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Conserved domains on  [gi|768017758|ref|XP_011527240|]
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collagen alpha-1(XX) chain isoform X2 [Homo sapiens]

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 ...
 178-341 4.18e-91

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: 291.11  E-value: 4.18e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  178 ADMVFLVDGSWSIGHSHFQQVKDFLASVIAPFEIGPDKVQVGLTQYSGDAQTEWDLNSLSTKEQVLAAVRRLRYKGGNTF 257
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  258 TGLALTHVLGQNLQPAAGLRPEAAKVVILVTDGKSQDDVHTAARVLKDLGVNVFAVGVKNADEAELRLLASPPRDITVHS 337
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                  ....
gi 768017758  338 VLDF 341
Cdd:cd01482   161 VADF 164
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 844-1038 1.55e-31

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


The actual alignment was detected with superfamily member smart00210:

Pssm-ID: 473984  Cd Length: 184  Bit Score: 122.08  E-value: 1.55e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758    844 GFDLMVAFSLVEKAYASIRGVAMEPsafgGTPTFTLFKDAQLTRRVSDVYPAPLPPEHTIVFLVRLlpeTPREAFALWQM 923
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEP----GSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758    924 TAEDFQPLLGVLLDAGKKSLTYFHRDPRAALQEATFdpqEVRKIFFGSFHKVHVAVGRSKVRLYVDCRKVAERPLGEMGS 1003
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSF---RNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ 150

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 768017758   1004 PP--AAGFVTLGRLAKARGPrsssAAFQLQMLQIVCS 1038
Cdd:smart00210  151 PPidTDGIEVRGAQAADRKP----FQGDLQQLKIVCD 183
fn3 pfam00041
Fibronectin type III domain;
743-822 1.09e-14

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 70.52  E-value: 1.09e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758   743 SPPSNLALASETPDSLQVSWTPPL---GRVLHYWLTYAPASGLGPEKSVSVPGARSHVTLPDLQAATKYRVLVSAIYAAG 819
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 768017758   820 RSE 822
Cdd:pfam00041   81 EGP 83
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
361-741 5.85e-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: 76.58  E-value: 5.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  361 GGSPRQGPAAAAPALDTLP-APTSLVLSQVTSSSIRLSWTPAPRHPLKYLIVWRASRGGTPREVVVEGPAASTELHNLAS 439
Cdd:COG3401   215 GGESAPSNEVSVTTPTTPPsAPTGLTATADTPGSVTLSWDPVTESDATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTN 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  440 RTEYLVSVFPIYEGGVGEGLRGLVT----TAPLPPPRALTLAAVTPRTVHLTWQPSAG--ATHYLV-RcspaspKGEEEE 512
Cdd:COG3401   295 GTTYYYRVTAVDAAGNESAPSNVVSvttdLTPPAAPSGLTATAVGSSSITLSWTASSDadVTGYNVyR------STSGGG 368

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  513 REVQVGR----PEVLLDGLEPGRDYEVSVQSL--RGPEGSEARGIRARTPTLAPPRHLGFS---DVSHDAARVFWE-GAP 582
Cdd:COG3401   369 TYTKIAEtvttTSYTDTGLTPGTTYYYKVTAVdaAGNESAPSEEVSATTASAASGESLTASvdaVPLTDVAGATAAaSAA 448

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  583 RPVRLVRVTYVSSEGGHSGQTEAPGNATSATLGPLSSSTTYTVRVTCLYPGGGSSTLTGRVTTKKAPSPSQLSMTELPGD 662
Cdd:COG3401   449 SNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTP 528

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768017758  663 AVQLAWVAAAPSGVLVYQITWTPlGEGKAHEISVPGNLGTAVLPGlgrHTEYDVTILAYYRDGARSDPVSLRYTPSTVS 741
Cdd:COG3401   529 NVTGASPVTVGASTGDVLITDLV-SLTTSASSSVSGAGLGSGNLY---LITTLGGSLLTTTSTNTNDVAGVHGGTLLVL 603
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1129-1225 8.02e-13

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: 72.25  E-value: 8.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758 1129 QGPVGPPGVKGEKGDHGLPGLQGHPGHQGIPGRVGLQGPKGMRGLEGTAGLPGPPGPRGFQGMAGARGTSGERGPPGTVG 1208
Cdd:NF038329  134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAG 213

                          90
                  ....*....|....*..
gi 768017758 1209 PTGLPGPKGERGEKGEP 1225
Cdd:NF038329  214 PDGEAGPAGEDGPAGPA 230
 
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 ...
 178-341 4.18e-91

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: 291.11  E-value: 4.18e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  178 ADMVFLVDGSWSIGHSHFQQVKDFLASVIAPFEIGPDKVQVGLTQYSGDAQTEWDLNSLSTKEQVLAAVRRLRYKGGNTF 257
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  258 TGLALTHVLGQNLQPAAGLRPEAAKVVILVTDGKSQDDVHTAARVLKDLGVNVFAVGVKNADEAELRLLASPPRDITVHS 337
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                  ....
gi 768017758  338 VLDF 341
Cdd:cd01482   161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
179-341 1.29e-60

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 205.20  E-value: 1.29e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758   179 DMVFLVDGSWSIGHSHFQQVKDFLASVIAPFEIGPDKVQVGLTQYSGDAQTEWDLNSLSTKEQVLAAVRRLRYKGGNT-F 257
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758   258 TGLALTHVLGQNLQPAAGLRPEAAKVVILVTDGKSQD-DVHTAARVLKDLGVNVFAVGVKNADEAELRLLASPPRDITVH 336
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160


                   ....*
gi 768017758   337 SVLDF 341
Cdd:pfam00092  161 TVSDF 165
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 179-341 1.59e-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: 164.94  E-value: 1.59e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758    179 DMVFLVDGSWSIGHSHFQQVKDFLASVIAPFEIGPDKVQVGLTQYSGDAQTEWDLNSLSTKEQVLAAVRRLRYK-GGNTF 257
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758    258 TGLALTHVLGQNLQPAAGLRPEAAKVVILVTDGKSQD---DVHTAARVLKDLGVNVFAVGVKNA-DEAELRLLASPPRDI 333
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160


                    ....*...
gi 768017758    334 TVHSVLDF 341
Cdd:smart00327  161 YVFLPELL 168
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 844-1038 1.55e-31

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 122.08  E-value: 1.55e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758    844 GFDLMVAFSLVEKAYASIRGVAMEPsafgGTPTFTLFKDAQLTRRVSDVYPAPLPPEHTIVFLVRLlpeTPREAFALWQM 923
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEP----GSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758    924 TAEDFQPLLGVLLDAGKKSLTYFHRDPRAALQEATFdpqEVRKIFFGSFHKVHVAVGRSKVRLYVDCRKVAERPLGEMGS 1003
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSF---RNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ 150

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 768017758   1004 PP--AAGFVTLGRLAKARGPrsssAAFQLQMLQIVCS 1038
Cdd:smart00210  151 PPidTDGIEVRGAQAADRKP----FQGDLQQLKIVCD 183
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 104-327 1.60e-16

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: 81.14  E-value: 1.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  104 FLLARREFVIEDLKSSSLDRSSQRPLGSGAPEPTPSHTGSPDPEQASEPQVAFTPSQDPRTPAGPQFRCLPPVPADMVFL 183
Cdd:COG1240    19 LLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  184 VDGSWS-IGHSHFQQVKDFLASVIAPFeigPDKVQVGLTQYSGDAQTEWDLNSlsTKEQVLAAVRRLRYKGGntfTglAL 262
Cdd:COG1240    99 VDASGSmAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTR--DREALKRALDELPPGGG---T--PL 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  263 THVLGQNLQPAAGLRPEAAKVVILVTDGK---SQDDVHTAARVLKDLGVNVFAVGV--KNADEAELRLLA 327
Cdd:COG1240   169 GDALALALELLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVgtEAVDEGLLREIA 238
fn3 pfam00041
Fibronectin type III domain;
743-822 1.09e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 70.52  E-value: 1.09e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758   743 SPPSNLALASETPDSLQVSWTPPL---GRVLHYWLTYAPASGLGPEKSVSVPGARSHVTLPDLQAATKYRVLVSAIYAAG 819
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 768017758   820 RSE 822
Cdd:pfam00041   81 EGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 743-827 2.95e-14

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: 69.45  E-value: 2.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  743 SPPSNLALASETPDSLQVSWTPPL---GRVLHYWLTYAPASGLGPEKSVSVPGARSHVTLPDLQAATKYRVLVSAIYAAG 819
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                  ....*...
gi 768017758  820 RSEAVSAT 827
Cdd:cd00063    82 ESPPSESV 89
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
361-741 5.85e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 76.58  E-value: 5.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  361 GGSPRQGPAAAAPALDTLP-APTSLVLSQVTSSSIRLSWTPAPRHPLKYLIVWRASRGGTPREVVVEGPAASTELHNLAS 439
Cdd:COG3401   215 GGESAPSNEVSVTTPTTPPsAPTGLTATADTPGSVTLSWDPVTESDATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTN 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  440 RTEYLVSVFPIYEGGVGEGLRGLVT----TAPLPPPRALTLAAVTPRTVHLTWQPSAG--ATHYLV-RcspaspKGEEEE 512
Cdd:COG3401   295 GTTYYYRVTAVDAAGNESAPSNVVSvttdLTPPAAPSGLTATAVGSSSITLSWTASSDadVTGYNVyR------STSGGG 368

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  513 REVQVGR----PEVLLDGLEPGRDYEVSVQSL--RGPEGSEARGIRARTPTLAPPRHLGFS---DVSHDAARVFWE-GAP 582
Cdd:COG3401   369 TYTKIAEtvttTSYTDTGLTPGTTYYYKVTAVdaAGNESAPSEEVSATTASAASGESLTASvdaVPLTDVAGATAAaSAA 448

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  583 RPVRLVRVTYVSSEGGHSGQTEAPGNATSATLGPLSSSTTYTVRVTCLYPGGGSSTLTGRVTTKKAPSPSQLSMTELPGD 662
Cdd:COG3401   449 SNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTP 528

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768017758  663 AVQLAWVAAAPSGVLVYQITWTPlGEGKAHEISVPGNLGTAVLPGlgrHTEYDVTILAYYRDGARSDPVSLRYTPSTVS 741
Cdd:COG3401   529 NVTGASPVTVGASTGDVLITDLV-SLTTSASSSVSGAGLGSGNLY---LITTLGGSLLTTTSTNTNDVAGVHGGTLLVL 603
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1129-1225 8.02e-13

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: 72.25  E-value: 8.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758 1129 QGPVGPPGVKGEKGDHGLPGLQGHPGHQGIPGRVGLQGPKGMRGLEGTAGLPGPPGPRGFQGMAGARGTSGERGPPGTVG 1208
Cdd:NF038329  134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAG 213

                          90
                  ....*....|....*..
gi 768017758 1209 PTGLPGPKGERGEKGEP 1225
Cdd:NF038329  214 PDGEAGPAGEDGPAGPA 230
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 743-821 1.68e-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: 64.17  E-value: 1.68e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758    743 SPPSNLALASETPDSLQVSWTPP-----LGRVLHYWLTYAPASGlgPEKSVSVPGARSHVTLPDLQAATKYRVLVSAIYA 817
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPpddgiTGYIVGYRVEYREEGS--EWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 768017758    818 AGRS 821
Cdd:smart00060   80 AGEG 83
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1126-1225 2.97e-12

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: 70.32  E-value: 2.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758 1126 RAVQGPVGPPGVKGEKGDHGLPGLQGHPGHQGIPGRVGLQGPKGMRGLEGTAGLPGPPGPRGFQGMAGARGTSGERGPPG 1205
Cdd:NF038329  119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198

                          90       100
                  ....*....|....*....|
gi 768017758 1206 TVGPTGLPGPKGERGEKGEP 1225
Cdd:NF038329  199 ETGPAGEQGPAGPAGPDGEA 218
fn3 pfam00041
Fibronectin type III domain;
469-542 5.46e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.82  E-value: 5.46e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758   469 PPPRALTLAAVTPRTVHLTWQPSAGA----THYLVRCSPASpkGEEEEREVQVGRPE--VLLDGLEPGRDYEVSVQSLRG 542
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGngpiTGYEVEYRPKN--SGEPWNEITVPGTTtsVTLTGLKPGTEYEVRVQAVNG 78
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1080-1225 1.53e-11

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 68.39  E-value: 1.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758 1080 GPPGLPgrnGTPGEQGFPGPRGEPGPPGQMGPEGPGGQQGSPGTQGRAvqGPVGPPGVKGEKGDHGLPGLQGHPGHQGIP 1159
Cdd:NF038329  126 GPAGPA---GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA--GPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768017758 1160 GRVGLQGPKGMRGL--EGTAGLPGPPGPRGFQGMAGARGTSGERGPPGTVGPTGLPGPKGERGEKGEP 1225
Cdd:NF038329  201 GPAGEQGPAGPAGPdgEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1129-1225 6.15e-11

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 66.47  E-value: 6.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758 1129 QGPVGPPGVKGEKGDHGLPGLQGHPGH-----QGIPGRVGLQGPKGMRGLEGTAGLPGPPGPRGFQGMAGARGTSGERGP 1203
Cdd:NF038329  206 QGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285

                          90       100
                  ....*....|....*....|....*
gi 768017758 1204 PG---TVGPTGLPGPKGERGEKGEP 1225
Cdd:NF038329  286 AGkdgQNGKDGLPGKDGKDGQNGKD 310
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 469-555 1.27e-10

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: 59.43  E-value: 1.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  469 PPPRALTLAAVTPRTVHLTWQPSAGA----THYLVRCSPASPKGEEEEREVQVGRPEVLLDGLEPGRDYEVSVQSL-RGP 543
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDDggpiTGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVnGGG 81

                          90
                  ....*....|..
gi 768017758  544 EGSEARGIRART 555
Cdd:cd00063    82 ESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 469-538 1.09e-09

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: 1.09e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768017758    469 PPPRALTLAAVTPRTVHLTWQP--SAGATHYLVRCSPASPKGEEEEREVQV--GRPEVLLDGLEPGRDYEVSVQ 538
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPppDDGITGYIVGYRVEYREEGSEWKEVNVtpSSTSYTLTGLKPGTEYEFRVR 75
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1129-1225 1.69e-08

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 58.76  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758 1129 QGPVGPPGVKGEKGDHGLPGLQGHPGHQGIPGRVGLQGPKGMRGlegtagLPGPPGPRGFQGMAGARGTSGERGPPGTVG 1208
Cdd:NF038329  250 QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG------KDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                          90
                  ....*....|....*..
gi 768017758 1209 PTGLPGPKGERGEKGEP 1225
Cdd:NF038329  324 KDGLPGKDGKDGQPGKP 340
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1129-1173 1.60e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 1.60e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 768017758  1129 QGPVGPPGVKGEKGDHGLPGLQGHPGHQGIPGRVGLQGPKGMRGL 1173
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 179-332 9.23e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 46.88  E-value: 9.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  179 DMVFLVDGSWSIG-HSHFQQVKDFLASVIAPFEIGPDKVQVGLTQYSGDAQTEWDLNSLST--KEQVLAAVRRLRyKG-- 253
Cdd:PTZ00441   44 DLYLLVDGSGSIGyHNWITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASkdKEQALIIVKSLR-KTyl 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  254 --GNTFTGLALTHVlGQNLQPAAGlRPEAAKVVILVTDG--KSQDDVHTAARVLKDLGVNVFAVGV-KNADEAELRLLAS 328
Cdd:PTZ00441  123 pyGKTNMTDALLEV-RKHLNDRVN-RENAIQLVILMTDGipNSKYRALEESRKLKDRNVKLAVIGIgQGINHQFNRLLAG 200


                  ....*
gi 768017758  329 -PPRD 332
Cdd:PTZ00441  201 cRPRE 205
 
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 ...
 178-341 4.18e-91

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: 291.11  E-value: 4.18e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  178 ADMVFLVDGSWSIGHSHFQQVKDFLASVIAPFEIGPDKVQVGLTQYSGDAQTEWDLNSLSTKEQVLAAVRRLRYKGGNTF 257
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  258 TGLALTHVLGQNLQPAAGLRPEAAKVVILVTDGKSQDDVHTAARVLKDLGVNVFAVGVKNADEAELRLLASPPRDITVHS 337
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                  ....
gi 768017758  338 VLDF 341
Cdd:cd01482   161 VADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 178-341 2.51e-74

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: 244.06  E-value: 2.51e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  178 ADMVFLVDGSWSIGHSHFQQVKDFLASVIAPFEIGPDKVQVGLTQYSGDAQTEWDLNSLSTKEQVLAAVRRLRYKGGNTF 257
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  258 TGLALTHVLGQNLQPAAGLRPEAAKVVILVTDGKSQDDVHTAARVLKDLGVNVFAVGVKNADEAELRLLASPPRDITVHS 337
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                  ....
gi 768017758  338 VLDF 341
Cdd:cd01472   161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
179-341 1.29e-60

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 205.20  E-value: 1.29e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758   179 DMVFLVDGSWSIGHSHFQQVKDFLASVIAPFEIGPDKVQVGLTQYSGDAQTEWDLNSLSTKEQVLAAVRRLRYKGGNT-F 257
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758   258 TGLALTHVLGQNLQPAAGLRPEAAKVVILVTDGKSQD-DVHTAARVLKDLGVNVFAVGVKNADEAELRLLASPPRDITVH 336
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160


                   ....*
gi 768017758   337 SVLDF 341
Cdd:pfam00092  161 TVSDF 165
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 178-332 2.01e-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: 2.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  178 ADMVFLVDGSWSIGHSHFQQVKDFLASVIAPFEIGPDKVQVGLTQYSGDAQTEWDLNSLSTKEQVLAAVRRLRYKGGN-T 256
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768017758  257 FTGLALTHVLGQNLQPAAGlRPEAAKVVILVTDGKSQD--DVHTAARVLKDLGVNVFAVGVKNADEAELRLLASPPRD 332
Cdd:cd01450    81 NTGKALQYALEQLFSESNA-RENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSE 157
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 179-341 1.59e-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: 164.94  E-value: 1.59e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758    179 DMVFLVDGSWSIGHSHFQQVKDFLASVIAPFEIGPDKVQVGLTQYSGDAQTEWDLNSLSTKEQVLAAVRRLRYK-GGNTF 257
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758    258 TGLALTHVLGQNLQPAAGLRPEAAKVVILVTDGKSQD---DVHTAARVLKDLGVNVFAVGVKNA-DEAELRLLASPPRDI 333
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160


                    ....*...
gi 768017758    334 TVHSVLDF 341
Cdd:smart00327  161 YVFLPELL 168
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 177-341 7.32e-45

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: 162.17  E-value: 7.32e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  177 PADMVFLVDGSWSIGHSHFQQVKDFLASVIAPFEIGPDKVQVGLTQYSGDAQTEWDLNSLSTKEQVLAAVRRLRYKGGNT 256
Cdd:cd01475     2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  257 FTGLALTHVLGQNLQPAAGLRPEAA---KVVILVTDGKSQDDVHTAARVLKDLGVNVFAVGVKNADEAELRLLASPPRDI 333
Cdd:cd01475    82 MTGLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161


                  ....*...
gi 768017758  334 TVHSVLDF 341
Cdd:cd01475   162 HVFYVEDF 169
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 178-341 1.70e-41

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: 150.17  E-value: 1.70e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  178 ADMVFLVDGSWSIGHSHFQQVKDFLASVIAPFEIGPDKVQVGLTQYSGDAQTEWDLNSLSTKEQVLAAVRRLRYKGGNTF 257
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  258 -TGLALTHVLGQNLQPAAGLRPEAA--KVVILVTDGKSQDDVHTAARVLKDLGVNVFAVGVKNADEAELRLLASPPRdiT 334
Cdd:cd01481    81 nTGSALDYVVKNLFTKSAGSRIEEGvpQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS--F 158


                  ....*..
gi 768017758  335 VHSVLDF 341
Cdd:cd01481   159 VFQVSDF 165
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 179-341 6.82e-35

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: 131.71  E-value: 6.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  179 DMVFLVDGSWSIGHSHFQQVKDFLASVIAPFEIGPDKVQVGLTQYSGDAQTEWDLNSLSTKEQVLAAVRRLRYKGGNTFT 258
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  259 GLALTHVLGQNLQPAAGLRPEAAKVVILVTDGKSQDD--VHTAARVLKDLGVNVFAVGV------KNADEaELRLLASPP 330
Cdd:cd01469    82 ATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDplLKDVIPQAEREGIIRYAIGVgghfqrENSRE-ELKTIASKP 160

                         170
                  ....*....|.
gi 768017758  331 RDITVHSVLDF 341
Cdd:cd01469   161 PEEHFFNVTDF 171
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 844-1038 1.55e-31

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 122.08  E-value: 1.55e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758    844 GFDLMVAFSLVEKAYASIRGVAMEPsafgGTPTFTLFKDAQLTRRVSDVYPAPLPPEHTIVFLVRLlpeTPREAFALWQM 923
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEP----GSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758    924 TAEDFQPLLGVLLDAGKKSLTYFHRDPRAALQEATFdpqEVRKIFFGSFHKVHVAVGRSKVRLYVDCRKVAERPLGEMGS 1003
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSF---RNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ 150

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 768017758   1004 PP--AAGFVTLGRLAKARGPrsssAAFQLQMLQIVCS 1038
Cdd:smart00210  151 PPidTDGIEVRGAQAADRKP----FQGDLQQLKIVCD 183
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 178-336 4.18e-30

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: 117.50  E-value: 4.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  178 ADMVFLVDGSWSIGHShFQQVKDFLASVIAPFEIGPDKVQVGLTQYSGDAQT--EWDLNSLSTKEQVLAAVRRLRYKGGN 255
Cdd:cd01476     1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  256 TFTGLALTHVLgQNLQPAAGLRPEAAKVVILVTDGKSQDDVHTAARVLKDL-GVNVFAVGVK---NADEAELRLLASPPR 331
Cdd:cd01476    80 TATGAAIEVAL-QQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGdpgTVDTEELHSITGNED 158


                  ....*
gi 768017758  332 DITVH 336
Cdd:cd01476   159 HIFTD 163
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 178-335 3.90e-29

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: 114.59  E-value: 3.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  178 ADMVFLVDGSWSIGHSHFQQVKDFLASVIAPFEIGPDKVQVGLTQYSGDAQTEWDLNSLSTKEQVLAAVRRLRYK-GGNT 256
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  257 FTGLALTHVLGQNLQPAaglRPEAAKVVILVTDGKSQDD---VHTAARVLKDLGVNVFAVGVKN-ADEAELRLLASPPRD 332
Cdd:cd00198    81 NIGAALRLALELLKSAK---RPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGDdANEDELKEIADKTTG 157


                  ...
gi 768017758  333 ITV 335
Cdd:cd00198   158 GAV 160
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 179-332 3.55e-26

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: 107.09  E-value: 3.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  179 DMVFLVDGSWSIGHSH-FQQVKDFLASVIAPFEIGPDKVQVGLTQYSGDAQTEWDLNSL--STKEQVLAAVRRLR---YK 252
Cdd:cd01471     2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPnsTNKDLALNAIRALLslyYP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  253 GGNTFTGLALTHVLgQNLQPAAGLRPEAAKVVILVTDGKSQDDVHT--AARVLKDLGVN--VFAVG--VKNadeAELRLL 326
Cdd:cd01471    82 NGSTNTTSALLVVE-KHLFDTRGNRENAPQLVIIMTDGIPDSKFRTlkEARKLRERGVIiaVLGVGqgVNH---EENRSL 157


                  ....*..
gi 768017758  327 AS-PPRD 332
Cdd:cd01471   158 VGcDPDD 164
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 177-328 5.94e-17

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: 80.51  E-value: 5.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  177 PADMVFLVDGSWSIGHSHFQQVKDFLASVIAPF------EIGPDKVQVGLTQYSGDAQTEW-DLNSLSTKEQVLAAVRRL 249
Cdd:cd01480     2 PVDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  250 RYKGGNTFTGLALTHVLGQNLQpaaGLRPEAAKVVILVTDGKSQ-DDVHTAARVLKD---LGVNVFAVGVKNADEAELRL 325
Cdd:cd01480    82 EYIGGGTFTDCALKYATEQLLE---GSHQKENKFLLVITDGHSDgSPDGGIEKAVNEadhLGIKIFFVAVGSQNEEPLSR 158


                  ...
gi 768017758  326 LAS 328
Cdd:cd01480   159 IAC 161
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 104-327 1.60e-16

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: 81.14  E-value: 1.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  104 FLLARREFVIEDLKSSSLDRSSQRPLGSGAPEPTPSHTGSPDPEQASEPQVAFTPSQDPRTPAGPQFRCLPPVPADMVFL 183
Cdd:COG1240    19 LLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  184 VDGSWS-IGHSHFQQVKDFLASVIAPFeigPDKVQVGLTQYSGDAQTEWDLNSlsTKEQVLAAVRRLRYKGGntfTglAL 262
Cdd:COG1240    99 VDASGSmAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTR--DREALKRALDELPPGGG---T--PL 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  263 THVLGQNLQPAAGLRPEAAKVVILVTDGK---SQDDVHTAARVLKDLGVNVFAVGV--KNADEAELRLLA 327
Cdd:COG1240   169 GDALALALELLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVgtEAVDEGLLREIA 238
fn3 pfam00041
Fibronectin type III domain;
743-822 1.09e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 70.52  E-value: 1.09e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758   743 SPPSNLALASETPDSLQVSWTPPL---GRVLHYWLTYAPASGLGPEKSVSVPGARSHVTLPDLQAATKYRVLVSAIYAAG 819
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 768017758   820 RSE 822
Cdd:pfam00041   81 EGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 743-827 2.95e-14

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: 69.45  E-value: 2.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  743 SPPSNLALASETPDSLQVSWTPPL---GRVLHYWLTYAPASGLGPEKSVSVPGARSHVTLPDLQAATKYRVLVSAIYAAG 819
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                  ....*...
gi 768017758  820 RSEAVSAT 827
Cdd:cd00063    82 ESPPSESV 89
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
361-741 5.85e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 76.58  E-value: 5.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  361 GGSPRQGPAAAAPALDTLP-APTSLVLSQVTSSSIRLSWTPAPRHPLKYLIVWRASRGGTPREVVVEGPAASTELHNLAS 439
Cdd:COG3401   215 GGESAPSNEVSVTTPTTPPsAPTGLTATADTPGSVTLSWDPVTESDATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTN 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  440 RTEYLVSVFPIYEGGVGEGLRGLVT----TAPLPPPRALTLAAVTPRTVHLTWQPSAG--ATHYLV-RcspaspKGEEEE 512
Cdd:COG3401   295 GTTYYYRVTAVDAAGNESAPSNVVSvttdLTPPAAPSGLTATAVGSSSITLSWTASSDadVTGYNVyR------STSGGG 368

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  513 REVQVGR----PEVLLDGLEPGRDYEVSVQSL--RGPEGSEARGIRARTPTLAPPRHLGFS---DVSHDAARVFWE-GAP 582
Cdd:COG3401   369 TYTKIAEtvttTSYTDTGLTPGTTYYYKVTAVdaAGNESAPSEEVSATTASAASGESLTASvdaVPLTDVAGATAAaSAA 448

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  583 RPVRLVRVTYVSSEGGHSGQTEAPGNATSATLGPLSSSTTYTVRVTCLYPGGGSSTLTGRVTTKKAPSPSQLSMTELPGD 662
Cdd:COG3401   449 SNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTP 528

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768017758  663 AVQLAWVAAAPSGVLVYQITWTPlGEGKAHEISVPGNLGTAVLPGlgrHTEYDVTILAYYRDGARSDPVSLRYTPSTVS 741
Cdd:COG3401   529 NVTGASPVTVGASTGDVLITDLV-SLTTSASSSVSGAGLGSGNLY---LITTLGGSLLTTTSTNTNDVAGVHGGTLLVL 603
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
600-832 7.32e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 76.19  E-value: 7.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  600 SGQTEAPGNATSATLGPLSSSTTYTVRVTCLYPGGGSSTLTG-RVTTKKAP--SPSQLSMTELPGDAVQLAWVAAAPSGV 676
Cdd:COG3401   182 TTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEvSVTTPTTPpsAPTGLTATADTPGSVTLSWDPVTESDA 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  677 LVYQI--------TWTPLGEGKAHEISVPGnlgtaVLPGlgrhTEYDVTILAYYRDGARSDP---VSLryTPSTVSRSPP 745
Cdd:COG3401   262 TGYRVyrsnsgdgPFTKVATVTTTSYTDTG-----LTNG----TTYYYRVTAVDAAGNESAPsnvVSV--TTDLTPPAAP 330

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  746 SNLALASETPDSLQVSWTPPLG-RVLHYWLTYAPASGLGPEKSVSVPGARSHvTLPDLQAATKYRVLVSAIYAAGR---- 820
Cdd:COG3401   331 SGLTATAVGSSSITLSWTASSDaDVTGYNVYRSTSGGGTYTKIAETVTTTSY-TDTGLTPGTTYYYKVTAVDAAGNesap 409

                         250
                  ....*....|..
gi 768017758  821 SEAVSATGQTAA 832
Cdd:COG3401   410 SEEVSATTASAA 421
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1129-1225 8.02e-13

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: 72.25  E-value: 8.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758 1129 QGPVGPPGVKGEKGDHGLPGLQGHPGHQGIPGRVGLQGPKGMRGLEGTAGLPGPPGPRGFQGMAGARGTSGERGPPGTVG 1208
Cdd:NF038329  134 QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAG 213

                          90
                  ....*....|....*..
gi 768017758 1209 PTGLPGPKGERGEKGEP 1225
Cdd:NF038329  214 PDGEAGPAGEDGPAGPA 230
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 743-821 1.68e-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: 64.17  E-value: 1.68e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758    743 SPPSNLALASETPDSLQVSWTPP-----LGRVLHYWLTYAPASGlgPEKSVSVPGARSHVTLPDLQAATKYRVLVSAIYA 817
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPpddgiTGYIVGYRVEYREEGS--EWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 768017758    818 AGRS 821
Cdd:smart00060   80 AGEG 83
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1126-1225 2.97e-12

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: 70.32  E-value: 2.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758 1126 RAVQGPVGPPGVKGEKGDHGLPGLQGHPGHQGIPGRVGLQGPKGMRGLEGTAGLPGPPGPRGFQGMAGARGTSGERGPPG 1205
Cdd:NF038329  119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198

                          90       100
                  ....*....|....*....|
gi 768017758 1206 TVGPTGLPGPKGERGEKGEP 1225
Cdd:NF038329  199 ETGPAGEQGPAGPAGPDGEA 218
fn3 pfam00041
Fibronectin type III domain;
469-542 5.46e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.82  E-value: 5.46e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758   469 PPPRALTLAAVTPRTVHLTWQPSAGA----THYLVRCSPASpkGEEEEREVQVGRPE--VLLDGLEPGRDYEVSVQSLRG 542
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGngpiTGYEVEYRPKN--SGEPWNEITVPGTTtsVTLTGLKPGTEYEVRVQAVNG 78
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 111-327 1.22e-11

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 67.05  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  111 FVIEDLKSSSLDRSSQRPLGSGAPEPTPSHTGSPDPEQASEPQVAFTPSQDPRTPAGPQFRCL---------PPVPADMV 181
Cdd:COG2304    16 SSADVDAASSSNRRRLLVGGEPPPAAAVRLEELVNFFPYDYPLPTGRLAQSPWNPQTRLLLVGlqppkaaaeERPPLNLV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  182 FLVDGSWSIGHSHFQQVKDFLASVIApfEIGPDkVQVGLTQYSGDAQTEWDLNSLSTKEQVLAAVRRLRyKGGNTFTGLA 261
Cdd:COG2304    96 FVIDVSGSMSGDKLELAKEAAKLLVD--QLRPG-DRVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQ-AGGGTALGAG 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768017758  262 LTHVLGQnlqPAAGLRPEAAKVVILVTDGK------SQDDVHTAARVLKDLGVNVFAVGV-KNADEAELRLLA 327
Cdd:COG2304   172 LELAYEL---ARKHFIPGRVNRVILLTDGDanvgitDPEELLKLAEEAREEGITLTTLGVgSDYNEDLLERLA 241
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1080-1225 1.53e-11

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 68.39  E-value: 1.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758 1080 GPPGLPgrnGTPGEQGFPGPRGEPGPPGQMGPEGPGGQQGSPGTQGRAvqGPVGPPGVKGEKGDHGLPGLQGHPGHQGIP 1159
Cdd:NF038329  126 GPAGPA---GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEA--GPQGPAGKDGEAGAKGPAGEKGPQGPRGET 200

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768017758 1160 GRVGLQGPKGMRGL--EGTAGLPGPPGPRGFQGMAGARGTSGERGPPGTVGPTGLPGPKGERGEKGEP 1225
Cdd:NF038329  201 GPAGEQGPAGPAGPdgEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
fn3 pfam00041
Fibronectin type III domain;
379-457 5.10e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.12  E-value: 5.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758   379 PAPTSLVLSQVTSSSIRLSWTPAP---RHPLKYLIVWRASRGGTP-REVVVEGPAASTELHNLASRTEYLVSVFPIYEGG 454
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 768017758   455 VGE 457
Cdd:pfam00041   81 EGP 83
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1129-1225 6.15e-11

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 66.47  E-value: 6.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758 1129 QGPVGPPGVKGEKGDHGLPGLQGHPGH-----QGIPGRVGLQGPKGMRGLEGTAGLPGPPGPRGFQGMAGARGTSGERGP 1203
Cdd:NF038329  206 QGPAGPAGPDGEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285

                          90       100
                  ....*....|....*....|....*
gi 768017758 1204 PG---TVGPTGLPGPKGERGEKGEP 1225
Cdd:NF038329  286 AGkdgQNGKDGLPGKDGKDGQNGKD 310
VWA_2 pfam13519
von Willebrand factor type A domain;
180-287 8.54e-11

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 60.00  E-value: 8.54e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758   180 MVFLVDGSWSI-----GHSHFQQVKDFLASVIAPFeigpDKVQVGLTQYSGDAQTEWDLNSlsTKEQVLAAVRRLRYKGG 254
Cdd:pfam13519    1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSL----PGDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|...
gi 768017758   255 NTFTGLALTHVlgQNLQPAAglRPEAAKVVILV 287
Cdd:pfam13519   75 GTNLAAALQLA--RAALKHR--RKNQPRRIVLI 103
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 469-555 1.27e-10

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: 59.43  E-value: 1.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  469 PPPRALTLAAVTPRTVHLTWQPSAGA----THYLVRCSPASPKGEEEEREVQVGRPEVLLDGLEPGRDYEVSVQSL-RGP 543
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDDggpiTGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVnGGG 81

                          90
                  ....*....|..
gi 768017758  544 EGSEARGIRART 555
Cdd:cd00063    82 ESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 379-457 1.51e-10

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: 59.05  E-value: 1.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  379 PAPTSLVLSQVTSSSIRLSWTPAP---RHPLKYLIVWRASRGGTPREVVVEGPAA-STELHNLASRTEYLVSVFPIYEGG 454
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSEtSYTLTGLKPGTEYEFRVRAVNGGG 81


                  ...
gi 768017758  455 VGE 457
Cdd:cd00063    82 ESP 84
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
441-764 5.11e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 63.87  E-value: 5.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  441 TEYLVSVFPIYEGGVG---EGLRGLVTTAPLPPPRALTLAAVTPRTVHLTWQPSA--GATHYLV-RcspaspKGEEEERE 514
Cdd:COG3401   203 TTYYYRVAATDTGGESapsNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTesDATGYRVyR------SNSGDGPF 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  515 VQVGRPEVL--LD-GLEPGRDYEVSVQSL--RGPEG--SEARGIRARTPTLAPPRHLGFSDVSHDAARVFWEGAP-RPVR 586
Cdd:COG3401   277 TKVATVTTTsyTDtGLTNGTTYYYRVTAVdaAGNESapSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSdADVT 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  587 LVRVTYVSSEGGHSGQTEAPGNATSATLGPLSSSTTYTVRVTCLYPGGGSSTLTGRVTTKKAPSPSQLSmTELPGDAVQL 666
Cdd:COG3401   357 GYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGES-LTASVDAVPL 435

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  667 AWVA---AAPSGVLVYQITWTPLGEGKAHEISVPGNLGTAVLPGLGRHTEYDVTILAYYRDGARSDPVSLRYTPSTVSRS 743
Cdd:COG3401   436 TDVAgatAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGAS 515

                         330       340
                  ....*....|....*....|.
gi 768017758  744 PPSNLALASETPDSLQVSWTP 764
Cdd:COG3401   516 AAAAVGGAPDGTPNVTGASPV 536
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 469-538 1.09e-09

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: 1.09e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768017758    469 PPPRALTLAAVTPRTVHLTWQP--SAGATHYLVRCSPASPKGEEEEREVQV--GRPEVLLDGLEPGRDYEVSVQ 538
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPppDDGITGYIVGYRVEYREEGSEWKEVNVtpSSTSYTLTGLKPGTEYEFRVR 75
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
525-886 2.53e-09

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 61.56  E-value: 2.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  525 DGLEPGRDYEVSVQSL-RGPEGSEARGIRARTPTLAP--PRHLGFSDVSHDAARVFWEgaprPVRLVRVT----YVSSEG 597
Cdd:COG3401   197 GDIEPGTTYYYRVAATdTGGESAPSNEVSVTTPTTPPsaPTGLTATADTPGSVTLSWD----PVTESDATgyrvYRSNSG 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  598 GHSGQTEAPGNATSATLGPLSSSTTYTVRVTCLYPGGGSSTLTG--RVTTKKAP--SPSQLSMTELPGDAVQLAWVAAAP 673
Cdd:COG3401   273 DGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNvvSVTTDLTPpaAPSGLTATAVGSSSITLSWTASSD 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  674 SGVLVYQITWTPLGEGKAHEISVPGN----LGTAVLPGlgrhTEYDVTILAYYRDGARSDPVSLRYTPSTVSRSPPSNLA 749
Cdd:COG3401   353 ADVTGYNVYRSTSGGGTYTKIAETVTttsyTDTGLTPG----TTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTA 428

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  750 LASETPDSLQVSWTPPLGRVLHYWLTYAPASGLGPEKSVSVPGARSHV--TLPDLQAATKYRVLVSAIYAAGRSEAVSAT 827
Cdd:COG3401   429 SVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTvtATTTDTTTANLSVTTGSLVGGSGASSVTNS 508

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 768017758  828 GQTAACPALRPDGSLPGFDLMVAFSLVEKAYASIRGVAMEPSAFGGTPTFTLFKDAQLT 886
Cdd:COG3401   509 VSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLG 567
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 379-456 1.27e-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: 53.39  E-value: 1.27e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758    379 PAPTSLVLSQVTSSSIRLSWTPAPR-HPLKYLIVWRASRGGTP---REVVVEGPAASTELHNLASRTEYLVSVFPIYEGG 454
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDdGITGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 768017758    455 VG 456
Cdd:smart00060   82 EG 83
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1129-1225 1.69e-08

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 58.76  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758 1129 QGPVGPPGVKGEKGDHGLPGLQGHPGHQGIPGRVGLQGPKGMRGlegtagLPGPPGPRGFQGMAGARGTSGERGPPGTVG 1208
Cdd:NF038329  250 QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG------KDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                          90
                  ....*....|....*..
gi 768017758 1209 PTGLPGPKGERGEKGEP 1225
Cdd:NF038329  324 KDGLPGKDGKDGQPGKP 340
fn3 pfam00041
Fibronectin type III domain;
649-725 1.82e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 52.80  E-value: 1.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758   649 PSPSQLSMTELPGDAVQLAWVAAAPSG--VLVYQITWTPLGEGKA-HEISVPGNLGTAVLPGLGRHTEYDVTILAYYRDG 725
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgpITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 178-330 8.41e-08

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: 53.67  E-value: 8.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  178 ADMVFLVDGSWSIGHsHFQQVKDFLASVIAPFeIGPDkVQVGLTQYSGDAQTEWDLNSLSTKEQVLAAVRRLRYKGGNTF 257
Cdd:cd01474     5 FDLYFVLDKSGSVAA-NWIEIYDFVEQLVDRF-NSPG-LRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTY 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768017758  258 TGLALTHVLGQNLQPAAGLRpEAAKVVILVTDGKSQDDVHTA----ARVLKDLGVNVFAVGVKNADEAELRLLASPP 330
Cdd:cd01474    82 IHEGLENANEQIFNRNGGGR-ETVSVIIALTDGQLLLNGHKYpeheAKLSRKLGAIVYCVGVTDFLKSQLINIADSK 157
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
542-832 1.19e-07

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 56.16  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  542 GPEGSEARGIRARTPTLAPPRHLGFSDVSHDAARVFWEG-APRPVRLVRVTYVSSEGGHSGQTEAPGNATSATLGPlsss 620
Cdd:COG3401    33 GKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGrAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATN---- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  621 TTYTVRVTCLYPGGGSSTLTGRVTTKKAPSPSQLSMTELPGDAVQLAWVAAAPSGVLVYQITWTPLGEGKA---HEISVP 697
Cdd:COG3401   109 TGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAvatTSLTVT 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  698 GNLGTAVLPGLGRHTEYDVTILAYYRDGARSDPVSLRYTPSTVSRSPPSNLALASETPDSLQVSWTP-PLGRVLHYWLTY 776
Cdd:COG3401   189 STTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPvTESDATGYRVYR 268

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  777 APASGlGPEKSVSVpGARSHVTLPDLQAATKYRVLVSAIYAAGR----SEAVSATGQTAA 832
Cdd:COG3401   269 SNSGD-GPFTKVAT-VTTTSYTDTGLTNGTTYYYRVTAVDAAGNesapSNVVSVTTDLTP 326
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 560-645 6.65e-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: 48.65  E-value: 6.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  560 PPRHLGFSDVSHDAARVFWEGAPRPVRLV---RVTYVSSEGGHSGQ-TEAPGNATSATLGPLSSSTTYTVRVTCLYPGG- 634
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPItgyVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGe 82

                          90
                  ....*....|.
gi 768017758  635 GSSTLTGRVTT 645
Cdd:cd00063    83 SPPSESVTVTT 93
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
661-832 1.35e-06

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 53.03  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  661 GDAVQLAWVA-AAPSGVLVYQI-------TWTPLGEGKAHEISVPGnlgtaVLPGlgrhtEYDVTILAYYRDGARSDPVS 732
Cdd:COG4733   548 GTAVTTLTVSwDAPAGAVAYEVewrrddgNWVSVPRTSGTSFEVPG-----IYAG-----DYEVRVRAINALGVSSAWAA 617

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  733 LRYTPSTVSRSPPSNLA--LASETPDSLQVSWTPPLG-RVLHYWLTYAPASGLGPEKSVSVPGARSHVTLPDLQAATKYR 809
Cdd:COG4733   618 SSETTVTGKTAPPPAPTglTATGGLGGITLSWSFPVDaDTLRTEIRYSTTGDWASATVAQALYPGNTYTLAGLKAGQTYY 697

                         170       180
                  ....*....|....*....|...
gi 768017758  810 VLVSAIYAAGRSEAVSATGQTAA 832
Cdd:COG4733   698 YRARAVDRSGNVSAWWVSGQASA 720
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 560-636 1.62e-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: 47.22  E-value: 1.62e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758    560 PPRHLGFSDVSHDAARVFWEGAPRPVRLVRVTYVSSEGGHSG----QTEAPGNATSATLGPLSSSTTYTVRVTCLYPGGG 635
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGsewkEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 768017758    636 S 636
Cdd:smart00060   83 G 83
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 179-327 2.67e-06

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: 49.62  E-value: 2.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  179 DMVFLVDGSWSIGHS-HFQQVKDFLASVIAPFEIGPDKVQVGLTQYSGDAQT--EWDLNSLSTKEQVLAAVRRLR--YK- 252
Cdd:cd01473     2 DLTLILDESASIGYSnWRKDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDvvPFSDEERYDKNELLKKINDLKnsYRs 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768017758  253 GGNTFTGLALTHVLgQNLQPAAGLRPEAAKVVILVTDG----KSQDDVHTAARVLKDLGVNVFAVGVKNADEAELRLLA 327
Cdd:cd01473    82 GGETYIVEALKYGL-KNYTKHGNRRKDAPKVTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLA 159
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 651-732 3.78e-06

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: 46.72  E-value: 3.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  651 PSQLSMTELPGDAVQLAWVAAAPSG--VLVYQITWTPLGEGKAHEISV-PGNLGTAVLPGLGRHTEYDVTILAYYRDGaR 727
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEDDGgpITGYVVEYREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVNGGG-E 82


                  ....*
gi 768017758  728 SDPVS 732
Cdd:cd00063    83 SPPSE 87
fn3 pfam00041
Fibronectin type III domain;
560-637 3.97e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.25  E-value: 3.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758   560 PPRHLGFSDVSHDAARVFWEGAP---RPVRLVRVTYVSSEGGHSGQTE-APGNATSATLGPLSSSTTYTVRVTcLYPGGG 635
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEItVPGTTTSVTLTGLKPGTEYEVRVQ-AVNGGG 80


                   ..
gi 768017758   636 SS 637
Cdd:pfam00041   81 EG 82
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1129-1173 1.60e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 1.60e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 768017758  1129 QGPVGPPGVKGEKGDHGLPGLQGHPGHQGIPGRVGLQGPKGMRGL 1173
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 649-725 2.46e-05

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: 44.14  E-value: 2.46e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758    649 PSPSQLSMTELPGDAVQLAWVAAAPSGVLVYQITWTPLGEGKA---HEISVPGNLGTAVLPGLGRHTEYDVTILAYYRDG 725
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1148-1225 2.66e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 2.66e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768017758  1148 GLQGHPGHQGIPGRVGLQGPkgmrglegtaglpgppgprgfqgmAGARGTSGERGPPGTVGPTGLPGPKGERGEKGEP 1225
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGP------------------------PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 178-327 3.93e-05

VWA subgroup: 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. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 45.73  E-value: 3.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  178 ADMVFLVDGSWSIGHSHFQQVKDFLASVIApfEIGPDKvQVGLTQYSGDAQTEWDLNSLSTKEQVLAAVRRLRYKGG-NT 256
Cdd:cd01465     1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVD--QLRPDD-RLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTAGGStAG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768017758  257 FTGLALTHVLGQnlqpaAGLRPEAAKVVILVTDGK----SQDDVHTAARVLKDL--GVNVFAVGV-KNADEAELRLLA 327
Cdd:cd01465    78 GAGIQLGYQEAQ-----KHFVPGGVNRILLATDGDfnvgETDPDELARLVAQKResGITLSTLGFgDNYNEDLMEAIA 150
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 179-332 9.23e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 46.88  E-value: 9.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  179 DMVFLVDGSWSIG-HSHFQQVKDFLASVIAPFEIGPDKVQVGLTQYSGDAQTEWDLNSLST--KEQVLAAVRRLRyKG-- 253
Cdd:PTZ00441   44 DLYLLVDGSGSIGyHNWITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASkdKEQALIIVKSLR-KTyl 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  254 --GNTFTGLALTHVlGQNLQPAAGlRPEAAKVVILVTDG--KSQDDVHTAARVLKDLGVNVFAVGV-KNADEAELRLLAS 328
Cdd:PTZ00441  123 pyGKTNMTDALLEV-RKHLNDRVN-RENAIQLVILMTDGipNSKYRALEESRKLKDRNVKLAVIGIgQGINHQFNRLLAG 200


                  ....*
gi 768017758  329 -PPRD 332
Cdd:PTZ00441  201 cRPRE 205
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1130-1205 5.50e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 5.50e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768017758  1130 GPVGPPGVKGEKGDHGLPGLQGHPGHQGIPGRVGLQGPKGmrglegtaglpgppgPrgfqgmAGARGTSGERGPPG 1205
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPG---------------P------PGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1136-1219 1.03e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017758  1136 GVKGEKGDHGLPGLQGHPGHQGIPGRVGLQGPKGmrglegtaglpgPPgprgfqgmagargtsGERGPPGTVGPTGLPGP 1215
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPG------------PP---------------GPPGPPGPPGPPGAPGA 53


                   ....
gi 768017758  1216 KGER 1219
Cdd:pfam01391   54 PGPP 57
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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