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Conserved domains on  [gi|1387538388|ref|XP_024895811|]
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collagen alpha-1(XX) chain isoform X2 [Pteropus alecto]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 15-177 6.94e-85

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


:

Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 272.62  E-value: 6.94e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   15 DLIFLVDGSWSIGHSHFRQVKDFLASIIKPFEIGPDKVQVGLTQYSGDPQTEWDLNTFHTKEEVLAAVHSLRYKGGNTFT 94
Cdd:cd01482      2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   95 GLALTHVLRQSLRPAAGPRPEAAKVVILVTDGKSQDDAHAAGRVLKDLDVDVFAVGVKNADEAELRLLASQPLDVTVHSV 174
Cdd:cd01482     82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFNV 161


                   ...
gi 1387538388  175 PDF 177
Cdd:cd01482    162 ADF 164
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 680-874 4.55e-29

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: 115.15  E-value: 4.55e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   680 GFDLMAAFGLAQKEYASIRGVAMEPSAlgPAmtFTLFKDAQLTRRASDIHLAALPTEHTVVFLLRLlpeTPREAFALWQM 759
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPGS--PA--YRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   760 TAEDFQPVLGVLLDASRRSLTYFSHHPRAALQEVTFdlpEVRRIFYGSFHKVHVAVGHSKVRLYVDCQKVAERPIGEAGS 839
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSF---RNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ 150

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1387538388   840 PPAT--GFVTLGRLAKARGPrsssAALQLQMLQIVCS 874
Cdd:smart00210  151 PPIDtdGIEVRGAQAADRKP----FQGDLQQLKIVCD 183
fn3 pfam00041
Fibronectin type III domain;
580-658 2.15e-15

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.45  E-value: 2.15e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  580 SPPSGLALDSESPNSLRVSWTPP---SGHVLYYRVTYVLASGSGPEKSVSIPGPRSQATLLDLLAATKYRVLVSAVYEAG 656
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ..
gi 1387538388  657 ES 658
Cdd:pfam00041   81 EG 82
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
439-680 2.94e-15

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 80.43  E-value: 2.94e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  439 SGQTEAPGNATSAILGPLASSTTYTVHVTCLHPGGRS--SRMTGRLTTRKVPS-PSQLSVTELPGDKVRLEWAAAAASGV 515
Cdd:COG3401    182 TTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESapSNEVSVTTPTTPPSaPTGLTATADTPGSVTLSWDPVTESDA 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  516 LVYQIKWLPLGDGKAHEISVPGNLG---TAVLPGlgrhSEYEITILAYYGDGARSEP---VSLRYTPLRWSPPSGLALDS 589
Cdd:COG3401    262 TGYRVYRSNSGDGPFTKVATVTTTSytdTGLTNG----TTYYYRVTAVDAAGNESAPsnvVSVTTDLTPPAAPSGLTATA 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  590 ESPNSLRVSWTPPSG-HVLYYRVtYVLASGSGPEKSVSIPGPRSQATLLDLLAATKYRVLVSAVYEAGE----SVAVSAT 664
Cdd:COG3401    338 VGSSSITLSWTASSDaDVTGYNV-YRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNesapSEEVSAT 416

                          250
                   ....*....|....*.
gi 1387538388  665 GRTACPALHPNSSVAG 680
Cdd:COG3401    417 TASAASGESLTASVDA 432
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
216-464 2.70e-14

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 77.35  E-value: 2.70e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  216 PLSAPTSLVLTQVTFSSVRLSWTPAPQLPLK-YLVtWRPSRGGAPREVVVEGPSASAELHNLTSSTEYLVSVAPVYEAGV 294
Cdd:COG3401    232 PPSAPTGLTATADTPGSVTLSWDPVTESDATgYRV-YRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGN 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  295 GEGLRGLVT----TGPLPPPQGLTLATVTPRTIRLTWQPSAG--ATQYLV-RcspaspKGEEDGMEVRVGL----PEVLL 363
Cdd:COG3401    311 ESAPSNVVSvttdLTPPAAPSGLTATAVGSSSITLSWTASSDadVTGYNVyR------STSGGGTYTKIAEtvttTSYTD 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  364 DGLEPGRDYSVWVRSL----RGSEASEARGIRAKTRPPGPPKHLGFSDVSHDSARVFWEGTPRPVRPCRVSYVSGEGGHS 439
Cdd:COG3401    385 TGLTPGTTYYYKVTAVdaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDT 464

                          250       260
                   ....*....|....*....|....*
gi 1387538388  440 GQTEAPGNATSAILGPLASSTTYTV 464
Cdd:COG3401    465 GNAVPFTTTSSTVTATTTDTTTANL 489
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1022-1185 2.29e-10

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 64.16  E-value: 2.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388 1022 QGTPGRVGLQGPKGMRGLEGAAGLPGPPGPRGFQGVAGARGTGGERGPAGAVGPTGLPGPKGERGEKGEPqslatiyqlv 1101
Cdd:NF038329   125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ---------- 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388 1102 SQACESAiqiyllKSSPFPHVSTRPPRPILEAPAPPSMHSEAGLPRSEDRGEPGAHGRASPP-PRRLGGVAGLAG-HGL- 1178
Cdd:NF038329   195 GPRGETG------PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQgPDGPAGKDGPRGdRGEa 268


                   ....*..
gi 1387538388 1179 GPQRQAG 1185
Cdd:NF038329   269 GPDGPDG 275
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 887-1091 5.85e-03

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: 40.66  E-value: 5.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  887 PALMDGEACPTPPSACTCPPQAPGPPGPqgppglpgrggapgqqgFPGPRGEPGPPGQMGPEGPGGQQGSPGTQGRTVQG 966
Cdd:NF038329   145 PAGPAGPPGPQGERGEKGPAGPQGEAGP-----------------QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  967 PMGPPGVKGQKGDHGLPGLQVAGSDHAQARggglgagppapgqarphlasasvlfQGTPGRVGLQGPKGMRGLEGAAGLP 1046
Cdd:NF038329   208 PAGPAGPDGEAGPAGEDGPAGPAGDGQQGP-------------------------DGDPGPTGEDGPQGPDGPAGKDGPR 262

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1387538388 1047 GPPGPRGFQGVAGARGTGGERGPAG---AVGPTGLPGPKGERGEKGEP 1091
Cdd:NF038329   263 GDRGEAGPDGPDGKDGERGPVGPAGkdgQNGKDGLPGKDGKDGQNGKD 310
 
Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 15-177 6.94e-85

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 272.62  E-value: 6.94e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   15 DLIFLVDGSWSIGHSHFRQVKDFLASIIKPFEIGPDKVQVGLTQYSGDPQTEWDLNTFHTKEEVLAAVHSLRYKGGNTFT 94
Cdd:cd01482      2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   95 GLALTHVLRQSLRPAAGPRPEAAKVVILVTDGKSQDDAHAAGRVLKDLDVDVFAVGVKNADEAELRLLASQPLDVTVHSV 174
Cdd:cd01482     82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFNV 161


                   ...
gi 1387538388  175 PDF 177
Cdd:cd01482    162 ADF 164
VWA pfam00092
von Willebrand factor type A domain;
15-181 6.57e-61

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 205.59  E-value: 6.57e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   15 DLIFLVDGSWSIGHSHFRQVKDFLASIIKPFEIGPDKVQVGLTQYSGDPQTEWDLNTFHTKEEVLAAVHSLRYKGGNT-F 93
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   94 TGLALTHVLRQSLRPAAGPRPEAAKVVILVTDGKSQD-DAHAAGRVLKDLDVDVFAVGVKNADEAELRLLASQPLDVTVH 172
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160


                   ....*....
gi 1387538388  173 SVPDFPQLG 181
Cdd:pfam00092  161 TVSDFEALE 169
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 15-180 2.59e-46

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 164.16  E-value: 2.59e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388    15 DLIFLVDGSWSIGHSHFRQVKDFLASIIKPFEIGPDKVQVGLTQYSGDPQTEWDLNTFHTKEEVLAAVHSLRYK-GGNTF 93
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388    94 TGLALTHVLRQSLRPAAGPRPEAAKVVILVTDGKSQD---DAHAAGRVLKDLDVDVFAVGVKNA-DEAELRLLASQPLDV 169
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160

                           170
                    ....*....|.
gi 1387538388   170 TVHSVPDFPQL 180
Cdd:smart00327  161 YVFLPELLDLL 171
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 680-874 4.55e-29

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 115.15  E-value: 4.55e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   680 GFDLMAAFGLAQKEYASIRGVAMEPSAlgPAmtFTLFKDAQLTRRASDIHLAALPTEHTVVFLLRLlpeTPREAFALWQM 759
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPGS--PA--YRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   760 TAEDFQPVLGVLLDASRRSLTYFSHHPRAALQEVTFdlpEVRRIFYGSFHKVHVAVGHSKVRLYVDCQKVAERPIGEAGS 839
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSF---RNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ 150

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1387538388   840 PPAT--GFVTLGRLAKARGPrsssAALQLQMLQIVCS 874
Cdd:smart00210  151 PPIDtdGIEVRGAQAADRKP----FQGDLQQLKIVCD 183
fn3 pfam00041
Fibronectin type III domain;
580-658 2.15e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.45  E-value: 2.15e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  580 SPPSGLALDSESPNSLRVSWTPP---SGHVLYYRVTYVLASGSGPEKSVSIPGPRSQATLLDLLAATKYRVLVSAVYEAG 656
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ..
gi 1387538388  657 ES 658
Cdd:pfam00041   81 EG 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
439-680 2.94e-15

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 80.43  E-value: 2.94e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  439 SGQTEAPGNATSAILGPLASSTTYTVHVTCLHPGGRS--SRMTGRLTTRKVPS-PSQLSVTELPGDKVRLEWAAAAASGV 515
Cdd:COG3401    182 TTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESapSNEVSVTTPTTPPSaPTGLTATADTPGSVTLSWDPVTESDA 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  516 LVYQIKWLPLGDGKAHEISVPGNLG---TAVLPGlgrhSEYEITILAYYGDGARSEP---VSLRYTPLRWSPPSGLALDS 589
Cdd:COG3401    262 TGYRVYRSNSGDGPFTKVATVTTTSytdTGLTNG----TTYYYRVTAVDAAGNESAPsnvVSVTTDLTPPAAPSGLTATA 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  590 ESPNSLRVSWTPPSG-HVLYYRVtYVLASGSGPEKSVSIPGPRSQATLLDLLAATKYRVLVSAVYEAGE----SVAVSAT 664
Cdd:COG3401    338 VGSSSITLSWTASSDaDVTGYNV-YRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNesapSEEVSAT 416

                          250
                   ....*....|....*.
gi 1387538388  665 GRTACPALHPNSSVAG 680
Cdd:COG3401    417 TASAASGESLTASVDA 432
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
216-464 2.70e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 77.35  E-value: 2.70e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  216 PLSAPTSLVLTQVTFSSVRLSWTPAPQLPLK-YLVtWRPSRGGAPREVVVEGPSASAELHNLTSSTEYLVSVAPVYEAGV 294
Cdd:COG3401    232 PPSAPTGLTATADTPGSVTLSWDPVTESDATgYRV-YRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGN 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  295 GEGLRGLVT----TGPLPPPQGLTLATVTPRTIRLTWQPSAG--ATQYLV-RcspaspKGEEDGMEVRVGL----PEVLL 363
Cdd:COG3401    311 ESAPSNVVSvttdLTPPAAPSGLTATAVGSSSITLSWTASSDadVTGYNVyR------STSGGGTYTKIAEtvttTSYTD 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  364 DGLEPGRDYSVWVRSL----RGSEASEARGIRAKTRPPGPPKHLGFSDVSHDSARVFWEGTPRPVRPCRVSYVSGEGGHS 439
Cdd:COG3401    385 TGLTPGTTYYYKVTAVdaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDT 464

                          250       260
                   ....*....|....*....|....*
gi 1387538388  440 GQTEAPGNATSAILGPLASSTTYTV 464
Cdd:COG3401    465 GNAVPFTTTSSTVTATTTDTTTANL 489
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 10-165 1.35e-13

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 72.28  E-value: 1.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   10 PPTPVDLIFLVDGSWS-IGHSHFRQVKDFLASIIKPFeigPDKVQVGLTQYSGDPQTEWDLNTfhTKEEVLAAVHSLRYK 88
Cdd:COG1240     89 PQRGRDVVLVVDASGSmAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTR--DREALKRALDELPPG 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   89 GGntfTglALTHVLRQSLRPAAGPRPEAAKVVILVTDGK---SQDDAHAAGRVLKDLDVDVFAVGV--KNADEAELRLLA 163
Cdd:COG1240    164 GG---T--PLGDALALALELLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVgtEAVDEGLLREIA 238


                   ..
gi 1387538388  164 SQ 165
Cdd:COG1240    239 EA 240
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 580-658 1.03e-12

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 65.21  E-value: 1.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  580 SPPSGLALDSESPNSLRVSWTPPS---GHVLYYRVTYVLASGSGPEKSVSIPGPRSQATLLDLLAATKYRVLVSAVYEAG 656
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                   ..
gi 1387538388  657 ES 658
Cdd:cd00063     82 ES 83
fn3 pfam00041
Fibronectin type III domain;
218-296 2.83e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 2.83e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  218 SAPTSLVLTQVTFSSVRLSWTPAPQLP---LKYLVTWRPSRGG-APREVVVEGPSASAELHNLTSSTEYLVSVAPVYEAG 293
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgpiTGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1387538388  294 VGE 296
Cdd:pfam00041   81 EGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 218-296 3.12e-12

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 63.67  E-value: 3.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  218 SAPTSLVLTQVTFSSVRLSWTPAPQLP---LKYLVTWRPSRGGAPREVVVEGPSA-SAELHNLTSSTEYLVSVAPVYEAG 293
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEDDGgpiTGYVVEYREKGSGDWKEVEVTPGSEtSYTLTGLKPGTEYEFRVRAVNGGG 81


                   ...
gi 1387538388  294 VGE 296
Cdd:cd00063     82 ESP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 580-658 4.66e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 63.02  E-value: 4.66e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   580 SPPSGLALDSESPNSLRVSWTPPS-----GHVLYYRVTYVlaSGSGPEKSVSIPGPRSQATLLDLLAATKYRVLVSAVYE 654
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYR--EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 1387538388   655 AGES 658
Cdd:smart00060   80 AGEG 83
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1022-1185 2.29e-10

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 64.16  E-value: 2.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388 1022 QGTPGRVGLQGPKGMRGLEGAAGLPGPPGPRGFQGVAGARGTGGERGPAGAVGPTGLPGPKGERGEKGEPqslatiyqlv 1101
Cdd:NF038329   125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ---------- 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388 1102 SQACESAiqiyllKSSPFPHVSTRPPRPILEAPAPPSMHSEAGLPRSEDRGEPGAHGRASPP-PRRLGGVAGLAG-HGL- 1178
Cdd:NF038329   195 GPRGETG------PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQgPDGPAGKDGPRGdRGEa 268


                   ....*..
gi 1387538388 1179 GPQRQAG 1185
Cdd:NF038329   269 GPDGPDG 275
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 965-1091 2.46e-10

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 64.16  E-value: 2.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  965 QGPMGPPGVKGQKGDHGLPGlqvagsdhaqarggglgagppapgQARPHLASASVLFQGTPGRVGLQGPKGMRGlEGAAG 1044
Cdd:NF038329   170 AGPQGPAGKDGEAGAKGPAG------------------------EKGPQGPRGETGPAGEQGPAGPAGPDGEAG-PAGED 224

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1387538388 1045 LPGPPGPRGFQGVAGARGTGGERGPAGAVGPTGLPGPKGERGEKGEP 1091
Cdd:NF038329   225 GPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD 271
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 965-1091 3.97e-10

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 63.39  E-value: 3.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  965 QGPMGPPGVKGQKGDHGLPGLQVAGSDHAQARGGGLGAGPPAPGQarphlasasvlfQGTPGRVGLQGPKGMRGLEGAAG 1044
Cdd:NF038329   122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGP------------QGEAGPQGPAGKDGEAGAKGPAG 189

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1387538388 1045 LPGPPGPRGFQGVAGARGTGGERGPAGAVGPTGLPGPKG-----ERGEKGEP 1091
Cdd:NF038329   190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDP 241
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 218-295 8.22e-10

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 56.47  E-value: 8.22e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   218 SAPTSLVLTQVTFSSVRLSWT-PAPQLPLKYLVTWRPSRGGAP---REVVVEGPSASAELHNLTSSTEYLVSVAPVYEAG 293
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEpPPDDGITGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1387538388   294 VG 295
Cdd:smart00060   82 EG 83
fn3 pfam00041
Fibronectin type III domain;
488-564 1.24e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.88  E-value: 1.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  488 PSPSQLSVTELPGDKVRLEWAAAAASG--VLVYQIKWLPLGDGKA-HEISVPGNLGTAVLPGLGRHSEYEITILAYYGDG 564
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgpITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1029-1091 1.36e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.41  E-value: 1.36e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387538388 1029 GLQGPKGMRGlegaaglpgPPGPRGFQGVAGARGTGGERGPAGAVGPTGLPGPKGERGEKGEP 1091
Cdd:pfam01391    1 GPPGPPGPPG---------PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 490-573 4.19e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 4.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  490 PSQLSVTELPGDKVRLEWAAAAASG--VLVYQIKWLPLGDGKAHEISV-PGNLGTAVLPGLGRHSEYEITILAYY--GDG 564
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDDGgpITGYVVEYREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVNggGES 83


                   ....*....
gi 1387538388  565 ARSEPVSLR 573
Cdd:cd00063     84 PPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 488-564 8.20e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 45.30  E-value: 8.20e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   488 PSPSQLSVTELPGDKVRLEWAAAAASGVLVYQIKWLPLGDGKA---HEISVPGNLGTAVLPGLGRHSEYEITILAYYGDG 564
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 14-151 9.83e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 46.50  E-value: 9.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   14 VDLIFLVDGSWSIG-HSHFRQVKDFLASIIKPFEIGPDKVQVGLTQYSGDPQTEWDLNTFHT--KEEVLAAVHSLRyKG- 89
Cdd:PTZ00441    43 VDLYLLVDGSGSIGyHNWITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASkdKEQALIIVKSLR-KTy 121

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387538388   90 ---GNTFTGLALTHVlRQSLRPAAGpRPEAAKVVILVTDG--KSQDDAHAAGRVLKDLDVDVFAVGV 151
Cdd:PTZ00441   122 lpyGKTNMTDALLEV-RKHLNDRVN-RENAIQLVILMTDGipNSKYRALEESRKLKDRNVKLAVIGI 186
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 887-1091 5.85e-03

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: 40.66  E-value: 5.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  887 PALMDGEACPTPPSACTCPPQAPGPPGPqgppglpgrggapgqqgFPGPRGEPGPPGQMGPEGPGGQQGSPGTQGRTVQG 966
Cdd:NF038329   145 PAGPAGPPGPQGERGEKGPAGPQGEAGP-----------------QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  967 PMGPPGVKGQKGDHGLPGLQVAGSDHAQARggglgagppapgqarphlasasvlfQGTPGRVGLQGPKGMRGLEGAAGLP 1046
Cdd:NF038329   208 PAGPAGPDGEAGPAGEDGPAGPAGDGQQGP-------------------------DGDPGPTGEDGPQGPDGPAGKDGPR 262

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1387538388 1047 GPPGPRGFQGVAGARGTGGERGPAG---AVGPTGLPGPKGERGEKGEP 1091
Cdd:NF038329   263 GDRGEAGPDGPDGKDGERGPVGPAGkdgQNGKDGLPGKDGKDGQNGKD 310
 
Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 15-177 6.94e-85

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 272.62  E-value: 6.94e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   15 DLIFLVDGSWSIGHSHFRQVKDFLASIIKPFEIGPDKVQVGLTQYSGDPQTEWDLNTFHTKEEVLAAVHSLRYKGGNTFT 94
Cdd:cd01482      2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   95 GLALTHVLRQSLRPAAGPRPEAAKVVILVTDGKSQDDAHAAGRVLKDLDVDVFAVGVKNADEAELRLLASQPLDVTVHSV 174
Cdd:cd01482     82 GKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFNV 161


                   ...
gi 1387538388  175 PDF 177
Cdd:cd01482    162 ADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 14-177 5.74e-71

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 233.66  E-value: 5.74e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   14 VDLIFLVDGSWSIGHSHFRQVKDFLASIIKPFEIGPDKVQVGLTQYSGDPQTEWDLNTFHTKEEVLAAVHSLRYKGGNTF 93
Cdd:cd01472      1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   94 TGLALTHVLRQSLRPAAGPRPEAAKVVILVTDGKSQDDAHAAGRVLKDLDVDVFAVGVKNADEAELRLLASQPLDVTVHS 173
Cdd:cd01472     81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                   ....
gi 1387538388  174 VPDF 177
Cdd:cd01472    161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
15-181 6.57e-61

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 205.59  E-value: 6.57e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   15 DLIFLVDGSWSIGHSHFRQVKDFLASIIKPFEIGPDKVQVGLTQYSGDPQTEWDLNTFHTKEEVLAAVHSLRYKGGNT-F 93
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   94 TGLALTHVLRQSLRPAAGPRPEAAKVVILVTDGKSQD-DAHAAGRVLKDLDVDVFAVGVKNADEAELRLLASQPLDVTVH 172
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160


                   ....*....
gi 1387538388  173 SVPDFPQLG 181
Cdd:pfam00092  161 TVSDFEALE 169
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 14-168 1.94e-55

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 189.81  E-value: 1.94e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   14 VDLIFLVDGSWSIGHSHFRQVKDFLASIIKPFEIGPDKVQVGLTQYSGDPQTEWDLNTFHTKEEVLAAVHSLRYKGGN-T 92
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387538388   93 FTGLALTHVLRQSLRPAAgPRPEAAKVVILVTDGKSQD--DAHAAGRVLKDLDVDVFAVGVKNADEAELRLLASQPLD 168
Cdd:cd01450     81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSE 157
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 15-180 2.59e-46

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 164.16  E-value: 2.59e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388    15 DLIFLVDGSWSIGHSHFRQVKDFLASIIKPFEIGPDKVQVGLTQYSGDPQTEWDLNTFHTKEEVLAAVHSLRYK-GGNTF 93
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388    94 TGLALTHVLRQSLRPAAGPRPEAAKVVILVTDGKSQD---DAHAAGRVLKDLDVDVFAVGVKNA-DEAELRLLASQPLDV 169
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160

                           170
                    ....*....|.
gi 1387538388   170 TVHSVPDFPQL 180
Cdd:smart00327  161 YVFLPELLDLL 171
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 13-193 6.87e-46

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 164.87  E-value: 6.87e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   13 PVDLIFLVDGSWSIGHSHFRQVKDFLASIIKPFEIGPDKVQVGLTQYSGDPQTEWDLNTFHTKEEVLAAVHSLRYKGGNT 92
Cdd:cd01475      2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   93 FTGLALTHVLRQSLRPAAGPRPEAA---KVVILVTDGKSQDDAHAAGRVLKDLDVDVFAVGVKNADEAELRLLASQPLDV 169
Cdd:cd01475     82 MTGLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161

                          170       180
                   ....*....|....*....|....
gi 1387538388  170 TVHSVPDFPQLGMLAGLLSRLICQ 193
Cdd:cd01475    162 HVFYVEDFSTIEELTKKFQGKICV 185
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 14-181 2.43e-39

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 144.04  E-value: 2.43e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   14 VDLIFLVDGSWSIGHSHFRQVKDFLASIIKPFEIGPDKVQVGLTQYSGDPQTEWDLNTFHTKEEVLAAVHSLRYKGGNTF 93
Cdd:cd01469      1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   94 TGLALTHVLRQSLRPAAGPRPEAAKVVILVTDGKSQDDA--HAAGRVLKDLDVDVFAVGV------KNADEaELRLLASQ 165
Cdd:cd01469     81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPllKDVIPQAEREGIIRYAIGVgghfqrENSRE-ELKTIASK 159

                          170
                   ....*....|....*.
gi 1387538388  166 PLDVTVHSVPDFPQLG 181
Cdd:cd01469    160 PPEEHFFNVTDFAALK 175
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 15-177 1.00e-38

VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238758  Cd Length: 165  Bit Score: 142.08  E-value: 1.00e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   15 DLIFLVDGSWSIGHSHFRQVKDFLASIIKPFEIGPDKVQVGLTQYSGDPQTEWDLNTFHTKEEVLAAVHSLRYKGGNTF- 93
Cdd:cd01481      2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLn 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   94 TGLALTHVLRQSLRPAAGPRPEAA--KVVILVTDGKSQDDAHAAGRVLKDLDVDVFAVGVKNADEAELRLLASQPldVTV 171
Cdd:cd01481     82 TGSALDYVVKNLFTKSAGSRIEEGvpQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP--SFV 159


                   ....*.
gi 1387538388  172 HSVPDF 177
Cdd:cd01481    160 FQVSDF 165
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 680-874 4.55e-29

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 115.15  E-value: 4.55e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   680 GFDLMAAFGLAQKEYASIRGVAMEPSAlgPAmtFTLFKDAQLTRRASDIHLAALPTEHTVVFLLRLlpeTPREAFALWQM 759
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPGS--PA--YRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   760 TAEDFQPVLGVLLDASRRSLTYFSHHPRAALQEVTFdlpEVRRIFYGSFHKVHVAVGHSKVRLYVDCQKVAERPIGEAGS 839
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSF---RNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ 150

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1387538388   840 PPAT--GFVTLGRLAKARGPrsssAALQLQMLQIVCS 874
Cdd:smart00210  151 PPIDtdGIEVRGAQAADRKP----FQGDLQQLKIVCD 183
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 15-163 1.22e-28

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 112.88  E-value: 1.22e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   15 DLIFLVDGSWSIGHShFRQVKDFLASIIKPFEIGPDKVQVGLTQYSGDPQT--EWDLNTFHTKEEVLAAVHSLRYKGGNT 92
Cdd:cd01476      2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387538388   93 FTGLALTHVLRQsLRPAAGPRPEAAKVVILVTDGKSQDDAHAAGRVLKDL-DVDVFAVGVK---NADEAELRLLA 163
Cdd:cd01476     81 ATGAAIEVALQQ-LDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGdpgTVDTEELHSIT 154
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 14-171 1.46e-28

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 112.66  E-value: 1.46e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   14 VDLIFLVDGSWSIGHSHFRQVKDFLASIIKPFEIGPDKVQVGLTQYSGDPQTEWDLNTFHTKEEVLAAVHSLRYK-GGNT 92
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   93 FTGLALTHVLRQSLRPAagpRPEAAKVVILVTDGKSQDD---AHAAGRVLKDLDVDVFAVGVKN-ADEAELRLLASQPLD 168
Cdd:cd00198     81 NIGAALRLALELLKSAK---RPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGDdANEDELKEIADKTTG 157


                   ...
gi 1387538388  169 VTV 171
Cdd:cd00198    158 GAV 160
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 14-168 5.51e-24

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 100.54  E-value: 5.51e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   14 VDLIFLVDGSWSIGHSH-FRQVKDFLASIIKPFEIGPDKVQVGLTQYSGDPQTEWDLNTFHT--KEEVLAAVHSLR---Y 87
Cdd:cd01471      1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNStnKDLALNAIRALLslyY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   88 KGGNTFTGLALTHVlRQSLRPAAGPRPEAAKVVILVTDGKSQDDAHA--AGRVLKDLDVD--VFAVG--VKNadeAELRL 161
Cdd:cd01471     81 PNGSTNTTSALLVV-EKHLFDTRGNRENAPQLVIIMTDGIPDSKFRTlkEARKLRERGVIiaVLGVGqgVNH---EENRS 156


                   ....*..
gi 1387538388  162 LASQPLD 168
Cdd:cd01471    157 LVGCDPD 163
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 13-167 5.88e-18

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 83.20  E-value: 5.88e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   13 PVDLIFLVDGSWSIGHSHFRQVKDFLASIIKPF------EIGPDKVQVGLTQYSGDPQTEWDLNTFHTKEEVLA-AVHSL 85
Cdd:cd01480      2 PVDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTSLKeAVDNL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   86 RYKGGNTFTGLALTHVLRQSLRpaaGPRPEAAKVVILVTDGKSQ-DDAHAAGRVLKDLD---VDVFAVGVKNADEAELRL 161
Cdd:cd01480     82 EYIGGGTFTDCALKYATEQLLE---GSHQKENKFLLVITDGHSDgSPDGGIEKAVNEADhlgIKIFFVAVGSQNEEPLSR 158


                   ....*.
gi 1387538388  162 LASQPL 167
Cdd:cd01480    159 IACDGK 164
fn3 pfam00041
Fibronectin type III domain;
580-658 2.15e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.45  E-value: 2.15e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  580 SPPSGLALDSESPNSLRVSWTPP---SGHVLYYRVTYVLASGSGPEKSVSIPGPRSQATLLDLLAATKYRVLVSAVYEAG 656
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ..
gi 1387538388  657 ES 658
Cdd:pfam00041   81 EG 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
439-680 2.94e-15

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 80.43  E-value: 2.94e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  439 SGQTEAPGNATSAILGPLASSTTYTVHVTCLHPGGRS--SRMTGRLTTRKVPS-PSQLSVTELPGDKVRLEWAAAAASGV 515
Cdd:COG3401    182 TTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESapSNEVSVTTPTTPPSaPTGLTATADTPGSVTLSWDPVTESDA 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  516 LVYQIKWLPLGDGKAHEISVPGNLG---TAVLPGlgrhSEYEITILAYYGDGARSEP---VSLRYTPLRWSPPSGLALDS 589
Cdd:COG3401    262 TGYRVYRSNSGDGPFTKVATVTTTSytdTGLTNG----TTYYYRVTAVDAAGNESAPsnvVSVTTDLTPPAAPSGLTATA 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  590 ESPNSLRVSWTPPSG-HVLYYRVtYVLASGSGPEKSVSIPGPRSQATLLDLLAATKYRVLVSAVYEAGE----SVAVSAT 664
Cdd:COG3401    338 VGSSSITLSWTASSDaDVTGYNV-YRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNesapSEEVSAT 416

                          250
                   ....*....|....*.
gi 1387538388  665 GRTACPALHPNSSVAG 680
Cdd:COG3401    417 TASAASGESLTASVDA 432
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
216-464 2.70e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 77.35  E-value: 2.70e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  216 PLSAPTSLVLTQVTFSSVRLSWTPAPQLPLK-YLVtWRPSRGGAPREVVVEGPSASAELHNLTSSTEYLVSVAPVYEAGV 294
Cdd:COG3401    232 PPSAPTGLTATADTPGSVTLSWDPVTESDATgYRV-YRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGN 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  295 GEGLRGLVT----TGPLPPPQGLTLATVTPRTIRLTWQPSAG--ATQYLV-RcspaspKGEEDGMEVRVGL----PEVLL 363
Cdd:COG3401    311 ESAPSNVVSvttdLTPPAAPSGLTATAVGSSSITLSWTASSDadVTGYNVyR------STSGGGTYTKIAEtvttTSYTD 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  364 DGLEPGRDYSVWVRSL----RGSEASEARGIRAKTRPPGPPKHLGFSDVSHDSARVFWEGTPRPVRPCRVSYVSGEGGHS 439
Cdd:COG3401    385 TGLTPGTTYYYKVTAVdaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDT 464

                          250       260
                   ....*....|....*....|....*
gi 1387538388  440 GQTEAPGNATSAILGPLASSTTYTV 464
Cdd:COG3401    465 GNAVPFTTTSSTVTATTTDTTTANL 489
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 10-165 1.35e-13

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 72.28  E-value: 1.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   10 PPTPVDLIFLVDGSWS-IGHSHFRQVKDFLASIIKPFeigPDKVQVGLTQYSGDPQTEWDLNTfhTKEEVLAAVHSLRYK 88
Cdd:COG1240     89 PQRGRDVVLVVDASGSmAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTR--DREALKRALDELPPG 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   89 GGntfTglALTHVLRQSLRPAAGPRPEAAKVVILVTDGK---SQDDAHAAGRVLKDLDVDVFAVGV--KNADEAELRLLA 163
Cdd:COG1240    164 GG---T--PLGDALALALELLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVgtEAVDEGLLREIA 238


                   ..
gi 1387538388  164 SQ 165
Cdd:COG1240    239 EA 240
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 580-658 1.03e-12

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 65.21  E-value: 1.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  580 SPPSGLALDSESPNSLRVSWTPPS---GHVLYYRVTYVLASGSGPEKSVSIPGPRSQATLLDLLAATKYRVLVSAVYEAG 656
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                   ..
gi 1387538388  657 ES 658
Cdd:cd00063     82 ES 83
fn3 pfam00041
Fibronectin type III domain;
218-296 2.83e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 2.83e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  218 SAPTSLVLTQVTFSSVRLSWTPAPQLP---LKYLVTWRPSRGG-APREVVVEGPSASAELHNLTSSTEYLVSVAPVYEAG 293
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgpiTGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1387538388  294 VGE 296
Cdd:pfam00041   81 EGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 218-296 3.12e-12

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 63.67  E-value: 3.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  218 SAPTSLVLTQVTFSSVRLSWTPAPQLP---LKYLVTWRPSRGGAPREVVVEGPSA-SAELHNLTSSTEYLVSVAPVYEAG 293
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEDDGgpiTGYVVEYREKGSGDWKEVEVTPGSEtSYTLTGLKPGTEYEFRVRAVNGGG 81


                   ...
gi 1387538388  294 VGE 296
Cdd:cd00063     82 ESP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 580-658 4.66e-12

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 63.02  E-value: 4.66e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   580 SPPSGLALDSESPNSLRVSWTPPS-----GHVLYYRVTYVlaSGSGPEKSVSIPGPRSQATLLDLLAATKYRVLVSAVYE 654
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYR--EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 1387538388   655 AGES 658
Cdd:smart00060   80 AGEG 83
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 15-163 1.55e-10

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 61.56  E-value: 1.55e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   15 DLIFLVDGSWSIGHSHFR-QVKDFLASIIKPFEIGPDKVQVGLTQYSG---DPQTEWDLNTFHtKEEVLAAVHSLR--YK 88
Cdd:cd01473      2 DLTLILDESASIGYSNWRkDVIPFTEKIINNLNISKDKVHVGILLFAEknrDVVPFSDEERYD-KNELLKKINDLKnsYR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   89 -GGNTFTGLALTHVLRQSLRpAAGPRPEAAKVVILVTDG----KSQDDAHAAGRVLKDLDVDVFAVGVKNADEAELRLLA 163
Cdd:cd01473     81 sGGETYIVEALKYGLKNYTK-HGNRRKDAPKVTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLA 159
VWA_2 pfam13519
von Willebrand factor type A domain;
16-123 2.14e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 58.84  E-value: 2.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   16 LIFLVDGSWSI-----GHSHFRQVKDFLASIIKPFeigpDKVQVGLTQYSGDPQTEWDLNTfhTKEEVLAAVHSLRYKGG 90
Cdd:pfam13519    1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSL----PGDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1387538388   91 NTFTGLALTHVLRQSLRPAAGPRpeaaKVVILV 123
Cdd:pfam13519   75 GTNLAAALQLARAALKHRRKNQP----RRIVLI 103
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1022-1185 2.29e-10

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 64.16  E-value: 2.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388 1022 QGTPGRVGLQGPKGMRGLEGAAGLPGPPGPRGFQGVAGARGTGGERGPAGAVGPTGLPGPKGERGEKGEPqslatiyqlv 1101
Cdd:NF038329   125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ---------- 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388 1102 SQACESAiqiyllKSSPFPHVSTRPPRPILEAPAPPSMHSEAGLPRSEDRGEPGAHGRASPP-PRRLGGVAGLAG-HGL- 1178
Cdd:NF038329   195 GPRGETG------PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQgPDGPAGKDGPRGdRGEa 268


                   ....*..
gi 1387538388 1179 GPQRQAG 1185
Cdd:NF038329   269 GPDGPDG 275
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
261-594 2.45e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 64.64  E-value: 2.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  261 EVVVEGPSASAELHNLTSSTEYLVSVAPVYEAGVG---EGLRGLVTTGPLPPPQGLTLATVTPRTIRLTWQPSA--GATQ 335
Cdd:COG3401    184 SLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESapsNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTesDATG 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  336 YLV-RcspaspKGEEDGMEVRVGLPEVL--LD-GLEPGRDYSVWVRSLRG----SEASEARGIRAKTRPPGPPKHLGFSD 407
Cdd:COG3401    264 YRVyR------SNSGDGPFTKVATVTTTsyTDtGLTNGTTYYYRVTAVDAagneSAPSNVVSVTTDLTPPAAPSGLTATA 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  408 VSHDSARVFWEGTP-RPVRPCRVSYVSGEGGHSGQTEAPGNATSAILGPLASSTTYTVHVTCLHPGGRSSRMTGRLTTRK 486
Cdd:COG3401    338 VGSSSITLSWTASSdADVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATT 417

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  487 VPSPSQLSVTELP-----GDKVRLEWAAAAASGVLVYQIKWLPLGDGKAHEISVPGNLGTAVLPGLGRHSEYEITILAYY 561
Cdd:COG3401    418 ASAASGESLTASVdavplTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLV 497

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1387538388  562 GDGARSEPVSLRYTPLRWSPPSGLALDSESPNS 594
Cdd:COG3401    498 GGSGASSVTNSVSVIGASAAAAVGGAPDGTPNV 530
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 965-1091 2.46e-10

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 64.16  E-value: 2.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  965 QGPMGPPGVKGQKGDHGLPGlqvagsdhaqarggglgagppapgQARPHLASASVLFQGTPGRVGLQGPKGMRGlEGAAG 1044
Cdd:NF038329   170 AGPQGPAGKDGEAGAKGPAG------------------------EKGPQGPRGETGPAGEQGPAGPAGPDGEAG-PAGED 224

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1387538388 1045 LPGPPGPRGFQGVAGARGTGGERGPAGAVGPTGLPGPKGERGEKGEP 1091
Cdd:NF038329   225 GPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD 271
fn3 pfam00041
Fibronectin type III domain;
308-381 3.31e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.81  E-value: 3.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  308 PPPQGLTLATVTPRTIRLTWQPSAGA----TQYLVRCSPASpkGEEDGMEVRVGLPE--VLLDGLEPGRDYSVWVRSLRG 381
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGngpiTGYEVEYRPKN--SGEPWNEITVPGTTtsVTLTGLKPGTEYEVRVQAVNG 78
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 965-1091 3.97e-10

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 63.39  E-value: 3.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  965 QGPMGPPGVKGQKGDHGLPGLQVAGSDHAQARGGGLGAGPPAPGQarphlasasvlfQGTPGRVGLQGPKGMRGLEGAAG 1044
Cdd:NF038329   122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGP------------QGEAGPQGPAGKDGEAGAKGPAG 189

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1387538388 1045 LPGPPGPRGFQGVAGARGTGGERGPAGAVGPTGLPGPKG-----ERGEKGEP 1091
Cdd:NF038329   190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDP 241
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 218-295 8.22e-10

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 56.47  E-value: 8.22e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   218 SAPTSLVLTQVTFSSVRLSWT-PAPQLPLKYLVTWRPSRGGAP---REVVVEGPSASAELHNLTSSTEYLVSVAPVYEAG 293
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEpPPDDGITGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1387538388   294 VG 295
Cdd:smart00060   82 EG 83
fn3 pfam00041
Fibronectin type III domain;
488-564 1.24e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.88  E-value: 1.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  488 PSPSQLSVTELPGDKVRLEWAAAAASG--VLVYQIKWLPLGDGKA-HEISVPGNLGTAVLPGLGRHSEYEITILAYYGDG 564
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgpITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 308-386 2.70e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.20  E-value: 2.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  308 PPPQGLTLATVTPRTIRLTWQPSAGA----TQYLVRCspaSPKGEEDGMEVRVGLP---EVLLDGLEPGRDYSVWVRSLR 380
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEDDggpiTGYVVEY---REKGSGDWKEVEVTPGsetSYTLTGLKPGTEYEFRVRAVN 78


                   ....*.
gi 1387538388  381 GSEASE 386
Cdd:cd00063     79 GGGESP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 308-377 1.24e-08

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.00  E-value: 1.24e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387538388   308 PPPQGLTLATVTPRTIRLTWQP--SAGATQYLVRCSPASPKGEEDGMEVRVGLPE--VLLDGLEPGRDYSVWVR 377
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPppDDGITGYIVGYRVEYREEGSEWKEVNVTPSStsYTLTGLKPGTEYEFRVR 75
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 1-165 3.57e-08

Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 56.26  E-value: 3.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388    1 MAGPQFRCTPPTPVDLIFLVDGSWSIGHSHFRQVKDFLASIIKpfEIGPDkVQVGLTQYSGDPQTEWDLNTFHTKEEVLA 80
Cdd:COG2304     79 LQPPKAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVD--QLRPG-DRVSIVTFAGDARVLLPPTPATDRAKILA 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   81 AVHSLRyKGGNTFTGLALTHVLRQslrPAAGPRPEAAKVVILVTDGK------SQDDAHAAGRVLKDLDVDVFAVGV-KN 153
Cdd:COG2304    156 AIDRLQ-AGGGTALGAGLELAYEL---ARKHFIPGRVNRVILLTDGDanvgitDPEELLKLAEEAREEGITLTTLGVgSD 231

                          170
                   ....*....|..
gi 1387538388  154 ADEAELRLLASQ 165
Cdd:COG2304    232 YNEDLLERLADA 243
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
214-378 6.34e-08

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 57.26  E-value: 6.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  214 LDPLSAPTSLVLTQVTFSS----VRLSWTPAPQLpLKYLVTWRPSRGG---APREvvvegPSASAELHNLTSSTeYLVSV 286
Cdd:COG4733    531 WPPVNVTTSESLSVVAQGTavttLTVSWDAPAGA-VAYEVEWRRDDGNwvsVPRT-----SGTSFEVPGIYAGD-YEVRV 603

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  287 APVYEAGVGEGLRGLVTT------GPLPPPQGLTlATVTPRTIRLTWQPSAGA--TQYLVRCSPASPKGEEDGMEVRVGL 358
Cdd:COG4733    604 RAINALGVSSAWAASSETtvtgktAPPPAPTGLT-ATGGLGGITLSWSFPVDAdtLRTEIRYSTTGDWASATVAQALYPG 682

                          170       180
                   ....*....|....*....|
gi 1387538388  359 PEVLLDGLEPGRDYSVWVRS 378
Cdd:COG4733    683 NTYTLAGLKAGQTYYYRARA 702
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1029-1091 1.36e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.41  E-value: 1.36e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387538388 1029 GLQGPKGMRGlegaaglpgPPGPRGFQGVAGARGTGGERGPAGAVGPTGLPGPKGERGEKGEP 1091
Cdd:pfam01391    1 GPPGPPGPPG---------PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 490-573 4.19e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 4.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  490 PSQLSVTELPGDKVRLEWAAAAASG--VLVYQIKWLPLGDGKAHEISV-PGNLGTAVLPGLGRHSEYEITILAYY--GDG 564
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDDGgpITGYVVEYREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVNggGES 83


                   ....*....
gi 1387538388  565 ARSEPVSLR 573
Cdd:cd00063     84 PPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 397-475 4.89e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 4.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  397 PGPPKHLGFSDVSHDSARVFWE---GTPRPVRPCRVSYV-SGEGGHSGQTEAPGNATSAILGPLASSTTYTVHVTCLHPG 472
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTppeDDGGPITGYVVEYReKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                   ...
gi 1387538388  473 GRS 475
Cdd:cd00063     81 GES 83
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1023-1091 1.33e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.33  E-value: 1.33e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387538388 1023 GTPGRVGLQGPKGMRGlegaaglpgPPGPRGFQGVAGARgtgGERGPAGAVGPTGLPGPKGERGEKGEP 1091
Cdd:pfam01391    1 GPPGPPGPPGPPGPPG---------PPGPPGPPGPPGPP---GEPGPPGPPGPPGPPGPPGAPGAPGPP 57
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 397-475 3.02e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 46.45  E-value: 3.02e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   397 PGPPKHLGFSDVSHDSARVFWEgtpRPVRPCRVSYV-------SGEGGHSGQTEAPGNATSAILGPLASSTTYTVHVTCL 469
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWE---PPPDDGITGYIvgyrveyREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77


                    ....*.
gi 1387538388   470 HPGGRS 475
Cdd:smart00060   78 NGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 488-564 8.20e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 45.30  E-value: 8.20e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   488 PSPSQLSVTELPGDKVRLEWAAAAASGVLVYQIKWLPLGDGKA---HEISVPGNLGTAVLPGLGRHSEYEITILAYYGDG 564
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 15-166 1.83e-05

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 46.73  E-value: 1.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   15 DLIFLVDGSWSIGHsHFRQVKDFLASIIKPFEigpdkvqvgltqysgDPQTEWDLNTFHTKEEVLAAVHSLRYK------ 88
Cdd:cd01474      6 DLYFVLDKSGSVAA-NWIEIYDFVEQLVDRFN---------------SPGLRFSFITFSTRATKILPLTDDSSAiikgle 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   89 -------GGNTFTGLALTHVLRQSLRPAAGPRpEAAKVVILVTDGKSQDDAHAA----GRVLKDLDVDVFAVGVKNADEA 157
Cdd:cd01474     70 vlkkvtpSGQTYIHEGLENANEQIFNRNGGGR-ETVSVIIALTDGQLLLNGHKYpeheAKLSRKLGAIVYCVGVTDFLKS 148


                   ....*....
gi 1387538388  158 ELRLLASQP 166
Cdd:cd01474    149 QLINIADSK 157
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 14-151 9.83e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 46.50  E-value: 9.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388   14 VDLIFLVDGSWSIG-HSHFRQVKDFLASIIKPFEIGPDKVQVGLTQYSGDPQTEWDLNTFHT--KEEVLAAVHSLRyKG- 89
Cdd:PTZ00441    43 VDLYLLVDGSGSIGyHNWITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASkdKEQALIIVKSLR-KTy 121

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387538388   90 ---GNTFTGLALTHVlRQSLRPAAGpRPEAAKVVILVTDG--KSQDDAHAAGRVLKDLDVDVFAVGV 151
Cdd:PTZ00441   122 lpyGKTNMTDALLEV-RKHLNDRVN-RENAIQLVILMTDGipNSKYRALEESRKLKDRNVKLAVIGI 186
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
492-680 4.78e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 44.55  E-value: 4.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  492 QLSVTELPGDKVRLEWAAAAASGVLVYQIKWLPlGDGKAheISVPGNLGTAVLPGLGRHSEYEITILAYYGDGARSEPVS 571
Cdd:COG4733    541 SLSVVAQGTAVTTLTVSWDAPAGAVAYEVEWRR-DDGNW--VSVPRTSGTSFEVPGIYAGDYEVRVRAINALGVSSAWAA 617

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  572 LRYTPLRW-----SPPSGLALDSeSPNSLRVSWTPPSG-HVLYYRVTYVLASGSGPEKSVSIPGPRSQATLLDLLAATKY 645
Cdd:COG4733    618 SSETTVTGktappPAPTGLTATG-GLGGITLSWSFPVDaDTLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLKAGQTY 696

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1387538388  646 RVLVSAVYEAGESVAVSATGRTACPALHPNSSVAG 680
Cdd:COG4733    697 YYRARAVDRSGNVSAWWVSGQASADAAGILDAITG 731
fn3 pfam00041
Fibronectin type III domain;
398-467 1.13e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 38.94  E-value: 1.13e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387538388  398 GPPKHLGFSDVSHDSARVFWEGTPRPVRPC---RVSYVSGEGGHSGQTE-APGNATSAILGPLASSTTYTVHVT 467
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPItgyEVEYRPKNSGEPWNEItVPGTTTSVTLTGLKPGTEYEVRVQ 74
COG3979 COG3979
Chitodextrinase [Carbohydrate transport and metabolism];
218-293 5.09e-03

Chitodextrinase [Carbohydrate transport and metabolism];


Pssm-ID: 443178 [Multi-domain]  Cd Length: 369  Bit Score: 40.53  E-value: 5.09e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387538388  218 SAPTSLVLTQVTFSSVRLSWTPAP--QLPLKYLVtwrpSRGGAprEVVVEGPSASAELHNLTSSTEYLVSVAPVYEAG 293
Cdd:COG3979      4 TAPTGLTASNVTSSSVSLSWDASTdnVGVTGYDV----YRGGD--QVATVTGLTAWTVTGLTPGTEYTFTVGACDAAG 75
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 887-1091 5.85e-03

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: 40.66  E-value: 5.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  887 PALMDGEACPTPPSACTCPPQAPGPPGPqgppglpgrggapgqqgFPGPRGEPGPPGQMGPEGPGGQQGSPGTQGRTVQG 966
Cdd:NF038329   145 PAGPAGPPGPQGERGEKGPAGPQGEAGP-----------------QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387538388  967 PMGPPGVKGQKGDHGLPGLQVAGSDHAQARggglgagppapgqarphlasasvlfQGTPGRVGLQGPKGMRGLEGAAGLP 1046
Cdd:NF038329   208 PAGPAGPDGEAGPAGEDGPAGPAGDGQQGP-------------------------DGDPGPTGEDGPQGPDGPAGKDGPR 262

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1387538388 1047 GPPGPRGFQGVAGARGTGGERGPAG---AVGPTGLPGPKGERGEKGEP 1091
Cdd:NF038329   263 GDRGEAGPDGPDGKDGERGPVGPAGkdgQNGKDGLPGKDGKDGQNGKD 310
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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