NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|11120710|ref|NP_068528|]
View 

collagen alpha-3(V) chain precursor [Rattus norvegicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1505-1735 2.74e-110

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: 349.72  E-value: 2.74e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   1505 GLEEVMASLNSLSLELEQLQRPPGTAESPGLICHELHRNHPHLPDGEYWIDPNQGCARDAFKVFCNFTAgGETCLYPDKK 1584
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   1585 FETvKLASWSREKPGGWYSTFRRGKK-FSY-VDADGSPVNVVQLTFLKLLSAAAHQRFTYTCQNSAAWLDEASGDHRHSI 1662
Cdd:pfam01410   80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11120710   1663 RFQGTNWEELSFNQTTAATIKVPHDGCRVRKGQ-AKTLFEFSSS-VGFLPLWDVAAVDFGQTNQKFGFELGSVCF 1735
Cdd:pfam01410  159 LLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQwGKTVIEYRTQkVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 680-921 1.86e-37

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 147.74  E-value: 1.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   680 GHPGHEGPTGEKGAQGPPGSAGPQGYPGPRGVKGTSGNRGLQGEKGERGEDGFPGFKGDEGPKGDRGNPGLPGPRGEDGP 759
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   760 EGQKGPEGLPGDEGPPGAAGEKGKLGVPGLPGYPGRpGPKGSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRG 839
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   840 QPGATGQPGPKGDVGQNGSPGAPGEKGlpglqgppgfpgpkgppgPQGKDGIPGHPGQRGELGFQGQTGPPGPAGVLGPQ 919
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDG------------------KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337


                  ..
gi 11120710   920 GK 921
Cdd:NF038329  338 GK 339
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 32-211 1.79e-31

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: 122.47  E-value: 1.79e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710      32 PVDVLETLGVHRDKAGVTKGPGFCPqripqGDRAFRVGKSSLLSVPTWQLFPDGhFPENFSVLLTLRAQPANQSVLLSIY 111
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEP-----GSPAYRLGDPALVPQPTRDLFPSG-LPEDFSLLTTFRQTPKSRGVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710     112 DENGVRQMG------------LALGPALGLLGDSFRSLPkqinLMDGRWHRVAVSISGDKVTLVVDCEP------QPPmf 173
Cdd:smart00210   75 DAQNVRQFGlevdgrantlllRYQGVDGKQHTVSFRNLP----LADGQWHKLALSVSGSSATLYVDCNEidsrplDRP-- 148

                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 11120710     174 gqGPRVISTAGLTVMGTQELGEESFEGDIQELLLIPDP 211
Cdd:smart00210  149 --GQPPIDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 900-1156 9.55e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 115.77  E-value: 9.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   900 ELGFQGQTGPPGPAGVLGPQGKVGDVGPLGERGPPGPPGPPGEPGLPGIEGREGAKGELGPLGSLGKEgppgpmgfpgpq 979
Cdd:NF038329  112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD------------ 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   980 gapGDPGPIGLKGDKGPPGPLGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGeKGSPGERGVPGPTGKDGIPGPpgl 1059
Cdd:NF038329  180 ---GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGP--- 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1060 qgppgaAGPSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGIRGPAGHPGPPGADGAQGRRGPPGLFGQKGDDGVRGFVG 1139
Cdd:NF038329  253 ------DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326

                         250
                  ....*....|....*..
gi 11120710  1140 VIGPPGLQGLPGPPGEK 1156
Cdd:NF038329  327 LPGKDGKDGQPGKPAPK 343
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 498-799 4.38e-26

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 113.46  E-value: 4.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   498 LKGELGEAGPQGPRglqgppgppgreGKTGRAGADGARGLPGDTGPKGDRGFDGLPGLPGEKGQRGDFGPVGQPGPPGED 577
Cdd:NF038329  115 GDGEKGEPGPAGPA------------GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   578 GIKGLQGPPGPTGQAGEPGPRGLIgprgppgplgrpgvtGSDGAPGAKGnvgppgepgppgqqgNHGSQGIPGPQGPIGt 657
Cdd:NF038329  183 GAKGPAGEKGPQGPRGETGPAGEQ---------------GPAGPAGPDG---------------EAGPAGEDGPAGPAG- 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   658 pgekgppgnpgipgvpgsegppghPGHEGPTGEKGAQGPPGSAGPQGYPGPRGVKGTSGNRGLQGEKGERGEDGFPGFKG 737
Cdd:NF038329  232 ------------------------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11120710   738 DEGPKGDRGNPglpgprGEDGPEGQKGPEGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPK 799
Cdd:NF038329  288 KDGQNGKDGLP------GKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1226-1465 1.37e-21

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 99.98  E-value: 1.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1226 GEKGDSGPSGAAGPPGKKGPPGEDGAKGNMGPTGLPGDLGPPGDPGVPGTDGIPGEKGNAGDiggpgppgasgepgaRGL 1305
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK---------------DGE 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1306 PGKRGSPGRMGPEGKEGEKGAKGDAGPDGPPGRTGPIGARGPPGRVGPDGlPGIPGPVGEPGLLGPPGLIGPPGPLGPPG 1385
Cdd:NF038329  182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1386 LPGLKGDAGLKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPGLQGDPGLPGPVGSLGHPGPPGVVGPLGQKGSKGSP 1465
Cdd:NF038329  261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 349-598 4.31e-15

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 79.95  E-value: 4.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   349 GPEFRAAEQSLQTEFQIFPGAGEKGAKGEPAtiEQGQQfeGPAGAPGPRGISGPSGPPGPPGFPGDRGLPGPAGLPGIPG 428
Cdd:NF038329  123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPG--PQGER--GEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   429 IDGVRGLPGTVimmpfhfASGSMKGPPVSFQQAQAQAVLQQAQLSMKGPPGPVGLTGRPGPVGLPGYPGLKGELGEAGPQ 508
Cdd:NF038329  199 ETGPAGEQGPA-------GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   509 GPRGLQGPPGPPgreGKTGRAGADGARGLPGDTGPKGDRGFDGLPGLPGEKGQrgdfgpvgqpgppgeDGIKGLQGPPGP 588
Cdd:NF038329  272 GPDGKDGERGPV---GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ---------------PGKDGLPGKDGK 333

                         250
                  ....*....|
gi 11120710   589 TGQAGEPGPR 598
Cdd:NF038329  334 DGQPGKPAPK 343
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1505-1735 2.74e-110

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: 349.72  E-value: 2.74e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   1505 GLEEVMASLNSLSLELEQLQRPPGTAESPGLICHELHRNHPHLPDGEYWIDPNQGCARDAFKVFCNFTAgGETCLYPDKK 1584
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   1585 FETvKLASWSREKPGGWYSTFRRGKK-FSY-VDADGSPVNVVQLTFLKLLSAAAHQRFTYTCQNSAAWLDEASGDHRHSI 1662
Cdd:pfam01410   80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11120710   1663 RFQGTNWEELSFNQTTAATIKVPHDGCRVRKGQ-AKTLFEFSSS-VGFLPLWDVAAVDFGQTNQKFGFELGSVCF 1735
Cdd:pfam01410  159 LLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQwGKTVIEYRTQkVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1506-1736 1.27e-85

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: 279.74  E-value: 1.27e-85
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710    1506 LEEVMASLNSLSLELEQLQRPPGTAESPGLICHELHRNHPHLPDGEYWIDPNQGCARDAFKVFCNFTAGgETCLYPDKKf 1585
Cdd:smart00038    1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETG-ETCVSPSPS- 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710    1586 eTVKLASWSREKPGG-WYS-TFRRGKKFSYVDADGSPVNVVQLTFLKLLSAAAHQRFTYTCQNSAAWLDEASGDHRHSIR 1663
Cdd:smart00038   79 -SIPRKTWYSGKSKHvWFGeTMNGGFKFSYGDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALR 157

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11120710    1664 FQGTNWEELSFNQTTAATIKVPHDGCRVRKGQ-AKTLFEFSSS-VGFLPLWDVAAVDFGQTNQKFGFELGSVCFS 1736
Cdd:smart00038  158 LRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKwGKTVIEYRTKkTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 680-921 1.86e-37

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 147.74  E-value: 1.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   680 GHPGHEGPTGEKGAQGPPGSAGPQGYPGPRGVKGTSGNRGLQGEKGERGEDGFPGFKGDEGPKGDRGNPGLPGPRGEDGP 759
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   760 EGQKGPEGLPGDEGPPGAAGEKGKLGVPGLPGYPGRpGPKGSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRG 839
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   840 QPGATGQPGPKGDVGQNGSPGAPGEKGlpglqgppgfpgpkgppgPQGKDGIPGHPGQRGELGFQGQTGPPGPAGVLGPQ 919
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDG------------------KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337


                  ..
gi 11120710   920 GK 921
Cdd:NF038329  338 GK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 642-866 3.71e-34

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: 137.73  E-value: 3.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   642 NHGSQGIPGPQGPIGTPGEKGPPGNPGIPGVPGSEGPPGHPGHEGPTGEKGAQGPPGSAGPQGYPGPRGVKGTSGNRGLQ 721
Cdd:NF038329  112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   722 GEKGERGEDGFPGFKGDEGPKGDRGNPGLPGPRGEDGPEGQkgpeGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGS 801
Cdd:NF038329  192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11120710   802 IGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGPKGDVGQNGSPGAPGEKG 866
Cdd:NF038329  268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 32-211 1.79e-31

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 122.47  E-value: 1.79e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710      32 PVDVLETLGVHRDKAGVTKGPGFCPqripqGDRAFRVGKSSLLSVPTWQLFPDGhFPENFSVLLTLRAQPANQSVLLSIY 111
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEP-----GSPAYRLGDPALVPQPTRDLFPSG-LPEDFSLLTTFRQTPKSRGVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710     112 DENGVRQMG------------LALGPALGLLGDSFRSLPkqinLMDGRWHRVAVSISGDKVTLVVDCEP------QPPmf 173
Cdd:smart00210   75 DAQNVRQFGlevdgrantlllRYQGVDGKQHTVSFRNLP----LADGQWHKLALSVSGSSATLYVDCNEidsrplDRP-- 148

                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 11120710     174 gqGPRVISTAGLTVMGTQELGEESFEGDIQELLLIPDP 211
Cdd:smart00210  149 --GQPPIDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 720-1014 3.01e-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: 120.01  E-value: 3.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   720 LQGEKGERGEDGFPGFKGDEGPKGDRGNPGLPGPRGEDGPEGQKGPEGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPK 799
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   800 GSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDrGQPGATGQPGPKGDVGQNGSPGAPGEKGlpglqgppgfpgp 879
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDG------------- 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   880 kgppgpqgKDGIPGHPGQRGELGFQGQTGPPGPAGVLGPQGKVGdvgplgergppgppgppgepglpgIEGREGAKGELG 959
Cdd:NF038329  261 --------PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG------------------------LPGKDGKDGQNG 308

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 11120710   960 PLGslgkegppgpmgfpgpqgAPGDPGPIGLKGDKGPPGPLGANGSPGERGPVGP 1014
Cdd:NF038329  309 KDG------------------LPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 900-1156 9.55e-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: 115.77  E-value: 9.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   900 ELGFQGQTGPPGPAGVLGPQGKVGDVGPLGERGPPGPPGPPGEPGLPGIEGREGAKGELGPLGSLGKEgppgpmgfpgpq 979
Cdd:NF038329  112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD------------ 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   980 gapGDPGPIGLKGDKGPPGPLGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGeKGSPGERGVPGPTGKDGIPGPpgl 1059
Cdd:NF038329  180 ---GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGP--- 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1060 qgppgaAGPSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGIRGPAGHPGPPGADGAQGRRGPPGLFGQKGDDGVRGFVG 1139
Cdd:NF038329  253 ------DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326

                         250
                  ....*....|....*..
gi 11120710  1140 VIGPPGLQGLPGPPGEK 1156
Cdd:NF038329  327 LPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 498-799 4.38e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 113.46  E-value: 4.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   498 LKGELGEAGPQGPRglqgppgppgreGKTGRAGADGARGLPGDTGPKGDRGFDGLPGLPGEKGQRGDFGPVGQPGPPGED 577
Cdd:NF038329  115 GDGEKGEPGPAGPA------------GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   578 GIKGLQGPPGPTGQAGEPGPRGLIgprgppgplgrpgvtGSDGAPGAKGnvgppgepgppgqqgNHGSQGIPGPQGPIGt 657
Cdd:NF038329  183 GAKGPAGEKGPQGPRGETGPAGEQ---------------GPAGPAGPDG---------------EAGPAGEDGPAGPAG- 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   658 pgekgppgnpgipgvpgsegppghPGHEGPTGEKGAQGPPGSAGPQGYPGPRGVKGTSGNRGLQGEKGERGEDGFPGFKG 737
Cdd:NF038329  232 ------------------------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11120710   738 DEGPKGDRGNPglpgprGEDGPEGQKGPEGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPK 799
Cdd:NF038329  288 KDGQNGKDGLP------GKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 815-1097 2.73e-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: 104.99  E-value: 2.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   815 GKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGPKGDVGQNGSPGAPGEKGlpglqgppgFPGPKGPPGPQGKDGIPGH 894
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------EAGPQGPAGKDGEAGAKGP 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   895 PGQRGELGFQGQTGPPGPAGVLGPQGKvgdvgplgergppgppgppgepglpgiEGREGAKGELGPLGSLGKEGPpgpmg 974
Cdd:NF038329  188 AGEKGPQGPRGETGPAGEQGPAGPAGP---------------------------DGEAGPAGEDGPAGPAGDGQQ----- 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   975 fpgpqgapGDPGPIGLKGDKGPPGPLGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGVPGPTGKDGIp 1054
Cdd:NF038329  236 --------GPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQ- 306

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 11120710  1055 gppglqgppgaAGPSGEEGDKGEVGMPGHKGSKGDKGDAGPPG 1097
Cdd:NF038329  307 -----------NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1004-1208 6.67e-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: 100.75  E-value: 6.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1004 GSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGVPGPTGKDGIPGPPGLQGPPGAAGPSGEEGDKGEVGMPGH 1083
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1084 KGSKGDKGDAGPPGPTGIRG-----PAGHPGPPGADGAQGRRGPPGLFGQKGDDGVRGFVGVIGPPGLQGLPGPPGEKGE 1158
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGeagpaGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 11120710  1159 VGDVGSMGPHGAPGPRGPPGPSGSAGSPGLPGGVGQPGAVGEKGEPGNAG 1208
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1226-1465 1.37e-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: 1.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1226 GEKGDSGPSGAAGPPGKKGPPGEDGAKGNMGPTGLPGDLGPPGDPGVPGTDGIPGEKGNAGDiggpgppgasgepgaRGL 1305
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK---------------DGE 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1306 PGKRGSPGRMGPEGKEGEKGAKGDAGPDGPPGRTGPIGARGPPGRVGPDGlPGIPGPVGEPGLLGPPGLIGPPGPLGPPG 1385
Cdd:NF038329  182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1386 LPGLKGDAGLKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPGLQGDPGLPGPVGSLGHPGPPGVVGPLGQKGSKGSP 1465
Cdd:NF038329  261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1276-1466 3.60e-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: 3.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1276 DGIPGEKGNAGDIGGPGPPGASGEPGARGLPGKRGSPGRMGPEGKEGEKGAKGDAGPDGPPGRTGPIGARGPPGRVGPDG 1355
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1356 LPGIPGPVGEPGLLGPPGLIGPPGPLGPPGLPGLKGD-----AGLKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPG 1430
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 11120710  1431 LQGDPGLPGPVGSLGHPGPPGVVGPLGQKGSKGSPG 1466
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1067-1362 2.63e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 93.05  E-value: 2.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1067 GPSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGIRGPAGHPGPPGADGAQGRRGPPGLFGQKGDDGVRGFVGVIGPPGL 1146
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1147 QGLPGPPGEKGEVGdvgsmgphgapgprgppgpsgsagspgLPGGVGQPGAVGEKGEPGNAGDagppgvpGIPGPKGEIG 1226
Cdd:NF038329  197 RGETGPAGEQGPAG---------------------------PAGPDGEAGPAGEDGPAGPAGD-------GQQGPDGDPG 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1227 EKGDSGPSGAAgppgkkGPPGEDGAKGNMGPTGLPGdlgppgdpgvpgTDGIPGEKGnagdiggpgppgasgepgARGLP 1306
Cdd:NF038329  243 PTGEDGPQGPD------GPAGKDGPRGDRGEAGPDG------------PDGKDGERG------------------PVGPA 286

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 11120710  1307 GKRGSPGRMGPEGKEGEKGAKGDAGPDGPPGRTGPIGARGPPGRVGPDGLPGIPGP 1362
Cdd:NF038329  287 GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1154-1450 9.68e-18

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: 88.04  E-value: 9.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1154 GEKGEVGDVGSMGPHGAPGPRGPPGPSGSAGSPGLPGGVGQPGAVGEKGEPGNAGDAgppgvpgipgpkgeiGEKGDSGp 1233
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKDG- 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1234 sgaagppgkkgppgEDGAKGNMGPTGLPGDLGPPGDPGVPGTDGIPGEKGNAGDIGGpgppgasgepgaRGLPGKRGSpG 1313
Cdd:NF038329  181 --------------EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGE------------DGPAGPAGD-G 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1314 RMGPEGKEGEKGAKGDAGPDGPPGRTGPIGARGPPGRVGPDGLPGIPGPVgepgllgppgligppgplgppglpglkgda 1393
Cdd:NF038329  234 QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV------------------------------ 283

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 11120710  1394 GLKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPGLQGDPGLPGPVGSLGHPGPP 1450
Cdd:NF038329  284 GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 389-623 3.42e-15

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 80.33  E-value: 3.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   389 GPAGAPGPRGISGPSGPPGPPGFPGDRGLPGPAGLPGIPGIDGVRGLPGTVimmpfhfasgsmkGPPvsfqqAQAQAVLQ 468
Cdd:NF038329  123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ-------------GPA-----GKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   469 QAQLSMKGPPGPVGLTGRPGPVGLPGYPGLKGELGEAGPQGPRGLQGPPGPPGR--EGKTGRAGADGARGLPGDTGPKGD 546
Cdd:NF038329  185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDgdPGPTGEDGPQGPDGPAGKDGPRGD 264

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11120710   547 RGFDGLPGLPGEKGQRGdfgPVGQPGPPGEDGIKGLQGPPGPTGQAGEPGPRGLIGPRGPPGPLGRPGVTGSDGAPG 623
Cdd:NF038329  265 RGEAGPDGPDGKDGERG---PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 349-598 4.31e-15

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 79.95  E-value: 4.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   349 GPEFRAAEQSLQTEFQIFPGAGEKGAKGEPAtiEQGQQfeGPAGAPGPRGISGPSGPPGPPGFPGDRGLPGPAGLPGIPG 428
Cdd:NF038329  123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPG--PQGER--GEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   429 IDGVRGLPGTVimmpfhfASGSMKGPPVSFQQAQAQAVLQQAQLSMKGPPGPVGLTGRPGPVGLPGYPGLKGELGEAGPQ 508
Cdd:NF038329  199 ETGPAGEQGPA-------GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   509 GPRGLQGPPGPPgreGKTGRAGADGARGLPGDTGPKGDRGFDGLPGLPGEKGQrgdfgpvgqpgppgeDGIKGLQGPPGP 588
Cdd:NF038329  272 GPDGKDGERGPV---GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ---------------PGKDGLPGKDGK 333

                         250
                  ....*....|
gi 11120710   589 TGQAGEPGPR 598
Cdd:NF038329  334 DGQPGKPAPK 343
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
617-864 4.10e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 61.20  E-value: 4.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  617 GSDGAPGAKGNVGPPGEPGPPGQQGNHGSQGIPGPQGPIGTPGEK------GPPGNPGIPGVPGSEGPPGHPGHEGPTGE 690
Cdd:COG5164    7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQgsttpaGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  691 KGAQGPPGSAGPQGYPGPRGVKGTSGNRGLQGEKGERGEDGfPGFKGDEGPKGDRG----NPGLPGPRGEDGPEGQKGPE 766
Cdd:COG5164   87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-PPSGGSTTPPGDGGstppGPGSTGPGGSTTPPGDGGST 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  767 GLPGDEGPPGAAGEKGKlGVPGLPGYPGRPGPKGSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTP-GTRGDRGQPGATG 845
Cdd:COG5164  166 TPPGPGGSTTPPDDGGS-TTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPkDQRPKTNPIERRG 244

                        250
                 ....*....|....*....
gi 11120710  846 QPGPKGDVGQNGSPGAPGE 864
Cdd:COG5164  245 PERPEAAALPAELTALEAE 263
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1343-1489 1.52e-07

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 56.07  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1343 GARGPPGRVGPDGLPGIPGPvgepgllgppgligppgplgppglpglKGDAGLKGEKGHIGLIGLIGPPGEAGEKGDQGL 1422
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGP---------------------------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11120710  1423 PGVQGPPGLQGDPGLPGPVGSLGHPGPPGVVGPLGQKGSKGSPGslgprgdpgPAGPPGPPGSPAEV 1489
Cdd:NF038329  170 AGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAG---------PDGEAGPAGEDGPA 227
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 137-207 8.87e-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: 47.41  E-value: 8.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  137 LPKQINLMDGRWHRVAVSISGDKVTLVVDCEP--QPPMFGQGPRVISTAGLTVMGTQELGE-------ESFEGDIQELLL 207
Cdd:cd00110   71 LSSKTPLNDGQWHSVSVERNGRSVTLSVDGERvvESGSPGGSALLNLDGPLYLGGLPEDLKspglpvsPGFVGCIRDLKV 150
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 725-780 1.48e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.02  E-value: 1.48e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 11120710    725 GERGEDGFPGFKGDEGPKGDRGNPGLPGPRGEDGPEGQKGPEGLPGDEGPPGAAGE 780
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03169 PHA03169
hypothetical protein; Provisional
 680-863 4.37e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 48.04  E-value: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   680 GHPGHEGPTGEKGAQGPPGSAGPQGYPGprgvkGTSGNRGLQGEKGERGEDGFPGFKGDEGPkGDRGNPGLPGPRGEDGP 759
Cdd:PHA03169   90 GGPSGSGSESVGSPTPSPSGSAEELASG-----LSPENTSGSSPESPASHSPPPSPPSHPGP-HEPAPPESHNPSPNQQP 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   760 EGQKGPEGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRG 839
Cdd:PHA03169  164 SSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPERE 243

                         170       180
                  ....*....|....*....|....
gi 11120710   840 QPGATGQPGPKGDVGQNGSPGAPG 863
Cdd:PHA03169  244 GPPFPGHRSHSYTVVGWKPSTRPG 267
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 1537-1575 1.12e-04

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


Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 41.01  E-value: 1.12e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 11120710  1537 CHELHRNHPHLPDGEYWIDPNQGCARDAFKVFCNFTAGG 1575
Cdd:NF040941    2 CWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTTDG 40
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1406-1455 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 11120710   1406 GLIGPPGEAGEKGDQGLPGVQGPPGLQGDPGLPGPVGSLGHPGPPGVVGP 1455
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
889-1155 2.90e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.41  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  889 DGIPGHPGQRGELGFQGQTGPPGPAGVLGPQGKVGDVGPLGERGPPGPPGPPGEPGLPGIEGREGAKGELG---PLGSLG 965
Cdd:COG5164    9 TGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGgttPAQNQG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  966 KEGPPGPMGFPGPQGAPGDPGPIGLKGDKGPPGPLGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGVP 1045
Cdd:COG5164   89 GTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPP 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710 1046 GPTGKDGIPGppglqgppgaAGPSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGirgpaGHPGPPGADGAQGRRGPPGL 1125
Cdd:COG5164  169 GPGGSTTPPD----------DGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDD-----KNGKGNPPDDRGGKTGPKDQ 233

                        250       260       270
                 ....*....|....*....|....*....|
gi 11120710 1126 FGQKGDDGVRGFVGVIGPPGLQGLPGPPGE 1155
Cdd:COG5164  234 RPKTNPIERRGPERPEAAALPAELTALEAE 263
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1004-1049 9.37e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 9.37e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 11120710   1004 GSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGVPGPTG 1049
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 135-169 1.07e-03

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: 40.87  E-value: 1.07e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 11120710    135 RSLPKQINlmDGRWHRVAVSISGDKVTLVVDCEPQ 169
Cdd:pfam02210   44 LSSGKNLN--DGQWHSVRVERNGNTLTLSVDGQTV 76
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1505-1735 2.74e-110

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: 349.72  E-value: 2.74e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   1505 GLEEVMASLNSLSLELEQLQRPPGTAESPGLICHELHRNHPHLPDGEYWIDPNQGCARDAFKVFCNFTAgGETCLYPDKK 1584
Cdd:pfam01410    1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFET-GETCIYPTKA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   1585 FETvKLASWSREKPGGWYSTFRRGKK-FSY-VDADGSPVNVVQLTFLKLLSAAAHQRFTYTCQNSAAWLDEASGDHRHSI 1662
Cdd:pfam01410   80 SIP-RKNWWTKESKHVWFGEFMNGGSqFSYgVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKAL 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11120710   1663 RFQGTNWEELSFNQTTAATIKVPHDGCRVRKGQ-AKTLFEFSSS-VGFLPLWDVAAVDFGQTNQKFGFELGSVCF 1735
Cdd:pfam01410  159 LLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQwGKTVIEYRTQkVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 1506-1736 1.27e-85

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: 279.74  E-value: 1.27e-85
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710    1506 LEEVMASLNSLSLELEQLQRPPGTAESPGLICHELHRNHPHLPDGEYWIDPNQGCARDAFKVFCNFTAGgETCLYPDKKf 1585
Cdd:smart00038    1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETG-ETCVSPSPS- 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710    1586 eTVKLASWSREKPGG-WYS-TFRRGKKFSYVDADGSPVNVVQLTFLKLLSAAAHQRFTYTCQNSAAWLDEASGDHRHSIR 1663
Cdd:smart00038   79 -SIPRKTWYSGKSKHvWFGeTMNGGFKFSYGDSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKALR 157

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11120710    1664 FQGTNWEELSFNQTTAATIKVPHDGCRVRKGQ-AKTLFEFSSS-VGFLPLWDVAAVDFGQTNQKFGFELGSVCFS 1736
Cdd:smart00038  158 LRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKwGKTVIEYRTKkTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 680-921 1.86e-37

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 147.74  E-value: 1.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   680 GHPGHEGPTGEKGAQGPPGSAGPQGYPGPRGVKGTSGNRGLQGEKGERGEDGFPGFKGDEGPKGDRGNPGLPGPRGEDGP 759
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   760 EGQKGPEGLPGDEGPPGAAGEKGKLGVPGLPGYPGRpGPKGSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRG 839
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   840 QPGATGQPGPKGDVGQNGSPGAPGEKGlpglqgppgfpgpkgppgPQGKDGIPGHPGQRGELGFQGQTGPPGPAGVLGPQ 919
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDG------------------KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337


                  ..
gi 11120710   920 GK 921
Cdd:NF038329  338 GK 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 642-866 3.71e-34

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: 137.73  E-value: 3.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   642 NHGSQGIPGPQGPIGTPGEKGPPGNPGIPGVPGSEGPPGHPGHEGPTGEKGAQGPPGSAGPQGYPGPRGVKGTSGNRGLQ 721
Cdd:NF038329  112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   722 GEKGERGEDGFPGFKGDEGPKGDRGNPGLPGPRGEDGPEGQkgpeGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGS 801
Cdd:NF038329  192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11120710   802 IGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGPKGDVGQNGSPGAPGEKG 866
Cdd:NF038329  268 AGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 32-211 1.79e-31

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 122.47  E-value: 1.79e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710      32 PVDVLETLGVHRDKAGVTKGPGFCPqripqGDRAFRVGKSSLLSVPTWQLFPDGhFPENFSVLLTLRAQPANQSVLLSIY 111
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEP-----GSPAYRLGDPALVPQPTRDLFPSG-LPEDFSLLTTFRQTPKSRGVLFAIY 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710     112 DENGVRQMG------------LALGPALGLLGDSFRSLPkqinLMDGRWHRVAVSISGDKVTLVVDCEP------QPPmf 173
Cdd:smart00210   75 DAQNVRQFGlevdgrantlllRYQGVDGKQHTVSFRNLP----LADGQWHKLALSVSGSSATLYVDCNEidsrplDRP-- 148

                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 11120710     174 gqGPRVISTAGLTVMGTQELGEESFEGDIQELLLIPDP 211
Cdd:smart00210  149 --GQPPIDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 720-1014 3.01e-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: 120.01  E-value: 3.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   720 LQGEKGERGEDGFPGFKGDEGPKGDRGNPGLPGPRGEDGPEGQKGPEGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPK 799
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   800 GSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDrGQPGATGQPGPKGDVGQNGSPGAPGEKGlpglqgppgfpgp 879
Cdd:NF038329  195 GPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDG------------- 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   880 kgppgpqgKDGIPGHPGQRGELGFQGQTGPPGPAGVLGPQGKVGdvgplgergppgppgppgepglpgIEGREGAKGELG 959
Cdd:NF038329  261 --------PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG------------------------LPGKDGKDGQNG 308

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 11120710   960 PLGslgkegppgpmgfpgpqgAPGDPGPIGLKGDKGPPGPLGANGSPGERGPVGP 1014
Cdd:NF038329  309 KDG------------------LPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 900-1156 9.55e-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: 115.77  E-value: 9.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   900 ELGFQGQTGPPGPAGVLGPQGKVGDVGPLGERGPPGPPGPPGEPGLPGIEGREGAKGELGPLGSLGKEgppgpmgfpgpq 979
Cdd:NF038329  112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD------------ 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   980 gapGDPGPIGLKGDKGPPGPLGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGeKGSPGERGVPGPTGKDGIPGPpgl 1059
Cdd:NF038329  180 ---GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGP--- 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1060 qgppgaAGPSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGIRGPAGHPGPPGADGAQGRRGPPGLFGQKGDDGVRGFVG 1139
Cdd:NF038329  253 ------DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326

                         250
                  ....*....|....*..
gi 11120710  1140 VIGPPGLQGLPGPPGEK 1156
Cdd:NF038329  327 LPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 498-799 4.38e-26

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 113.46  E-value: 4.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   498 LKGELGEAGPQGPRglqgppgppgreGKTGRAGADGARGLPGDTGPKGDRGFDGLPGLPGEKGQRGDFGPVGQPGPPGED 577
Cdd:NF038329  115 GDGEKGEPGPAGPA------------GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   578 GIKGLQGPPGPTGQAGEPGPRGLIgprgppgplgrpgvtGSDGAPGAKGnvgppgepgppgqqgNHGSQGIPGPQGPIGt 657
Cdd:NF038329  183 GAKGPAGEKGPQGPRGETGPAGEQ---------------GPAGPAGPDG---------------EAGPAGEDGPAGPAG- 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   658 pgekgppgnpgipgvpgsegppghPGHEGPTGEKGAQGPPGSAGPQGYPGPRGVKGTSGNRGLQGEKGERGEDGFPGFKG 737
Cdd:NF038329  232 ------------------------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11120710   738 DEGPKGDRGNPglpgprGEDGPEGQKGPEGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPK 799
Cdd:NF038329  288 KDGQNGKDGLP------GKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 815-1097 2.73e-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: 104.99  E-value: 2.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   815 GKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGPKGDVGQNGSPGAPGEKGlpglqgppgFPGPKGPPGPQGKDGIPGH 894
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG---------EAGPQGPAGKDGEAGAKGP 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   895 PGQRGELGFQGQTGPPGPAGVLGPQGKvgdvgplgergppgppgppgepglpgiEGREGAKGELGPLGSLGKEGPpgpmg 974
Cdd:NF038329  188 AGEKGPQGPRGETGPAGEQGPAGPAGP---------------------------DGEAGPAGEDGPAGPAGDGQQ----- 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   975 fpgpqgapGDPGPIGLKGDKGPPGPLGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGVPGPTGKDGIp 1054
Cdd:NF038329  236 --------GPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQ- 306

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 11120710  1055 gppglqgppgaAGPSGEEGDKGEVGMPGHKGSKGDKGDAGPPG 1097
Cdd:NF038329  307 -----------NGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1004-1208 6.67e-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: 100.75  E-value: 6.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1004 GSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGVPGPTGKDGIPGPPGLQGPPGAAGPSGEEGDKGEVGMPGH 1083
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1084 KGSKGDKGDAGPPGPTGIRG-----PAGHPGPPGADGAQGRRGPPGLFGQKGDDGVRGFVGVIGPPGLQGLPGPPGEKGE 1158
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGeagpaGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 11120710  1159 VGDVGSMGPHGAPGPRGPPGPSGSAGSPGLPGGVGQPGAVGEKGEPGNAG 1208
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1226-1465 1.37e-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: 1.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1226 GEKGDSGPSGAAGPPGKKGPPGEDGAKGNMGPTGLPGDLGPPGDPGVPGTDGIPGEKGNAGDiggpgppgasgepgaRGL 1305
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK---------------DGE 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1306 PGKRGSPGRMGPEGKEGEKGAKGDAGPDGPPGRTGPIGARGPPGRVGPDGlPGIPGPVGEPGLLGPPGLIGPPGPLGPPG 1385
Cdd:NF038329  182 AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1386 LPGLKGDAGLKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPGLQGDPGLPGPVGSLGHPGPPGVVGPLGQKGSKGSP 1465
Cdd:NF038329  261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1276-1466 3.60e-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: 3.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1276 DGIPGEKGNAGDIGGPGPPGASGEPGARGLPGKRGSPGRMGPEGKEGEKGAKGDAGPDGPPGRTGPIGARGPPGRVGPDG 1355
Cdd:NF038329  116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1356 LPGIPGPVGEPGLLGPPGLIGPPGPLGPPGLPGLKGD-----AGLKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPG 1430
Cdd:NF038329  196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 11120710  1431 LQGDPGLPGPVGSLGHPGPPGVVGPLGQKGSKGSPG 1466
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1067-1362 2.63e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 93.05  E-value: 2.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1067 GPSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGIRGPAGHPGPPGADGAQGRRGPPGLFGQKGDDGVRGFVGVIGPPGL 1146
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1147 QGLPGPPGEKGEVGdvgsmgphgapgprgppgpsgsagspgLPGGVGQPGAVGEKGEPGNAGDagppgvpGIPGPKGEIG 1226
Cdd:NF038329  197 RGETGPAGEQGPAG---------------------------PAGPDGEAGPAGEDGPAGPAGD-------GQQGPDGDPG 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1227 EKGDSGPSGAAgppgkkGPPGEDGAKGNMGPTGLPGdlgppgdpgvpgTDGIPGEKGnagdiggpgppgasgepgARGLP 1306
Cdd:NF038329  243 PTGEDGPQGPD------GPAGKDGPRGDRGEAGPDG------------PDGKDGERG------------------PVGPA 286

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 11120710  1307 GKRGSPGRMGPEGKEGEKGAKGDAGPDGPPGRTGPIGARGPPGRVGPDGLPGIPGP 1362
Cdd:NF038329  287 GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1154-1450 9.68e-18

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: 88.04  E-value: 9.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1154 GEKGEVGDVGSMGPHGAPGPRGPPGPSGSAGSPGLPGGVGQPGAVGEKGEPGNAGDAgppgvpgipgpkgeiGEKGDSGp 1233
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ---------------GPAGKDG- 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1234 sgaagppgkkgppgEDGAKGNMGPTGLPGDLGPPGDPGVPGTDGIPGEKGNAGDIGGpgppgasgepgaRGLPGKRGSpG 1313
Cdd:NF038329  181 --------------EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGE------------DGPAGPAGD-G 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1314 RMGPEGKEGEKGAKGDAGPDGPPGRTGPIGARGPPGRVGPDGLPGIPGPVgepgllgppgligppgplgppglpglkgda 1393
Cdd:NF038329  234 QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV------------------------------ 283

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 11120710  1394 GLKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPGLQGDPGLPGPVGSLGHPGPP 1450
Cdd:NF038329  284 GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 389-623 3.42e-15

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 80.33  E-value: 3.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   389 GPAGAPGPRGISGPSGPPGPPGFPGDRGLPGPAGLPGIPGIDGVRGLPGTVimmpfhfasgsmkGPPvsfqqAQAQAVLQ 468
Cdd:NF038329  123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ-------------GPA-----GKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   469 QAQLSMKGPPGPVGLTGRPGPVGLPGYPGLKGELGEAGPQGPRGLQGPPGPPGR--EGKTGRAGADGARGLPGDTGPKGD 546
Cdd:NF038329  185 KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDgdPGPTGEDGPQGPDGPAGKDGPRGD 264

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11120710   547 RGFDGLPGLPGEKGQRGdfgPVGQPGPPGEDGIKGLQGPPGPTGQAGEPGPRGLIGPRGPPGPLGRPGVTGSDGAPG 623
Cdd:NF038329  265 RGEAGPDGPDGKDGERG---PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 349-598 4.31e-15

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 79.95  E-value: 4.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   349 GPEFRAAEQSLQTEFQIFPGAGEKGAKGEPAtiEQGQQfeGPAGAPGPRGISGPSGPPGPPGFPGDRGLPGPAGLPGIPG 428
Cdd:NF038329  123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPG--PQGER--GEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   429 IDGVRGLPGTVimmpfhfASGSMKGPPVSFQQAQAQAVLQQAQLSMKGPPGPVGLTGRPGPVGLPGYPGLKGELGEAGPQ 508
Cdd:NF038329  199 ETGPAGEQGPA-------GPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   509 GPRGLQGPPGPPgreGKTGRAGADGARGLPGDTGPKGDRGFDGLPGLPGEKGQrgdfgpvgqpgppgeDGIKGLQGPPGP 588
Cdd:NF038329  272 GPDGKDGERGPV---GPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ---------------PGKDGLPGKDGK 333

                         250
                  ....*....|
gi 11120710   589 TGQAGEPGPR 598
Cdd:NF038329  334 DGQPGKPAPK 343
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
617-864 4.10e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 61.20  E-value: 4.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  617 GSDGAPGAKGNVGPPGEPGPPGQQGNHGSQGIPGPQGPIGTPGEK------GPPGNPGIPGVPGSEGPPGHPGHEGPTGE 690
Cdd:COG5164    7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQgsttpaGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  691 KGAQGPPGSAGPQGYPGPRGVKGTSGNRGLQGEKGERGEDGfPGFKGDEGPKGDRG----NPGLPGPRGEDGPEGQKGPE 766
Cdd:COG5164   87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-PPSGGSTTPPGDGGstppGPGSTGPGGSTTPPGDGGST 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  767 GLPGDEGPPGAAGEKGKlGVPGLPGYPGRPGPKGSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTP-GTRGDRGQPGATG 845
Cdd:COG5164  166 TPPGPGGSTTPPDDGGS-TTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPkDQRPKTNPIERRG 244

                        250
                 ....*....|....*....
gi 11120710  846 QPGPKGDVGQNGSPGAPGE 864
Cdd:COG5164  245 PERPEAAALPAELTALEAE 263
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1343-1489 1.52e-07

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 56.07  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  1343 GARGPPGRVGPDGLPGIPGPvgepgllgppgligppgplgppglpglKGDAGLKGEKGHIGLIGLIGPPGEAGEKGDQGL 1422
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGP---------------------------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11120710  1423 PGVQGPPGLQGDPGLPGPVGSLGHPGPPGVVGPLGQKGSKGSPGslgprgdpgPAGPPGPPGSPAEV 1489
Cdd:NF038329  170 AGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAG---------PDGEAGPAGEDGPA 227
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
790-1049 7.11e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 53.88  E-value: 7.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  790 PGYPGRPGPKGSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGPKGDVGQNGSPGAPGEKGlpg 869
Cdd:COG5164    6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTT--- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  870 lqgppgfpgpkgPPGPQGKDGIPGHPGQRGELGFQGQTGPPGPAGVLGPQGKVGDVGPLGERGPPGPPGPPGEPGLPGIE 949
Cdd:COG5164   83 ------------PAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGST 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  950 GREGAKGELGPLGSL-----GKEGPPGPMGFPGPQGAPGDPGPIGLKGDKGPPGPLGANGSPGERGPVGPSGGI-GLPGQ 1023
Cdd:COG5164  151 GPGGSTTPPGDGGSTtppgpGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRgGKTGP 230

                        250       260
                 ....*....|....*....|....*.
gi 11120710 1024 SGGQGPIGPAGEKGSPGERGVPGPTG 1049
Cdd:COG5164  231 KDQRPKTNPIERRGPERPEAAALPAE 256
LamG smart00282
Laminin G domain;
133-207 1.45e-06

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 49.26  E-value: 1.45e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710     133 SFRSLPKQINlmDGRWHRVAVSISGDKVTLVVDCEPQPPM--FGQGPRVISTAGLTVMGT-------QELGEESFEGDIQ 203
Cdd:smart00282   48 RLTSDPTPLN--DGQWHRVAVERNGRSVTLSVDGGNRVSGesPGGLTILNLDGPLYLGGLpedlklpPLPVTPGFRGCIR 125


                    ....
gi 11120710     204 ELLL 207
Cdd:smart00282  126 NLKV 129
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 137-207 8.87e-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: 47.41  E-value: 8.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  137 LPKQINLMDGRWHRVAVSISGDKVTLVVDCEP--QPPMFGQGPRVISTAGLTVMGTQELGE-------ESFEGDIQELLL 207
Cdd:cd00110   71 LSSKTPLNDGQWHSVSVERNGRSVTLSVDGERvvESGSPGGSALLNLDGPLYLGGLPEDLKspglpvsPGFVGCIRDLKV 150
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 725-780 1.48e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.02  E-value: 1.48e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 11120710    725 GERGEDGFPGFKGDEGPKGDRGNPGLPGPRGEDGPEGQKGPEGLPGDEGPPGAAGE 780
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 719-775 3.09e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 3.09e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 11120710    719 GLQGEKGERGEDGFPGFKGDEGPKGDRGNPGLPGPRGEDGPEGQKGPEGLPGDEGPP 775
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 806-862 3.76e-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: 3.76e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 11120710    806 GPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGPKGDVGQNGSPGAP 862
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 680-863 4.37e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 48.04  E-value: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   680 GHPGHEGPTGEKGAQGPPGSAGPQGYPGprgvkGTSGNRGLQGEKGERGEDGFPGFKGDEGPkGDRGNPGLPGPRGEDGP 759
Cdd:PHA03169   90 GGPSGSGSESVGSPTPSPSGSAEELASG-----LSPENTSGSSPESPASHSPPPSPPSHPGP-HEPAPPESHNPSPNQQP 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   760 EGQKGPEGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRG 839
Cdd:PHA03169  164 SSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPERE 243

                         170       180
                  ....*....|....*....|....
gi 11120710   840 QPGATGQPGPKGDVGQNGSPGAPG 863
Cdd:PHA03169  244 GPPFPGHRSHSYTVVGWKPSTRPG 267
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 743-798 5.91e-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: 42.10  E-value: 5.91e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 11120710    743 GDRGNPGLPGPRGEDGPEGQKGPEGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGP 798
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03169 PHA03169
hypothetical protein; Provisional
 644-824 8.94e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.89  E-value: 8.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   644 GSQGIPGPQGPIGTPGEKGPPGNPGIPGVPGSEGPPghpghEGPTGEKGAQGPPGSAGPqGYPGPRGVKGTSGNRGLQGE 723
Cdd:PHA03169   93 SGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSP-----ESPASHSPPPSPPSHPGP-HEPAPPESHNPSPNQQPSSF 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   724 KGERGEDGF-PGFKGDEGPKGDRGNPGlPGPRGEDGPEGQKGPE--GLPGDEGPPGAAGEKGKLGVPGL--PGYPGRPGP 798
Cdd:PHA03169  167 LQPSHEDSPeEPEPPTSEPEPDSPGPP-QSETPTSSPPPQSPPDepGEPQSPTPQQAPSPNTQQAVEHEdePTEPEREGP 245

                         170       180
                  ....*....|....*....|....*.
gi 11120710   799 kgsiGFPGPLGPLGEKGKRGKAGQPG 824
Cdd:PHA03169  246 ----PFPGHRSHSYTVVGWKPSTRPG 267
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 1537-1575 1.12e-04

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


Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 41.01  E-value: 1.12e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 11120710  1537 CHELHRNHPHLPDGEYWIDPNQGCARDAFKVFCNFTAGG 1575
Cdd:NF040941    2 CWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTTDG 40
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 698-754 1.31e-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: 1.31e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 11120710    698 GSAGPQGYPGPRGVKGTSGNRGLQGEKGERGEDGFPGFKGDEGPKGDRGNPGLPGPR 754
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 761-817 1.98e-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: 1.98e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 11120710    761 GQKGPEGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGSIGFPGPLGPLGEKGKR 817
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1406-1455 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 11120710   1406 GLIGPPGEAGEKGDQGLPGVQGPPGLQGDPGLPGPVGSLGHPGPPGVVGP 1455
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 734-790 2.41e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 2.41e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 11120710    734 GFKGDEGPKGDRGNPGLPGPRGEDGPEGQKGPEGLPGDEGPPGAAGEKGKLGVPGLP 790
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
889-1155 2.90e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.41  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  889 DGIPGHPGQRGELGFQGQTGPPGPAGVLGPQGKVGDVGPLGERGPPGPPGPPGEPGLPGIEGREGAKGELG---PLGSLG 965
Cdd:COG5164    9 TGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGgttPAQNQG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  966 KEGPPGPMGFPGPQGAPGDPGPIGLKGDKGPPGPLGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGVP 1045
Cdd:COG5164   89 GTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPP 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710 1046 GPTGKDGIPGppglqgppgaAGPSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGirgpaGHPGPPGADGAQGRRGPPGL 1125
Cdd:COG5164  169 GPGGSTTPPD----------DGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDD-----KNGKGNPPDDRGGKTGPKDQ 233

                        250       260       270
                 ....*....|....*....|....*....|
gi 11120710 1126 FGQKGDDGVRGFVGVIGPPGLQGLPGPPGE 1155
Cdd:COG5164  234 RPKTNPIERRGPERPEAAALPAELTALEAE 263
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 812-866 3.21e-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: 3.21e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 11120710    812 GEKGKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGPKGDVGQNGSPGAPGEKG 866
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 713-769 3.61e-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: 3.61e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 11120710    713 GTSGNRGLQGEKGERGEDGFPGFKGDEGPKGDRGNPGLPGPRGEDGPEGQKGPEGLP 769
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 803-859 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 11120710    803 GFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGPKGDVGQNGSP 859
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 794-849 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 11120710    794 GRPGPKGSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGP 849
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 770-825 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 11120710    770 GDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGSIGFPGPLGPLGEKGKRGKAGQPGE 825
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1004-1049 9.37e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 9.37e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 11120710   1004 GSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGVPGPTG 1049
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 135-169 1.07e-03

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: 40.87  E-value: 1.07e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 11120710    135 RSLPKQINlmDGRWHRVAVSISGDKVTLVVDCEPQ 169
Cdd:pfam02210   44 LSSGKNLN--DGQWHSVRVERNGNTLTLSVDGQTV 76
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1313-1362 1.11e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 1.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 11120710   1313 GRMGPEGKEGEKGAKGDAGPDGPPGRTGPIGARGPPGRVGPDGLPGIPGP 1362
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
728-915 1.26e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 43.48  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  728 GEDGFPGFKGDEGPKGDRGNPGLPGPRGEDGPEGQKGPEGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGSIGFPGP 807
Cdd:COG5164    7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710  808 LGPLGEKGKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGPKgdvgQNGSPGAPGEKG-LPGLQGPPGFPGPKGPPGPQ 886
Cdd:COG5164   87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPP----SGGSTTPPGDGGsTPPGPGSTGPGGSTTPPGDG 162

                        170       180
                 ....*....|....*....|....*....
gi 11120710  887 GKDGIPGHPGQRGELGFQGQTGPPGPAGV 915
Cdd:COG5164  163 GSTTPPGPGGSTTPPDDGGSTTPPNKGET 191
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 764-820 1.49e-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: 1.49e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 11120710    764 GPEGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGSIGFPGPLGPLGEKGKRGKA 820
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 723-866 2.29e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.27  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   723 EKGERGEDGFPGFKGDEGPKGDRGNPGLPGPRGEDGPEGQKGPEGLPGDEGPPGAAGEKGKLGVPGLPGyPGRPGPKGSI 802
Cdd:PHA03169   77 EESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPG-PHEPAPPESH 155

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11120710   803 GFPGPLGPLGEKGKRGKAG-QPGEEGERGTPGTRGDRGQPGATGQPGPKGDVGQngSPGAPGEKG 866
Cdd:PHA03169  156 NPSPNQQPSSFLQPSHEDSpEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPD--EPGEPQSPT 218
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1394-1450 2.53e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 2.53e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 11120710   1394 GLKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPGLQGDPGLPGPVGSLGHPGPP 1450
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 981-1033 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 11120710    981 APGDPGPIGLKGDKGPPGPLGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPA 1033
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 677-727 4.18e-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: 4.18e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 11120710    677 GPPGHPGHEGPTGEKGAQGPPGSAGPQGYPGPRGVKGTSGNRGLQGEKGER 727
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 690-862 4.40e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.49  E-value: 4.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   690 EKGAQGPPGSAGPQGYPGPRGVKGTSGNRGLQGEKGERGEDGFPgfKGDEGPKGDRGNPGLPGPrGEDGPEGQKGPEGlp 769
Cdd:PHA03169   85 EERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSP--ESPASHSPPPSPPSHPGP-HEPAPPESHNPSP-- 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   770 gDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGSIGFPGPLGPLGEKGKRGkAGQPGEEGERGTPGTRGDRGQPGATGQPGP 849
Cdd:PHA03169  160 -NQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSP-PDEPGEPQSPTPQQAPSPNTQQAVEHEDEP 237

                         170
                  ....*....|...
gi 11120710   850 KGDVGQNGSPGAP 862
Cdd:PHA03169  238 TEPEREGPPFPGH 250
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 584-920 4.65e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 4.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   584 GPPGPTGQAGEPGPRGLIGPRGPPGPLGRPGVTGSDGAPGAKGNVGPPGEPGPPGQQGNHGSQGIPGPQGPIGTPGEKGP 663
Cdd:PRK07764  388 AGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPA 467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   664 PGNPGIPGVPGSEGPPGHPGHEGPTGEKGAQGPPGSAGPQGYPGPRG--------VKGTS--------------GNRG-- 719
Cdd:PRK07764  468 PAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRErwpeilaaVPKRSrktwaillpeatvlGVRGdt 547

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   720 --------------------------LQGEKGER--------GEDGFPGFKGDEGPKGDRGNPGLPGPRGEDGPEGQKGP 765
Cdd:PRK07764  548 lvlgfstgglarrfaspgnaevlvtaLAEELGGDwqveavvgPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAP 627

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11120710   766 eglpgdeGPPGAAGEKGKLGVPGLPGYPGRPGPKGSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTPG-TRGDRGQPGAT 844
Cdd:PRK07764  628 -------APAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAaPAAPAGAAPAQ 700

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11120710   845 GQPGPkgdvgqngSPGAPGEKGLPGLQGPPGFPGPKGPPGPQGKDGIPGHPGQRGELGFQGQTGPPGPAGVLGPQG 920
Cdd:PRK07764  701 PAPAP--------AATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAA 768
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH