E-value: 9.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1227 GEKGDSGPSGAAGPPGKKGPPGEDGSKGNMGPTGLPGDLGPPGDPGVPGIDGIPGEKGNAGDiggpgppgasgepgaRGL 1306
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK---------------DGE 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1307 PGKRGSPGRMGPEGREGEKGAKGDAGPDGPPGRTGPIGARGPPGRIGPDGlPGIPGPVGEPGLLGPPGLIGPPGPLGPPG 1386
Cdd:NF038329  182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1387 LPGLKGDAGPKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPGLQGDPGLPGPVGSLGHPGPPGVVGPLGQKGSKGSP 1466
Cdd:NF038329  261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 690-1015 1.48e-21

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 99.98  E-value: 1.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  690 GEKGAQGPPGSAGPRGYPGLRGVKGTSGNRGLQGEKGERGEDGFPGFKGDEGPKgdrgnpgppgprgedgpegqkGPGGL 769
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA---------------------GPQGP 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  770 PGDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGSIGFPGPLGPLGEKGKRGKAGQPGEegergtpGTRGDRGQPGATGQPG 849
Cdd:NF038329  176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-------GQQGPDGDPGPTGEDG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  850 PKGDVGQNgspgppgekglpglqgppgfpgpkgppGPQGKDGISGHPGQRGELGFQGLTGPPGPAGVLGPQGKVGdvgpl 929
Cdd:NF038329  249 PQGPDGPA---------------------------GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG----- 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  930 gergppgppgppgeqglpgIEGREGAKGELGPLGsvgkegppgprgfpgpqgAPGDPGPIGLKGDKGPPGPVGANGSPGE 1009
Cdd:NF038329  297 -------------------LPGKDGKDGQNGKDG------------------LPGKDGKDGQPGKDGLPGKDGKDGQPGK 339


                  ....*.
gi 959092927 1010 RGPVGP 1015
Cdd:NF038329  340 PAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1277-1467 3.32e-21

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 98.82  E-value: 3.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1277 DGIPGEKGNAGDIGGPGPPGASGEPGARGLPGKRGSPGRMGPEGREGEKGAKGDAGPDGPPGRTGPIGARGPPGRIGPDG 1356
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1357 LPGIPGPVGEPGLLGPPGLIGPPGPLGPPGLPGLKGD-----AGPKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPG 1431
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 959092927 1432 LQGDPGLPGPVGSLGHPGPPGVVGPLGQKGSKGSPG 1467
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1068-1363 7.02e-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: 94.59  E-value: 7.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1068 GPSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGIRGPAGHSGLPGADGAQGRRGPPGLFGQKGDDGVRGFVGVIGPPGL 1147
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1148 QGLPGPPGEKGEVgdvgsmgphgapgprgppgpsgsegppGLPGGVGQPGAVGEKGEPGDAGDagppgipgipgpkGEIG 1227
Cdd:NF038329  197 RGETGPAGEQGPA---------------------------GPAGPDGEAGPAGEDGPAGPAGD-------------GQQG 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1228 EKGDSGPSGAAGPPGKKGPPGEDGSKGNMGPTGLPGDlgppgdpgvpgiDGIPGEKGnagdiggpgppgasgepgARGLP 1307
Cdd:NF038329  237 PDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP------------DGKDGERG------------------PVGPA 286

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 959092927 1308 GKRGSPGRMGPEGREGEKGAKGDAGPDGPPGRTGPIGARGPPGRIGPDGLPGIPGP 1363
Cdd:NF038329  287 GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 370-614 4.44e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 92.28  E-value: 4.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  370 AGEKGAKGEPATveqgQQFEGPAGAPGPRGISGPSGPPGPPGFPGDRGLPGPAGLPGIPGIDGARGLPGTvimmpfhfas 449
Cdd:NF038329  125 AGPAGPAGEQGP----RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE---------- 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  450 ssmKGPPvsfqqAQAQAVLQQAQLSMKGPPGPVGLTGRPGPVGLPGYP--------GLKGELGEVGPQGPRglqgppgpp 521
Cdd:NF038329  191 ---KGPQ-----GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqgpdGDPGPTGEDGPQGPD--------- 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  522 greGKTGRAGADGARGLPGDTGPKGDRGFDGLPGLPGEKGQRGDfgrVGQPGPPGEDGVKGLQGPPGPTGQAGEPGPRGL 601
Cdd:NF038329  254 ---GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGK---DGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327

                         250
                  ....*....|...
gi 959092927  602 IGPRGLPGPLGRP 614
Cdd:NF038329  328 PGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1115-1451 9.11e-17

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 84.96  E-value: 9.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1115 DGAQGRRGPPGLFGQKGDDGVRGFVGVIGPPGLQGLPGPPGEKGEVGdvgsmgphgapgprgppgpsgsegppglpggvg 1194
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKG--------------------------------- 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1195 qpgAVGEKGEPGDAGDAgppgipgipgpkgeiGEKGdsgpsgaagppgkkgppgEDGSKGNMGPTGLPGDLGPPGDPGVP 1274
Cdd:NF038329  163 ---PAGPQGEAGPQGPA---------------GKDG------------------EAGAKGPAGEKGPQGPRGETGPAGEQ 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1275 GIDGIPGEKGNAGDIGGpgppgasgepgaRGLPGKRGSpGRMGPEGREGEKGAKGDAGPDGPPGRTGPIGARGPPGRIGP 1354
Cdd:NF038329  207 GPAGPAGPDGEAGPAGE------------DGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1355 DGLPGIPGPVgepgllgppgligppgplgppglpglkgdaGPKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPGLQG 1434
Cdd:NF038329  274 DGKDGERGPV------------------------------GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                         330
                  ....*....|....*..
gi 959092927 1435 DPGLPGPVGSLGHPGPP 1451
Cdd:NF038329  324 KDGLPGKDGKDGQPGKP 340
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
951-1161 5.18e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 60.81  E-value: 5.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  951 GREGAKGELGPLGSVGKEGPPGPRGFPGPQGAPGDPGPIGLKGDKGPPGPVGANGSPGERGPVGPS---GGIGLPGQSGG 1027
Cdd:COG5164    10 GPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAqnqGGTTPAQNQGG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1028 QGPIGPAGEKGSPGERGTPGPTGKDGIPGPPGLQGPSGAAGPSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGIRGPAG 1107
Cdd:COG5164    90 TRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPG 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 959092927 1108 HSGLPGADGAQGRRGPP-----GLFGQKGDDGVRGFVGVIGPPGLQGLPGPPGEKGEVG 1161
Cdd:COG5164   170 PGGSTTPPDDGGSTTPPnkgetGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKT 228
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
585-868 1.46e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 59.27  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  585 GPPGPTGQAGEPGPRGLIGPRGLPGPLGRPGVTGSDGAPGakgnvgppgepgppgqqgNHGSQGIPGPQGPIGTPGekgp 664
Cdd:COG5164    10 GPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQ------------------NQGSTTPAGNTGGTRPAG---- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  665 pgnpgipgVPGSEGPPGHPGHEGPTGEKGAQGPPGSAGPRGYPGLRGVKGTSGNRGLQGEKGERGEDGFPGFKGDEGPKG 744
Cdd:COG5164    68 --------NQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGD 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  745 DRGNPGPPGPRGEDGPEGQKGPGGLPGDEGPPGAAGEKGKLGV--PGLPGYPGRPGPKGSIGFPGPLGPLGEKGKRGKAG 822
Cdd:COG5164   140 GGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSttPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGN 219

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 959092927  823 QPGEEGergtpGTRGDRGQPGATGQPGPKGDVGQNGSPGPPGEKGL 868
Cdd:COG5164   220 PPDDRG-----GKTGPKDQRPKTNPIERRGPERPEAAALPAELTAL 260
LamG smart00282
Laminin G domain;
133-206 9.64e-08

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 52.73  E-value: 9.64e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927    133 FRPLPKQVNIMDGRWHRVAVSISGNKVTLVVDCEPQP--PTFGQGPRFISTAGLTVMGTQDTRE-------ESFEGDIQE 203
Cdd:smart00282   47 ARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGGNRVsgESPGGLTILNLDGPLYLGGLPEDLKlpplpvtPGFRGCIRN 126


                    ...
gi 959092927    204 LLL 206
Cdd:smart00282  127 LKV 129
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 136-206 1.20e-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: 50.11  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  136 LPKQVNIMDGRWHRVAVSISGNKVTLVVDCEP--QPPTFGQGPRFISTAGLTVMGTQDTRE-------ESFEGDIQELLL 206
Cdd:cd00110    71 LSSKTPLNDGQWHSVSVERNGRSVTLSVDGERvvESGSPGGSALLNLDGPLYLGGLPEDLKspglpvsPGFVGCIRDLKV 150
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1005-1059 6.12e-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: 6.12e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 959092927  1005 GSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGTPGPTGKDGIPGPPG 1059
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
890-1128 2.26e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 49.26  E-value: 2.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  890 DGISGHPGQRGELGFQGLTGPPGPAGVLGPQGKVGDVGPLGERGPPGPPGPPGEQGLPGIEGREGAKGELG---PLGSVG 966
Cdd:COG5164     9 TGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGgttPAQNQG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  967 KEGPPGPRGFPGPQGAPGDPGPIGLKGDKGPPGPVGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGTP 1046
Cdd:COG5164    89 GTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPP 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1047 GPTGK--------DGIPGPPGLQGPSGAAGPSGEEGDKGEVGMPGHKGSKGDKGD----AGPPGPTGIRGPAGHSGLPGA 1114
Cdd:COG5164   169 GPGGSttppddggSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDrggkTGPKDQRPKTNPIERRGPERP 248

                         250
                  ....*....|....
gi 959092927 1115 DGAQGRRGPPGLFG 1128
Cdd:COG5164   249 EAAALPAELTALEA 262
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 807-863 2.37e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 2.37e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 959092927   807 GPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGPKGDVGQNGSPGPP 863
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 555-610 2.91e-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: 43.25  E-value: 2.91e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 959092927   555 GLPGEKGQRGDFGRVGQPGPPGEDGVKGLQGPPGPTGQAGEPGPRGLIGPRGLPGP 610
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1023-1079 3.25e-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: 3.25e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 959092927  1023 GQSGGQGPIGPAGEKGSPGERGTPGPTGKDGIPGPPGLQGPSGAAGPSGEEGDKGEV 1079
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 1538-1576 5.30e-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: 42.16  E-value: 5.30e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 959092927 1538 CRELHRDHPHLPDGEYWIDPNQGCARDAFKVFCNFTAGG 1576
Cdd:NF040941    2 CWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTTDG 40
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 996-1162 8.90e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.29  E-value: 8.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  996 GPPGPVGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGTPGPTGKDGIPGPPGLQGPSGAAGPSGEEGD 1075
Cdd:PRK07764  599 GPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAP 678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927 1076 KGEVGMPGhkgskgdkgDAGPPGPTGIRGPAGHSGLPGADGAQGRRGPPGLFGQKGDDGVRGFVGVIGPPGLQGLPGPPG 1155
Cdd:PRK07764  679 AAPPPAPA---------PAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749


                  ....*..
gi 959092927 1156 EKGEVGD 1162
Cdd:PRK07764  750 DPAGAPA 756
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 996-1051 1.06e-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: 1.06e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 959092927   996 GPPGPVGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGTPGPTGK 1051
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1029-1083 1.11e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 1.11e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 959092927  1029 GPIGPAGEKGSPGERGTPGPTGKDGIPGPPGLQGPSGAAGPSGEEGDKGEVGMPG 1083
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1032-1086 1.38e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 1.38e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 959092927  1032 GPAGEKGSPGERGTPGPTGKDGIPGPPGLQGPSGAAGPSGEEGDKGEVGMPGHKG 1086
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 134-204 1.59e-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: 43.18  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927   134 RPLPKQVNimDGRWHRVAVSISGNKVTLVVD-CEPQPPTFGQGPRFISTAGLTVMG--------TQDTREESFEGDIQEL 204
Cdd:pfam02210   44 LSSGKNLN--DGQWHSVRVERNGNTLTLSVDgQTVVSSLPPGESLLLNLNGPLYLGglppllllPALPVRAGFVGCIRDV 121
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 543-599 1.74e-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: 40.94  E-value: 1.74e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 959092927   543 GPKGDRGFDGLPGLPGEKGQRGDFGRVGQPGPPGEDGVKGLQGPPGPTGQAGEPGPR 599
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1407-1456 2.27e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 2.27e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 959092927  1407 GLIGPPGEAGEKGDQGLPGVQGPPGLQGDPGLPGPVGSLGHPGPPGVVGP 1456
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 983-1036 2.36e-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: 2.36e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 959092927   983 PGDPGPIGLKGDKGPPGPVGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGE 1036
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 813-867 2.46e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 2.46e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 959092927   813 GEKGKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGPKGDVGQNGSPGPPGEKG 867
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1053-1107 3.30e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 3.30e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 959092927  1053 GIPGPPGLQGPSGAAGPSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGIRGPAG 1107
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1080-1134 3.50e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 3.50e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 959092927  1080 GMPGHKGSKGDKGDAGPPGPTGIRGPAGHSGLPGADGAQGRRGPPGLFGQKGDDG 1134
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 990-1134 3.85e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 44.96  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  990 GLKGDKGPPGPVGANGSPGERGPVGPSGGIglPGQSGGQGPIGPAGEKGSPGERGTPGPtgkdgipgppGLQGPSGAAGP 1069
Cdd:PHA03169   90 GGPSGSGSESVGSPTPSPSGSAEELASGLS--PENTSGSSPESPASHSPPPSPPSHPGP----------HEPAPPESHNP 157

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 959092927 1070 SGEEGDKGEVGMPGHKG---SKGDKGDAGPPGPTGIRGPAGHSGLPGADGAQGRRGPPGLFGQKGDDG 1134
Cdd:PHA03169  158 SPNQQPSSFLQPSHEDSpeePEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSP 225
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 795-850 7.85e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 7.85e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 959092927   795 GRPGPKGSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGP 850
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 771-826 8.49e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 8.49e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 959092927   771 GDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGSIGFPGPLGPLGEKGKRGKAGQPGE 826
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 582-628 1.20e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 1.20e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 959092927   582 GLQGPPGPTGQAGEPGPRGLIGPRGLPGPLGRPGVTGSDGAPGAKGN 628
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1395-1451 1.28e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 1.28e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 959092927  1395 GPKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPGLQGDPGLPGPVGSLGHPGPP 1451
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1314-1363 1.43e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 1.43e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 959092927  1314 GRMGPEGREGEKGAKGDAGPDGPPGRTGPIGARGPPGRIGPDGLPGIPGP 1363
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1089-1146 1.68e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 1.68e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 959092927  1089 GDKGDAGPPGPTGIRGPAGHSGLPGADGAQGRRGPPglfGQKGDDGVRGFVGVIGPPG 1146
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPP---GPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 765-821 1.79e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 1.79e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 959092927   765 GPGGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGSIGFPGPLGPLGEKGKRGKA 821
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 558-614 1.87e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 1.87e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 959092927   558 GEKGQRGDFGRVGQPGPPGEDGVKGLQGPPGPTGQAGEPGPRGLIGPRGLPGPLGRP 614
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
477-693 2.49e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 42.32  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  477 GPPGPVGLTGRPGPVGL---PGYPGLKGELGEVGPQGPRGLQGPPGPPGREGKTGRAGADGARGLPGDTGPKGDRGFDGL 553
Cdd:COG5164    46 RPAQNQGSTTPAGNTGGtrpAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGS 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  554 PGLPGEKGQRGDFGRVGQPGPPGEDGVKGLQGPPGPTGQAGEPGPRGLIGPRGLPGPlGRPGVTGSDGAPGAKGNVGPPG 633
Cdd:COG5164   126 TTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGS-TTPPNKGETGTDIPTGGTPRQG 204

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 959092927  634 EPGPPGQQGNHGSQGIPGPQGpiGTPGEKGPPGNPGIPGVPGSEGPPGHPGHEGPTGEKG 693
Cdd:COG5164   205 PDGPVKKDDKNGKGNPPDDRG--GKTGPKDQRPKTNPIERRGPERPEAAALPAELTALEA 262
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 579-628 3.02e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.47  E-value: 3.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 959092927   579 GVKGLQGPPGPTGQAGEPGPRGLIGPRGLPGPLGRPGVTGSDGAPGAKGN 628
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1303-1354 3.02e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.47  E-value: 3.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 959092927  1303 ARGLPGKRGSPGRMGPEGREGEKGAKGDAGPDGPPGRTGPIGARGPPGRIGP 1354
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1391-1442 3.68e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 3.68e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 959092927  1391 KGDAGPKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPGLQGDPGLPGPV 1442
Cdd:pfam01391    6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 546-600 4.67e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 4.67e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 959092927   546 GDRGFDGLPGLPGEKGQRGDFGRVGQPGPPGEDGVKGLQGPPGPTGQAGEPGPRG 600
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 678-728 6.03e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.70  E-value: 6.03e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 959092927   678 GPPGHPGHEGPTGEKGAQGPPGSAGPRGYPGLRGVKGTSGNRGLQGEKGER 728
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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