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Conserved domains on  [gi|1864118215|ref|NP_001371876|]
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collagen alpha-1(XIV) chain isoform 2 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1031-1195 1.58e-88

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: 284.95  E-value: 1.58e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1031 ADLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGNT 1110
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFE-IGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1111 KTGKAIKYVRDTLFTAESGTRRGIPKVIVVITDGRSQDDVNKISREMQLDGYSIFAIGVADADYSELVSIGSKPSARHVF 1190
Cdd:cd01482     80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159


                   ....*
gi 1864118215 1191 FVDDF 1195
Cdd:cd01482    160 NVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 157-320 5.97e-83

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: 269.16  E-value: 5.97e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  157 ADIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGNTL 236
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  237 TGLALNYIFENSFKPEAGSRTGVSKIGILITDGKSQDDIIPPSRNLRESGVELFAIGVKNADVNELQEIASEPDSTHVYN 316
Cdd:cd01482     81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                   ....
gi 1864118215  317 VAEF 320
Cdd:cd01482    161 VADF 164
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 1229-1424 1.63e-53

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


:

Pssm-ID: 214560  Cd Length: 184  Bit Score: 185.64  E-value: 1.63e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  1229 GFKMMEMFGLVEKDFSSVEGVSMEPGtfnvFPCYQLHKDALVSQPTRYLHPEGLPSDYTISFLFRIlpdTPQEPFALWEI 1308
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPG----SPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  1309 LNKNSDPLVGVILDNGGKTLTYFNYDQSGDFQTVTFEGpeiRKIFYGSFHKLHIVVSETLVKVVIDCKQVGEKAMNASA- 1387
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGq 150

                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1864118215  1388 -NITSDGVEVLGKMVRSRGPggnsAPFQLQMFDIVCST 1424
Cdd:smart00210  151 pPIDTDGIEVRGAQAADRKP----FQGDLQQLKIVCDP 184
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1478-1608 1.84e-18

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 90.35  E-value: 1.84e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1478 QQGEPGPKGPDGPRGEiglpgpqgppgpqgpsglsiQGMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRGLPG 1557
Cdd:NF038329   118 EKGEPGPAGPAGPAGE--------------------QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG 177

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1864118215 1558 KDGSSGPPGPPGPIGIPGTPGVPGITGSMGPQGALGPPGVPGAKGERGERG 1608
Cdd:NF038329   178 KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG 228
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
396-781 3.58e-18

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 90.45  E-value: 3.58e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  396 DEVVVDGTVSSTVLKNLMSLTEYQIAVFAI---YAHTASEGLRGTeTTLALPMA-SDLLLYDVTENSMRVKWDAVP--GA 469
Cdd:COG3401    183 TSLTVTSTTLVDGGGDIEPGTTYYYRVAATdtgGESAPSNEVSVT-TPTTPPSApTGLTATADTPGSVTLSWDPVTesDA 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  470 SGYLILYAPlteglAGDEKEMKIGE-THTDIELSGLLPNTEYTVTVYAM--FGEE--ASDPVTGQETTLALSPPRNLRIS 544
Cdd:COG3401    262 TGYRVYRSN-----SGDGPFTKVATvTTTSYTDTGLTNGTTYYYRVTAVdaAGNEsaPSNVVSVTTDLTPPAAPSGLTAT 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  545 NVGSNSARLTWDP-TSRQINGYRIVYNNADGTEINEV-EVDPITTFPLKGLTPLTEYTIAIFSIYDEG----QSEPLTGV 618
Cdd:COG3401    337 AVGSSSITLSWTAsSDADVTGYNVYRSTSGGGTYTKIaETVTTTSYTDTGLTPGTTYYYKVTAVDAAGnesaPSEEVSAT 416

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  619 FTTEEVPAQQYLEIDEVTTDSFRVTWHPLSADEGLHKLMWIPVYGGKTEEVVLKEEQDSHVIEGLEPGTEYEVSLLAVLD 698
Cdd:COG3401    417 TASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSL 496

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  699 DGSESEVVTAVGTTLDSFWTEPATTIVPTTSVTSVFQTGIRNLV-VGDETTSSLRVKWDISDSDVQQFRVTYMTAQGDPE 777
Cdd:COG3401    497 VGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGAsTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITT 576


                   ....
gi 1864118215  778 EEVI 781
Cdd:COG3401    577 LGGS 580
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 32-112 1.50e-12

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 65.21  E-value: 1.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215   32 PPTRLRYNVISHDSIQISWKAPRGKFG---GYKLLVTPTSGGKTNQLNLQN-TATKAIIQGLMPDQNYTVQIIAYNKDKE 107
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDDGGpitGYVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVNGGGE 82


                   ....*
gi 1864118215  108 SKPAQ 112
Cdd:cd00063     83 SPPSE 87
fn3 pfam00041
Fibronectin type III domain;
832-901 1.99e-12

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.36  E-value: 1.99e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1864118215  832 PQNLRVSEEWYNRLRITWDPP---SSPVKGYRIVYKPVSVPGPTLETFVGADINTILITNLLSGMDYNVKIFA 901
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
fn3 pfam00041
Fibronectin type III domain;
354-432 1.04e-10

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.74  E-value: 1.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  354 GPPTELITSEVTARSFMVNWTHAP---GNVEKYRVVYYPTRGGKPD-EVVVDGTVSSTVLKNLMSLTEYQIAVFAIYAHT 429
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1864118215  430 ASE 432
Cdd:pfam00041   81 EGP 83
fn3 pfam00041
Fibronectin type III domain;
922-997 8.49e-05

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 42.79  E-value: 8.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  922 VTNLQAKHVEMTSLCAHWQ----VHRHATAYRVVIESLQD-RQKQESTVGGGTTRHCFYGLQPDSEYKISVYTKLQEIEG 996
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTpppdGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   .
gi 1864118215  997 P 997
Cdd:pfam00041   83 P 83
 
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 ...
 1031-1195 1.58e-88

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: 284.95  E-value: 1.58e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1031 ADLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGNT 1110
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFE-IGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1111 KTGKAIKYVRDTLFTAESGTRRGIPKVIVVITDGRSQDDVNKISREMQLDGYSIFAIGVADADYSELVSIGSKPSARHVF 1190
Cdd:cd01482     80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159


                   ....*
gi 1864118215 1191 FVDDF 1195
Cdd:cd01482    160 NVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 157-320 5.97e-83

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: 269.16  E-value: 5.97e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  157 ADIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGNTL 236
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  237 TGLALNYIFENSFKPEAGSRTGVSKIGILITDGKSQDDIIPPSRNLRESGVELFAIGVKNADVNELQEIASEPDSTHVYN 316
Cdd:cd01482     81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                   ....
gi 1864118215  317 VAEF 320
Cdd:cd01482    161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
158-328 9.07e-67

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 223.31  E-value: 9.07e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  158 DIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGNTL- 236
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  237 TGLALNYIFENSFKPEAGSRTGVSKIGILITDGKSQD-DIIPPSRNLRESGVELFAIGVKNADVNELQEIASEPDSTHVY 315
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                          170
                   ....*....|...
gi 1864118215  316 NVAEFDLMHTVVE 328
Cdd:pfam00092  161 TVSDFEALEDLQD 173
VWA pfam00092
von Willebrand factor type A domain;
1032-1204 1.27e-65

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 219.84  E-value: 1.27e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1032 DLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGNTK 1111
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLD-IGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1112 -TGKAIKYVRDTLFTAESGTRRGIPKVIVVITDGRSQD-DVNKISREMQLDGYSIFAIGVADADYSELVSIGSKPSARHV 1189
Cdd:pfam00092   80 nTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHV 159

                          170
                   ....*....|....*
gi 1864118215 1190 FFVDDFDAFKKIEDE 1204
Cdd:pfam00092  160 FTVSDFEALEDLQDQ 174
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 1229-1424 1.63e-53

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 185.64  E-value: 1.63e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  1229 GFKMMEMFGLVEKDFSSVEGVSMEPGtfnvFPCYQLHKDALVSQPTRYLHPEGLPSDYTISFLFRIlpdTPQEPFALWEI 1308
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPG----SPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  1309 LNKNSDPLVGVILDNGGKTLTYFNYDQSGDFQTVTFEGpeiRKIFYGSFHKLHIVVSETLVKVVIDCKQVGEKAMNASA- 1387
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGq 150

                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1864118215  1388 -NITSDGVEVLGKMVRSRGPggnsAPFQLQMFDIVCST 1424
Cdd:smart00210  151 pPIDTDGIEVRGAQAADRKP----FQGDLQQLKIVCDP 184
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 158-323 2.65e-50

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: 176.11  E-value: 2.65e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215   158 DIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYK-GGNTL 236
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215   237 TGLALNYIFENSFKPEAGSRTGVSKIGILITDGKSQD---DIIPPSRNLRESGVELFAIGVKNA-DVNELQEIASEPDST 312
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160

                           170
                    ....*....|.
gi 1864118215   313 HVYNVAEFDLM 323
Cdd:smart00327  161 YVFLPELLDLL 171
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1032-1198 2.71e-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: 173.02  E-value: 2.71e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  1032 DLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYK-GGNT 1110
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLD-IGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGT 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  1111 KTGKAIKYVRDTLFTAESGTRRGIPKVIVVITDGRSQD---DVNKISREMQLDGYSIFAIGV-ADADYSELVSIGSKPSA 1186
Cdd:smart00327   80 NLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGG 159

                           170
                    ....*....|..
gi 1864118215  1187 RHVFFVDDFDAF 1198
Cdd:smart00327  160 VYVFLPELLDLL 171
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1478-1608 1.84e-18

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 90.35  E-value: 1.84e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1478 QQGEPGPKGPDGPRGEiglpgpqgppgpqgpsglsiQGMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRGLPG 1557
Cdd:NF038329   118 EKGEPGPAGPAGPAGE--------------------QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG 177

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1864118215 1558 KDGSSGPPGPPGPIGIPGTPGVPGITGSMGPQGALGPPGVPGAKGERGERG 1608
Cdd:NF038329   178 KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG 228
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
396-781 3.58e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 90.45  E-value: 3.58e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  396 DEVVVDGTVSSTVLKNLMSLTEYQIAVFAI---YAHTASEGLRGTeTTLALPMA-SDLLLYDVTENSMRVKWDAVP--GA 469
Cdd:COG3401    183 TSLTVTSTTLVDGGGDIEPGTTYYYRVAATdtgGESAPSNEVSVT-TPTTPPSApTGLTATADTPGSVTLSWDPVTesDA 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  470 SGYLILYAPlteglAGDEKEMKIGE-THTDIELSGLLPNTEYTVTVYAM--FGEE--ASDPVTGQETTLALSPPRNLRIS 544
Cdd:COG3401    262 TGYRVYRSN-----SGDGPFTKVATvTTTSYTDTGLTNGTTYYYRVTAVdaAGNEsaPSNVVSVTTDLTPPAAPSGLTAT 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  545 NVGSNSARLTWDP-TSRQINGYRIVYNNADGTEINEV-EVDPITTFPLKGLTPLTEYTIAIFSIYDEG----QSEPLTGV 618
Cdd:COG3401    337 AVGSSSITLSWTAsSDADVTGYNVYRSTSGGGTYTKIaETVTTTSYTDTGLTPGTTYYYKVTAVDAAGnesaPSEEVSAT 416

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  619 FTTEEVPAQQYLEIDEVTTDSFRVTWHPLSADEGLHKLMWIPVYGGKTEEVVLKEEQDSHVIEGLEPGTEYEVSLLAVLD 698
Cdd:COG3401    417 TASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSL 496

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  699 DGSESEVVTAVGTTLDSFWTEPATTIVPTTSVTSVFQTGIRNLV-VGDETTSSLRVKWDISDSDVQQFRVTYMTAQGDPE 777
Cdd:COG3401    497 VGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGAsTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITT 576


                   ....
gi 1864118215  778 EEVI 781
Cdd:COG3401    577 LGGS 580
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1478-1608 4.22e-18

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 89.19  E-value: 4.22e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1478 QQGEPGPKGPDGPRGEiglpgpqgppgpqgpsglsiQGMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSP---GQRG 1554
Cdd:NF038329   166 PQGEAGPQGPAGKDGE--------------------AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAgpaGEDG 225

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1864118215 1555 LPGKDGSSGPPGPPGpigipgtpgvPGITGSMGPQGALGPPGVPGAKGERGERG 1608
Cdd:NF038329   226 PAGPAGDGQQGPDGD----------PGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1479-1609 1.45e-17

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 87.65  E-value: 1.45e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1479 QGEPGPKGPDGPRGEiglpgpqgppgpqgPSGLSIQGMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRGLPGK 1558
Cdd:NF038329   125 AGPAGPAGEQGPRGD--------------RGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1864118215 1559 DGSSGPPGPPGPIGIPGTPGVPGITGSMGPQGALGPPGVPGaKGERGERGD 1609
Cdd:NF038329   191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGD 240
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 536-621 5.30e-16

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: 74.84  E-value: 5.30e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  536 SPPRNLRISNVGSNSARLTWDP---TSRQINGYRIVYNNADGTEINEVEVDPI--TTFPLKGLTPLTEYTIAIFSIYDEG 610
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPpedDGGPITGYVVEYREKGSGDWKEVEVTPGseTSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 1864118215  611 QSEPLTGV-FTT 621
Cdd:cd00063     82 ESPPSESVtVTT 93
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1479-1608 8.72e-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: 75.71  E-value: 8.72e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1479 QGEPGPKGPDGPRGEI-GLPGPQGPPGPQGPSGLSIQGMPGMPGE--KGEKGDTGLPGPQGIP---GGVGSPGRDGSPGQ 1552
Cdd:NF038329   185 KGPAGEKGPQGPRGETgPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDgpqGPDGPAGKDGPRGD 264

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1864118215 1553 RGLPGKDgssgppgppgpigipgtpgvpGITGSMGPQGALGPPGVPGAKGERGERG 1608
Cdd:NF038329   265 RGEAGPD---------------------GPDGKDGERGPVGPAGKDGQNGKDGLPG 299
fn3 pfam00041
Fibronectin type III domain;
536-614 1.84e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.44  E-value: 1.84e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  536 SPPRNLRISNVGSNSARLTWDP---TSRQINGYRIVYNNADGTEI-NEVEVDP-ITTFPLKGLTPLTEYTIAIFSIYDEG 610
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPppdGNGPITGYEVEYRPKNSGEPwNEITVPGtTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 1864118215  611 QSEP 614
Cdd:pfam00041   81 EGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 536-612 1.23e-12

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 64.94  E-value: 1.23e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215   536 SPPRNLRISNVGSNSARLTWDPTSRQIN-----GYRIVYNNADGTEINEVEVDPITTFPLKGLTPLTEYTIAIFSIYDEG 610
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGItgyivGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1864118215   611 QS 612
Cdd:smart00060   82 EG 83
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1480-1608 1.48e-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: 71.86  E-value: 1.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1480 GEPGPKGPDGPRGEIGLPGPQGPPGPQGPSGLSIQGMPGMPGEKGEKGDTGLPGPQGIPGG------VGSPGRDGSPGQR 1553
Cdd:NF038329   216 GEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKdgergpVGPAGKDGQNGKD 295

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1864118215 1554 GLPGKDgssgppgppgpigipgtpgvpgitgsmGPQGALGPPGVPGAKGERGERG 1608
Cdd:NF038329   296 GLPGKD---------------------------GKDGQNGKDGLPGKDGKDGQPG 323
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 32-112 1.50e-12

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 65.21  E-value: 1.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215   32 PPTRLRYNVISHDSIQISWKAPRGKFG---GYKLLVTPTSGGKTNQLNLQN-TATKAIIQGLMPDQNYTVQIIAYNKDKE 107
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDDGGpitGYVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVNGGGE 82


                   ....*
gi 1864118215  108 SKPAQ 112
Cdd:cd00063     83 SPPSE 87
fn3 pfam00041
Fibronectin type III domain;
832-901 1.99e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.36  E-value: 1.99e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1864118215  832 PQNLRVSEEWYNRLRITWDPP---SSPVKGYRIVYKPVSVPGPTLETFVGADINTILITNLLSGMDYNVKIFA 901
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 157-308 5.84e-12

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: 68.04  E-value: 5.84e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  157 ADIVILVDGSWSIGRFN-FRLVRHFLENLVTAFDvgsEKTRIGLAQYSGdpRIEWHLNAFSTKDEVIEAVRNLPYKGGnT 235
Cdd:COG1240     93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGG--EAEVLLPLTRDREALKRALDELPPGGG-T 166

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1864118215  236 LTGLALNYIFEnSFKPEAGSRtgvSKIGILITDGKSQDDIIPP---SRNLRESGVELFAIGVKNADVNE--LQEIASE 308
Cdd:COG1240    167 PLGDALALALE-LLKRADPAR---RKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEAVDEglLREIAEA 240
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1515-1604 1.37e-11

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: 60.97  E-value: 1.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1515 GMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRglpgkdgssgppgppgpigipgtpgvpgitgsmGPQGALGP 1594
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPP---------------------------------GPPGPPGP 47

                           90
                   ....*....|
gi 1864118215 1595 PGVPGAKGER 1604
Cdd:pfam01391   48 PGAPGAPGPP 57
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 830-912 2.08e-11

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: 61.74  E-value: 2.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  830 SGPQNLRVSEEWYNRLRITWDPPS---SPVKGYRIVYKPVSVPGPTLETFVGADINTILITNLLSGMDYNVKIFASQASG 906
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                   ....*.
gi 1864118215  907 FSDALT 912
Cdd:cd00063     82 ESPPSE 87
fn3 pfam00041
Fibronectin type III domain;
32-110 5.17e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.51  E-value: 5.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215   32 PPTRLRYNVISHDSIQISWKAPR---GKFGGYKLLVTPT-SGGKTNQLNLQNTATKAIIQGLMPDQNYTVQIIAYNKDKE 107
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 1864118215  108 SKP 110
Cdd:pfam00041   82 GPP 84
fn3 pfam00041
Fibronectin type III domain;
354-432 1.04e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.74  E-value: 1.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  354 GPPTELITSEVTARSFMVNWTHAP---GNVEKYRVVYYPTRGGKPD-EVVVDGTVSSTVLKNLMSLTEYQIAVFAIYAHT 429
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1864118215  430 ASE 432
Cdd:pfam00041   81 EGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 354-432 1.46e-09

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 56.74  E-value: 1.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  354 GPPTELITSEVTARSFMVNWTHAP---GNVEKYRVVYYPTRGGKPDEV-VVDGTVSSTVLKNLMSLTEYQIAVFAIYAHT 429
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                   ...
gi 1864118215  430 ASE 432
Cdd:cd00063     82 ESP 84
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1031-1201 4.61e-09

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: 59.18  E-value: 4.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1031 ADLVFMVDGSWSIGDEN-FNKIISFLYSTVGALNKigtdGTQVAMVQFTDDPRTEFKLNayKTKETLLDAIKHISYKGGn 1109
Cdd:COG1240     93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRP----RDRVGLVAFGGEAEVLLPLT--RDREALKRALDELPPGGG- 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1110 TKTGKAIKYVRDTLFTAESGTRrgipKVIVVITDGR---SQDDVNKISREMQLDGYSIFAIGVADADYSE--LVSIGSKP 1184
Cdd:COG1240    166 TPLGDALALALELLKRADPARR----KVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEglLREIAEAT 241

                          170
                   ....*....|....*..
gi 1864118215 1185 SARHvFFVDDFDAFKKI 1201
Cdd:COG1240    242 GGRY-FRADDLSELAAI 257
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 32-108 8.46e-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: 54.16  E-value: 8.46e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215    32 PPTRLRYNVISHDSIQISWKAP-RGKFGGYKL---LVTPTSGGKTNQLNLQNTATKAIIQGLMPDQNYTVQIIAYNKDKE 107
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPpDDGITGYIVgyrVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 1864118215   108 S 108
Cdd:smart00060   83 G 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 830-908 9.18e-08

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 51.08  E-value: 9.18e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215   830 SGPQNLRVSEEWYNRLRITWDPPSSP-VKGYRIVYKPVSVPGPTLETFVGADI--NTILITNLLSGMDYNVKIFASQASG 906
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDgITGYIVGYRVEYREEGSEWKEVNVTPssTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1864118215   907 FS 908
Cdd:smart00060   82 EG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 354-431 1.38e-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: 50.69  E-value: 1.38e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215   354 GPPTELITSEVTARSFMVNWTH-APGNVEKYRVVYYPTRGGKPD---EVVVDGTVSSTVLKNLMSLTEYQIAVFAIYAHT 429
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPpPDDGITGYIVGYRVEYREEGSewkEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1864118215   430 AS 431
Cdd:smart00060   82 EG 83
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1478-1558 2.22e-07

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 55.30  E-value: 2.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1478 QQGEPGPKGPDGPRGEiglpgpqgppgpqgpsglsiQGMPGMPGEKGEKGDTGLPGP---------QGIPGG---VGSPG 1545
Cdd:NF038329   264 DRGEAGPDGPDGKDGE--------------------RGPVGPAGKDGQNGKDGLPGKdgkdgqngkDGLPGKdgkDGQPG 323

                           90
                   ....*....|....*.
gi 1864118215 1546 RDGSPGQR---GLPGK 1558
Cdd:NF038329   324 KDGLPGKDgkdGQPGK 339
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1023-1196 6.32e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 47.65  E-value: 6.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1023 KEVCKAaKADLVFMVDGSWSIGDENF-NKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKL--NAYKTKETLLDA 1099
Cdd:PTZ00441    36 EEVCNE-EVDLYLLVDGSGSIGYHNWiTHVIPMLMGLIQQLN-LSDDAINLYMSLFSNNTTELIRLgsGASKDKEQALII 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1100 IKHISyKG----GNTKTGKAIKYVRDTLftAESGTRRGIPKVIVVITDG--RSQDDVNKISREMQLDGYSIFAIGVA--- 1170
Cdd:PTZ00441   114 VKSLR-KTylpyGKTNMTDALLEVRKHL--NDRVNRENAIQLVILMTDGipNSKYRALEESRKLKDRNVKLAVIGIGqgi 190

                          170       180
                   ....*....|....*....|....*.
gi 1864118215 1171 DADYSELVsIGSKPSARHVFFVDDFD 1196
Cdd:PTZ00441   191 NHQFNRLL-AGCRPREGKCKFYSDAD 215
fn3 pfam00041
Fibronectin type III domain;
922-997 8.49e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 42.79  E-value: 8.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  922 VTNLQAKHVEMTSLCAHWQ----VHRHATAYRVVIESLQD-RQKQESTVGGGTTRHCFYGLQPDSEYKISVYTKLQEIEG 996
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTpppdGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   .
gi 1864118215  997 P 997
Cdd:pfam00041   83 P 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
31-112 1.49e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 43.45  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215   31 APPTRLRYNVISHDSIQISWKAPRGK-FGGYKLLVTPTSGGKTNQLNLQNTATKAIIQGLMPDQNYTVQIIAYNKD-KES 108
Cdd:COG3401    328 AAPSGLTATAVGSSSITLSWTASSDAdVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAgNES 407


                   ....
gi 1864118215  109 KPAQ 112
Cdd:COG3401    408 APSE 411
 
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 ...
 1031-1195 1.58e-88

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: 284.95  E-value: 1.58e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1031 ADLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGNT 1110
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFE-IGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1111 KTGKAIKYVRDTLFTAESGTRRGIPKVIVVITDGRSQDDVNKISREMQLDGYSIFAIGVADADYSELVSIGSKPSARHVF 1190
Cdd:cd01482     80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159


                   ....*
gi 1864118215 1191 FVDDF 1195
Cdd:cd01482    160 NVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 157-320 5.97e-83

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: 269.16  E-value: 5.97e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  157 ADIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGNTL 236
Cdd:cd01482      1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  237 TGLALNYIFENSFKPEAGSRTGVSKIGILITDGKSQDDIIPPSRNLRESGVELFAIGVKNADVNELQEIASEPDSTHVYN 316
Cdd:cd01482     81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                   ....
gi 1864118215  317 VAEF 320
Cdd:cd01482    161 VADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 157-320 3.96e-75

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: 246.76  E-value: 3.96e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  157 ADIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGNTL 236
Cdd:cd01472      1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  237 TGLALNYIFENSFKPEAGSRTGVSKIGILITDGKSQDDIIPPSRNLRESGVELFAIGVKNADVNELQEIASEPDSTHVYN 316
Cdd:cd01472     81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                   ....
gi 1864118215  317 VAEF 320
Cdd:cd01472    161 VADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1031-1195 4.08e-74

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


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 243.67  E-value: 4.08e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1031 ADLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGNT 1110
Cdd:cd01472      1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLD-IGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1111 KTGKAIKYVRDTLFTAESGTRRGIPKVIVVITDGRSQDDVNKISREMQLDGYSIFAIGVADADYSELVSIGSKPSARHVF 1190
Cdd:cd01472     80 NTGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVF 159


                   ....*
gi 1864118215 1191 FVDDF 1195
Cdd:cd01472    160 NVADF 164
VWA pfam00092
von Willebrand factor type A domain;
158-328 9.07e-67

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 223.31  E-value: 9.07e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  158 DIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGNTL- 236
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  237 TGLALNYIFENSFKPEAGSRTGVSKIGILITDGKSQD-DIIPPSRNLRESGVELFAIGVKNADVNELQEIASEPDSTHVY 315
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                          170
                   ....*....|...
gi 1864118215  316 NVAEFDLMHTVVE 328
Cdd:pfam00092  161 TVSDFEALEDLQD 173
VWA pfam00092
von Willebrand factor type A domain;
1032-1204 1.27e-65

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 219.84  E-value: 1.27e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1032 DLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGNTK 1111
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLD-IGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1112 -TGKAIKYVRDTLFTAESGTRRGIPKVIVVITDGRSQD-DVNKISREMQLDGYSIFAIGVADADYSELVSIGSKPSARHV 1189
Cdd:pfam00092   80 nTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHV 159

                          170
                   ....*....|....*
gi 1864118215 1190 FFVDDFDAFKKIEDE 1204
Cdd:pfam00092  160 FTVSDFEALEDLQDQ 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 157-315 9.92e-54

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: 185.19  E-value: 9.92e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  157 ADIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGN-T 235
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  236 LTGLALNYIFENSFKPeAGSRTGVSKIGILITDGKSQD--DIIPPSRNLRESGVELFAIGVKNADVNELQEIASEPDSTH 313
Cdd:cd01450     81 NTGKALQYALEQLFSE-SNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSERH 159


                   ..
gi 1864118215  314 VY 315
Cdd:cd01450    160 VF 161
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 1229-1424 1.63e-53

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 185.64  E-value: 1.63e-53
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  1229 GFKMMEMFGLVEKDFSSVEGVSMEPGtfnvFPCYQLHKDALVSQPTRYLHPEGLPSDYTISFLFRIlpdTPQEPFALWEI 1308
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPG----SPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  1309 LNKNSDPLVGVILDNGGKTLTYFNYDQSGDFQTVTFEGpeiRKIFYGSFHKLHIVVSETLVKVVIDCKQVGEKAMNASA- 1387
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGq 150

                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1864118215  1388 -NITSDGVEVLGKMVRSRGPggnsAPFQLQMFDIVCST 1424
Cdd:smart00210  151 pPIDTDGIEVRGAQAADRKP----FQGDLQQLKIVCDP 184
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1031-1190 2.09e-52

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: 181.34  E-value: 2.09e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1031 ADLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGN- 1109
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLD-IGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGg 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1110 TKTGKAIKYVRDTLFTaESGTRRGIPKVIVVITDGRSQD--DVNKISREMQLDGYSIFAIGVADADYSELVSIGSKPSAR 1187
Cdd:cd01450     80 TNTGKALQYALEQLFS-ESNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSER 158


                   ...
gi 1864118215 1188 HVF 1190
Cdd:cd01450    159 HVF 161
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 157-360 2.49e-52

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: 183.74  E-value: 2.49e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  157 ADIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGNTL 236
Cdd:cd01475      3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  237 TGLALNYIFENSFKPEAGSRTG---VSKIGILITDGKSQDDIIPPSRNLRESGVELFAIGVKNADVNELQEIASEPDSTH 313
Cdd:cd01475     83 TGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLADH 162

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1864118215  314 VYNVAEFDLMHTVVESLTRTLCSRVEEQDREIKASAHAITGPPTELI 360
Cdd:cd01475    163 VFYVEDFSTIEELTKKFQGKICVVPDLCATLSHVCQQVCISTPGSYL 209
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 157-320 2.55e-51

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: 178.67  E-value: 2.55e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  157 ADIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGNTL 236
Cdd:cd01481      1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  237 -TGLALNYIFENSFKPEAGSRT--GVSKIGILITDGKSQDDIIPPSRNLRESGVELFAIGVKNADVNELQEIASEPDstH 313
Cdd:cd01481     81 nTGSALDYVVKNLFTKSAGSRIeeGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS--F 158


                   ....*..
gi 1864118215  314 VYNVAEF 320
Cdd:cd01481    159 VFQVSDF 165
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 158-323 2.65e-50

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: 176.11  E-value: 2.65e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215   158 DIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYK-GGNTL 236
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215   237 TGLALNYIFENSFKPEAGSRTGVSKIGILITDGKSQD---DIIPPSRNLRESGVELFAIGVKNA-DVNELQEIASEPDST 312
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160

                           170
                    ....*....|.
gi 1864118215   313 HVYNVAEFDLM 323
Cdd:smart00327  161 YVFLPELLDLL 171
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1032-1198 2.71e-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: 173.02  E-value: 2.71e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  1032 DLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYK-GGNT 1110
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLD-IGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGT 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  1111 KTGKAIKYVRDTLFTAESGTRRGIPKVIVVITDGRSQD---DVNKISREMQLDGYSIFAIGV-ADADYSELVSIGSKPSA 1186
Cdd:smart00327   80 NLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGG 159

                           170
                    ....*....|..
gi 1864118215  1187 RHVFFVDDFDAF 1198
Cdd:smart00327  160 VYVFLPELLDLL 171
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1031-1214 1.05e-46

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 167.56  E-value: 1.05e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1031 ADLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGNT 1110
Cdd:cd01475      3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLD-VGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1111 KTGKAIKYVRDTLFTAESGTRRG---IPKVIVVITDGRSQDDVNKISREMQLDGYSIFAIGVADADYSELVSIGSKPSAR 1187
Cdd:cd01475     82 MTGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161

                          170       180
                   ....*....|....*....|....*..
gi 1864118215 1188 HVFFVDDFDAFKKIEDELITFVCETAS 1214
Cdd:cd01475    162 HVFYVEDFSTIEELTKKFQGKICVVPD 188
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1031-1195 1.75e-43

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: 155.94  E-value: 1.75e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1031 ADLVFMVDGSWSIGDENFNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGN- 1109
Cdd:cd01481      1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLD-VGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSq 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1110 TKTGKAIKYVRDTLFTAESGTR--RGIPKVIVVITDGRSQDDVNKISREMQLDGYSIFAIGVADADYSELVSIGSKPSar 1187
Cdd:cd01481     80 LNTGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS-- 157


                   ....*...
gi 1864118215 1188 HVFFVDDF 1195
Cdd:cd01481    158 FVFQVSDF 165
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1032-1201 2.57e-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: 155.98  E-value: 2.57e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1032 DLVFMVDGSWSIGDENFNKIISFLYSTVGALnKIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGNTK 1111
Cdd:cd01469      2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKL-DIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1112 TGKAIKYVRDTLFTAESGTRRGIPKVIVVITDGRSQDD--VNKISREMQLDGYSIFAIGVADA-----DYSELVSIGSKP 1184
Cdd:cd01469     81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDplLKDVIPQAEREGIIRYAIGVGGHfqrenSREELKTIASKP 160

                          170
                   ....*....|....*..
gi 1864118215 1185 SARHVFFVDDFDAFKKI 1201
Cdd:cd01469    161 PEEHFFNVTDFAALKDI 177
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 158-321 9.45e-39

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 142.88  E-value: 9.45e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  158 DIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYKGGNTLT 237
Cdd:cd01469      2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  238 GLALNYIFENSFKPEAGSRTGVSKIGILITDGKSQDD-----IIPPSrnlRESGVELFAIGV-----KNADVNELQEIAS 307
Cdd:cd01469     82 ATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDpllkdVIPQA---EREGIIRYAIGVgghfqRENSREELKTIAS 158

                          170
                   ....*....|....
gi 1864118215  308 EPDSTHVYNVAEFD 321
Cdd:cd01469    159 KPPEEHFFNVTDFA 172
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 157-315 5.51e-34

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: 128.84  E-value: 5.51e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  157 ADIVILVDGSWSIGRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYK-GGNT 235
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  236 LTGLALNYIFENSFKPEagsRTGVSKIGILITDGKSQDDIIPP---SRNLRESGVELFAIGVKN-ADVNELQEIASEPDS 311
Cdd:cd00198     81 NIGAALRLALELLKSAK---RPNARRVIILLTDGEPNDGPELLaeaARELRKLGITVYTIGIGDdANEDELKEIADKTTG 157


                   ....
gi 1864118215  312 THVY 315
Cdd:cd00198    158 GAVF 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1031-1190 8.12e-28

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 111.12  E-value: 8.12e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1031 ADLVFMVDGSWSIGDENFNKIISFLYSTVGALnKIGTDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYK-GGN 1109
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSL-SASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1110 TKTGKAIKYVRDTLFtaeSGTRRGIPKVIVVITDGRSQDD---VNKISREMQLDGYSIFAIGV-ADADYSELVSIGSKPS 1185
Cdd:cd00198     80 TNIGAALRLALELLK---SAKRPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIgDDANEDELKEIADKTT 156


                   ....*
gi 1864118215 1186 ARHVF 1190
Cdd:cd00198    157 GGAVF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1031-1191 4.53e-26

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: 106.33  E-value: 4.53e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1031 ADLVFMVDGSWSIGDEnFNKIISFLYSTVGALnKIGTDGTQVAMVQFTDDPRT--EFKLNAYKTKETLLDAIKHISYKGG 1108
Cdd:cd01476      1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGL-EIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1109 NTKTGKAIKYVRDtLFTAESGTRRGIPKVIVVITDGRSQDDVNKISREMQ-LDGYSIFAIGVAD---ADYSELVSIGSKP 1184
Cdd:cd01476     79 TTATGAAIEVALQ-QLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRaVPNIETFAVGTGDpgtVDTEELHSITGNE 157


                   ....*..
gi 1864118215 1185 saRHVFF 1191
Cdd:cd01476    158 --DHIFT 162
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 157-312 3.45e-25

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: 103.63  E-value: 3.45e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  157 ADIVILVDGSWSIgRFNFRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPR--IEWHLNAFSTKDEVIEAVRNLPYKGGN 234
Cdd:cd01476      1 LDLLFVLDSSGSV-RGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  235 TLTGLALNYIFeNSFKPEAGSRTGVSKIGILITDGKSQDDIIPPSRNLRES-GVELFAIGVKN---ADVNELQEIASEPD 310
Cdd:cd01476     80 TATGAAIEVAL-QQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGDpgtVDTEELHSITGNED 158


                   ..
gi 1864118215  311 ST 312
Cdd:cd01476    159 HI 160
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 158-294 3.46e-19

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: 87.06  E-value: 3.46e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  158 DIVILVDGSWSIGRFN-FRLVRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIEWHLNAFSTKDE-----VIEAVRNLPYK 231
Cdd:cd01471      2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKdlalnAIRALLSLYYP 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1864118215  232 GGNTLTGLALNYIFENSFKPeAGSRTGVSKIGILITDGKSQDD--IIPPSRNLRESGVELFAIGV 294
Cdd:cd01471     82 NGSTNTTSALLVVEKHLFDT-RGNRENAPQLVIIMTDGIPDSKfrTLKEARKLRERGVIIAVLGV 145
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1478-1608 1.84e-18

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 90.35  E-value: 1.84e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1478 QQGEPGPKGPDGPRGEiglpgpqgppgpqgpsglsiQGMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRGLPG 1557
Cdd:NF038329   118 EKGEPGPAGPAGPAGE--------------------QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG 177

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1864118215 1558 KDGSSGPPGPPGPIGIPGTPGVPGITGSMGPQGALGPPGVPGAKGERGERG 1608
Cdd:NF038329   178 KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG 228
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
396-781 3.58e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 90.45  E-value: 3.58e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  396 DEVVVDGTVSSTVLKNLMSLTEYQIAVFAI---YAHTASEGLRGTeTTLALPMA-SDLLLYDVTENSMRVKWDAVP--GA 469
Cdd:COG3401    183 TSLTVTSTTLVDGGGDIEPGTTYYYRVAATdtgGESAPSNEVSVT-TPTTPPSApTGLTATADTPGSVTLSWDPVTesDA 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  470 SGYLILYAPlteglAGDEKEMKIGE-THTDIELSGLLPNTEYTVTVYAM--FGEE--ASDPVTGQETTLALSPPRNLRIS 544
Cdd:COG3401    262 TGYRVYRSN-----SGDGPFTKVATvTTTSYTDTGLTNGTTYYYRVTAVdaAGNEsaPSNVVSVTTDLTPPAAPSGLTAT 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  545 NVGSNSARLTWDP-TSRQINGYRIVYNNADGTEINEV-EVDPITTFPLKGLTPLTEYTIAIFSIYDEG----QSEPLTGV 618
Cdd:COG3401    337 AVGSSSITLSWTAsSDADVTGYNVYRSTSGGGTYTKIaETVTTTSYTDTGLTPGTTYYYKVTAVDAAGnesaPSEEVSAT 416

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  619 FTTEEVPAQQYLEIDEVTTDSFRVTWHPLSADEGLHKLMWIPVYGGKTEEVVLKEEQDSHVIEGLEPGTEYEVSLLAVLD 698
Cdd:COG3401    417 TASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSL 496

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  699 DGSESEVVTAVGTTLDSFWTEPATTIVPTTSVTSVFQTGIRNLV-VGDETTSSLRVKWDISDSDVQQFRVTYMTAQGDPE 777
Cdd:COG3401    497 VGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGAsTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITT 576


                   ....
gi 1864118215  778 EEVI 781
Cdd:COG3401    577 LGGS 580
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1478-1608 4.22e-18

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 89.19  E-value: 4.22e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1478 QQGEPGPKGPDGPRGEiglpgpqgppgpqgpsglsiQGMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSP---GQRG 1554
Cdd:NF038329   166 PQGEAGPQGPAGKDGE--------------------AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAgpaGEDG 225

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1864118215 1555 LPGKDGSSGPPGPPGpigipgtpgvPGITGSMGPQGALGPPGVPGAKGERGERG 1608
Cdd:NF038329   226 PAGPAGDGQQGPDGD----------PGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1479-1609 1.45e-17

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 87.65  E-value: 1.45e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1479 QGEPGPKGPDGPRGEiglpgpqgppgpqgPSGLSIQGMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRGLPGK 1558
Cdd:NF038329   125 AGPAGPAGEQGPRGD--------------RGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1864118215 1559 DGSSGPPGPPGPIGIPGTPGVPGITGSMGPQGALGPPGVPGaKGERGERGD 1609
Cdd:NF038329   191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGD 240
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1032-1169 5.47e-17

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: 80.89  E-value: 5.47e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1032 DLVFMVDGSWSIGDEN-FNKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKLNAYKT--KETLLDAIKH---ISY 1105
Cdd:cd01471      2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLN-ISPDEINLYLVTFSTNAKELIRLSSPNStnKDLALNAIRAllsLYY 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1864118215 1106 KGGNTKTGKAIKYVRDTLFTAEsGTRRGIPKVIVVITDGRSQDDVN--KISREMQLDGYSIFAIGV 1169
Cdd:cd01471     81 PNGSTNTTSALLVVEKHLFDTR-GNRENAPQLVIIMTDGIPDSKFRtlKEARKLRERGVIIAVLGV 145
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 536-621 5.30e-16

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: 74.84  E-value: 5.30e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  536 SPPRNLRISNVGSNSARLTWDP---TSRQINGYRIVYNNADGTEINEVEVDPI--TTFPLKGLTPLTEYTIAIFSIYDEG 610
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPpedDGGPITGYVVEYREKGSGDWKEVEVTPGseTSYTLTGLKPGTEYEFRVRAVNGGG 81

                           90
                   ....*....|..
gi 1864118215  611 QSEPLTGV-FTT 621
Cdd:cd00063     82 ESPPSESVtVTT 93
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 157-319 9.91e-16

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: 77.04  E-value: 9.91e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  157 ADIVILVDGSWSIGRFNFRLVRHFLENLVTAF------DVGSEKTRIGLAQYSGDPRIEWHLNAF-STKDEVIEAVRNLP 229
Cdd:cd01480      3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDiRNYTSLKEAVDNLE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  230 YKGGNTLTGLALNYIFENSFKpeaGSRTGVSKIGILITDGKSQ---DDIIPPSRNLRES-GVELFAIGVkNADVNE-LQE 304
Cdd:cd01480     83 YIGGGTFTDCALKYATEQLLE---GSHQKENKFLLVITDGHSDgspDGGIEKAVNEADHlGIKIFFVAV-GSQNEEpLSR 158

                          170
                   ....*....|....*.
gi 1864118215  305 IASEPDSTHV-YNVAE 319
Cdd:cd01480    159 IACDGKSALYrENFAE 174
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 1031-1210 1.52e-15

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: 76.78  E-value: 1.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1031 ADLVFMVDGSWSIGDeNFNKIISFLYSTVGALNKigtDGTQVAMVQFTDDPRTEFKLNAYKTKETL-LDAIKHISyKGGN 1109
Cdd:cd01474      5 FDLYFVLDKSGSVAA-NWIEIYDFVEQLVDRFNS---PGLRFSFITFSTRATKILPLTDDSSAIIKgLEVLKKVT-PSGQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1110 TKTGKAIKYVRDTLFTAESGTRRgIPKVIVVITDGRSQDDV-------NKISREMqldGYSIFAIGVADADYSELVSIGS 1182
Cdd:cd01474     80 TYIHEGLENANEQIFNRNGGGRE-TVSVIIALTDGQLLLNGhkypeheAKLSRKL---GAIVYCVGVTDFLKSQLINIAD 155

                          170       180
                   ....*....|....*....|....*....
gi 1864118215 1183 KPSarHVFFVDD-FDAFKKIEDELITFVC 1210
Cdd:cd01474    156 SKE--YVFPVTSgFQALSGIIESVVKKAC 182
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1031-1194 2.02e-14

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: 73.57  E-value: 2.02e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1031 ADLVFMVDGSWSIGDENFN-------KIISFLYSTvgALNKIGTDGTQVAMVQFTDDPRTEF-KLNAYKTKETLLDAIKH 1102
Cdd:cd01480      3 VDITFVLDSSESVGLQNFDitknfvkRVAERFLKD--YYRKDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1103 ISYKGGNTKTGKAIKYVRDTLFTAESGTRRgipKVIVVITDGRSQ---DDVNKIS-REMQLDGYSIFAIGVADADYSELV 1178
Cdd:cd01480     81 LEYIGGGTFTDCALKYATEQLLEGSHQKEN---KFLLVITDGHSDgspDGGIEKAvNEADHLGIKIFFVAVGSQNEEPLS 157

                          170       180
                   ....*....|....*....|....*.
gi 1864118215 1179 SIGSKPSARHV----------FFVDD 1194
Cdd:cd01480    158 RIACDGKSALYrenfaellwsFFIDD 183
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1479-1608 8.72e-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: 75.71  E-value: 8.72e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1479 QGEPGPKGPDGPRGEI-GLPGPQGPPGPQGPSGLSIQGMPGMPGE--KGEKGDTGLPGPQGIP---GGVGSPGRDGSPGQ 1552
Cdd:NF038329   185 KGPAGEKGPQGPRGETgPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDgpqGPDGPAGKDGPRGD 264

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1864118215 1553 RGLPGKDgssgppgppgpigipgtpgvpGITGSMGPQGALGPPGVPGAKGERGERG 1608
Cdd:NF038329   265 RGEAGPD---------------------GPDGKDGERGPVGPAGKDGQNGKDGLPG 299
fn3 pfam00041
Fibronectin type III domain;
536-614 1.84e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.44  E-value: 1.84e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  536 SPPRNLRISNVGSNSARLTWDP---TSRQINGYRIVYNNADGTEI-NEVEVDP-ITTFPLKGLTPLTEYTIAIFSIYDEG 610
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPppdGNGPITGYEVEYRPKNSGEPwNEITVPGtTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 1864118215  611 QSEP 614
Cdd:pfam00041   81 EGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 536-612 1.23e-12

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 64.94  E-value: 1.23e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215   536 SPPRNLRISNVGSNSARLTWDPTSRQIN-----GYRIVYNNADGTEINEVEVDPITTFPLKGLTPLTEYTIAIFSIYDEG 610
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGItgyivGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1864118215   611 QS 612
Cdd:smart00060   82 EG 83
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1480-1608 1.48e-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: 71.86  E-value: 1.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1480 GEPGPKGPDGPRGEIGLPGPQGPPGPQGPSGLSIQGMPGMPGEKGEKGDTGLPGPQGIPGG------VGSPGRDGSPGQR 1553
Cdd:NF038329   216 GEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKdgergpVGPAGKDGQNGKD 295

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1864118215 1554 GLPGKDgssgppgppgpigipgtpgvpgitgsmGPQGALGPPGVPGAKGERGERG 1608
Cdd:NF038329   296 GLPGKD---------------------------GKDGQNGKDGLPGKDGKDGQPG 323
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 32-112 1.50e-12

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 65.21  E-value: 1.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215   32 PPTRLRYNVISHDSIQISWKAPRGKFG---GYKLLVTPTSGGKTNQLNLQN-TATKAIIQGLMPDQNYTVQIIAYNKDKE 107
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDDGGpitGYVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVNGGGE 82


                   ....*
gi 1864118215  108 SKPAQ 112
Cdd:cd00063     83 SPPSE 87
fn3 pfam00041
Fibronectin type III domain;
832-901 1.99e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.36  E-value: 1.99e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1864118215  832 PQNLRVSEEWYNRLRITWDPP---SSPVKGYRIVYKPVSVPGPTLETFVGADINTILITNLLSGMDYNVKIFA 901
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
VWA_2 pfam13519
von Willebrand factor type A domain;
1033-1141 3.02e-12

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 64.62  E-value: 3.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1033 LVFMVDGSWSIGDE-----NFNKIISFLYSTVGALNkigtdGTQVAMVQFTDDPRTEFKLNayKTKETLLDAIKHISYKG 1107
Cdd:pfam13519    1 LVFVLDTSGSMRNGdygptRLEAAKDAVLALLKSLP-----GDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKG 73

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1864118215 1108 GNTKTGKAIKYVRDTLFTAesgtRRGIPKVIVVI 1141
Cdd:pfam13519   74 GGTNLAAALQLARAALKHR----RKNQPRRIVLI 103
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 157-308 5.84e-12

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: 68.04  E-value: 5.84e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  157 ADIVILVDGSWSIGRFN-FRLVRHFLENLVTAFDvgsEKTRIGLAQYSGdpRIEWHLNAFSTKDEVIEAVRNLPYKGGnT 235
Cdd:COG1240     93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGG--EAEVLLPLTRDREALKRALDELPPGGG-T 166

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1864118215  236 LTGLALNYIFEnSFKPEAGSRtgvSKIGILITDGKSQDDIIPP---SRNLRESGVELFAIGVKNADVNE--LQEIASE 308
Cdd:COG1240    167 PLGDALALALE-LLKRADPAR---RKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEAVDEglLREIAEA 240
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1515-1604 1.37e-11

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: 60.97  E-value: 1.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1515 GMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRglpgkdgssgppgppgpigipgtpgvpgitgsmGPQGALGP 1594
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPP---------------------------------GPPGPPGP 47

                           90
                   ....*....|
gi 1864118215 1595 PGVPGAKGER 1604
Cdd:pfam01391   48 PGAPGAPGPP 57
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 830-912 2.08e-11

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: 61.74  E-value: 2.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  830 SGPQNLRVSEEWYNRLRITWDPPS---SPVKGYRIVYKPVSVPGPTLETFVGADINTILITNLLSGMDYNVKIFASQASG 906
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                   ....*.
gi 1864118215  907 FSDALT 912
Cdd:cd00063     82 ESPPSE 87
fn3 pfam00041
Fibronectin type III domain;
32-110 5.17e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.51  E-value: 5.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215   32 PPTRLRYNVISHDSIQISWKAPR---GKFGGYKLLVTPT-SGGKTNQLNLQNTATKAIIQGLMPDQNYTVQIIAYNKDKE 107
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 1864118215  108 SKP 110
Cdd:pfam00041   82 GPP 84
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1514-1557 6.00e-11

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: 59.43  E-value: 6.00e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1864118215 1514 QGMPGMPGEKGEKGDTGLPGPQGIPGGVGSPGRDGSPGQRGLPG 1557
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
fn3 pfam00041
Fibronectin type III domain;
354-432 1.04e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 59.74  E-value: 1.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  354 GPPTELITSEVTARSFMVNWTHAP---GNVEKYRVVYYPTRGGKPD-EVVVDGTVSSTVLKNLMSLTEYQIAVFAIYAHT 429
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1864118215  430 ASE 432
Cdd:pfam00041   81 EGP 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 354-432 1.46e-09

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 56.74  E-value: 1.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  354 GPPTELITSEVTARSFMVNWTHAP---GNVEKYRVVYYPTRGGKPDEV-VVDGTVSSTVLKNLMSLTEYQIAVFAIYAHT 429
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                   ...
gi 1864118215  430 ASE 432
Cdd:cd00063     82 ESP 84
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
355-620 1.53e-09

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 62.71  E-value: 1.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  355 PPTELITSEVTARSFMVNWT-HAPGNVEKYRVvYYPTRGGKPDEVVVDGTVSSTVLKNLMSLTEYQIAVFAIYAH----T 429
Cdd:COG3401    235 APTGLTATADTPGSVTLSWDpVTESDATGYRV-YRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAgnesA 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  430 ASEGLRGTETTLALPMASDLLLYDVTENSMRVKWDAVPG--ASGYLILYAPLTEGLAGdekemKIGETHTDIEL--SGLL 505
Cdd:COG3401    314 PSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDadVTGYNVYRSTSGGGTYT-----KIAETVTTTSYtdTGLT 388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  506 PNTEYTVTVYAM----FGEEASDPVTGQETTLALSPPRNLRISNVGSN-SARLTWDPTSRQINGYRIVYNNADGTEINEV 580
Cdd:COG3401    389 PGTTYYYKVTAVdaagNESAPSEEVSATTASAASGESLTASVDAVPLTdVAGATAAASAASNPGVSAAVLADGGDTGNAV 468

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1864118215  581 EVDPITTFPLKGLTPLTEYTIAIFSIYDEGQSEPLTGVFT 620
Cdd:COG3401    469 PFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNS 508
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 447-516 3.48e-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: 55.31  E-value: 3.48e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1864118215   447 SDLLLYDVTENSMRVKWDAV--PGASGYLILYAPLTEGLAGDEKEMKIGETHTDIELSGLLPNTEYTVTVYA 516
Cdd:smart00060    5 SNLRVTDVTSTSVTLSWEPPpdDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1031-1201 4.61e-09

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: 59.18  E-value: 4.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1031 ADLVFMVDGSWSIGDEN-FNKIISFLYSTVGALNKigtdGTQVAMVQFTDDPRTEFKLNayKTKETLLDAIKHISYKGGn 1109
Cdd:COG1240     93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRP----RDRVGLVAFGGEAEVLLPLT--RDREALKRALDELPPGGG- 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1110 TKTGKAIKYVRDTLFTAESGTRrgipKVIVVITDGR---SQDDVNKISREMQLDGYSIFAIGVADADYSE--LVSIGSKP 1184
Cdd:COG1240    166 TPLGDALALALELLKRADPARR----KVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEglLREIAEAT 241

                          170
                   ....*....|....*..
gi 1864118215 1185 SARHvFFVDDFDAFKKI 1201
Cdd:COG1240    242 GGRY-FRADDLSELAAI 257
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 32-108 8.46e-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: 54.16  E-value: 8.46e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215    32 PPTRLRYNVISHDSIQISWKAP-RGKFGGYKL---LVTPTSGGKTNQLNLQNTATKAIIQGLMPDQNYTVQIIAYNKDKE 107
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPpDDGITGYIVgyrVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 1864118215   108 S 108
Cdd:smart00060   83 G 83
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 158-335 9.10e-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: 56.94  E-value: 9.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  158 DIVILVDGSWSIGRFNFRL-VRHFLENLVTAFDVGSEKTRIGLAQYSGDPRIewhLNAFS-----TKDEVIEAVRNLP-- 229
Cdd:cd01473      2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRD---VVPFSdeeryDKNELLKKINDLKns 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  230 YK-GGNTLTGLALNYIFENSFKPEaGSRTGVSKIGILITDG----KSQDDIIPPSRNLRESGVELFAIGVKNADVNELQE 304
Cdd:cd01473     79 YRsGGETYIVEALKYGLKNYTKHG-NRRKDAPKVTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVGAASENKLKL 157

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1864118215  305 IA--SEPDSTHVYNV-AEFDLMHTVVESLTRTLC 335
Cdd:cd01473    158 LAgcDINNDNCPNVIkTEWNNLNGISKFLTDKIC 191
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 158-328 1.10e-08

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: 56.91  E-value: 1.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  158 DIVILVDGSWSIGRFNFRLVRHFLENLVT---AFDVgseKTRIGLAQYSGDPRIEWHLNAFST--KDEVIEAVRNLPYK- 231
Cdd:cd01470      2 NIYIALDASDSIGEEDFDEAKNAIKTLIEkisSYEV---SPRYEIISYASDPKEIVSIRDFNSndADDVIKRLEDFNYDd 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  232 ---GGNTLTGLALNYIFENSFKPEAGSRTGVSKIG---ILITDGKSQ---------DDII------PPSRNLRESGVELF 290
Cdd:cd01470     79 hgdKTGTNTAAALKKVYERMALEKVRNKEAFNETRhviILFTDGKSNmggsplptvDKIKnlvyknNKSDNPREDYLDVY 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1864118215  291 AIGV-KNADVNELQEIASE-PDSTHVYNVAEFDLMHTVVE 328
Cdd:cd01470    159 VFGVgDDVNKEELNDLASKkDNERHFFKLKDYEDLQEVFD 198
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 630-701 1.14e-08

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.77  E-value: 1.14e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1864118215   630 LEIDEVTTDSFRVTWHPLSADEGLH-KLMWIPVY---GGKTEEVVLKEEQDSHVIEGLEPGTEYEVSLLAVLDDGS 701
Cdd:smart00060    7 LRVTDVTSTSVTLSWEPPPDDGITGyIVGYRVEYreeGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82
fn3 pfam00041
Fibronectin type III domain;
447-516 1.69e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.19  E-value: 1.69e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864118215  447 SDLLLYDVTENSMRVKWDAVPGASG----YLILYAPLTEGlaGDEKEMKIGETHTDIELSGLLPNTEYTVTVYA 516
Cdd:pfam00041    4 SNLTVTDVTSTSLTVSWTPPPDGNGpitgYEVEYRPKNSG--EPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 630-707 2.78e-08

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: 52.88  E-value: 2.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  630 LEIDEVTTDSFRVTWHPLSADEGLH---KLMWIPVYGGKTEEVVLKEEQD-SHVIEGLEPGTEYEVSLLAVLDDG----S 701
Cdd:cd00063      7 LRVTDVTSTSVTLSWTPPEDDGGPItgyVVEYREKGSGDWKEVEVTPGSEtSYTLTGLKPGTEYEFRVRAVNGGGesppS 86


                   ....*.
gi 1864118215  702 ESEVVT 707
Cdd:cd00063     87 ESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 447-532 8.87e-08

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: 51.34  E-value: 8.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  447 SDLLLYDVTENSMRVKWDAVPGA----SGYLILYAPLTEGlaGDEKEMKIGETHTDIELSGLLPNTEYTVTVYAMFGEEA 522
Cdd:cd00063      5 TNLRVTDVTSTSVTLSWTPPEDDggpiTGYVVEYREKGSG--DWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGE 82

                           90
                   ....*....|
gi 1864118215  523 SDPVTGQETT 532
Cdd:cd00063     83 SPPSESVTVT 92
VWA_2 pfam13519
von Willebrand factor type A domain;
159-266 9.05e-08

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 51.91  E-value: 9.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  159 IVILVDGSWSI-----GRFNFRLVRHFLENLVTAFDvgseKTRIGLAQYSGDPRIEWHLNafSTKDEVIEAVRNLPYKGG 233
Cdd:pfam13519    1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1864118215  234 NTLTGLALNYIFENSFKPeagsRTGVSKIGILI 266
Cdd:pfam13519   75 GTNLAAALQLARAALKHR----RKNQPRRIVLI 103
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 830-908 9.18e-08

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 51.08  E-value: 9.18e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215   830 SGPQNLRVSEEWYNRLRITWDPPSSP-VKGYRIVYKPVSVPGPTLETFVGADI--NTILITNLLSGMDYNVKIFASQASG 906
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDgITGYIVGYRVEYREEGSEWKEVNVTPssTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1864118215   907 FS 908
Cdd:smart00060   82 EG 83
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 156-335 1.28e-07

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


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 53.67  E-value: 1.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  156 IADIVILVDGSWSIGRfNFRLVRHFLENLVTAFDvgSEKTRIGLAQYSGDPRIEWHLNAFSTKD----EVIEAVrnLPyk 231
Cdd:cd01474      4 HFDLYFVLDKSGSVAA-NWIEIYDFVEQLVDRFN--SPGLRFSFITFSTRATKILPLTDDSSAIikglEVLKKV--TP-- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  232 GGNTLTGLALNYIFENSFKPEAGSRTgVSKIGILITDGKSQDDiiPPSRNLRES------GVELFAIGVKNADVNELQEI 305
Cdd:cd01474     77 SGQTYIHEGLENANEQIFNRNGGGRE-TVSVIIALTDGQLLLN--GHKYPEHEAklsrklGAIVYCVGVTDFLKSQLINI 153

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1864118215  306 ASEPDstHVYNVAE-FDLMHTVVESLTRTLC 335
Cdd:cd01474    154 ADSKE--YVFPVTSgFQALSGIIESVVKKAC 182
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 354-431 1.38e-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: 50.69  E-value: 1.38e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215   354 GPPTELITSEVTARSFMVNWTH-APGNVEKYRVVYYPTRGGKPD---EVVVDGTVSSTVLKNLMSLTEYQIAVFAIYAHT 429
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPpPDDGITGYIVGYRVEYREEGSewkEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 1864118215   430 AS 431
Cdd:smart00060   82 EG 83
fn3 pfam00041
Fibronectin type III domain;
625-700 1.50e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.49  E-value: 1.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  625 PAQQYLEIDEVTTDSFRVTWHPLSADEG---LHKLMWIPVYGGKTE-EVVLKEEQDSHVIEGLEPGTEYEVSLLAVLDDG 700
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGpitGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1478-1558 2.22e-07

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 55.30  E-value: 2.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1478 QQGEPGPKGPDGPRGEiglpgpqgppgpqgpsglsiQGMPGMPGEKGEKGDTGLPGP---------QGIPGG---VGSPG 1545
Cdd:NF038329   264 DRGEAGPDGPDGKDGE--------------------RGPVGPAGKDGQNGKDGLPGKdgkdgqngkDGLPGKdgkDGQPG 323

                           90
                   ....*....|....*.
gi 1864118215 1546 RDGSPGQR---GLPGK 1558
Cdd:NF038329   324 KDGLPGKDgkdGQPGK 339
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 1032-1180 2.41e-07

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 54.30  E-value: 2.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1032 DLVFMVDGSWSIGDENFNKIISFLYSTVGALNkigtDGTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHISYKGGnTK 1111
Cdd:COG2425    120 PVVLCVDTSGSMAGSKEAAAKAAALALLRALR----PNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFAGGG-TD 194

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1864118215 1112 TGKAIKYVRDTLftAESGTRRgipKVIVVITDGRSQDDVNKISREM--QLDGYSIFAIGVADADYSELVSI 1180
Cdd:COG2425    195 IAPALRAALELL--EEPDYRN---ADIVLITDGEAGVSPEELLREVraKESGVRLFTVAIGDAGNPGLLEA 260
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
424-826 5.30e-07

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 54.95  E-value: 5.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  424 AIYAHTASEGL-----RGTETTLALPMASDLLLYDVTENSMRVKWDAVPGASGYLILYapltegLAGDEKEMKIGETH-T 497
Cdd:COG4733    514 EKYAAIDAGAFddvppQWPPVNVTTSESLSVVAQGTAVTTLTVSWDAPAGAVAYEVEW------RRDDGNWVSVPRTSgT 587

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  498 DIELSGLLPNTeYTVTVYAM-FGEEASDPVTGQETTL-----ALSPPRNLRISNvGSNSARLTWD-PTSRQINGYRIVYN 570
Cdd:COG4733    588 SFEVPGIYAGD-YEVRVRAInALGVSSAWAASSETTVtgktaPPPAPTGLTATG-GLGGITLSWSfPVDADTLRTEIRYS 665

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  571 NADGTEINEVEVD--PITTFPLKGLTPLTEYTIAIFSIYDEGQSEPLTGVFTTEEVPAQQYLEIDEVTTDSfrVTWHPLS 648
Cdd:COG4733    666 TTGDWASATVAQAlyPGNTYTLAGLKAGQTYYYRARAVDRSGNVSAWWVSGQASADAAGILDAITGQILET--ELGQELD 743

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  649 ADE------GLHKLMWIPVYGGKTEEVVLKEEQDSHVIEGLEPGTEYEVSLLAVLDDGSESEVVTAVGTTLDSFWTEPAT 722
Cdd:COG4733    744 AIIqnatvaEVVAATVTDVTAQIDTAVLFAGVATAAAIGAEARVAATVAESATAAAATGTAADAAGDASGGVTAGTSGTT 823

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  723 TIvPTTSVTSVFQTGIRNLVVGDETTSSLRVKWDISDSDVQQFRVTymTAQGDPEEEVIGTVMVPGSQNNLLLKPLLPDT 802
Cdd:COG4733    824 GA-GDTAASTTRVAAAVVLAGVVVYGDAIIESGNTGDIVATGDIAS--AAAGAVATTVSGTTAADVSAVADSTAASLTAI 900

                          410       420
                   ....*....|....*....|....
gi 1864118215  803 EYKVTVTPIYTDGEGVSVSAPGKT 826
Cdd:COG4733    901 VIAATTIIDAIGDGTTREPAGDIG 924
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1533-1608 8.56e-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: 47.49  E-value: 8.56e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1864118215 1533 GPQGIPGGVGSPGRDGSPGQRglpgkdgssgppGPpgpigipgtpgvPGITGSMGPQGALGPPGVPGAKGERGERG 1608
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPP------------GP------------PGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
439-913 4.10e-06

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 51.54  E-value: 4.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  439 TTLALPMASDLLLYDVTENSMRVKWDAVPGASGYLILYAPLTEGLAGDEKEMKIGETHTDIELSGLLPNTEYTVTVYAMF 518
Cdd:COG3401     45 SVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGT 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  519 GEEASDPVTGQETTLALSPPRNLriSNVGSNSARLTWDPTSRQINGYRIVYNNADGTEINEVEVDPITTFPLKGLT--PL 596
Cdd:COG3401    125 ATTATAVAGGAATAGTYALGAGL--YGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDiePG 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  597 TEYTIAIFSIYDEGQSEPLTGV--FTTEEVPAQ-QYLEIDEVTTDSFRVTWHPLSADEglhkLMWIPVYGGKTEE---VV 670
Cdd:COG3401    203 TTYYYRVAATDTGGESAPSNEVsvTTPTTPPSApTGLTATADTPGSVTLSWDPVTESD----ATGYRVYRSNSGDgpfTK 278

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  671 LKEEQDSHVI-EGLEPGTEYEVSLLAVLDDGSESEVVTAVGTTLDsfwtepatTIVPTTsvtsvfqtgIRNLVVGDETTS 749
Cdd:COG3401    279 VATVTTTSYTdTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTTD--------LTPPAA---------PSGLTATAVGSS 341

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  750 SLRVKWD-ISDSDVQQFRVTYMTAQGDPEEEVIGTVmvpgSQNNLLLKPLLPDTEYKVTVTPIYTDGEGVSVSAP---GK 825
Cdd:COG3401    342 SITLSWTaSSDADVTGYNVYRSTSGGGTYTKIAETV----TTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEvsaTT 417

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  826 TLPSSGPQNLRVSEEWYNRLRITWDPPSSPVKGYRIVYKPVSVPGPTLETFVGADINTILITNLLSGMDYNVKIFASQAS 905
Cdd:COG3401    418 ASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLV 497


                   ....*...
gi 1864118215  906 GFSDALTG 913
Cdd:COG3401    498 GGSGASSV 505
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 152-308 1.99e-05

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 48.14  E-value: 1.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  152 QTPAIADIVILVDGSWSIGRFNFRLVRHFLENLVTAFdvgSEKTRIGLAQYSGDPRIEWHLNAFSTKDEVIEAVRNLPYK 231
Cdd:COG2425    114 VPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRAL---RPNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFAG 190

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1864118215  232 GGnTLTGLALNYIFEnSFKPEAGSRTGVskigILITDGKSQDDIIPPSRNLR--ESGVELFAIGVKNADVNELQEIASE 308
Cdd:COG2425    191 GG-TDIAPALRAALE-LLEEPDYRNADI----VLITDGEAGVSPEELLREVRakESGVRLFTVAIGDAGNPGLLEALAD 263
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1023-1196 6.32e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 47.65  E-value: 6.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1023 KEVCKAaKADLVFMVDGSWSIGDENF-NKIISFLYSTVGALNkIGTDGTQVAMVQFTDDPRTEFKL--NAYKTKETLLDA 1099
Cdd:PTZ00441    36 EEVCNE-EVDLYLLVDGSGSIGYHNWiTHVIPMLMGLIQQLN-LSDDAINLYMSLFSNNTTELIRLgsGASKDKEQALII 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1100 IKHISyKG----GNTKTGKAIKYVRDTLftAESGTRRGIPKVIVVITDG--RSQDDVNKISREMQLDGYSIFAIGVA--- 1170
Cdd:PTZ00441   114 VKSLR-KTylpyGKTNMTDALLEVRKHL--NDRVNRENAIQLVILMTDGipNSKYRALEESRKLKDRNVKLAVIGIGqgi 190

                          170       180
                   ....*....|....*....|....*.
gi 1864118215 1171 DADYSELVsIGSKPSARHVFFVDDFD 1196
Cdd:PTZ00441   191 NHQFNRLL-AGCRPREGKCKFYSDAD 215
fn3 pfam00041
Fibronectin type III domain;
922-997 8.49e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 42.79  E-value: 8.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  922 VTNLQAKHVEMTSLCAHWQ----VHRHATAYRVVIESLQD-RQKQESTVGGGTTRHCFYGLQPDSEYKISVYTKLQEIEG 996
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTpppdGNGPITGYEVEYRPKNSgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   .
gi 1864118215  997 P 997
Cdd:pfam00041   83 P 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
632-927 8.74e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 47.30  E-value: 8.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  632 IDEVTTDSFRVTWHPLSADEGLHKLMWIPVYGGKTEEVVLKEEQDSHVIEGLEPGTEYEVSLLAVLDDG--SESEVVTAV 709
Cdd:COG3401     28 KAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTltGSGSVGGAT 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  710 GTTLDSFWTEPATTIVPTTSVTSVFQ-TGIRNLVVGDETTSSLRVKWDISDSDVQQFRVTYMTAQGDPEEEVIGTVM--V 786
Cdd:COG3401    108 NTGLTSSDEVPSPAVGTATTATAVAGgAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSltV 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  787 PGSQNNLLLKPLLPDTEYKVTVTPIYTDGEG-----VSVSAPGkTLPSSgPQNLRVSEEWYNRLRITWDPPSSP-VKGYR 860
Cdd:COG3401    188 TSTTLVDGGGDIEPGTTYYYRVAATDTGGESapsneVSVTTPT-TPPSA-PTGLTATADTPGSVTLSWDPVTESdATGYR 265

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1864118215  861 IVYKpvSVPGPTLETFVGADINTILITNLLSGMDYNVKIFASQA----SGFSDALTG-MVKTLFLGVTNLQA 927
Cdd:COG3401    266 VYRS--NSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAagneSAPSNVVSVtTDLTPPAAPSGLTA 335
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 1032-1190 2.01e-04

VWA F09G8.8 type: 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. The members of this subgroup lack the MIDAS motif. This subgroup is found only in C. elegans and the members identified thus far are always found fused to a C-Lectin type domain. Biochemical function thus far has not be attributed to any of the members of this subgroup.


Pssm-ID: 238754 [Multi-domain]  Cd Length: 193  Bit Score: 44.34  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1032 DLVFMVDGSWSIGDENFNKIISFLYSTVGALNKIGTD-----GTQVAMVQFTDDPRTEFKLNAYKTKETLLDAIKHI--- 1103
Cdd:cd01477     21 DIVFVVDNSKGMTQGGLWQVRATISSLFGSSSQIGTDyddprSTRVGLVTYNSNATVVADLNDLQSFDDLYSQIQGSltd 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1104 --SYKGGNTKTGkaIKYVRDTLFTAESGTRRGIPKVIVVIT---DGRSQDDVNKISREMQLDGYSIfaIGVA---DADYS 1175
Cdd:cd01477    101 vsSTNASYLDTG--LQAAEQMLAAGKRTSRENYKKVVIVFAsdyNDEGSNDPRPIAARLKSTGIAI--ITVAftqDESSN 176

                          170
                   ....*....|....*
gi 1864118215 1176 ELVSIGSKPSARHVF 1190
Cdd:cd01477    177 LLDKLGKIASPGMNF 191
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 739-817 2.63e-04

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: 41.45  E-value: 2.63e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1864118215   739 RNLVVGDETTSSLRVKWDISDSDVQQFRVTYMTAQGDPEEEVIGTVMVPGSQNNLLLKPLLPDTEYKVTVTPIYTDGEG 817
Cdd:smart00060    5 SNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1580-1609 3.92e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 3.92e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1864118215 1580 PGITGSMGPQGALGPPGVPGAKGERGERGD 1609
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGE 32
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
31-112 1.49e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 43.45  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215   31 APPTRLRYNVISHDSIQISWKAPRGK-FGGYKLLVTPTSGGKTNQLNLQNTATKAIIQGLMPDQNYTVQIIAYNKD-KES 108
Cdd:COG3401    328 AAPSGLTATAVGSSSITLSWTASSDAdVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAgNES 407


                   ....
gi 1864118215  109 KPAQ 112
Cdd:COG3401    408 APSE 411
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 1032-1159 1.62e-03

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: 41.53  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1032 DLVFMVDGSWSIGDENFNK-IISFLYSTVGALNkIGTDGTQVAM----------VQFTDDPRTEfklnayktKETLLDAI 1100
Cdd:cd01473      2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLN-ISKDKVHVGIllfaeknrdvVPFSDEERYD--------KNELLKKI 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1864118215 1101 KHI--SYK-GGNTKTGKAIKYVRDTlFTAESGTRRGIPKVIVVITDGRSQDDVNKISREMQL 1159
Cdd:cd01473     73 NDLknSYRsGGETYIVEALKYGLKN-YTKHGNRRKDAPKVTMLFTDGNDTSASKKELQDISL 133
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 1037-1203 2.06e-03

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: 41.50  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1037 VDGSWSIGDENFNKiisFLYSTVGALNKIGTDGT--QVAMVQFTDDPR-----TEFKLNAYKTKETLLDAIKHISYKGGN 1109
Cdd:cd01470      7 LDASDSIGEEDFDE---AKNAIKTLIEKISSYEVspRYEIISYASDPKeivsiRDFNSNDADDVIKRLEDFNYDDHGDKT 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1110 -TKTGKAIKYVRDTLFTAESGTRRG---IPKVIVVITDGRS-------------QDDVNK-----ISREMQLDGYsIFAI 1167
Cdd:cd01470     84 gTNTAAALKKVYERMALEKVRNKEAfneTRHVIILFTDGKSnmggsplptvdkiKNLVYKnnksdNPREDYLDVY-VFGV 162

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1864118215 1168 GvADADYSELVSIGS-KPSARHVFFVDDFDAFKKIED 1203
Cdd:cd01470    163 G-DDVNKEELNDLASkKDNERHFFKLKDYEDLQEVFD 198
fn3 pfam00041
Fibronectin type III domain;
739-817 4.88e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 37.78  E-value: 4.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215  739 RNLVVGDETTSSLRVKWDIS---DSDVQQFRVTYmTAQGDPEEEVigTVMVPGSQNNLLLKPLLPDTEYKVTVTPIYTDG 815
Cdd:pfam00041    4 SNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEY-RPKNSGEPWN--EITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ..
gi 1864118215  816 EG 817
Cdd:pfam00041   81 EG 82
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
1107-1201 6.58e-03

Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 39.91  E-value: 6.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864118215 1107 GGNTKTGKAIKYVRDTLfTAESGTRRGIPK-----VIVVITDGRSQDD-----VNKISREMQLDGYSIFAIGV-ADADYS 1175
Cdd:COG4245     78 SGGTPLGAALELLLDLI-ERRVQKYTAEGKgdwrpVVFLITDGEPTDSdweaaLQRLKDGEAAKKANIFAIGVgPDADTE 156

                           90       100
                   ....*....|....*....|....*.
gi 1864118215 1176 ELVSIGskpSARHVFFVDDFDAFKKI 1201
Cdd:COG4245    157 VLKQLT---DPVRALDALDGLDFREF 179
 
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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