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Conserved domains on  [gi|1907143554|ref|XP_036018508|]
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collagen alpha-1(XX) chain isoform X2 [Mus musculus]

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 ...
 218-381 1.00e-86

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: 278.79  E-value: 1.00e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  218 ADIIFLVDGSWSIGHNHFQQVKDFLASIITQFAIGPDKVQVGLTQYSGDPQTEWDLNSFQTKEQVLAAVHHLRYKGGNTF 297
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  298 TGLALTHVLEQNLKPAAGVRPEAAKVLILVTDGKSQDDVRTAARILKDQDIDVFVVGVKNVDEAELKLLASQPLDITVHN 377
Cdd:cd01482     81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                   ....
gi 1907143554  378 VLDF 381
Cdd:cd01482    161 VADF 164
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 881-1075 1.27e-31

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


The actual alignment was detected with superfamily member smart00210:

Pssm-ID: 473984  Cd Length: 184  Bit Score: 122.47  E-value: 1.27e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554   881 GFDLMVAFGLVAKEYASIRGVAMEPSalgvVPTFTLFKDAQLMRRVSDIYPATLPPEHTIVFLVRLlpeTPREAFALWQM 960
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPG----SPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554   961 MAEDFQPILGVLLDAGRKSLTYFNHDSRAALQEVTFDlqdAKKIFFGSFHKVHIAVGHSKVRLYVDCRKVAERPIGDAGS 1040
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFR---NLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ 150

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1907143554  1041 PP--TGGFITLGRLAKARGPrsssATFQLQMLQIVCS 1075
Cdd:smart00210  151 PPidTDGIEVRGAQAADRKP----FQGDLQQLKIVCD 183
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1126-1262 1.22e-14

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 78.02  E-value: 1.22e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554 1126 GPPGQQGHPGPKGEPGPPGQTGPEGPGGQQGSPGTQG----RAVQGPMGPPGAKGEKGDQGLSGLQGLSGQQGIPGKTGL 1201
Cdd:NF038329   126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGpagpQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907143554 1202 QGPKGMRGL--EGPAGLPGPPGPRGFQGLAGARGTNGERGAPGAVGPTGLPGSKGERGEKGEP 1262
Cdd:NF038329   206 QGPAGPAGPdgEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
fn3 pfam00041
Fibronectin type III domain;
792-860 1.34e-11

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.66  E-value: 1.34e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907143554  792 TPNSLQVNWTPP---SGHVLHYRLNYTLASGSGPEKSISVPGTRSHAVLRDLMSATKYRVLVSAVYRAGESM 860
Cdd:pfam00041   12 TSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGP 83
fn3 pfam00041
Fibronectin type III domain;
418-496 1.17e-10

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.97  E-value: 1.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  418 PTPTRLILTHATSSSIHLSWTPALY---PPLKYLIVWQPSRGG-APKEVVVEGPVSSMELGNLTSSTEYLVSVLPVYESG 493
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDgngPITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1907143554  494 VGK 496
Cdd:pfam00041   81 EGP 83
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
643-878 1.56e-10

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: 65.41  E-value: 1.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  643 VPGNLTSATLGPLSSSTMYTVRVTCFYLGGGSS---VLTGHVTTQKAPSPGQLSVMELPGDAVKLSWLATALSGVLVYQI 719
Cdd:COG3401    187 VTSTTLVDGGGDIEPGTTYYYRVAATDTGGESApsnEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYRV 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  720 KWMPLGEGKAREI-SVPGTlgTATLPGLMKHVEYEITILAYYRDGTRSD----------------PVSLRYTPSaasrsp 782
Cdd:COG3401    267 YRSNSGDGPFTKVaTVTTT--SYTDTGLTNGTTYYYRVTAVDAAGNESApsnvvsvttdltppaaPSGLTATAV------ 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  783 psslalsseTPNSLQVNWTPPSG-HVLHYRLnYTLASGSGPEKSISVPGTRSHAVLRDLMSATKYRVLVSAVYRAGE--- 858
Cdd:COG3401    339 ---------GSSSITLSWTASSDaDVTGYNV-YRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNesa 408

                          250       260
                   ....*....|....*....|.
gi 1907143554  859 -SMAVSATYRTACPALHPDSS 878
Cdd:COG3401    409 pSEEVSATTASAASGESLTAS 429
fn3 pfam00041
Fibronectin type III domain;
598-666 3.34e-08

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 52.03  E-value: 3.34e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907143554  598 GPPRHLTFSDVRYNSTCVSWEA----QRPVRLVKVSYISSDGSHSGQTQ-VPGNLTSATLGPLSSSTMYTVRVT 666
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKNSGEPWNEItVPGTTTSVTLTGLKPGTEYEVRVQ 74
fn3 pfam00041
Fibronectin type III domain;
517-581 1.74e-07

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.11  E-value: 1.74e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907143554  517 AVTPRTLHVTW-PPSAG---VTQYLVQYLLATSTGEEQKREVHVGQPEVLLDGLEPGQDYDVSVQSLRG 581
Cdd:pfam00041   10 DVTSTSLTVSWtPPPDGngpITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78
 
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 ...
 218-381 1.00e-86

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: 278.79  E-value: 1.00e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  218 ADIIFLVDGSWSIGHNHFQQVKDFLASIITQFAIGPDKVQVGLTQYSGDPQTEWDLNSFQTKEQVLAAVHHLRYKGGNTF 297
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  298 TGLALTHVLEQNLKPAAGVRPEAAKVLILVTDGKSQDDVRTAARILKDQDIDVFVVGVKNVDEAELKLLASQPLDITVHN 377
Cdd:cd01482     81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                   ....
gi 1907143554  378 VLDF 381
Cdd:cd01482    161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
219-387 4.45e-62

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 209.44  E-value: 4.45e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  219 DIIFLVDGSWSIGHNHFQQVKDFLASIITQFAIGPDKVQVGLTQYSGDPQTEWDLNSFQTKEQVLAAVHHLRYKGGNT-F 297
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  298 TGLALTHVLEQNLKPAAGVRPEAAKVLILVTDGKSQD-DVRTAARILKDQDIDVFVVGVKNVDEAELKLLASQPLDITVH 376
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                          170
                   ....*....|.
gi 1907143554  377 NVLDFPQLDTL 387
Cdd:pfam00092  161 TVSDFEALEDL 171
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 219-384 9.44e-49

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: 171.10  E-value: 9.44e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554   219 DIIFLVDGSWSIGHNHFQQVKDFLASIITQFAIGPDKVQVGLTQYSGDPQTEWDLNSFQTKEQVLAAVHHLRYK-GGNTF 297
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554   298 TGLALTHVLEQNLKPAAGVRPEAAKVLILVTDGKSQD---DVRTAARILKDQDIDVFVVGVKN-VDEAELKLLASQPLDI 373
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNdVDEEELKKLASAPGGV 160

                           170
                    ....*....|.
gi 1907143554   374 TVHNVLDFPQL 384
Cdd:smart00327  161 YVFLPELLDLL 171
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 881-1075 1.27e-31

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 122.47  E-value: 1.27e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554   881 GFDLMVAFGLVAKEYASIRGVAMEPSalgvVPTFTLFKDAQLMRRVSDIYPATLPPEHTIVFLVRLlpeTPREAFALWQM 960
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPG----SPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554   961 MAEDFQPILGVLLDAGRKSLTYFNHDSRAALQEVTFDlqdAKKIFFGSFHKVHIAVGHSKVRLYVDCRKVAERPIGDAGS 1040
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFR---NLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ 150

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1907143554  1041 PP--TGGFITLGRLAKARGPrsssATFQLQMLQIVCS 1075
Cdd:smart00210  151 PPidTDGIEVRGAQAADRKP----FQGDLQQLKIVCD 183
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 126-369 8.17e-21

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: 93.85  E-value: 8.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  126 RLAGATLEPTSLPLRGPDSEKTSEPSIAFTLSRDLPILGVASKDQRKLKQGLGVQNSAQTTTDLERQSHTAASVGKQGKL 205
Cdd:COG1240      1 DLALALLALLLLLALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  206 DHPQFQCTPPTPADIIFLVDGSWS-IGHNHFQQVKDFLASIITQFaigPDKVQVGLTQYSGDPQTEWDLNSfqTKEQVLA 284
Cdd:COG1240     81 LAPLALARPQRGRDVVLVVDASGSmAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTR--DREALKR 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  285 AVHHLRYKGGnTFTGLALTHVLEQnlkpAAGVRPEAAKVLILVTDGK---SQDDVRTAARILKDQDIDVFVVGV--KNVD 359
Cdd:COG1240    156 ALDELPPGGG-TPLGDALALALEL----LKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVgtEAVD 230

                          250
                   ....*....|
gi 1907143554  360 EAELKLLASQ 369
Cdd:COG1240    231 EGLLREIAEA 240
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1126-1262 1.22e-14

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 78.02  E-value: 1.22e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554 1126 GPPGQQGHPGPKGEPGPPGQTGPEGPGGQQGSPGTQG----RAVQGPMGPPGAKGEKGDQGLSGLQGLSGQQGIPGKTGL 1201
Cdd:NF038329   126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGpagpQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907143554 1202 QGPKGMRGL--EGPAGLPGPPGPRGFQGLAGARGTNGERGAPGAVGPTGLPGSKGERGEKGEP 1262
Cdd:NF038329   206 QGPAGPAGPdgEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1163-1262 1.10e-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: 74.94  E-value: 1.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554 1163 RAVQGPMGPPGAKGEKGDQGLSGLQGLSGQQGIPGKTGLQGPKGMRGLEGPaglpgppgprgfQGLAGARGTNGERGAPG 1242
Cdd:NF038329   119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE------------AGPQGPAGKDGEAGAKG 186

                           90       100
                   ....*....|....*....|
gi 1907143554 1243 AVGPTGLPGSKGERGEKGEP 1262
Cdd:NF038329   187 PAGEKGPQGPRGETGPAGEQ 206
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1088-1262 6.11e-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: 69.55  E-value: 6.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554 1088 PALRDGETCPAFPSAcaysseTPGPPGPQGPPGLPGRNGPPGQQGHPGPKGEPGPPGQTGPEGPGGQQGSPGTQGRAVQG 1167
Cdd:NF038329   163 PAGPQGEAGPQGPAG------KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQG 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554 1168 PMGPPGAKGEKGDQGLSGLQGLSGQQGIPGKTGLQGPKGMRGLEGPAglpgppgprgfqGLAGARGTNGERGAPGAVGP- 1246
Cdd:NF038329   237 PDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV------------GPAGKDGQNGKDGLPGKDGKd 304

                          170
                   ....*....|....*...
gi 1907143554 1247 --TGLPGSKGERGEKGEP 1262
Cdd:NF038329   305 gqNGKDGLPGKDGKDGQP 322
fn3 pfam00041
Fibronectin type III domain;
792-860 1.34e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.66  E-value: 1.34e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907143554  792 TPNSLQVNWTPP---SGHVLHYRLNYTLASGSGPEKSISVPGTRSHAVLRDLMSATKYRVLVSAVYRAGESM 860
Cdd:pfam00041   12 TSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGP 83
fn3 pfam00041
Fibronectin type III domain;
418-496 1.17e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.97  E-value: 1.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  418 PTPTRLILTHATSSSIHLSWTPALY---PPLKYLIVWQPSRGG-APKEVVVEGPVSSMELGNLTSSTEYLVSVLPVYESG 493
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDgngPITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1907143554  494 VGK 496
Cdd:pfam00041   81 EGP 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
643-878 1.56e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 65.41  E-value: 1.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  643 VPGNLTSATLGPLSSSTMYTVRVTCFYLGGGSS---VLTGHVTTQKAPSPGQLSVMELPGDAVKLSWLATALSGVLVYQI 719
Cdd:COG3401    187 VTSTTLVDGGGDIEPGTTYYYRVAATDTGGESApsnEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYRV 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  720 KWMPLGEGKAREI-SVPGTlgTATLPGLMKHVEYEITILAYYRDGTRSD----------------PVSLRYTPSaasrsp 782
Cdd:COG3401    267 YRSNSGDGPFTKVaTVTTT--SYTDTGLTNGTTYYYRVTAVDAAGNESApsnvvsvttdltppaaPSGLTATAV------ 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  783 psslalsseTPNSLQVNWTPPSG-HVLHYRLnYTLASGSGPEKSISVPGTRSHAVLRDLMSATKYRVLVSAVYRAGE--- 858
Cdd:COG3401    339 ---------GSSSITLSWTASSDaDVTGYNV-YRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNesa 408

                          250       260
                   ....*....|....*....|.
gi 1907143554  859 -SMAVSATYRTACPALHPDSS 878
Cdd:COG3401    409 pSEEVSATTASAASGESLTAS 429
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 792-859 6.24e-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: 57.12  E-value: 6.24e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907143554  792 TPNSLQVNWTPPS---GHVLHYRLNYTLASGSGPEKSISVPGTRSHAVLRDLMSATKYRVLVSAVYRAGES 859
Cdd:cd00063     13 TSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGES 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 420-499 7.73e-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: 57.12  E-value: 7.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  420 PTRLILTHATSSSIHLSWTPALY---PPLKYLIVWQPSRGGAPKEV-VVEGPVSSMELGNLTSSTEYLVSVLPVYESGVG 495
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDdggPITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGES 83


                   ....
gi 1907143554  496 KSLQ 499
Cdd:cd00063     84 PPSE 87
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 792-859 3.03e-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: 54.93  E-value: 3.03e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907143554   792 TPNSLQVNWTPPS-----GHVLHYRLNYTlaSGSGPEKSISVPGTRSHAVLRDLMSATKYRVLVSAVYRAGES 859
Cdd:smart00060   13 TSTSVTLSWEPPPddgitGYIVGYRVEYR--EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
687-763 9.29e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.57  E-value: 9.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  687 PSPGQLSVMELPGDAVKLSWLA-TALSGVLV-YQIKWMPLGEGKA-REISVPGTLGTATLPGLMKHVEYEITILAYYRDG 763
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPpPDGNGPITgYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 418-495 9.79e-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: 53.77  E-value: 9.79e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554   418 PTPTRLILTHATSSSIHLSWTPALYP-PLKYLIVWQPSRGGAP---KEVVVEGPVSSMELGNLTSSTEYLVSVLPVYESG 493
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDgITGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1907143554   494 VG 495
Cdd:smart00060   82 EG 83
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1194-1262 2.18e-08

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: 51.73  E-value: 2.18e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907143554 1194 GIPGKTGLQGPKGMRGlegpagLPgppgprgfqGLAGARGTNGERGAPGAVGPTGLPGSKGERGEKGEP 1262
Cdd:pfam01391    1 GPPGPPGPPGPPGPPG------PP---------GPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
fn3 pfam00041
Fibronectin type III domain;
598-666 3.34e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 52.03  E-value: 3.34e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907143554  598 GPPRHLTFSDVRYNSTCVSWEA----QRPVRLVKVSYISSDGSHSGQTQ-VPGNLTSATLGPLSSSTMYTVRVT 666
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKNSGEPWNEItVPGTTTSVTLTGLKPGTEYEVRVQ 74
fn3 pfam00041
Fibronectin type III domain;
517-581 1.74e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.11  E-value: 1.74e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907143554  517 AVTPRTLHVTW-PPSAG---VTQYLVQYLLATSTGEEQKREVHVGQPEVLLDGLEPGQDYDVSVQSLRG 581
Cdd:pfam00041   10 DVTSTSLTVSWtPPPDGngpITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 517-577 2.32e-07

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: 49.54  E-value: 2.32e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907143554   517 AVTPRTLHVTW--PPSAGVTQYLVQYLLATSTGEEQKREVHV--GQPEVLLDGLEPGQDYDVSVQ 577
Cdd:smart00060   11 DVTSTSVTLSWepPPDDGITGYIVGYRVEYREEGSEWKEVNVtpSSTSYTLTGLKPGTEYEFRVR 75
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 517-594 5.43e-07

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 5.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  517 AVTPRTLHVTWPPSAG----VTQYLVQYLLATSTGEEQKREVHVGQPEVLLDGLEPGQDYDVSVQSLRGPEASE-VQSIR 591
Cdd:cd00063     11 DVTSTSVTLSWTPPEDdggpITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPpSESVT 90


                   ...
gi 1907143554  592 ART 594
Cdd:cd00063     91 VTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 689-770 8.18e-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: 48.26  E-value: 8.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  689 PGQLSVMELPGDAVKLSWLATALSG--VLVYQIKWMPLGEGKAREISV-PGTLGTATLPGLMKHVEYEITILAYYRDGtR 765
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDDGgpITGYVVEYREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVNGGG-E 82


                   ....*
gi 1907143554  766 SDPVS 770
Cdd:cd00063     83 SPPSE 87
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 219-367 1.02e-06

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 53.04  E-value: 1.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  219 DIIFLVDGSWSIG-HNHFQQVKDFLASIITQFAIGPDKVQVGLTQYSGDPQTEWDLNSFQT--KEQVLAAVHHLRyKG-- 293
Cdd:PTZ00441    44 DLYLLVDGSGSIGyHNWITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASkdKEQALIIVKSLR-KTyl 122

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907143554  294 --GNTFTGLALTHVlEQNLKPAAGvRPEAAKVLILVTDG--KSQDDVRTAARILKDQDIDVFVVGV-KNVDEAELKLLA 367
Cdd:PTZ00441   123 pyGKTNMTDALLEV-RKHLNDRVN-RENAIQLVILMTDGipNSKYRALEESRKLKDRNVKLAVIGIgQGINHQFNRLLA 199
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 598-674 9.18e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 45.30  E-value: 9.18e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554   598 GPPRHLTFSDVRYNSTCVSWE--AQRPVRLVKVSYISSDGSHSGQTQ---VPGNLTSATLGPLSSSTMYTVRVTCFYLGG 672
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEppPDDGITGYIVGYRVEYREEGSEWKevnVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1907143554   673 GS 674
Cdd:smart00060   82 EG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 687-763 1.34e-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: 44.53  E-value: 1.34e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554   687 PSPGQLSVMELPGDAVKLSWLATALSGVLVYQIKWMPLGEGKA---REISVPGTLGTATLPGLMKHVEYEITILAYYRDG 763
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 598-683 1.41e-05

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: 44.79  E-value: 1.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  598 GPPRHLTFSDVRYNSTCVSWEA----QRPVRLVKVSYISSDGSHSGQ-TQVPGNLTSATLGPLSSSTMYTVRVTCFYLGG 672
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPpeddGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 1907143554  673 -GSSVLTGHVTT 683
Cdd:cd00063     82 eSPPSESVTVTT 93
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1167-1209 1.64e-03

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 42.58  E-value: 1.64e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1907143554 1167 GPMGPPGAKGEKGDQGLSGLQGLSGQQGIPGKTGLQGPKGMRG 1209
Cdd:NF038329   293 GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
 
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 ...
 218-381 1.00e-86

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: 278.79  E-value: 1.00e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  218 ADIIFLVDGSWSIGHNHFQQVKDFLASIITQFAIGPDKVQVGLTQYSGDPQTEWDLNSFQTKEQVLAAVHHLRYKGGNTF 297
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  298 TGLALTHVLEQNLKPAAGVRPEAAKVLILVTDGKSQDDVRTAARILKDQDIDVFVVGVKNVDEAELKLLASQPLDITVHN 377
Cdd:cd01482     81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                   ....
gi 1907143554  378 VLDF 381
Cdd:cd01482    161 VADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 218-381 7.53e-73

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: 239.82  E-value: 7.53e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  218 ADIIFLVDGSWSIGHNHFQQVKDFLASIITQFAIGPDKVQVGLTQYSGDPQTEWDLNSFQTKEQVLAAVHHLRYKGGNTF 297
Cdd:cd01472      1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  298 TGLALTHVLEQNLKPAAGVRPEAAKVLILVTDGKSQDDVRTAARILKDQDIDVFVVGVKNVDEAELKLLASQPLDITVHN 377
Cdd:cd01472     81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                   ....
gi 1907143554  378 VLDF 381
Cdd:cd01472    161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
219-387 4.45e-62

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 209.44  E-value: 4.45e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  219 DIIFLVDGSWSIGHNHFQQVKDFLASIITQFAIGPDKVQVGLTQYSGDPQTEWDLNSFQTKEQVLAAVHHLRYKGGNT-F 297
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  298 TGLALTHVLEQNLKPAAGVRPEAAKVLILVTDGKSQD-DVRTAARILKDQDIDVFVVGVKNVDEAELKLLASQPLDITVH 376
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                          170
                   ....*....|.
gi 1907143554  377 NVLDFPQLDTL 387
Cdd:pfam00092  161 TVSDFEALEDL 171
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 218-372 2.41e-56

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: 192.51  E-value: 2.41e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  218 ADIIFLVDGSWSIGHNHFQQVKDFLASIITQFAIGPDKVQVGLTQYSGDPQTEWDLNSFQTKEQVLAAVHHLRYKGGN-T 296
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907143554  297 FTGLALTHVLEQNLKPAAgVRPEAAKVLILVTDGKSQD--DVRTAARILKDQDIDVFVVGVKNVDEAELKLLASQPLD 372
Cdd:cd01450     81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSE 157
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 219-384 9.44e-49

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: 171.10  E-value: 9.44e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554   219 DIIFLVDGSWSIGHNHFQQVKDFLASIITQFAIGPDKVQVGLTQYSGDPQTEWDLNSFQTKEQVLAAVHHLRYK-GGNTF 297
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554   298 TGLALTHVLEQNLKPAAGVRPEAAKVLILVTDGKSQD---DVRTAARILKDQDIDVFVVGVKN-VDEAELKLLASQPLDI 373
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNdVDEEELKKLASAPGGV 160

                           170
                    ....*....|.
gi 1907143554   374 TVHNVLDFPQL 384
Cdd:smart00327  161 YVFLPELLDLL 171
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 217-397 5.03e-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: 162.55  E-value: 5.03e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  217 PADIIFLVDGSWSIGHNHFQQVKDFLASIITQFAIGPDKVQVGLTQYSGDPQTEWDLNSFQTKEQVLAAVHHLRYKGGNT 296
Cdd:cd01475      2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  297 FTGLALTHVLEQNLKPAAGVRPEAA---KVLILVTDGKSQDDVRTAARILKDQDIDVFVVGVKNVDEAELKLLASQPLDI 373
Cdd:cd01475     82 MTGLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161

                          170       180
                   ....*....|....*....|....
gi 1907143554  374 TVHNVLDFPQLDTLAPLLSRLICQ 397
Cdd:cd01475    162 HVFYVEDFSTIEELTKKFQGKICV 185
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 219-387 8.70e-43

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: 154.44  E-value: 8.70e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  219 DIIFLVDGSWSIGHNHFQQVKDFLASIITQFAIGPDKVQVGLTQYSGDPQTEWDLNSFQTKEQVLAAVHHLRYKGGNTFT 298
Cdd:cd01469      2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  299 GLALTHVLEQNLKPAAGVRPEAAKVLILVTDGKSQDDVRTAARI--LKDQDIDVFVVGV------KNVDEaELKLLASQP 370
Cdd:cd01469     82 ATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDVIpqAEREGIIRYAIGVgghfqrENSRE-ELKTIASKP 160

                          170
                   ....*....|....*..
gi 1907143554  371 LDITVHNVLDFPQLDTL 387
Cdd:cd01469    161 PEEHFFNVTDFAALKDI 177
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 218-381 4.86e-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: 148.63  E-value: 4.86e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  218 ADIIFLVDGSWSIGHNHFQQVKDFLASIITQFAIGPDKVQVGLTQYSGDPQTEWDLNSFQTKEQVLAAVHHLRYKGGNTF 297
Cdd:cd01481      1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  298 -TGLALTHVLEQNLKPAAGVRPEAA--KVLILVTDGKSQDDVRTAARILKDQDIDVFVVGVKNVDEAELKLLASQPLdiT 374
Cdd:cd01481     81 nTGSALDYVVKNLFTKSAGSRIEEGvpQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS--F 158


                   ....*..
gi 1907143554  375 VHNVLDF 381
Cdd:cd01481    159 VFQVSDF 165
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 218-367 7.78e-33

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: 125.20  E-value: 7.78e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  218 ADIIFLVDGSWSIGHNhFQQVKDFLASIITQFAIGPDKVQVGLTQYSGDPQT--EWDLNSFQTKEQVLAAVHHLRYKGGN 295
Cdd:cd01476      1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGT 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907143554  296 TFTGLALTHVLEQnLKPAAGVRPEAAKVLILVTDGKSQDDVRTAARILKDQ-DIDVFVVGVK---NVDEAELKLLA 367
Cdd:cd01476     80 TATGAAIEVALQQ-LDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGdpgTVDTEELHSIT 154
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 881-1075 1.27e-31

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 122.47  E-value: 1.27e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554   881 GFDLMVAFGLVAKEYASIRGVAMEPSalgvVPTFTLFKDAQLMRRVSDIYPATLPPEHTIVFLVRLlpeTPREAFALWQM 960
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPG----SPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554   961 MAEDFQPILGVLLDAGRKSLTYFNHDSRAALQEVTFDlqdAKKIFFGSFHKVHIAVGHSKVRLYVDCRKVAERPIGDAGS 1040
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFR---NLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ 150

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1907143554  1041 PP--TGGFITLGRLAKARGPrsssATFQLQMLQIVCS 1075
Cdd:smart00210  151 PPidTDGIEVRGAQAADRKP----FQGDLQQLKIVCD 183
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 218-375 8.08e-31

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: 119.21  E-value: 8.08e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  218 ADIIFLVDGSWSIGHNHFQQVKDFLASIITQFAIGPDKVQVGLTQYSGDPQTEWDLNSFQTKEQVLAAVHHLRYK-GGNT 296
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  297 FTGLALTHVLEQNLKPAagvRPEAAKVLILVTDGKSQDD---VRTAARILKDQDIDVFVVGVKN-VDEAELKLLASQPLD 372
Cdd:cd00198     81 NIGAALRLALELLKSAK---RPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGDdANEDELKEIADKTTG 157


                   ...
gi 1907143554  373 ITV 375
Cdd:cd00198    158 GAV 160
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 219-372 1.49e-27

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: 110.94  E-value: 1.49e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  219 DIIFLVDGSWSIG-HNHFQQVKDFLASIITQFAIGPDKVQVGLTQYSGDPQTEWDLNSF--QTKEQVLAAVHHLR---YK 292
Cdd:cd01471      2 DLYLLVDGSGSIGySNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPnsTNKDLALNAIRALLslyYP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  293 GGNTFTGLALTHVlEQNLKPAAGVRPEAAKVLILVTDGKSQDDVRT--AARILKDQDIDVFVVGV-KNVDEAELKLLASQ 369
Cdd:cd01471     82 NGSTNTTSALLVV-EKHLFDTRGNRENAPQLVIIMTDGIPDSKFRTlkEARKLRERGVIIAVLGVgQGVNHEENRSLVGC 160


                   ...
gi 1907143554  370 PLD 372
Cdd:cd01471    161 DPD 163
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 126-369 8.17e-21

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: 93.85  E-value: 8.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  126 RLAGATLEPTSLPLRGPDSEKTSEPSIAFTLSRDLPILGVASKDQRKLKQGLGVQNSAQTTTDLERQSHTAASVGKQGKL 205
Cdd:COG1240      1 DLALALLALLLLLALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  206 DHPQFQCTPPTPADIIFLVDGSWS-IGHNHFQQVKDFLASIITQFaigPDKVQVGLTQYSGDPQTEWDLNSfqTKEQVLA 284
Cdd:COG1240     81 LAPLALARPQRGRDVVLVVDASGSmAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTR--DREALKR 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  285 AVHHLRYKGGnTFTGLALTHVLEQnlkpAAGVRPEAAKVLILVTDGK---SQDDVRTAARILKDQDIDVFVVGV--KNVD 359
Cdd:COG1240    156 ALDELPPGGG-TPLGDALALALEL----LKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVgtEAVD 230

                          250
                   ....*....|
gi 1907143554  360 EAELKLLASQ 369
Cdd:COG1240    231 EGLLREIAEA 240
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 217-388 1.08e-18

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 85.51  E-value: 1.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  217 PADIIFLVDGSWSIGHNHFQQVKDFLASIITQF------AIGPDKVQVGLTQYSGDPQTEW-DLNSFQTKEQVLAAVHHL 289
Cdd:cd01480      2 PVDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  290 RYKGGNTFTGLALTHVLEQNLKpaaGVRPEAAKVLILVTDGKSQ-DDVRTAARILKDQD---IDVFVVGVKNVDEAELKL 365
Cdd:cd01480     82 EYIGGGTFTDCALKYATEQLLE---GSHQKENKFLLVITDGHSDgSPDGGIEKAVNEADhlgIKIFFVAVGSQNEEPLSR 158

                          170       180
                   ....*....|....*....|...
gi 1907143554  366 LASQPLdiTVHNVLDFPQLDTLA 388
Cdd:cd01480    159 IACDGK--SALYRENFAELLWSF 179
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1126-1262 1.22e-14

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 78.02  E-value: 1.22e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554 1126 GPPGQQGHPGPKGEPGPPGQTGPEGPGGQQGSPGTQG----RAVQGPMGPPGAKGEKGDQGLSGLQGLSGQQGIPGKTGL 1201
Cdd:NF038329   126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGpagpQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907143554 1202 QGPKGMRGL--EGPAGLPGPPGPRGFQGLAGARGTNGERGAPGAVGPTGLPGSKGERGEKGEP 1262
Cdd:NF038329   206 QGPAGPAGPdgEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1163-1262 1.10e-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: 74.94  E-value: 1.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554 1163 RAVQGPMGPPGAKGEKGDQGLSGLQGLSGQQGIPGKTGLQGPKGMRGLEGPaglpgppgprgfQGLAGARGTNGERGAPG 1242
Cdd:NF038329   119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE------------AGPQGPAGKDGEAGAKG 186

                           90       100
                   ....*....|....*....|
gi 1907143554 1243 AVGPTGLPGSKGERGEKGEP 1262
Cdd:NF038329   187 PAGEKGPQGPRGETGPAGEQ 206
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1088-1262 6.11e-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: 69.55  E-value: 6.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554 1088 PALRDGETCPAFPSAcaysseTPGPPGPQGPPGLPGRNGPPGQQGHPGPKGEPGPPGQTGPEGPGGQQGSPGTQGRAVQG 1167
Cdd:NF038329   163 PAGPQGEAGPQGPAG------KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQG 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554 1168 PMGPPGAKGEKGDQGLSGLQGLSGQQGIPGKTGLQGPKGMRGLEGPAglpgppgprgfqGLAGARGTNGERGAPGAVGP- 1246
Cdd:NF038329   237 PDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPV------------GPAGKDGQNGKDGLPGKDGKd 304

                          170
                   ....*....|....*...
gi 1907143554 1247 --TGLPGSKGERGEKGEP 1262
Cdd:NF038329   305 gqNGKDGLPGKDGKDGQP 322
fn3 pfam00041
Fibronectin type III domain;
792-860 1.34e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.66  E-value: 1.34e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907143554  792 TPNSLQVNWTPP---SGHVLHYRLNYTLASGSGPEKSISVPGTRSHAVLRDLMSATKYRVLVSAVYRAGESM 860
Cdd:pfam00041   12 TSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGP 83
fn3 pfam00041
Fibronectin type III domain;
418-496 1.17e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 58.97  E-value: 1.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  418 PTPTRLILTHATSSSIHLSWTPALY---PPLKYLIVWQPSRGG-APKEVVVEGPVSSMELGNLTSSTEYLVSVLPVYESG 493
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDgngPITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1907143554  494 VGK 496
Cdd:pfam00041   81 EGP 83
VWA_2 pfam13519
von Willebrand factor type A domain;
220-327 1.20e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 59.61  E-value: 1.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  220 IIFLVDGSWSI-----GHNHFQQVKDFLASIITQFAIgpdkVQVGLTQYSGDPQTEWDLNSfqTKEQVLAAVHHLRYKGG 294
Cdd:pfam13519    1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSLPG----DRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1907143554  295 NTFTGLALTHVLEQnlkpAAGVRPEAAKVLILV 327
Cdd:pfam13519   75 GTNLAAALQLARAA----LKHRRKNQPRRIVLI 103
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
643-878 1.56e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 65.41  E-value: 1.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  643 VPGNLTSATLGPLSSSTMYTVRVTCFYLGGGSS---VLTGHVTTQKAPSPGQLSVMELPGDAVKLSWLATALSGVLVYQI 719
Cdd:COG3401    187 VTSTTLVDGGGDIEPGTTYYYRVAATDTGGESApsnEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYRV 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  720 KWMPLGEGKAREI-SVPGTlgTATLPGLMKHVEYEITILAYYRDGTRSD----------------PVSLRYTPSaasrsp 782
Cdd:COG3401    267 YRSNSGDGPFTKVaTVTTT--SYTDTGLTNGTTYYYRVTAVDAAGNESApsnvvsvttdltppaaPSGLTATAV------ 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  783 psslalsseTPNSLQVNWTPPSG-HVLHYRLnYTLASGSGPEKSISVPGTRSHAVLRDLMSATKYRVLVSAVYRAGE--- 858
Cdd:COG3401    339 ---------GSSSITLSWTASSDaDVTGYNV-YRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNesa 408

                          250       260
                   ....*....|....*....|.
gi 1907143554  859 -SMAVSATYRTACPALHPDSS 878
Cdd:COG3401    409 pSEEVSATTASAASGESLTAS 429
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 792-859 6.24e-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: 57.12  E-value: 6.24e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907143554  792 TPNSLQVNWTPPS---GHVLHYRLNYTLASGSGPEKSISVPGTRSHAVLRDLMSATKYRVLVSAVYRAGES 859
Cdd:cd00063     13 TSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGES 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 420-499 7.73e-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: 57.12  E-value: 7.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  420 PTRLILTHATSSSIHLSWTPALY---PPLKYLIVWQPSRGGAPKEV-VVEGPVSSMELGNLTSSTEYLVSVLPVYESGVG 495
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDdggPITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGES 83


                   ....
gi 1907143554  496 KSLQ 499
Cdd:cd00063     84 PPSE 87
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 792-859 3.03e-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: 54.93  E-value: 3.03e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907143554   792 TPNSLQVNWTPPS-----GHVLHYRLNYTlaSGSGPEKSISVPGTRSHAVLRDLMSATKYRVLVSAVYRAGES 859
Cdd:smart00060   13 TSTSVTLSWEPPPddgitGYIVGYRVEYR--EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 219-367 5.03e-09

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: 57.33  E-value: 5.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  219 DIIFLVDGSWSIGH-NHFQQVKDFLASIITQFAIGPDKVQVGLTQYSG---DPQTEWDLNSFQtKEQVLAAVHHLR--YK 292
Cdd:cd01473      2 DLTLILDESASIGYsNWRKDVIPFTEKIINNLNISKDKVHVGILLFAEknrDVVPFSDEERYD-KNELLKKINDLKnsYR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  293 -GGNTFTGLALTHVLEQNLKpAAGVRPEAAKVLILVTDG----KSQDDVRTAARILKDQDIDVFVVGVKNVDEAELKLLA 367
Cdd:cd01473     81 sGGETYIVEALKYGLKNYTK-HGNRRKDAPKVTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLA 159
fn3 pfam00041
Fibronectin type III domain;
687-763 9.29e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.57  E-value: 9.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  687 PSPGQLSVMELPGDAVKLSWLA-TALSGVLV-YQIKWMPLGEGKA-REISVPGTLGTATLPGLMKHVEYEITILAYYRDG 763
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPpPDGNGPITgYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 418-495 9.79e-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: 53.77  E-value: 9.79e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554   418 PTPTRLILTHATSSSIHLSWTPALYP-PLKYLIVWQPSRGGAP---KEVVVEGPVSSMELGNLTSSTEYLVSVLPVYESG 493
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDgITGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1907143554   494 VG 495
Cdd:smart00060   82 EG 83
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1194-1262 2.18e-08

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: 51.73  E-value: 2.18e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907143554 1194 GIPGKTGLQGPKGMRGlegpagLPgppgprgfqGLAGARGTNGERGAPGAVGPTGLPGSKGERGEKGEP 1262
Cdd:pfam01391    1 GPPGPPGPPGPPGPPG------PP---------GPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
fn3 pfam00041
Fibronectin type III domain;
598-666 3.34e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 52.03  E-value: 3.34e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907143554  598 GPPRHLTFSDVRYNSTCVSWEA----QRPVRLVKVSYISSDGSHSGQTQ-VPGNLTSATLGPLSSSTMYTVRVT 666
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKNSGEPWNEItVPGTTTSVTLTGLKPGTEYEVRVQ 74
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1166-1209 4.37e-08

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: 50.96  E-value: 4.37e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1907143554 1166 QGPMGPPGAKGEKGDQGLSGLQGLSGQQGIPGKTGLQGPKGMRG 1209
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1166-1262 1.27e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.41  E-value: 1.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554 1166 QGPMGPPGAKGEKgdqglsglqglsGQQGIPGKTGLQGPKgmrglegpaglpgppgprgfqglagargtnGERGAPGAVG 1245
Cdd:pfam01391    3 PGPPGPPGPPGPP------------GPPGPPGPPGPPGPP------------------------------GEPGPPGPPG 40

                           90
                   ....*....|....*..
gi 1907143554 1246 PTGLPGSKGERGEKGEP 1262
Cdd:pfam01391   41 PPGPPGPPGAPGAPGPP 57
fn3 pfam00041
Fibronectin type III domain;
517-581 1.74e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.11  E-value: 1.74e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907143554  517 AVTPRTLHVTW-PPSAG---VTQYLVQYLLATSTGEEQKREVHVGQPEVLLDGLEPGQDYDVSVQSLRG 581
Cdd:pfam00041   10 DVTSTSLTVSWtPPPDGngpITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 517-577 2.32e-07

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: 49.54  E-value: 2.32e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907143554   517 AVTPRTLHVTW--PPSAGVTQYLVQYLLATSTGEEQKREVHV--GQPEVLLDGLEPGQDYDVSVQ 577
Cdd:smart00060   11 DVTSTSVTLSWepPPDDGITGYIVGYRVEYREEGSEWKEVNVtpSSTSYTLTGLKPGTEYEFRVR 75
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 517-594 5.43e-07

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 5.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  517 AVTPRTLHVTWPPSAG----VTQYLVQYLLATSTGEEQKREVHVGQPEVLLDGLEPGQDYDVSVQSLRGPEASE-VQSIR 591
Cdd:cd00063     11 DVTSTSVTLSWTPPEDdggpITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPpSESVT 90


                   ...
gi 1907143554  592 ART 594
Cdd:cd00063     91 VTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 689-770 8.18e-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: 48.26  E-value: 8.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  689 PGQLSVMELPGDAVKLSWLATALSG--VLVYQIKWMPLGEGKAREISV-PGTLGTATLPGLMKHVEYEITILAYYRDGtR 765
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPPEDDGgpITGYVVEYREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVNGGG-E 82


                   ....*
gi 1907143554  766 SDPVS 770
Cdd:cd00063     83 SPPSE 87
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 219-367 1.02e-06

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 53.04  E-value: 1.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  219 DIIFLVDGSWSIG-HNHFQQVKDFLASIITQFAIGPDKVQVGLTQYSGDPQTEWDLNSFQT--KEQVLAAVHHLRyKG-- 293
Cdd:PTZ00441    44 DLYLLVDGSGSIGyHNWITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASkdKEQALIIVKSLR-KTyl 122

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907143554  294 --GNTFTGLALTHVlEQNLKPAAGvRPEAAKVLILVTDG--KSQDDVRTAARILKDQDIDVFVVGV-KNVDEAELKLLA 367
Cdd:PTZ00441   123 pyGKTNMTDALLEV-RKHLNDRVN-RENAIQLVILMTDGipNSKYRALEESRKLKDRNVKLAVIGIgQGINHQFNRLLA 199
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 218-370 7.08e-06

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: 48.28  E-value: 7.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  218 ADIIFLVDGSWSIGHNhFQQVKDFLASIITQFaIGPDkVQVGLTQYSGDPQTEWDLNSFQTKEQVLAAVHHLRYKGGNTF 297
Cdd:cd01474      5 FDLYFVLDKSGSVAAN-WIEIYDFVEQLVDRF-NSPG-LRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTY 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907143554  298 TGLALTHVLEQNLKPAAGVRpEAAKVLILVTDGKSQDDV----RTAARILKDQDIDVFVVGVKNVDEAELKLLASQP 370
Cdd:cd01474     82 IHEGLENANEQIFNRNGGGR-ETVSVIIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSK 157
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 598-674 9.18e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 45.30  E-value: 9.18e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554   598 GPPRHLTFSDVRYNSTCVSWE--AQRPVRLVKVSYISSDGSHSGQTQ---VPGNLTSATLGPLSSSTMYTVRVTCFYLGG 672
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEppPDDGITGYIVGYRVEYREEGSEWKevnVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1907143554   673 GS 674
Cdd:smart00060   82 EG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 687-763 1.34e-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: 44.53  E-value: 1.34e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554   687 PSPGQLSVMELPGDAVKLSWLATALSGVLVYQIKWMPLGEGKA---REISVPGTLGTATLPGLMKHVEYEITILAYYRDG 763
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 598-683 1.41e-05

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: 44.79  E-value: 1.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  598 GPPRHLTFSDVRYNSTCVSWEA----QRPVRLVKVSYISSDGSHSGQ-TQVPGNLTSATLGPLSSSTMYTVRVTCFYLGG 672
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPpeddGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 1907143554  673 -GSSVLTGHVTT 683
Cdd:cd00063     82 eSPPSESVTVTT 93
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 219-369 2.55e-05

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 46.51  E-value: 2.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  219 DIIFLVDGSWSIGHNHFQQVKDFLASIITQFAIGPDKVQVGLTQYSGDPQTEWDLNSF--QTKEQVLAAVHHLRYK---- 292
Cdd:cd01470      2 NIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFnsNDADDVIKRLEDFNYDdhgd 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  293 GGNTFTGLALTHVLEQnlKPAAGVRPEAA-----KVLILVTDGKSQ---------DDVR------TAARILKDQDIDVFV 352
Cdd:cd01470     82 KTGTNTAAALKKVYER--MALEKVRNKEAfnetrHVIILFTDGKSNmggsplptvDKIKnlvyknNKSDNPREDYLDVYV 159

                          170
                   ....*....|....*...
gi 1907143554  353 VGV-KNVDEAELKLLASQ 369
Cdd:cd01470    160 FGVgDDVNKEELNDLASK 177
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
564-866 6.24e-04

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 44.22  E-value: 6.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  564 DGLEPGQDYDVSVQSL---RGPEASEVQSIRARTSALGPPRHLTFSDVRYNSTCVSWEAQRPVRLV--KVsYISSDGSHS 638
Cdd:COG3401    197 GDIEPGTTYYYRVAATdtgGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATgyRV-YRSNSGDGP 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  639 GQTQVPGNLTSATLGPLSSSTMYTVRVTCFYLGGGSSVLTG--HVTTQKAP--SPGQLSVMELPGDAVKLSWLATALSGV 714
Cdd:COG3401    276 FTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNvvSVTTDLTPpaAPSGLTATAVGSSSITLSWTASSDADV 355

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  715 LVYQIKWMPLGEGKAREISVPGTLGTATLPGLMKHVEYEITILAYYRDGTRSDPVSLRYTPSAASRSPPSSLALSSETPN 794
Cdd:COG3401    356 TGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPL 435

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907143554  795 SLQVNWTPPSGHVLHYRLNYTLASGSGPEKSISVPGTRSHAVLR---DLMSATKYRVLVSAVYRAGESMAVSATY 866
Cdd:COG3401    436 TDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTAtttDTTTANLSVTTGSLVGGSGASSVTNSVS 510
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1167-1209 1.64e-03

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 42.58  E-value: 1.64e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1907143554 1167 GPMGPPGAKGEKGDQGLSGLQGLSGQQGIPGKTGLQGPKGMRG 1209
Cdd:NF038329   293 GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
404-713 2.64e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 42.30  E-value: 2.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  404 PVKPAAGTRVLDPLPTPTRLILTHATSSSIHLSWTPALYPPLKYLIVWQPSRGGAPKEVVVEGPVSSMELGNLTSSTEYL 483
Cdd:COG3401    220 PSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYY 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  484 VSVLPVYESGV--GKS--LQGRATTAPLPPPGPLTLAAVTPRTLHVTWPPSAG--VTQYLVqYLLATSTGEEQKREVHVG 557
Cdd:COG3401    300 YRVTAVDAAGNesAPSnvVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDadVTGYNV-YRSTSGGGTYTKIAETVT 378

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  558 QPEVLLDGLEPGQDYDVSVQSL--RGPEASEVQSIRARTSALGPPRHLTFSDVRYNSTCVSWEAQRPV--RLVKVSYISS 633
Cdd:COG3401    379 TTSYTDTGLTPGTTYYYKVTAVdaAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASaaSNPGVSAAVL 458

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  634 DGSHSGQTQVPGNLTSATLGPLSSSTMYTVRVTCFYLGGGSSVLTGHVTTQKAPSPGQLSVMELPGDAVKLSWLATALSG 713
Cdd:COG3401    459 ADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTV 538
Periplasmic_Binding_Protein_Type_2 cd00648
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
 327-427 9.95e-03

Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.


Pssm-ID: 270214 [Multi-domain]  Cd Length: 196  Bit Score: 38.71  E-value: 9.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143554  327 VTDGKSQDDVRTAariLKDQDIDVFVVGVKNVDEAELKLLASQPLDItvhnvldfpqLDTLAPLLSRLICQK---IQGRG 403
Cdd:cd00648     33 LVPGSSIGTLIEA---LAAGDADVAVGPIAPALEAAADKLAPGGLYI----------VPELYVGGYVLVVRKgssIKGLL 99

                           90       100
                   ....*....|....*....|....
gi 1907143554  404 PVKPAAGTRVLDPLPTPTRLILTH 427
Cdd:cd00648    100 AVADLDGKRVGVGDPGSTAVRQAR 123
 
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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