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Conserved domains on  [gi|568960715|ref|XP_006510860|]
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collagen alpha-1(XII) chain isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1198-1361 5.97e-92

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: 295.74  E-value: 5.97e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1198 ADIVLLVDGSWSIGRANFRTVRSFISRIVEVFEIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTL 1277
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1278 TGMALNFIRQQSFKTQAGMRPRARKIGVLITDGKSQDDVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDDTHAYN 1357
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                  ....
gi 568960715 1358 VADF 1361
Cdd:cd01482   161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 139-302 2.26e-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: 285.33  E-value: 2.26e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  139 TDLVFLVDGSWSVGRNNFKYILDFIVALVSAFDIGEEKTRVGVVQYSSDTRTEFNLNQYYRREDLLAAVKKIPYKGGNTM 218
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  219 TGDAIDYLVKNTFTESAGSRAGFPKVAIIITDGKSQDEVEIPARELRNIGVEVFSLGIKAADAKELKQIASTPSLNHVFN 298
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                  ....
gi 568960715  299 VANF 302
Cdd:cd01482   161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 439-602 5.12e-85

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


:

Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 275.70  E-value: 5.12e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  439 ADIVFLVDGSYSIGIANFVKVRAFLEVLAKSFEISPNRVQISLVQYSRDPHTEFTLKEFNRVEDIIKAINTFPYRGGSTN 518
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  519 TGKAMTYVREKIFVPNKGSRSNVPKVMILITDGKSSDAFRDPAIKLRNSDVEIFAVGVKDAVRSELEAIASPPAETHVFT 598
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                  ....
gi 568960715  599 VEDF 602
Cdd:cd01482   161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 2324-2488 3.52e-82

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: 267.62  E-value: 3.52e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2324 ADIVFLTDASWSIGDDNFNKVVKFIFNTVGAFdEVNPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNT 2403
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAF-EIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2404 RTGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQDEVKKAAFVIQQSGFSVFVVGVADVDYNELANIASKPSERHVF 2483
Cdd:cd01482    80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159


                  ....*
gi 568960715 2484 IVDDF 2488
Cdd:cd01482   160 NVADF 164
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 2522-2714 1.95e-57

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


:

Pssm-ID: 214560  Cd Length: 184  Bit Score: 197.58  E-value: 1.95e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   2522 GFKMLEAYNLTEKNFASVQGVSLEsgsfPSYSAYRLQKNAFINQPTAELHPNGLPPSYTIILLFRLlpeTPSDPFAIWQI 2601
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPE----PGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   2602 TDRDYRPQVGVIADPSSKTLSFFNKDTRGEVQTVTFdtdEVKTLFYGSFHKVHIVVTSKSVKIYIDCYEIIEKDIKEAG- 2680
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSF---RNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGq 150

                           170       180       190
                    ....*....|....*....|....*....|....*
gi 568960715   2681 -NITTDGYEILGKLLKGeRKSATFQIQSFDIVCSP 2714
Cdd:smart00210  151 pPIDTDGIEVRGAQAAD-RKPFQGDLQQLKIVCDP 184
fn3 pfam00041
Fibronectin type III domain;
1758-1836 1.58e-16

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 76.68  E-value: 1.58e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1758 PRNLQVYNATSNSLTVKWDPA---SGRVQKYRITYQPSTGEGNEQTITVGGRQNSVLLQKLKPDTPYTITVYSQYPDGEG 1834
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   ..
gi 568960715  1835 GR 1836
Cdd:pfam00041   83 PP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 724-805 5.26e-15

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: 72.91  E-value: 5.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  724 GVPRNLKVTDETTDSFKLTWSQAP---GRVLRYRIRYRPVSGGESKEVST-PANQRRKTLENLTPDTKYEISVIAEYSSG 799
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                  ....*.
gi 568960715  800 PGSPLT 805
Cdd:cd00063    82 ESPPSE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 634-719 1.88e-14

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 71.37  E-value: 1.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  634 PPKDLRFTQVTANSFKAEWSPP---GDNVFSYHVTYKDANGDDEVTV-VEPASSTSVVLNNLRPETLYLVNVTAEYEDGF 709
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPeddGGPITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGE 82

                          90
                  ....*....|
gi 568960715  710 SVPITGEETT 719
Cdd:cd00063    83 SPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 2120-2199 5.34e-14

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 69.83  E-value: 5.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2120 PPQNIHIFDEWYTRFRVSWDPSP---SPVLGYKIVYKPVGSNEPMEA--FVGEVTSYTLHNLNPSTTYDVSVYAQYDSGL 2194
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNGGGE 82


                  ....*
gi 568960715 2195 SVPLT 2199
Cdd:cd00063    83 SPPSE 87
fn3 pfam00041
Fibronectin type III domain;
1387-1465 5.36e-14

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.75  E-value: 5.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1387 APTNLVISERTHRSFRVSWTPPSDS---VDRYKVEYYPVSGGKR-QEFYVSRLDTSTVLKDLKPETDYVVNVYSVVEDEY 1462
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGngpITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 568960715  1463 SEP 1465
Cdd:pfam00041   82 GPP 84
fn3 pfam00041
Fibronectin type III domain;
1940-2018 2.16e-13

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.83  E-value: 2.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1940 RNIQVYNPTPNSLDVRWDPAP---GPVQQYRIVYSPVAGTRPSESIVVPGNTRTVHLERLIPDTPYSVNIVALYSDGEGN 2016
Cdd:pfam00041    4 SNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGP 83


                   ..
gi 568960715  2017 PS 2018
Cdd:pfam00041   84 PS 85
fn3 pfam00041
Fibronectin type III domain;
336-416 3.91e-13

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.05  E-value: 3.91e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   336 PPSNLVVTELSSKYIRLSWDPSP---SAVTGYKILLTPMAAGSRHHALSVGPQTTTLNVRDLTADTEYQISVFAMKGLTS 412
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ....
gi 568960715   413 SEPT 416
Cdd:pfam00041   82 GPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1474-1548 5.09e-13

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: 66.87  E-value: 5.09e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960715   1474 PVPVVSLNIYDVGPTTMHVQWQPV--GGATGYTVSYQPTRSPEGTKPKEMRVGPTVNDVQLTGLLPNTEYEVTVQAV 1548
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPpdDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
634-992 1.03e-12

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 73.88  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  634 PPKDLRFTQVTANSFKAEWSP-PGDNVFSYHVtYKDANGDDEVTVVEPASSTSVVLNNLRPETLYLVNVTAEYEDG---- 708
Cdd:COG3401   235 APTGLTATADTPGSVTLSWDPvTESDATGYRV-YRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnesa 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  709 FSVPITGeETTAEVKGVPRNLKVTDETTDSFKLTWSQAPG-RVLRYRIRYRPVSGGESKEVSTPANQRRKTLENLTPDTK 787
Cdd:COG3401   314 PSNVVSV-TTDLTPPAAPSGLTATAVGSSSITLSWTASSDaDVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTT 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  788 YEISVIAEYSSGPGSPLTGN--AATEEVRGNPRDLRVSDATTSTLKLSWSRAPGKVKQYLVTYTPAAGGETQEVTVRGDT 865
Cdd:COG3401   393 YYYKVTAVDAAGNESAPSEEvsATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTT 472

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  866 TTTMLRKLKEGTQYDLSVTALYASGAGEALSGKGSTLEERG--SPQNLVTKDITDTSIGAYWTSAPGMVRGYRVS-WKSL 942
Cdd:COG3401   473 TSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGasAAAAVGGAPDGTPNVTGASPVTVGASTGDVLItDLVS 552

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 568960715  943 YDDIEAGETTLPGDAIHTMIENLQPETKYKISVFATYSSGEGEPVTGDAT 992
Cdd:COG3401   553 LTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNTNDVAGVHGGTLLV 602
fn3 pfam00041
Fibronectin type III domain;
26-105 5.72e-12

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.97  E-value: 5.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715    26 DPPSDLNFKIIDENTVHMSWERPVD---PIVGYRITVDPTTDG-PTKEFTLAASTTETLLSDLIPETQYVVTITSYNEVE 101
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDgngPITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 568960715   102 ESVP 105
Cdd:pfam00041   81 EGPP 84
fn3 pfam00041
Fibronectin type III domain;
1656-1728 6.68e-12

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 6.68e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960715  1656 PAPTNLQFTEVTPESFRGTW---DHGASDVSLYRITWAPVGNPDKM-ETILNGDENTLVFENLNPNTPYEVSITAIY 1728
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWtppPDGNGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1569-1652 1.85e-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: 62.51  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1569 PQDVKLRDVTHSTMNVVWEPVL---GKVRKYIVRYK-TPDEEFKEVEVDRSRA-STILKDLSSQTQYTVSVSAVYDEGTS 1643
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYReKGSGDWKEVEVTPGSEtSYTLTGLKPGTEYEFRVRAVNGGGES 83


                  ....*....
gi 568960715 1644 PPATAYDTT 1652
Cdd:cd00063    84 PPSESVTVT 92
fn3 pfam00041
Fibronectin type III domain;
1849-1927 3.25e-11

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.66  E-value: 3.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1849 VRNLRVYDPSTSSLSVRWDHAE---GNPRQYKLFYAPTSGGPEEL-VPIPGNTNYAILRNLQPDTPYTITVVPVYTEGDG 1924
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   ...
gi 568960715  1925 GRT 1927
Cdd:pfam00041   83 PPS 85
fn3 pfam00041
Fibronectin type III domain;
2030-2107 4.02e-11

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.28  E-value: 4.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  2030 PRNIRVFGETTNSLSVAW---DHADGPVQQYRIIYSPTVGDPIDEYTTVPGRRNNVILQPLQPDTPYKITVIAIYEDGDG 2106
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWtppPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   .
gi 568960715  2107 G 2107
Cdd:pfam00041   83 P 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1090-1176 1.14e-10

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 60.59  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1090 PRNLKTSDPTMSSFRVTWEPAP---GEVKGYKVTFHPTGDDRRLGELVLGPYDNTVVLEELRAGTTYRVNVFGMFDGGES 1166
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGES 83

                          90
                  ....*....|
gi 568960715 1167 LPLVGQEMTT 1176
Cdd:cd00063    84 PPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1002-1075 4.88e-10

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 58.66  E-value: 4.88e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568960715 1002 LRVDEETEHTMRVTWKAAP---GKVVNYRVVYRPQGGGR-QMVAKVPPTVTSTVLKRLQPQTTYDITVLPMYKTGEGK 1075
Cdd:cd00063     7 LRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESP 84
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2766-2898 2.08e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 56.45  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2766 RGERGI---NGAVGPPGPRGDTGPPGPQGPPGPQGPNGLsiPGEQGRQGMKGDAGEPGLPGRTGTPGLPGPPGPMGPPGD 2842
Cdd:NF038329  119 KGEPGPagpAGPAGEQGPRGDRGETGPAGPAGPPGPQGE--RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568960715 2843 RGFTGKDGAMGPRGPPGPPGSPGSPGVTGPSGKPGKP--GDHGRPGQSGLKGEKGDRG 2898
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDG 254
fn3 pfam00041
Fibronectin type III domain;
2209-2284 1.30e-05

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.87  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  2209 VTDLKTYQVGWDTFCVKWSP----HRAATSYRLKLSPADGTRG-QEITVRGSETSHCFTGLSPEAEYGVTVFVQTPNLEG 2283
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   .
gi 568960715  2284 P 2284
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 ...
 1198-1361 5.97e-92

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: 295.74  E-value: 5.97e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1198 ADIVLLVDGSWSIGRANFRTVRSFISRIVEVFEIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTL 1277
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1278 TGMALNFIRQQSFKTQAGMRPRARKIGVLITDGKSQDDVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDDTHAYN 1357
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                  ....
gi 568960715 1358 VADF 1361
Cdd:cd01482   161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 139-302 2.26e-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: 285.33  E-value: 2.26e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  139 TDLVFLVDGSWSVGRNNFKYILDFIVALVSAFDIGEEKTRVGVVQYSSDTRTEFNLNQYYRREDLLAAVKKIPYKGGNTM 218
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  219 TGDAIDYLVKNTFTESAGSRAGFPKVAIIITDGKSQDEVEIPARELRNIGVEVFSLGIKAADAKELKQIASTPSLNHVFN 298
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                  ....
gi 568960715  299 VANF 302
Cdd:cd01482   161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 439-602 5.12e-85

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 275.70  E-value: 5.12e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  439 ADIVFLVDGSYSIGIANFVKVRAFLEVLAKSFEISPNRVQISLVQYSRDPHTEFTLKEFNRVEDIIKAINTFPYRGGSTN 518
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  519 TGKAMTYVREKIFVPNKGSRSNVPKVMILITDGKSSDAFRDPAIKLRNSDVEIFAVGVKDAVRSELEAIASPPAETHVFT 598
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                  ....
gi 568960715  599 VEDF 602
Cdd:cd01482   161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 2324-2488 3.52e-82

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: 267.62  E-value: 3.52e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2324 ADIVFLTDASWSIGDDNFNKVVKFIFNTVGAFdEVNPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNT 2403
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAF-EIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2404 RTGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQDEVKKAAFVIQQSGFSVFVVGVADVDYNELANIASKPSERHVF 2483
Cdd:cd01482    80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159


                  ....*
gi 568960715 2484 IVDDF 2488
Cdd:cd01482   160 NVADF 164
VWA pfam00092
von Willebrand factor type A domain;
1199-1370 7.82e-67

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 224.08  E-value: 7.82e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1199 DIVLLVDGSWSIGRANFRTVRSFISRIVEVFEIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTL- 1277
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1278 TGMALNFIRQQSFKTQAGMRPRARKIGVLITDGKSQD-DVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDDTHAY 1356
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                          170
                   ....*....|....
gi 568960715  1357 NVADFESLSKIVDD 1370
Cdd:pfam00092  161 TVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
140-311 1.08e-66

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 223.69  E-value: 1.08e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   140 DLVFLVDGSWSVGRNNFKYILDFIVALVSAFDIGEEKTRVGVVQYSSDTRTEFNLNQYYRREDLLAAVKKIPYKGGNTM- 218
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   219 TGDAIDYLVKNTFTESAGSRAGFPKVAIIITDGKSQD-EVEIPARELRNIGVEVFSLGIKAADAKELKQIASTPSLNHVF 297
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                          170
                   ....*....|....
gi 568960715   298 NVANFDAIVDIQNE 311
Cdd:pfam00092  161 TVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
440-608 8.10e-61

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 206.74  E-value: 8.10e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   440 DIVFLVDGSYSIGIANFVKVRAFLEVLAKSFEISPNRVQISLVQYSRDPHTEFTLKEFNRVEDIIKAINTFPYRGGST-N 518
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   519 TGKAMTYVREKIFVPNKGSRSNVPKVMILITDGKSSD-AFRDPAIKLRNSDVEIFAVGVKDAVRSELEAIASPPAETHVF 597
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                          170
                   ....*....|.
gi 568960715   598 TVEDFDAFQRI 608
Cdd:pfam00092  161 TVSDFEALEDL 171
VWA pfam00092
von Willebrand factor type A domain;
2325-2497 6.37e-60

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 204.43  E-value: 6.37e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  2325 DIVFLTDASWSIGDDNFNKVVKFIFNTVGAFDeVNPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNTR 2404
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLD-IGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  2405 -TGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQD-EVKKAAFVIQQSGFSVFVVGVADVDYNELANIASKPSERHV 2482
Cdd:pfam00092   80 nTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHV 159

                          170
                   ....*....|....*
gi 568960715  2483 FIVDDFESFEKIEDN 2497
Cdd:pfam00092  160 FTVSDFEALEDLQDQ 174
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 2522-2714 1.95e-57

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 197.58  E-value: 1.95e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   2522 GFKMLEAYNLTEKNFASVQGVSLEsgsfPSYSAYRLQKNAFINQPTAELHPNGLPPSYTIILLFRLlpeTPSDPFAIWQI 2601
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPE----PGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   2602 TDRDYRPQVGVIADPSSKTLSFFNKDTRGEVQTVTFdtdEVKTLFYGSFHKVHIVVTSKSVKIYIDCYEIIEKDIKEAG- 2680
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSF---RNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGq 150

                           170       180       190
                    ....*....|....*....|....*....|....*
gi 568960715   2681 -NITTDGYEILGKLLKGeRKSATFQIQSFDIVCSP 2714
Cdd:smart00210  151 pPIDTDGIEVRGAQAAD-RKPFQGDLQQLKIVCDP 184
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 140-309 5.51e-54

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: 187.28  E-value: 5.51e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715    140 DLVFLVDGSWSVGRNNFKYILDFIVALVSAFDIGEEKTRVGVVQYSSDTRTEFNLNQYYRREDLLAAVKKIPYK-GGNTM 218
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715    219 TGDAIDYLVKNTFTESAGSRAGFPKVAIIITDGKSQD---EVEIPARELRNIGVEVFSLGIK-AADAKELKQIASTPSLN 294
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGnDVDEEELKKLASAPGGV 160

                           170
                    ....*....|....*
gi 568960715    295 HVFNVANFDAIVDIQ 309
Cdd:smart00327  161 YVFLPELLDLLIDLL 175
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 440-609 3.57e-51

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: 179.19  E-value: 3.57e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715    440 DIVFLVDGSYSIGIANFVKVRAFLEVLAKSFEISPNRVQISLVQYSRDPHTEFTLKEFNRVEDIIKAINTFPYR-GGSTN 518
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715    519 TGKAMTYVREKIFVPNKGSRSNVPKVMILITDGKSSDA---FRDPAIKLRNSDVEIFAVGVKDAV-RSELEAIASPPAET 594
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNDVdEEELKKLASAPGGV 160

                           170
                    ....*....|....*
gi 568960715    595 HVFTVEDFDAFQRIS 609
Cdd:smart00327  161 YVFLPELLDLLIDLL 175
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1199-1368 7.83e-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: 175.34  E-value: 7.83e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   1199 DIVLLVDGSWSIGRANFRTVRSFISRIVEVFEIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYK-GGNTL 1277
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   1278 TGMALNFIRQQSFKTQAGMRPRARKIGVLITDGKSQD---DVEAPSKKLKDEGVELFAIGIKNA-DEVELKMIATDPDDT 1353
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160

                           170
                    ....*....|....*
gi 568960715   1354 HAYNVADFESLSKIV 1368
Cdd:smart00327  161 YVFLPELLDLLIDLL 175
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 2325-2494 9.06e-44

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: 158.00  E-value: 9.06e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   2325 DIVFLTDASWSIGDDNFNKVVKFIFNTVGAFDeVNPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYR-GGNT 2403
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLD-IGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGT 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   2404 RTGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQD---EVKKAAFVIQQSGFSVFVVGV-ADVDYNELANIASKPSE 2479
Cdd:smart00327   80 NLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 568960715   2480 RHVFIVDDFESFEKI 2494
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
fn3 pfam00041
Fibronectin type III domain;
1758-1836 1.58e-16

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 76.68  E-value: 1.58e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1758 PRNLQVYNATSNSLTVKWDPA---SGRVQKYRITYQPSTGEGNEQTITVGGRQNSVLLQKLKPDTPYTITVYSQYPDGEG 1834
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   ..
gi 568960715  1835 GR 1836
Cdd:pfam00041   83 PP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 724-805 5.26e-15

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: 72.91  E-value: 5.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  724 GVPRNLKVTDETTDSFKLTWSQAP---GRVLRYRIRYRPVSGGESKEVST-PANQRRKTLENLTPDTKYEISVIAEYSSG 799
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                  ....*.
gi 568960715  800 PGSPLT 805
Cdd:cd00063    82 ESPPSE 87
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1195-1371 1.19e-14

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: 76.90  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1195 RAEADIVLLVDGSWSIGRAN-FRTVRSFISRIVEVFeigPKRVQIALAQYSGDPrtEWQLNAHRDKKSLLQAVANLPYKG 1273
Cdd:COG1240    90 QRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEA--EVLLPLTRDREALKRALDELPPGG 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1274 GnTLTGMALnfirQQSFKTQAGMRPRARKIGVLITDGK---SQDDVEAPSKKLKDEGVELFAIGI--KNADEVELKMIAt 1348
Cdd:COG1240   165 G-TPLGDAL----ALALELLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVgtEAVDEGLLREIA- 238

                         170       180
                  ....*....|....*....|....*
gi 568960715 1349 dpDDTHA--YNVADFESLSKIVDDL 1371
Cdd:COG1240   239 --EATGGryFRADDLSELAAIYREI 261
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 634-719 1.88e-14

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 71.37  E-value: 1.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  634 PPKDLRFTQVTANSFKAEWSPP---GDNVFSYHVTYKDANGDDEVTV-VEPASSTSVVLNNLRPETLYLVNVTAEYEDGF 709
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPeddGGPITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGE 82

                          90
                  ....*....|
gi 568960715  710 SVPITGEETT 719
Cdd:cd00063    83 SPPSESVTVT 92
fn3 pfam00041
Fibronectin type III domain;
726-803 3.26e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 70.14  E-value: 3.26e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   726 PRNLKVTDETTDSFKLTWS---QAPGRVLRYRIRYRPVSGGE-SKEVSTPANQRRKTLENLTPDTKYEISVIAEYSSGPG 801
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTpppDGNGPITGYEVEYRPKNSGEpWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   ..
gi 568960715   802 SP 803
Cdd:pfam00041   83 PP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 2120-2199 5.34e-14

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 69.83  E-value: 5.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2120 PPQNIHIFDEWYTRFRVSWDPSP---SPVLGYKIVYKPVGSNEPMEA--FVGEVTSYTLHNLNPSTTYDVSVYAQYDSGL 2194
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNGGGE 82


                  ....*
gi 568960715 2195 SVPLT 2199
Cdd:cd00063    83 SPPSE 87
fn3 pfam00041
Fibronectin type III domain;
1387-1465 5.36e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.75  E-value: 5.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1387 APTNLVISERTHRSFRVSWTPPSDS---VDRYKVEYYPVSGGKR-QEFYVSRLDTSTVLKDLKPETDYVVNVYSVVEDEY 1462
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGngpITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 568960715  1463 SEP 1465
Cdd:pfam00041   82 GPP 84
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 439-608 2.01e-13

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 73.05  E-value: 2.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  439 ADIVFLVDGSYSIGIAN-FVKVRAFLEVLAKSFeisPNRVQISLVQYSRDPHT--EFTlkefNRVEDIIKAINTFPYRGG 515
Cdd:COG1240    93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVllPLT----RDREALKRALDELPPGGG 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  516 sTNTGKAMTYVREKIfvpnKGSRSNVPKVMILITDGKSSDAFRDP---AIKLRNSDVEIFAVGVKDAVRSE--LEAIAsp 590
Cdd:COG1240   166 -TPLGDALALALELL----KRADPARRKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEAVDEglLREIA-- 238

                         170       180
                  ....*....|....*....|
gi 568960715  591 pAET--HVFTVEDFDAFQRI 608
Cdd:COG1240   239 -EATggRYFRADDLSELAAI 257
fn3 pfam00041
Fibronectin type III domain;
1940-2018 2.16e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.83  E-value: 2.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1940 RNIQVYNPTPNSLDVRWDPAP---GPVQQYRIVYSPVAGTRPSESIVVPGNTRTVHLERLIPDTPYSVNIVALYSDGEGN 2016
Cdd:pfam00041    4 SNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGP 83


                   ..
gi 568960715  2017 PS 2018
Cdd:pfam00041   84 PS 85
fn3 pfam00041
Fibronectin type III domain;
336-416 3.91e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.05  E-value: 3.91e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   336 PPSNLVVTELSSKYIRLSWDPSP---SAVTGYKILLTPMAAGSRHHALSVGPQTTTLNVRDLTADTEYQISVFAMKGLTS 412
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ....
gi 568960715   413 SEPT 416
Cdd:pfam00041   82 GPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1474-1548 5.09e-13

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: 66.87  E-value: 5.09e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960715   1474 PVPVVSLNIYDVGPTTMHVQWQPV--GGATGYTVSYQPTRSPEGTKPKEMRVGPTVNDVQLTGLLPNTEYEVTVQAV 1548
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPpdDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1386-1470 6.72e-13

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: 66.75  E-value: 6.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1386 EAPTNLVISERTHRSFRVSWTPPSDS---VDRYKVEYYPVSGGKRQEFYVSRLD-TSTVLKDLKPETDYVVNVYSVVEDE 1461
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNGGG 81


                  ....*....
gi 568960715 1462 YSEPLKGTE 1470
Cdd:cd00063    82 ESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1940-2020 8.74e-13

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: 66.37  E-value: 8.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1940 RNIQVYNPTPNSLDVRWDPAP---GPVQQYRIVYSPVAGTRPSESIVVPGNTRTVHLERLIPDTPYSVNIVALYSDGEGN 2016
Cdd:cd00063     5 TNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESP 84


                  ....
gi 568960715 2017 PSPS 2020
Cdd:cd00063    85 PSES 88
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
634-992 1.03e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 73.88  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  634 PPKDLRFTQVTANSFKAEWSP-PGDNVFSYHVtYKDANGDDEVTVVEPASSTSVVLNNLRPETLYLVNVTAEYEDG---- 708
Cdd:COG3401   235 APTGLTATADTPGSVTLSWDPvTESDATGYRV-YRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnesa 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  709 FSVPITGeETTAEVKGVPRNLKVTDETTDSFKLTWSQAPG-RVLRYRIRYRPVSGGESKEVSTPANQRRKTLENLTPDTK 787
Cdd:COG3401   314 PSNVVSV-TTDLTPPAAPSGLTATAVGSSSITLSWTASSDaDVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTT 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  788 YEISVIAEYSSGPGSPLTGN--AATEEVRGNPRDLRVSDATTSTLKLSWSRAPGKVKQYLVTYTPAAGGETQEVTVRGDT 865
Cdd:COG3401   393 YYYKVTAVDAAGNESAPSEEvsATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTT 472

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  866 TTTMLRKLKEGTQYDLSVTALYASGAGEALSGKGSTLEERG--SPQNLVTKDITDTSIGAYWTSAPGMVRGYRVS-WKSL 942
Cdd:COG3401   473 TSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGasAAAAVGGAPDGTPNVTGASPVTVGASTGDVLItDLVS 552

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 568960715  943 YDDIEAGETTLPGDAIHTMIENLQPETKYKISVFATYSSGEGEPVTGDAT 992
Cdd:COG3401   553 LTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNTNDVAGVHGGTLLV 602
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1756-1834 1.36e-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: 65.98  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1756 SGPRNLQVYNATSNSLTVKWDPAS---GRVQKYRITYQPSTGEGNEQTITVGGRQNSVLLQKLKPDTPYTITVYSQYPDG 1832
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                  ..
gi 568960715 1833 EG 1834
Cdd:cd00063    82 ES 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 724-801 1.59e-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: 65.33  E-value: 1.59e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715    724 GVPRNLKVTDETTDSFKLTWSQAP-----GRVLRYRIRYRPvSGGESKEVSTPANQRRKTLENLTPDTKYEISVIAEYSS 798
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYRE-EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 568960715    799 GPG 801
Cdd:smart00060   81 GEG 83
fn3 pfam00041
Fibronectin type III domain;
634-712 1.94e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.13  E-value: 1.94e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   634 PPKDLRFTQVTANSFKAEWSPP---GDNVFSYHVTYKDAN-GDDEVTVVEPASSTSVVLNNLRPETLYLVNVTAEYEDGF 709
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNsGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 568960715   710 SVP 712
Cdd:pfam00041   82 GPP 84
fn3 pfam00041
Fibronectin type III domain;
817-893 3.76e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.36  E-value: 3.76e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   817 PRDLRVSDATTSTLKLSWSRAP---GKVKQYLVTYTPA-AGGETQEVTVRGDTTTTMLRKLKEGTQYDLSVTALYASGAG 892
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   .
gi 568960715   893 E 893
Cdd:pfam00041   83 P 83
fn3 pfam00041
Fibronectin type III domain;
2120-2197 3.95e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.36  E-value: 3.95e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  2120 PPQNIHIFDEWYTRFRVSWDPSP---SPVLGYKIVYKPVGSNEPMEAF--VGEVTSYTLHNLNPSTTYDVSVYAQYDSGL 2194
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEItvPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 568960715  2195 SVP 2197
Cdd:pfam00041   82 GPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1756-1834 3.99e-12

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 64.17  E-value: 3.99e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   1756 SGPRNLQVYNATSNSLTVKWD-PASGRVQKYRITYQPSTGE--GNEQTITVGGRQNSVLLQKLKPDTPYTITVYSQYPDG 1832
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEpPPDDGITGYIVGYRVEYREegSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 568960715   1833 EG 1834
Cdd:smart00060   82 EG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 634-710 5.34e-12

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 63.79  E-value: 5.34e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715    634 PPKDLRFTQVTANSFKAEWSPP-GDNVFSYHVTYK---DANGDDEVTVVEPASSTSVVLNNLRPETLYLVNVTAEYEDGF 709
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPpDDGITGYIVGYRveyREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 568960715    710 S 710
Cdd:smart00060   83 G 83
fn3 pfam00041
Fibronectin type III domain;
26-105 5.72e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.97  E-value: 5.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715    26 DPPSDLNFKIIDENTVHMSWERPVD---PIVGYRITVDPTTDG-PTKEFTLAASTTETLLSDLIPETQYVVTITSYNEVE 101
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDgngPITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 568960715   102 ESVP 105
Cdd:pfam00041   81 EGPP 84
fn3 pfam00041
Fibronectin type III domain;
1656-1728 6.68e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 6.68e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960715  1656 PAPTNLQFTEVTPESFRGTW---DHGASDVSLYRITWAPVGNPDKM-ETILNGDENTLVFENLNPNTPYEVSITAIY 1728
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWtppPDGNGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 335-420 9.70e-12

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 63.67  E-value: 9.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  335 EPPSNLVVTELSSKYIRLSWDPSP---SAVTGYKILLTPMAAGSRHHALSVGPQTTTLNVRDLTADTEYQISVFAMKGLT 411
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                  ....*....
gi 568960715  412 SSEPTSVME 420
Cdd:cd00063    82 ESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 815-896 1.10e-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: 63.28  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  815 GNPRDLRVSDATTSTLKLSWSRAP---GKVKQYLVTYTPAAGGETQEVTV-RGDTTTTMLRKLKEGTQYDLSVTALYASG 890
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                  ....*.
gi 568960715  891 AGEALS 896
Cdd:cd00063    82 ESPPSE 87
fn3 pfam00041
Fibronectin type III domain;
1476-1548 1.30e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.82  E-value: 1.30e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960715  1476 PVVSLNIYDVGPTTMHVQWQPV----GGATGYTVSYQPTRSPEgtKPKEMRVGPTVNDVQLTGLLPNTEYEVTVQAV 1548
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgnGPITGYEVEYRPKNSGE--PWNEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 2120-2195 1.32e-11

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: 62.63  E-value: 1.32e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   2120 PPQNIHIFDEWYTRFRVSWDPSP-----SPVLGYKIVYKPVGSNEPMEAFVGEVTSYTLHNLNPSTTYDVSVYAQYDSGL 2194
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 568960715   2195 S 2195
Cdd:smart00060   83 G 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1474-1563 1.46e-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: 62.90  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1474 PVPVVSLNIYDVGPTTMHVQWQPV----GGATGYTVSYQPTRSPEGTKPKemRVGPTVNDVQLTGLLPNTEYEVTVQAVL 1549
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPeddgGPITGYVVEYREKGSGDWKEVE--VTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                          90
                  ....*....|....
gi 568960715 1550 YDLTSEPAKAREVT 1563
Cdd:cd00063    79 GGGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1569-1652 1.85e-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: 62.51  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1569 PQDVKLRDVTHSTMNVVWEPVL---GKVRKYIVRYK-TPDEEFKEVEVDRSRA-STILKDLSSQTQYTVSVSAVYDEGTS 1643
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYReKGSGDWKEVEVTPGSEtSYTLTGLKPGTEYEFRVRAVNGGGES 83


                  ....*....
gi 568960715 1644 PPATAYDTT 1652
Cdd:cd00063    84 PPSESVTVT 92
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 139-312 2.56e-11

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: 66.89  E-value: 2.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  139 TDLVFLVDGSWSVGRNNfkyILDFIVALVSAF-DIGEEKTRVGVVQYSSDTRTEFNLNqyYRREDLLAAVKKIPYKGGnT 217
Cdd:COG1240    93 RDVVLVVDASGSMAAEN---RLEAAKGALLDFlDDYRPRDRVGLVAFGGEAEVLLPLT--RDREALKRALDELPPGGG-T 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  218 MTGDAIdYLVKNTFTESAGSRagfPKVAIIITDGK---SQDEVEIPARELRNIGVEVFSLGI--KAADAKELKQIASTps 292
Cdd:COG1240   167 PLGDAL-ALALELLKRADPAR---RKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVgtEAVDEGLLREIAEA-- 240

                         170       180
                  ....*....|....*....|.
gi 568960715  293 LN-HVFNVANFDAIVDIQNEI 312
Cdd:COG1240   241 TGgRYFRADDLSELAAIYREI 261
fn3 pfam00041
Fibronectin type III domain;
1849-1927 3.25e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.66  E-value: 3.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1849 VRNLRVYDPSTSSLSVRWDHAE---GNPRQYKLFYAPTSGGPEEL-VPIPGNTNYAILRNLQPDTPYTITVVPVYTEGDG 1924
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   ...
gi 568960715  1925 GRT 1927
Cdd:pfam00041   83 PPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 26-106 3.28e-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: 62.13  E-value: 3.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   26 DPPSDLNFKIIDENTVHMSWERPVD---PIVGYRITVDPTTDGPTKEF-TLAASTTETLLSDLIPETQYVVTITSYNEVE 101
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDdggPITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                  ....*
gi 568960715  102 ESVPV 106
Cdd:cd00063    82 ESPPS 86
fn3 pfam00041
Fibronectin type III domain;
2030-2107 4.02e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.28  E-value: 4.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  2030 PRNIRVFGETTNSLSVAW---DHADGPVQQYRIIYSPTVGDPIDEYTTVPGRRNNVILQPLQPDTPYKITVIAIYEDGDG 2106
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWtppPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   .
gi 568960715  2107 G 2107
Cdd:pfam00041   83 P 83
fn3 pfam00041
Fibronectin type III domain;
1567-1645 4.18e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.28  E-value: 4.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1567 PRPQDVKLRDVTHSTMNVVWEPVL---GKVRKYIVRYKTPDEE--FKEVEVDRSRASTILKDLSSQTQYTVSVSAVYDEG 1641
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGepWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 568960715  1642 TSPP 1645
Cdd:pfam00041   81 EGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 2028-2106 5.09e-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: 61.36  E-value: 5.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2028 SGPRNIRVFGETTNSLSVAWDHAD---GPVQQYRIIYSPTVGDPIDEYTTVPGRRNNVILQPLQPDTPYKITVIAIYEDG 2104
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                  ..
gi 568960715 2105 DG 2106
Cdd:cd00063    82 ES 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1569-1643 1.10e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 60.32  E-value: 1.10e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   1569 PQDVKLRDVTHSTMNVVWEP-----VLGKVRKYIVRYKTPDEEFKEVEVDRSRASTILKDLSSQTQYTVSVSAVYDEGTS 1643
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPppddgITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1090-1176 1.14e-10

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 60.59  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1090 PRNLKTSDPTMSSFRVTWEPAP---GEVKGYKVTFHPTGDDRRLGELVLGPYDNTVVLEELRAGTTYRVNVFGMFDGGES 1166
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGES 83

                          90
                  ....*....|
gi 568960715 1167 LPLVGQEMTT 1176
Cdd:cd00063    84 PPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1002-1075 4.88e-10

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 58.66  E-value: 4.88e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568960715 1002 LRVDEETEHTMRVTWKAAP---GKVVNYRVVYRPQGGGR-QMVAKVPPTVTSTVLKRLQPQTTYDITVLPMYKTGEGK 1075
Cdd:cd00063     7 LRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1387-1457 6.25e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.01  E-value: 6.25e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568960715   1387 APTNLVISERTHRSFRVSWTPP-SDSVDRYKVEY---YPVSGGKRQEFYVSRLDTSTVLKDLKPETDYVVNVYSV 1457
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPpDDGITGYIVGYrveYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 2324-2474 2.14e-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: 61.11  E-value: 2.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2324 ADIVFLTDASWSIGDDNFNKVVKfifNTVGAFDEVNPAGIQVSFVQYSDEVksEFKLNTYNDKALALGALQNIRYRGGnT 2403
Cdd:COG1240    93 RDVVLVVDASGSMAAENRLEAAK---GALLDFLDDYRPRDRVGLVAFGGEA--EVLLPLTRDREALKRALDELPPGGG-T 166

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568960715 2404 RTGKALtfikEKVLTWESGMRKNVPKVLVVVTDGR---SQDEVKKAAFVIQQSGFSVFVVGVAD--VDYNELANIA 2474
Cdd:COG1240   167 PLGDAL----ALALELLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTeaVDEGLLREIA 238
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 26-103 2.65e-09

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 56.08  E-value: 2.65e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715     26 DPPSDLNFKIIDENTVHMSWERPVDP-----IVGYRItVDPTTDGPTKEFTLAASTTETLLSDLIPETQYVVTITSYNEV 100
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDgitgyIVGYRV-EYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 568960715    101 EES 103
Cdd:smart00060   81 GEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 815-892 3.45e-09

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 56.08  E-value: 3.45e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715    815 GNPRDLRVSDATTSTLKLSWSRAPGKVKQ-YLVTYTPA---AGGETQEVTVRGDTTTTMLRKLKEGTQYDLSVTALYASG 890
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEyreEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 568960715    891 AG 892
Cdd:smart00060   82 EG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1849-1924 7.41e-09

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.20  E-value: 7.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1849 VRNLRVYDPSTSSLSVRWDHAE---GNPRQYKLFYAPT-SGGPEELVPIPGNTNYAILRNLQPDTPYTITVVPVYTEGDG 1924
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKgSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGES 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 336-413 1.41e-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: 54.16  E-value: 1.41e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715    336 PPSNLVVTELSSKYIRLSWDPSPSAVTGYKIL---LTPMAAGSRHHALSVGPQTTTLNVRDLTADTEYQISVFAMKGLTS 412
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVgyrVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 568960715    413 S 413
Cdd:smart00060   83 G 83
fn3 pfam00041
Fibronectin type III domain;
1089-1166 1.69e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.96  E-value: 1.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1089 SPRNLKTSDPTMSSFRVTWEPAP---GEVKGYKVTFHPTGDDRRLGELVLGPYDNTVVLEELRAGTTYRVNVF---GMFD 1162
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQavnGGGE 81


                   ....
gi 568960715  1163 GGES 1166
Cdd:pfam00041   82 GPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1940-2015 1.80e-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: 1.80e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   1940 RNIQVYNPTPNSLDVRWDPAP-----GPVQQYRIVYSPVAGTrpSESIVVPGNTRTVHLERLIPDTPYSVNIVALYSDGE 2014
Cdd:smart00060    5 SNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYREEGSE--WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 568960715   2015 G 2015
Cdd:smart00060   83 G 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 2028-2106 1.85e-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: 1.85e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   2028 SGPRNIRVFGETTNSLSVAWDHADGPVQQ-YRIIYSPTVGDPIDEYTTV--PGRRNNVILQPLQPDTPYKITVIAIYEDG 2104
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGSEWKEVnvTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 568960715   2105 DG 2106
Cdd:smart00060   82 EG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1002-1074 2.99e-08

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.39  E-value: 2.99e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568960715   1002 LRVDEETEHTMRVTWKAAP-----GKVVNYRVVYRPQGGGRQMVaKVPPTVTSTVLKRLQPQTTYDITVLPMYKTGEG 1074
Cdd:smart00060    7 LRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYREEGSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1849-1924 8.10e-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: 51.85  E-value: 8.10e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   1849 VRNLRVYDPSTSSLSVRWDHAEGNPR-----QYKLFYAPTSGGPEELVPIPGNTNYaILRNLQPDTPYTITVVPVYTEGD 1923
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGItgyivGYRVEYREEGSEWKEVNVTPSSTSY-TLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 568960715   1924 G 1924
Cdd:smart00060   83 G 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1656-1728 8.33e-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: 52.50  E-value: 8.33e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960715 1656 PAPTNLQFTEVTPESFRGTWD---HGASDVSLYRITWAPVGNPDKME-TILNGDENTLVFENLNPNTPYEVSITAIY 1728
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTppeDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1197-1402 9.48e-08

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 57.67  E-value: 9.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1197 EADIVLLVDGSWSIGRANFRT-VRSFISRIVEVFEIGPKRVQIALAQYSGDPRTEWQL--NAHRDKKSLLQAV-----AN 1268
Cdd:PTZ00441   42 EVDLYLLVDGSGSIGYHNWIThVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLgsGASKDKEQALIIVkslrkTY 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1269 LPYkgGNTLTGMALNFIRQQsFKTQAGmRPRARKIGVLITDG--KSQDDVEAPSKKLKDEGVELFAIGIKNADEVELK-- 1344
Cdd:PTZ00441  122 LPY--GKTNMTDALLEVRKH-LNDRVN-RENAIQLVILMTDGipNSKYRALEESRKLKDRNVKLAVIGIGQGINHQFNrl 197

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568960715 1345 MIATDPDDTHA--YNVADFESLSKIVDDLTINLCNSVK-----GPGDLEAPTNLVISERTHRSFR 1402
Cdd:PTZ00441  198 LAGCRPREGKCkfYSDADWEEAKNLIKPFIAKVCTEVErtascGPWDEWTPCSVTCGKGTHSRSR 262
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2766-2898 2.08e-07

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 56.45  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2766 RGERGI---NGAVGPPGPRGDTGPPGPQGPPGPQGPNGLsiPGEQGRQGMKGDAGEPGLPGRTGTPGLPGPPGPMGPPGD 2842
Cdd:NF038329  119 KGEPGPagpAGPAGEQGPRGDRGETGPAGPAGPPGPQGE--RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568960715 2843 RGFTGKDGAMGPRGPPGPPGSPGSPGVTGPSGKPGKP--GDHGRPGQSGLKGEKGDRG 2898
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDG 254
fn3 pfam00041
Fibronectin type III domain;
1002-1075 2.39e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.88  E-value: 2.39e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568960715  1002 LRVDEETEHTMRVTWKAAP---GKVVNYRVVYRPQGGGRQMVAK-VPPTVTSTVLKRLQPQTTYDITVLPMYKTGEGK 1075
Cdd:pfam00041    6 LTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEItVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGP 83
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2766-2898 4.84e-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: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2766 RGERGINGAVGPPGPRGDTGPPGPQGPPGPQGPNGLSIPGEQGRQGMKGDAGEPGLPGRTGTpglpgppgpmgppgdrgf 2845
Cdd:NF038329  194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGP------------------ 255

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568960715 2846 TGKDGAMGPRGPPGPPGSPGSPGVTGPSGKPGK---------PGDHGRPGQSGLKGEKGDRG 2898
Cdd:NF038329  256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKdgqngkdglPGKDGKDGQNGKDGLPGKDG 317
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1089-1166 7.98e-07

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 49.15  E-value: 7.98e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   1089 SPRNLKTSDPTMSSFRVTWE-PAPGEVKGYKVTFHPTGDDRRLGELVL--GPYDNTVVLEELRAGTTYRVNVFGMFDGGE 1165
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEpPPDDGITGYIVGYRVEYREEGSEWKEVnvTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 568960715   1166 S 1166
Cdd:smart00060   83 G 83
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2767-2898 1.23e-06

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: 53.76  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2767 GERGINGAVGPPGPRGDTGPPGPQGPPGPQGPNGLSipGEQGRQGMKGDAGEPGLPGRTGTPGLPGPPGPMGPPGDRGFT 2846
Cdd:NF038329  144 GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD--GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA 221

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2847 GKDGAMGPRGPPGPPGSPGSPGV--------TGPSGKPGKPGDHGRPGQSGLKGEKGDRG 2898
Cdd:NF038329  222 GEDGPAGPAGDGQQGPDGDPGPTgedgpqgpDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1656-1728 1.49e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 48.38  E-value: 1.49e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568960715   1656 PAPTNLQFTEVTPESFRGTWDHGASDVSL-----YRITWAPVgNPDKMETILNGDENTLVFENLNPNTPYEVSITAIY 1728
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITgyivgYRVEYREE-GSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2767-2898 2.33e-06

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: 52.99  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2767 GERGINGAVGPPGPRGDtgppgpqgppgpqgpnglsiPGEQGRQGMKGDAGEPGLPGRTGTPGLPGPPGPMGPPGDRGFT 2846
Cdd:NF038329  117 GEKGEPGPAGPAGPAGE--------------------QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568960715 2847 GKDGAMGPRGPPGPPGSPGSPGVTGPSGKPGKPGDHGRPGQSGLKGEKGDRG 2898
Cdd:NF038329  177 GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG 228
fn3 pfam00041
Fibronectin type III domain;
2209-2284 1.30e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.87  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  2209 VTDLKTYQVGWDTFCVKWSP----HRAATSYRLKLSPADGTRG-QEITVRGSETSHCFTGLSPEAEYGVTVFVQTPNLEG 2283
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   .
gi 568960715  2284 P 2284
Cdd:pfam00041   83 P 83
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2767-2893 1.22e-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: 42.10  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  2767 GERGINGAVGPPGPRGDtgppgpqgppgpqgpnglsiPGEQGRQGMKGDAGEPGLPGrtgtpglpgppgpmgppgdrgft 2846
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGP--------------------PGPPGPPGPPGPPGEPGPPG----------------------- 37

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 568960715  2847 gkdgamgprgppgPpgspgspgvtgpsgkPGKPGDHGRPGQSGLKGE 2893
Cdd:pfam01391   38 -------------P---------------PGPPGPPGPPGAPGAPGP 56
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 2208-2293 3.68e-04

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: 42.10  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2208 NVTDLKTYQVGWDTFCVKWSP----HRAATSYRLKLSPADGTRGQEITVRGSETSHC-FTGLSPEAEYGVTVFVQTPNLE 2282
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPpeddGGPITGYVVEYREKGSGDWKEVEVTPGSETSYtLTGLKPGTEYEFRVRAVNGGGE 82

                          90
                  ....*....|.
gi 568960715 2283 GPGVPIKEQTT 2293
Cdd:cd00063    83 SPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 2208-2283 3.21e-03

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: 39.13  E-value: 3.21e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   2208 NVTDLKTYQVGWDTFCVKWSP--HRAATSYRLKLSPADGTRG---QEITVRGSETSHCFTGLSPEAEYGVTVFVQTPNLE 2282
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPppDDGITGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 568960715   2283 G 2283
Cdd:smart00060   83 G 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
336-422 6.75e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 41.91  E-value: 6.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  336 PPSNLVVTELSSKYIRLSWDPSPSA-VTGYKILLTPMAAGSrHHALSVGPQTTTLNVRDLTADTEYQISVFAM-KGLTSS 413
Cdd:COG3401   329 APSGLTATAVGSSSITLSWTASSDAdVTGYNVYRSTSGGGT-YTKIAETVTTTSYTDTGLTPGTTYYYKVTAVdAAGNES 407


                  ....*....
gi 568960715  414 EPTSVMEKT 422
Cdd:COG3401   408 APSEEVSAT 416
 
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 ...
 1198-1361 5.97e-92

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: 295.74  E-value: 5.97e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1198 ADIVLLVDGSWSIGRANFRTVRSFISRIVEVFEIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTL 1277
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1278 TGMALNFIRQQSFKTQAGMRPRARKIGVLITDGKSQDDVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDDTHAYN 1357
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                  ....
gi 568960715 1358 VADF 1361
Cdd:cd01482   161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 139-302 2.26e-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: 285.33  E-value: 2.26e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  139 TDLVFLVDGSWSVGRNNFKYILDFIVALVSAFDIGEEKTRVGVVQYSSDTRTEFNLNQYYRREDLLAAVKKIPYKGGNTM 218
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  219 TGDAIDYLVKNTFTESAGSRAGFPKVAIIITDGKSQDEVEIPARELRNIGVEVFSLGIKAADAKELKQIASTPSLNHVFN 298
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                  ....
gi 568960715  299 VANF 302
Cdd:cd01482   161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 439-602 5.12e-85

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 275.70  E-value: 5.12e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  439 ADIVFLVDGSYSIGIANFVKVRAFLEVLAKSFEISPNRVQISLVQYSRDPHTEFTLKEFNRVEDIIKAINTFPYRGGSTN 518
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  519 TGKAMTYVREKIFVPNKGSRSNVPKVMILITDGKSSDAFRDPAIKLRNSDVEIFAVGVKDAVRSELEAIASPPAETHVFT 598
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFN 160


                  ....
gi 568960715  599 VEDF 602
Cdd:cd01482   161 VADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 2324-2488 3.52e-82

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: 267.62  E-value: 3.52e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2324 ADIVFLTDASWSIGDDNFNKVVKFIFNTVGAFdEVNPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNT 2403
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAF-EIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2404 RTGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQDEVKKAAFVIQQSGFSVFVVGVADVDYNELANIASKPSERHVF 2483
Cdd:cd01482    80 RTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVF 159


                  ....*
gi 568960715 2484 IVDDF 2488
Cdd:cd01482   160 NVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 139-302 1.42e-78

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: 257.16  E-value: 1.42e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  139 TDLVFLVDGSWSVGRNNFKYILDFIVALVSAFDIGEEKTRVGVVQYSSDTRTEFNLNQYYRREDLLAAVKKIPYKGGNTM 218
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  219 TGDAIDYLVKNTFTESAGSRAGFPKVAIIITDGKSQDEVEIPARELRNIGVEVFSLGIKAADAKELKQIASTPSLNHVFN 298
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                  ....
gi 568960715  299 VANF 302
Cdd:cd01472   161 VADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1198-1361 7.86e-78

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: 255.23  E-value: 7.86e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1198 ADIVLLVDGSWSIGRANFRTVRSFISRIVEVFEIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTL 1277
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1278 TGMALNFIRQQSFKTQAGMRPRARKIGVLITDGKSQDDVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDDTHAYN 1357
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                  ....
gi 568960715 1358 VADF 1361
Cdd:cd01472   161 VADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 439-602 2.69e-70

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


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 233.66  E-value: 2.69e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  439 ADIVFLVDGSYSIGIANFVKVRAFLEVLAKSFEISPNRVQISLVQYSRDPHTEFTLKEFNRVEDIIKAINTFPYRGGSTN 518
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  519 TGKAMTYVREKIFVPNKGSRSNVPKVMILITDGKSSDAFRDPAIKLRNSDVEIFAVGVKDAVRSELEAIASPPAETHVFT 598
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVFN 160


                  ....
gi 568960715  599 VEDF 602
Cdd:cd01472   161 VADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 2324-2488 4.87e-69

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: 229.81  E-value: 4.87e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2324 ADIVFLTDASWSIGDDNFNKVVKFIFNTVGAFDeVNPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNT 2403
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLD-IGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2404 RTGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQDEVKKAAFVIQQSGFSVFVVGVADVDYNELANIASKPSERHVF 2483
Cdd:cd01472    80 NTGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVF 159


                  ....*
gi 568960715 2484 IVDDF 2488
Cdd:cd01472   160 NVADF 164
VWA pfam00092
von Willebrand factor type A domain;
1199-1370 7.82e-67

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 224.08  E-value: 7.82e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1199 DIVLLVDGSWSIGRANFRTVRSFISRIVEVFEIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTL- 1277
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1278 TGMALNFIRQQSFKTQAGMRPRARKIGVLITDGKSQD-DVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDDTHAY 1356
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                          170
                   ....*....|....
gi 568960715  1357 NVADFESLSKIVDD 1370
Cdd:pfam00092  161 TVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
140-311 1.08e-66

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 223.69  E-value: 1.08e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   140 DLVFLVDGSWSVGRNNFKYILDFIVALVSAFDIGEEKTRVGVVQYSSDTRTEFNLNQYYRREDLLAAVKKIPYKGGNTM- 218
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   219 TGDAIDYLVKNTFTESAGSRAGFPKVAIIITDGKSQD-EVEIPARELRNIGVEVFSLGIKAADAKELKQIASTPSLNHVF 297
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                          170
                   ....*....|....
gi 568960715   298 NVANFDAIVDIQNE 311
Cdd:pfam00092  161 TVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
440-608 8.10e-61

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 206.74  E-value: 8.10e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   440 DIVFLVDGSYSIGIANFVKVRAFLEVLAKSFEISPNRVQISLVQYSRDPHTEFTLKEFNRVEDIIKAINTFPYRGGST-N 518
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   519 TGKAMTYVREKIFVPNKGSRSNVPKVMILITDGKSSD-AFRDPAIKLRNSDVEIFAVGVKDAVRSELEAIASPPAETHVF 597
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160

                          170
                   ....*....|.
gi 568960715   598 TVEDFDAFQRI 608
Cdd:pfam00092  161 TVSDFEALEDL 171
VWA pfam00092
von Willebrand factor type A domain;
2325-2497 6.37e-60

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 204.43  E-value: 6.37e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  2325 DIVFLTDASWSIGDDNFNKVVKFIFNTVGAFDeVNPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNTR 2404
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLD-IGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  2405 -TGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQD-EVKKAAFVIQQSGFSVFVVGVADVDYNELANIASKPSERHV 2482
Cdd:pfam00092   80 nTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHV 159

                          170
                   ....*....|....*
gi 568960715  2483 FIVDDFESFEKIEDN 2497
Cdd:pfam00092  160 FTVSDFEALEDLQDQ 174
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 2522-2714 1.95e-57

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 197.58  E-value: 1.95e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   2522 GFKMLEAYNLTEKNFASVQGVSLEsgsfPSYSAYRLQKNAFINQPTAELHPNGLPPSYTIILLFRLlpeTPSDPFAIWQI 2601
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPE----PGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQ---TPKSRGVLFAI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   2602 TDRDYRPQVGVIADPSSKTLSFFNKDTRGEVQTVTFdtdEVKTLFYGSFHKVHIVVTSKSVKIYIDCYEIIEKDIKEAG- 2680
Cdd:smart00210   74 YDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSF---RNLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGq 150

                           170       180       190
                    ....*....|....*....|....*....|....*
gi 568960715   2681 -NITTDGYEILGKLLKGeRKSATFQIQSFDIVCSP 2714
Cdd:smart00210  151 pPIDTDGIEVRGAQAAD-RKPFQGDLQQLKIVCDP 184
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 139-297 1.46e-56

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 194.05  E-value: 1.46e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  139 TDLVFLVDGSWSVGRNNFKYILDFIVALVSAFDIGEEKTRVGVVQYSSDTRTEFNLNQYYRREDLLAAVKKIPYKGGN-T 217
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  218 MTGDAIDYLVKNTFTESAgSRAGFPKVAIIITDGKSQD--EVEIPARELRNIGVEVFSLGIKAADAKELKQIASTPSLNH 295
Cdd:cd01450    81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSERH 159


                  ..
gi 568960715  296 VF 297
Cdd:cd01450   160 VF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 140-309 5.51e-54

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: 187.28  E-value: 5.51e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715    140 DLVFLVDGSWSVGRNNFKYILDFIVALVSAFDIGEEKTRVGVVQYSSDTRTEFNLNQYYRREDLLAAVKKIPYK-GGNTM 218
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715    219 TGDAIDYLVKNTFTESAGSRAGFPKVAIIITDGKSQD---EVEIPARELRNIGVEVFSLGIK-AADAKELKQIASTPSLN 294
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGnDVDEEELKKLASAPGGV 160

                           170
                    ....*....|....*
gi 568960715    295 HVFNVANFDAIVDIQ 309
Cdd:smart00327  161 YVFLPELLDLLIDLL 175
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 139-322 9.46e-54

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: 188.75  E-value: 9.46e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  139 TDLVFLVDGSWSVGRNNFKYILDFIVALVSAFDIGEEKTRVGVVQYSSDTRTEFNLNQYYRREDLLAAVKKIPYKGGNTM 218
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  219 TGDAIDYLVKNTFTESAGSRAG---FPKVAIIITDGKSQDEVEIPARELRNIGVEVFSLGIKAADAKELKQIASTPSLNH 295
Cdd:cd01475    83 TGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLADH 162

                         170       180
                  ....*....|....*....|....*..
gi 568960715  296 VFNVANFDAIVDIQNEIISQVCSGVDE 322
Cdd:cd01475   163 VFYVEDFSTIEELTKKFQGKICVVPDL 189
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1198-1356 1.22e-53

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: 185.96  E-value: 1.22e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1198 ADIVLLVDGSWSIGRANFRTVRSFISRIVEVFEIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGN-T 1276
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1277 LTGMALNFIRQQSFkTQAGMRPRARKIGVLITDGKSQD--DVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDDTH 1354
Cdd:cd01450    81 NTGKALQYALEQLF-SESNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSERH 159


                  ..
gi 568960715 1355 AY 1356
Cdd:cd01450   160 VF 161
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 439-597 1.52e-53

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: 185.57  E-value: 1.52e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  439 ADIVFLVDGSYSIGIANFVKVRAFLEVLAKSFEISPNRVQISLVQYSRDPHTEFTLKEFNRVEDIIKAINTFPYRGGS-T 517
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  518 NTGKAMTYVREKIFVPnKGSRSNVPKVMILITDGKSSD--AFRDPAIKLRNSDVEIFAVGVKDAVRSELEAIASPPAETH 595
Cdd:cd01450    81 NTGKALQYALEQLFSE-SNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSERH 159


                  ..
gi 568960715  596 VF 597
Cdd:cd01450   160 VF 161
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2324-2483 2.74e-51

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: 179.02  E-value: 2.74e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2324 ADIVFLTDASWSIGDDNFNKVVKFIFNTVGAFDeVNPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGN- 2402
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLD-IGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGg 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2403 TRTGKALTFIKEKVLTwESGMRKNVPKVLVVVTDGRSQD--EVKKAAFVIQQSGFSVFVVGVADVDYNELANIASKPSER 2480
Cdd:cd01450    80 TNTGKALQYALEQLFS-ESNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSER 158


                  ...
gi 568960715 2481 HVF 2483
Cdd:cd01450   159 HVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 440-609 3.57e-51

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: 179.19  E-value: 3.57e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715    440 DIVFLVDGSYSIGIANFVKVRAFLEVLAKSFEISPNRVQISLVQYSRDPHTEFTLKEFNRVEDIIKAINTFPYR-GGSTN 518
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715    519 TGKAMTYVREKIFVPNKGSRSNVPKVMILITDGKSSDA---FRDPAIKLRNSDVEIFAVGVKDAV-RSELEAIASPPAET 594
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNDVdEEELKKLASAPGGV 160

                           170
                    ....*....|....*
gi 568960715    595 HVFTVEDFDAFQRIS 609
Cdd:smart00327  161 YVFLPELLDLLIDLL 175
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 140-302 7.57e-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: 177.90  E-value: 7.57e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  140 DLVFLVDGSWSVGRNNFKYILDFIVALVSAFDIGEEKTRVGVVQYSSDTRTEFNLNQYYRREDLLAAVKKIPYKGGNTM- 218
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLn 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  219 TGDAIDYLVKNTFTESAGSRA--GFPKVAIIITDGKSQDEVEIPARELRNIGVEVFSLGIKAADAKELKQIASTPSLnhV 296
Cdd:cd01481    82 TGSALDYVVKNLFTKSAGSRIeeGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSF--V 159


                  ....*.
gi 568960715  297 FNVANF 302
Cdd:cd01481   160 FQVSDF 165
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1199-1368 7.83e-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: 175.34  E-value: 7.83e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   1199 DIVLLVDGSWSIGRANFRTVRSFISRIVEVFEIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYK-GGNTL 1277
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   1278 TGMALNFIRQQSFKTQAGMRPRARKIGVLITDGKSQD---DVEAPSKKLKDEGVELFAIGIKNA-DEVELKMIATDPDDT 1353
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGGV 160

                           170
                    ....*....|....*
gi 568960715   1354 HAYNVADFESLSKIV 1368
Cdd:smart00327  161 YVFLPELLDLLIDLL 175
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 439-617 2.65e-47

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: 170.26  E-value: 2.65e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  439 ADIVFLVDGSYSIGIANFVKVRAFLEVLAKSFEISPNRVQISLVQYSRDPHTEFTLKEFNRVEDIIKAINTFPYRGGSTN 518
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  519 TGKAMTYVREKIFVPNKGSRS---NVPKVMILITDGKSSDAFRDPAIKLRNSDVEIFAVGVKDAVRSELEAIASPPAETH 595
Cdd:cd01475    83 TGLAIQYAMNNAFSEAEGARPgseRVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLADH 162

                         170       180
                  ....*....|....*....|..
gi 568960715  596 VFTVEDFDAFQRISFELTQSIC 617
Cdd:cd01475   163 VFYVEDFSTIEELTKKFQGKIC 184
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1198-1376 8.47e-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: 165.64  E-value: 8.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1198 ADIVLLVDGSWSIGRANFRTVRSFISRIVEVFEIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTL 1277
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1278 TGMALNFIRQQSFKTQAGMRPRAR---KIGVLITDGKSQDDVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDDTH 1354
Cdd:cd01475    83 TGLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLADH 162

                         170       180
                  ....*....|....*....|..
gi 568960715 1355 AYNVADFESLSKIVDDLTINLC 1376
Cdd:cd01475   163 VFYVEDFSTIEELTKKFQGKIC 184
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1198-1361 1.08e-45

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: 163.26  E-value: 1.08e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1198 ADIVLLVDGSWSIGRANFRTVRSFISRIVEVFEIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTL 1277
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1278 -TGMALNFIRQQSFKTQAGMRPR--ARKIGVLITDGKSQDDVEAPSKKLKDEGVELFAIGIKNADEVELKMIATDPDdtH 1354
Cdd:cd01481    81 nTGSALDYVVKNLFTKSAGSRIEegVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS--F 158


                  ....*..
gi 568960715 1355 AYNVADF 1361
Cdd:cd01481   159 VFQVSDF 165
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 139-308 3.24e-44

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: 159.44  E-value: 3.24e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  139 TDLVFLVDGSWSVGRNNFKYILDFIVALVSAFDIGEEKTRVGVVQYSSDTRTEFNLNQYYRREDLLAAVKKIPYKGGNTM 218
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  219 TGDAIDYLVKNTFTESAGSRAGFPKVAIIITDGKSQD----EVEIPARELRNIgvEVFSLGIKAA-----DAKELKQIAS 289
Cdd:cd01469    81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDdpllKDVIPQAEREGI--IRYAIGVGGHfqrenSREELKTIAS 158

                         170
                  ....*....|....*....
gi 568960715  290 TPSLNHVFNVANFDAIVDI 308
Cdd:cd01469   159 KPPEEHFFNVTDFAALKDI 177
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 2325-2494 9.06e-44

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: 158.00  E-value: 9.06e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   2325 DIVFLTDASWSIGDDNFNKVVKFIFNTVGAFDeVNPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYR-GGNT 2403
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLD-IGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGT 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   2404 RTGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQD---EVKKAAFVIQQSGFSVFVVGV-ADVDYNELANIASKPSE 2479
Cdd:smart00327   80 NLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 568960715   2480 RHVFIVDDFESFEKI 2494
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 440-608 3.93e-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: 156.36  E-value: 3.93e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  440 DIVFLVDGSYSIGIANFVKVRAFLEVLAKSFEISPNRVQISLVQYSRDPHTEFTLKEFNRVEDIIKAINTFPYRGGSTNT 519
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  520 GKAMTYVREKIFVPNKGSRSNVPKVMILITDGKSSDAFRDPAI--KLRNSDVEIFAVGVKDAVRS-----ELEAIASPPA 592
Cdd:cd01469    82 ATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDVipQAEREGIIRYAIGVGGHFQRensreELKTIASKPP 161

                         170
                  ....*....|....*.
gi 568960715  593 ETHVFTVEDFDAFQRI 608
Cdd:cd01469   162 EEHFFNVTDFAALKDI 177
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 439-602 2.47e-41

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 150.55  E-value: 2.47e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  439 ADIVFLVDGSYSIGIANFVKVRAFLEVLAKSFEISPNRVQISLVQYSRDPHTEFTLKEFNRVEDIIKAINTFPYRGGST- 517
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  518 NTGKAMTYVREKIFVPNKGSR--SNVPKVMILITDGKSSDAFRDPAIKLRNSDVEIFAVGVKDAVRSELEAIASPPaeTH 595
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP--SF 158


                  ....*..
gi 568960715  596 VFTVEDF 602
Cdd:cd01481   159 VFQVSDF 165
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 2324-2527 3.17e-41

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: 152.54  E-value: 3.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2324 ADIVFLTDASWSIGDDNFNKVVKFIfNTVGAFDEVNPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNT 2403
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFL-NQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2404 RTGKALTFIKEKVLTWESGMRK---NVPKVLVVVTDGRSQDEVKKAAFVIQQSGFSVFVVGVADVDYNELANIASKPSER 2480
Cdd:cd01475    82 MTGLAIQYAMNNAFSEAEGARPgseRVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAD 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2481 HVFIVDDFESFEKIEDNL-------------ITFVCETATSSCPLIYLDGYTSpGFKMLE 2527
Cdd:cd01475   162 HVFYVEDFSTIEELTKKFqgkicvvpdlcatLSHVCQQVCISTPGSYLCACTE-GYALLE 220
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1199-1367 5.56e-40

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: 147.12  E-value: 5.56e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1199 DIVLLVDGSWSIGRANFRTVRSFISRIVEVFEIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTLT 1278
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1279 GMALNFIRQQSFKTQAGMRPRARKIGVLITDGKSQDDVEAPS--KKLKDEGVELFAIGI------KNADEvELKMIATDP 1350
Cdd:cd01469    82 ATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDviPQAEREGIIRYAIGVgghfqrENSRE-ELKTIASKP 160

                         170
                  ....*....|....*..
gi 568960715 1351 DDTHAYNVADFESLSKI 1367
Cdd:cd01469   161 PEEHFFNVTDFAALKDI 177
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 2324-2488 2.68e-38

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 142.08  E-value: 2.68e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2324 ADIVFLTDASWSIGDDNFNKVVKFIFNTVGAFDeVNPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNT 2403
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLD-VGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2404 -RTGKALTFIKEKVLTWESG--MRKNVPKVLVVVTDGRSQDEVKKAAFVIQQSGFSVFVVGVADVDYNELANIASKPSer 2480
Cdd:cd01481    80 lNTGSALDYVVKNLFTKSAGsrIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPS-- 157


                  ....*...
gi 568960715 2481 HVFIVDDF 2488
Cdd:cd01481   158 FVFQVSDF 165
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 2325-2494 1.11e-36

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: 137.87  E-value: 1.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2325 DIVFLTDASWSIGDDNFNKVVKFIFNTVGAFDEvNPAGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYRGGNTR 2404
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDI-GPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2405 TGKALTFIKEKVLTWESGMRKNVPKVLVVVTDGRSQDEVKKAAfVIQQS---GFSVFVVGVADV-----DYNELANIASK 2476
Cdd:cd01469    81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKD-VIPQAereGIIRYAIGVGGHfqrenSREELKTIASK 159

                         170
                  ....*....|....*...
gi 568960715 2477 PSERHVFIVDDFESFEKI 2494
Cdd:cd01469   160 PPEEHFFNVTDFAALKDI 177
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 140-297 4.19e-32

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: 124.22  E-value: 4.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  140 DLVFLVDGSWSVGRNNFKYILDFIVALVSAFDIGEEKTRVGVVQYSSDTRTEFNLNQYYRREDLLAAVKKIPYK-GGNTM 218
Cdd:cd00198     2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGTN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  219 TGDAIDYLVKNTFtesAGSRAGFPKVAIIITDGKSQDEVEIP---ARELRNIGVEVFSLGIK-AADAKELKQIASTPSLN 294
Cdd:cd00198    82 IGAALRLALELLK---SAKRPNARRVIILLTDGEPNDGPELLaeaARELRKLGITVYTIGIGdDANEDELKEIADKTTGG 158


                  ...
gi 568960715  295 HVF 297
Cdd:cd00198   159 AVF 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 439-597 1.00e-31

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 123.06  E-value: 1.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  439 ADIVFLVDGSYSIGIANFVKVRAFLEVLAKSFEISPNRVQISLVQYSRDPHTEFTLKEFNRVEDIIKAINTFPYR-GGST 517
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  518 NTGKAMTYVREKIfvpNKGSRSNVPKVMILITDGKSSDA---FRDPAIKLRNSDVEIFAVGVKD-AVRSELEAIASPPAE 593
Cdd:cd00198    81 NIGAALRLALELL---KSAKRPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGDdANEDELKEIADKTTG 157


                  ....
gi 568960715  594 THVF 597
Cdd:cd00198   158 GAVF 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1198-1356 3.59e-30

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: 118.44  E-value: 3.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1198 ADIVLLVDGSWSIGRANFRTVRSFISRIVEVFEIGPKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYK-GGNT 1276
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1277 LTGMALNFIRQQSFKTQagmRPRARKIGVLITDGKSQDD---VEAPSKKLKDEGVELFAIGIKN-ADEVELKMIATDPDD 1352
Cdd:cd00198    81 NIGAALRLALELLKSAK---RPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGDdANEDELKEIADKTTG 157


                  ....
gi 568960715 1353 THAY 1356
Cdd:cd00198   158 GAVF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 140-297 2.91e-29

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: 115.96  E-value: 2.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  140 DLVFLVDGSWSVGRNNFKYIlDFIVALVSAFDIGEEKTRVGVVQYSSDTRT--EFNLNQYYRREDLLAAVKKIPYKGGNT 217
Cdd:cd01476     2 DLLFVLDSSGSVRGKFEKYK-KYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  218 MTGDAIDYLVkNTFTESAGSRAGFPKVAIIITDGKSQDEVEIPARELRNI-GVEVFSLGIK---AADAKELKQIASTPsl 293
Cdd:cd01476    81 ATGAAIEVAL-QQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGdpgTVDTEELHSITGNE-- 157


                  ....
gi 568960715  294 NHVF 297
Cdd:cd01476   158 DHIF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 2324-2484 9.72e-27

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: 108.64  E-value: 9.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2324 ADIVFLTDASWSIgDDNFNKVVKFIFNTVGAFDeVNPAGIQVSFVQYSDEVKS--EFKLNTYNDKALALGALQNIRYRGG 2401
Cdd:cd01476     1 LDLLFVLDSSGSV-RGKFEKYKKYIERIVEGLE-IGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2402 NTRTGKALTFiKEKVLTWESGMRKNVPKVLVVVTDGRSQDEVKKAAFVIQ-QSGFSVFVVGVAD---VDYNELANIASkp 2477
Cdd:cd01476    79 TTATGAAIEV-ALQQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRaVPNIETFAVGTGDpgtVDTEELHSITG-- 155


                  ....*..
gi 568960715 2478 SERHVFI 2484
Cdd:cd01476   156 NEDHIFT 162
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1198-1351 1.20e-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: 105.56  E-value: 1.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1198 ADIVLLVDGSWSIgRANFRTVRSFISRIVEVFEIGPKRVQIALAQYSGDPRT--EWQLNAHRDKKSLLQAVANLPYKGGN 1275
Cdd:cd01476     1 LDLLFVLDSSGSV-RGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1276 TLTGMALNFIRQQsFKTQAGMRPRARKIGVLITDGKSQDDVEAPSKKLKDE-GVELFAIGIKN---ADEVELKMIATDPD 1351
Cdd:cd01476    80 TATGAAIEVALQQ-LDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGDpgtVDTEELHSITGNED 158
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 439-598 2.80e-24

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: 101.71  E-value: 2.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  439 ADIVFLVDGSYSIGiANFVKVRAFLEVLAKSFEISPNRVQISLVQYS--RDPHTEFTLKEFNRVEDIIKAINTFPYRGGS 516
Cdd:cd01476     1 LDLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  517 TNTGKAMTYVREkIFVPNKGSRSNVPKVMILITDGKSSDAFRDPAIKLRNS-DVEIFAVGVKD---AVRSELEAIASppA 592
Cdd:cd01476    80 TATGAAIEVALQ-QLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGDpgtVDTEELHSITG--N 156


                  ....*.
gi 568960715  593 ETHVFT 598
Cdd:cd01476   157 EDHIFT 162
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2324-2483 5.68e-24

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: 100.72  E-value: 5.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2324 ADIVFLTDASWSIGDDNFNKVVKFIFNTVGAFDEVNPaGIQVSFVQYSDEVKSEFKLNTYNDKALALGALQNIRYR-GGN 2402
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPP-GDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2403 TRTGKALTFIKEkvlTWESGMRKNVPKVLVVVTDGRSQD---EVKKAAFVIQQSGFSVFVVGV-ADVDYNELANIASKPS 2478
Cdd:cd00198    80 TNIGAALRLALE---LLKSAKRPNARRVIILLTDGEPNDgpeLLAEAARELRKLGITVYTIGIgDDANEDELKEIADKTT 156


                  ....*
gi 568960715 2479 ERHVF 2483
Cdd:cd00198   157 GGAVF 161
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 440-583 7.04e-23

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: 98.61  E-value: 7.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  440 DIVFLVDGSYSIGIANFV-KVRAFLEVLAKSFEISPNRVQISLVQYSRDPHTEFTLKEFNRVE-----DIIKAINTFPYR 513
Cdd:cd01471     2 DLYLLVDGSGSIGYSNWVtHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNkdlalNAIRALLSLYYP 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568960715  514 GGSTNTGKAMTYVREKIFvPNKGSRSNVPKVMILITDGKSSDAFR--DPAIKLRNSDVEIFAVGVKDAVRSE 583
Cdd:cd01471    82 NGSTNTTSALLVVEKHLF-DTRGNRENAPQLVIIMTDGIPDSKFRtlKEARKLRERGVIIAVLGVGQGVNHE 152
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 140-296 4.74e-22

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: 96.30  E-value: 4.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  140 DLVFLVDGSWSVGRNNFKYILDFIVALVSAF------DIGEEKTRVGVVQYSSDTRTEFNLNQYYR-REDLLAAVKKIPY 212
Cdd:cd01480     4 DITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRnYTSLKEAVDNLEY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  213 KGGNTMTGDAIDYlVKNTFTEsaGSRAGFPKVAIIITDGKSQDE----VEIPARELRNIGVEVFSLGIKAADAKELKQIA 288
Cdd:cd01480    84 IGGGTFTDCALKY-ATEQLLE--GSHQKENKFLLVITDGHSDGSpdggIEKAVNEADHLGIKIFFVAVGSQNEEPLSRIA 160


                  ....*...
gi 568960715  289 STPSLNHV 296
Cdd:cd01480   161 CDGKSALY 168
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1199-1335 9.67e-22

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: 95.14  E-value: 9.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1199 DIVLLVDGSWSIGRAN-FRTVRSFISRIVEVFEIGPKRVQIALAQYSGDPRTEWQLNAHR--DKKSLLQAVA---NLPYK 1272
Cdd:cd01471     2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNstNKDLALNAIRallSLYYP 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568960715 1273 GGNTLTGMALNFIRQQSFKTqAGMRPRARKIGVLITDGKSQDDVEA--PSKKLKDEGVELFAIGI 1335
Cdd:cd01471    82 NGSTNTTSALLVVEKHLFDT-RGNRENAPQLVIIMTDGIPDSKFRTlkEARKLRERGVIIAVLGV 145
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 140-276 2.12e-18

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: 85.51  E-value: 2.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  140 DLVFLVDGSWSVGRNN-FKYILDFIVALVSAFDIGEEKTRVGVVQYSSDTRTEFNLNQYY-----RREDLLAAVKKIPYK 213
Cdd:cd01471     2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNstnkdLALNAIRALLSLYYP 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568960715  214 GGNTMTGDAIDYLVKNTFtESAGSRAGFPKVAIIITDGKS---QDEVEIpARELRNIGVEVFSLGI 276
Cdd:cd01471    82 NGSTNTTSALLVVEKHLF-DTRGNRENAPQLVIIMTDGIPdskFRTLKE-ARKLRERGVIIAVLGV 145
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1198-1373 7.40e-18

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 83.97  E-value: 7.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1198 ADIVLLVDGSWSIGRANFRTVRSFISRIVEVF------EIGPKRVQIALAQYSGDPRTEWQ-LNAHRDKKSLLQAVANLP 1270
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGfLRDIRNYTSLKEAVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1271 YKGGNTLTGMALNFIRQQSFKTQagmRPRARKIGVLITDGKSQ-DDVEAPSKKLKD---EGVELFAIGIKNADEVELKMI 1346
Cdd:cd01480    83 YIGGGTFTDCALKYATEQLLEGS---HQKENKFLLVITDGHSDgSPDGGIEKAVNEadhLGIKIFFVAVGSQNEEPLSRI 159

                         170       180
                  ....*....|....*....|....*...
gi 568960715 1347 ATDPDDTH-AYNVADfESLSKIVDDLTI 1373
Cdd:cd01480   160 ACDGKSALyRENFAE-LLWSFFIDDETA 186
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 439-620 2.79e-17

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: 82.56  E-value: 2.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  439 ADIVFLVDGSYSIGiANFVKVRAFLEVLAKSFeISPNrVQISLVQYSRDPHTEFTLKEFNrvEDIIKAINTF----PyrG 514
Cdd:cd01474     5 FDLYFVLDKSGSVA-ANWIEIYDFVEQLVDRF-NSPG-LRFSFITFSTRATKILPLTDDS--SAIIKGLEVLkkvtP--S 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  515 GSTNTGKAMTYVREKIFVPNKGSRSNVpKVMILITDGK-SSDAFRDP---AIKLRNSDVEIFAVGVKDAVRSELEAIASp 590
Cdd:cd01474    78 GQTYIHEGLENANEQIFNRNGGGRETV-SVIIALTDGQlLLNGHKYPeheAKLSRKLGAIVYCVGVTDFLKSQLINIAD- 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 568960715  591 pAETHVFTVED-FDAFQRISFELTQSICLRI 620
Cdd:cd01474   156 -SKEYVFPVTSgFQALSGIIESVVKKACIEI 185
fn3 pfam00041
Fibronectin type III domain;
1758-1836 1.58e-16

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 76.68  E-value: 1.58e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1758 PRNLQVYNATSNSLTVKWDPA---SGRVQKYRITYQPSTGEGNEQTITVGGRQNSVLLQKLKPDTPYTITVYSQYPDGEG 1834
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   ..
gi 568960715  1835 GR 1836
Cdd:pfam00041   83 PP 84
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 439-605 1.68e-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: 80.12  E-value: 1.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  439 ADIVFLVDGSYSIGIANFVKVRAFLEVLAKSF------EISPNRVQISLVQYSRDPHTEFTLKEFNR-VEDIIKAINTFP 511
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRnYTSLKEAVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  512 YRGGSTNTGKAMTYVREKIFvpnKGSRSNVPKVMILITDGKsSDAFRDPAIK-----LRNSDVEIFAVGVKDAVRSELEA 586
Cdd:cd01480    83 YIGGGTFTDCALKYATEQLL---EGSHQKENKFLLVITDGH-SDGSPDGGIEkavneADHLGIKIFFVAVGSQNEEPLSR 158

                         170       180
                  ....*....|....*....|..
gi 568960715  587 IASPPAETHV---FTVEDFDAF 605
Cdd:cd01480   159 IACDGKSALYrenFAELLWSFF 180
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 2324-2482 3.28e-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: 79.35  E-value: 3.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2324 ADIVFLTDASWSIGDDNF----NKVVKFIFNTVGAFDEVNPAG-IQVSFVQYSDEVKSEFKL--NTYNDKALAlGALQNI 2396
Cdd:cd01480     3 VDITFVLDSSESVGLQNFditkNFVKRVAERFLKDYYRKDPAGsWRVGVVQYSDQQEVEAGFlrDIRNYTSLK-EAVDNL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2397 RYRGGNTRTGKALTFIKEKVLtweSGMRKNVPKVLVVVTDGRSQDE----VKKAAFVIQQSGFSVFVVGVADVDYNELAN 2472
Cdd:cd01480    82 EYIGGGTFTDCALKYATEQLL---EGSHQKENKFLLVITDGHSDGSpdggIEKAVNEADHLGIKIFFVAVGSQNEEPLSR 158

                         170
                  ....*....|
gi 568960715 2473 IASKPSERHV 2482
Cdd:cd01480   159 IACDGKSALY 168
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 2319-2503 1.21e-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: 77.55  E-value: 1.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2319 CKGAkADIVFLTDASWSIGDdNFNKVVKFIFNTVGAFdeVNPaGIQVSFVQYSDEVKSEFKLNTYNDKAL-ALGALQNIr 2397
Cdd:cd01474     1 CAGH-FDLYFVLDKSGSVAA-NWIEIYDFVEQLVDRF--NSP-GLRFSFITFSTRATKILPLTDDSSAIIkGLEVLKKV- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2398 YRGGNTRTGKALTFIKEKVLTWESGMRKNVpKVLVVVTDGRSQDEV----KKAAFVIQQSGFSVFVVGVADVDYNELANI 2473
Cdd:cd01474    75 TPSGQTYIHEGLENANEQIFNRNGGGRETV-SVIIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGVTDFLKSQLINI 153

                         170       180       190
                  ....*....|....*....|....*....|.
gi 568960715 2474 ASkpSERHVFIVDD-FESFEKIEDNLITFVC 2503
Cdd:cd01474   154 AD--SKEYVFPVTSgFQALSGIIESVVKKAC 182
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 724-805 5.26e-15

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: 72.91  E-value: 5.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  724 GVPRNLKVTDETTDSFKLTWSQAP---GRVLRYRIRYRPVSGGESKEVST-PANQRRKTLENLTPDTKYEISVIAEYSSG 799
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                  ....*.
gi 568960715  800 PGSPLT 805
Cdd:cd00063    82 ESPPSE 87
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1195-1371 1.19e-14

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: 76.90  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1195 RAEADIVLLVDGSWSIGRAN-FRTVRSFISRIVEVFeigPKRVQIALAQYSGDPrtEWQLNAHRDKKSLLQAVANLPYKG 1273
Cdd:COG1240    90 QRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEA--EVLLPLTRDREALKRALDELPPGG 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1274 GnTLTGMALnfirQQSFKTQAGMRPRARKIGVLITDGK---SQDDVEAPSKKLKDEGVELFAIGI--KNADEVELKMIAt 1348
Cdd:COG1240   165 G-TPLGDAL----ALALELLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVgtEAVDEGLLREIA- 238

                         170       180
                  ....*....|....*....|....*
gi 568960715 1349 dpDDTHA--YNVADFESLSKIVDDL 1371
Cdd:COG1240   239 --EATGGryFRADDLSELAAIYREI 261
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 634-719 1.88e-14

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 71.37  E-value: 1.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  634 PPKDLRFTQVTANSFKAEWSPP---GDNVFSYHVTYKDANGDDEVTV-VEPASSTSVVLNNLRPETLYLVNVTAEYEDGF 709
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPeddGGPITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGE 82

                          90
                  ....*....|
gi 568960715  710 SVPITGEETT 719
Cdd:cd00063    83 SPPSESVTVT 92
fn3 pfam00041
Fibronectin type III domain;
726-803 3.26e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 70.14  E-value: 3.26e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   726 PRNLKVTDETTDSFKLTWS---QAPGRVLRYRIRYRPVSGGE-SKEVSTPANQRRKTLENLTPDTKYEISVIAEYSSGPG 801
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTpppDGNGPITGYEVEYRPKNSGEpWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   ..
gi 568960715   802 SP 803
Cdd:pfam00041   83 PP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 2120-2199 5.34e-14

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 69.83  E-value: 5.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2120 PPQNIHIFDEWYTRFRVSWDPSP---SPVLGYKIVYKPVGSNEPMEA--FVGEVTSYTLHNLNPSTTYDVSVYAQYDSGL 2194
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVevTPGSETSYTLTGLKPGTEYEFRVRAVNGGGE 82


                  ....*
gi 568960715 2195 SVPLT 2199
Cdd:cd00063    83 SPPSE 87
fn3 pfam00041
Fibronectin type III domain;
1387-1465 5.36e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 69.75  E-value: 5.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1387 APTNLVISERTHRSFRVSWTPPSDS---VDRYKVEYYPVSGGKR-QEFYVSRLDTSTVLKDLKPETDYVVNVYSVVEDEY 1462
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGngpITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 568960715  1463 SEP 1465
Cdd:pfam00041   82 GPP 84
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 2325-2462 6.37e-14

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: 72.80  E-value: 6.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2325 DIVFLTDASWSIGDDN-FNKVVKFIFNTVGAFDeVNPAGIQVSFVQYSDEVKSEFKLNTYN--DKALALGALQNIR---Y 2398
Cdd:cd01471     2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLN-ISPDEINLYLVTFSTNAKELIRLSSPNstNKDLALNAIRALLslyY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568960715 2399 RGGNTRTGKALTFIKeKVLTWESGMRKNVPKVLVVVTDGRSQDEVK--KAAFVIQQSGFSVFVVGV 2462
Cdd:cd01471    81 PNGSTNTTSALLVVE-KHLFDTRGNRENAPQLVIIMTDGIPDSKFRtlKEARKLRERGVIIAVLGV 145
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 439-608 2.01e-13

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 73.05  E-value: 2.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  439 ADIVFLVDGSYSIGIAN-FVKVRAFLEVLAKSFeisPNRVQISLVQYSRDPHT--EFTlkefNRVEDIIKAINTFPYRGG 515
Cdd:COG1240    93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVllPLT----RDREALKRALDELPPGGG 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  516 sTNTGKAMTYVREKIfvpnKGSRSNVPKVMILITDGKSSDAFRDP---AIKLRNSDVEIFAVGVKDAVRSE--LEAIAsp 590
Cdd:COG1240   166 -TPLGDALALALELL----KRADPARRKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEAVDEglLREIA-- 238

                         170       180
                  ....*....|....*....|
gi 568960715  591 pAET--HVFTVEDFDAFQRI 608
Cdd:COG1240   239 -EATggRYFRADDLSELAAI 257
fn3 pfam00041
Fibronectin type III domain;
1940-2018 2.16e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.83  E-value: 2.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1940 RNIQVYNPTPNSLDVRWDPAP---GPVQQYRIVYSPVAGTRPSESIVVPGNTRTVHLERLIPDTPYSVNIVALYSDGEGN 2016
Cdd:pfam00041    4 SNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGP 83


                   ..
gi 568960715  2017 PS 2018
Cdd:pfam00041   84 PS 85
fn3 pfam00041
Fibronectin type III domain;
336-416 3.91e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 67.05  E-value: 3.91e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   336 PPSNLVVTELSSKYIRLSWDPSP---SAVTGYKILLTPMAAGSRHHALSVGPQTTTLNVRDLTADTEYQISVFAMKGLTS 412
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ....
gi 568960715   413 SEPT 416
Cdd:pfam00041   82 GPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1474-1548 5.09e-13

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: 66.87  E-value: 5.09e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960715   1474 PVPVVSLNIYDVGPTTMHVQWQPV--GGATGYTVSYQPTRSPEGTKPKEMRVGPTVNDVQLTGLLPNTEYEVTVQAV 1548
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPpdDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1386-1470 6.72e-13

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: 66.75  E-value: 6.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1386 EAPTNLVISERTHRSFRVSWTPPSDS---VDRYKVEYYPVSGGKRQEFYVSRLD-TSTVLKDLKPETDYVVNVYSVVEDE 1461
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGSeTSYTLTGLKPGTEYEFRVRAVNGGG 81


                  ....*....
gi 568960715 1462 YSEPLKGTE 1470
Cdd:cd00063    82 ESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1940-2020 8.74e-13

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: 66.37  E-value: 8.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1940 RNIQVYNPTPNSLDVRWDPAP---GPVQQYRIVYSPVAGTRPSESIVVPGNTRTVHLERLIPDTPYSVNIVALYSDGEGN 2016
Cdd:cd00063     5 TNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESP 84


                  ....
gi 568960715 2017 PSPS 2020
Cdd:cd00063    85 PSES 88
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 140-317 9.77e-13

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: 69.27  E-value: 9.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  140 DLVFLVDGSWSVGRNNF-KYILDFIVALVSAFDIGEEKTRVGVVQYSSDTRT--EFNLNQYYRREDLLAAVKKIP--YK- 213
Cdd:cd01473     2 DLTLILDESASIGYSNWrKDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDvvPFSDEERYDKNELLKKINDLKnsYRs 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  214 GGNTMTGDAIDYLVKNtFTESAGSRAGFPKVAIIITDGKSQDEVEipaRELRNIG-------VEVFSLGIKAADAKELKQ 286
Cdd:cd01473    82 GGETYIVEALKYGLKN-YTKHGNRRKDAPKVTMLFTDGNDTSASK---KELQDISllykeenVKLLVVGVGAASENKLKL 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 568960715  287 IA--STPSLNHVFNV-ANFDAIVDIQNEIISQVC 317
Cdd:cd01473   158 LAgcDINNDNCPNVIkTEWNNLNGISKFLTDKIC 191
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
634-992 1.03e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 73.88  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  634 PPKDLRFTQVTANSFKAEWSP-PGDNVFSYHVtYKDANGDDEVTVVEPASSTSVVLNNLRPETLYLVNVTAEYEDG---- 708
Cdd:COG3401   235 APTGLTATADTPGSVTLSWDPvTESDATGYRV-YRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGnesa 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  709 FSVPITGeETTAEVKGVPRNLKVTDETTDSFKLTWSQAPG-RVLRYRIRYRPVSGGESKEVSTPANQRRKTLENLTPDTK 787
Cdd:COG3401   314 PSNVVSV-TTDLTPPAAPSGLTATAVGSSSITLSWTASSDaDVTGYNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTT 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  788 YEISVIAEYSSGPGSPLTGN--AATEEVRGNPRDLRVSDATTSTLKLSWSRAPGKVKQYLVTYTPAAGGETQEVTVRGDT 865
Cdd:COG3401   393 YYYKVTAVDAAGNESAPSEEvsATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTT 472

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  866 TTTMLRKLKEGTQYDLSVTALYASGAGEALSGKGSTLEERG--SPQNLVTKDITDTSIGAYWTSAPGMVRGYRVS-WKSL 942
Cdd:COG3401   473 TSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGasAAAAVGGAPDGTPNVTGASPVTVGASTGDVLItDLVS 552

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 568960715  943 YDDIEAGETTLPGDAIHTMIENLQPETKYKISVFATYSSGEGEPVTGDAT 992
Cdd:COG3401   553 LTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNTNDVAGVHGGTLLV 602
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 1195-1379 1.24e-12

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: 69.08  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1195 RAEADIVLLVDGSWSIGrANFRTVRSFISRIVEVFeIGPKrVQIALAQYSGDPRTEWQLNAHRDK--KSLLQAVANLPyk 1272
Cdd:cd01474     2 AGHFDLYFVLDKSGSVA-ANWIEIYDFVEQLVDRF-NSPG-LRFSFITFSTRATKILPLTDDSSAiiKGLEVLKKVTP-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1273 GGNTLTGMALNFIRQQSFKTQAGMRpRARKIGVLITDGKSQDDV----EAPSKKLKDEGVELFAIGIKNADEVELKMIAT 1348
Cdd:cd01474    77 SGQTYIHEGLENANEQIFNRNGGGR-ETVSVIIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGVTDFLKSQLINIAD 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 568960715 1349 DPDdtHAYNVAD-FESLSKIVDDLTINLCNSV 1379
Cdd:cd01474   156 SKE--YVFPVTSgFQALSGIIESVVKKACIEI 185
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1756-1834 1.36e-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: 65.98  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1756 SGPRNLQVYNATSNSLTVKWDPAS---GRVQKYRITYQPSTGEGNEQTITVGGRQNSVLLQKLKPDTPYTITVYSQYPDG 1832
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                  ..
gi 568960715 1833 EG 1834
Cdd:cd00063    82 ES 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 724-801 1.59e-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: 65.33  E-value: 1.59e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715    724 GVPRNLKVTDETTDSFKLTWSQAP-----GRVLRYRIRYRPvSGGESKEVSTPANQRRKTLENLTPDTKYEISVIAEYSS 798
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYRE-EGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 568960715    799 GPG 801
Cdd:smart00060   81 GEG 83
fn3 pfam00041
Fibronectin type III domain;
634-712 1.94e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 65.13  E-value: 1.94e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   634 PPKDLRFTQVTANSFKAEWSPP---GDNVFSYHVTYKDAN-GDDEVTVVEPASSTSVVLNNLRPETLYLVNVTAEYEDGF 709
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNsGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 568960715   710 SVP 712
Cdd:pfam00041   82 GPP 84
fn3 pfam00041
Fibronectin type III domain;
817-893 3.76e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.36  E-value: 3.76e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   817 PRDLRVSDATTSTLKLSWSRAP---GKVKQYLVTYTPA-AGGETQEVTVRGDTTTTMLRKLKEGTQYDLSVTALYASGAG 892
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKnSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   .
gi 568960715   893 E 893
Cdd:pfam00041   83 P 83
fn3 pfam00041
Fibronectin type III domain;
2120-2197 3.95e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 64.36  E-value: 3.95e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  2120 PPQNIHIFDEWYTRFRVSWDPSP---SPVLGYKIVYKPVGSNEPMEAF--VGEVTSYTLHNLNPSTTYDVSVYAQYDSGL 2194
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEItvPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 568960715  2195 SVP 2197
Cdd:pfam00041   82 GPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1756-1834 3.99e-12

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 64.17  E-value: 3.99e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   1756 SGPRNLQVYNATSNSLTVKWD-PASGRVQKYRITYQPSTGE--GNEQTITVGGRQNSVLLQKLKPDTPYTITVYSQYPDG 1832
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEpPPDDGITGYIVGYRVEYREegSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 568960715   1833 EG 1834
Cdd:smart00060   82 EG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 634-710 5.34e-12

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 63.79  E-value: 5.34e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715    634 PPKDLRFTQVTANSFKAEWSPP-GDNVFSYHVTYK---DANGDDEVTVVEPASSTSVVLNNLRPETLYLVNVTAEYEDGF 709
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPpDDGITGYIVGYRveyREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 568960715    710 S 710
Cdd:smart00060   83 G 83
fn3 pfam00041
Fibronectin type III domain;
26-105 5.72e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.97  E-value: 5.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715    26 DPPSDLNFKIIDENTVHMSWERPVD---PIVGYRITVDPTTDG-PTKEFTLAASTTETLLSDLIPETQYVVTITSYNEVE 101
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDgngPITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 568960715   102 ESVP 105
Cdd:pfam00041   81 EGPP 84
fn3 pfam00041
Fibronectin type III domain;
1656-1728 6.68e-12

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 63.59  E-value: 6.68e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960715  1656 PAPTNLQFTEVTPESFRGTW---DHGASDVSLYRITWAPVGNPDKM-ETILNGDENTLVFENLNPNTPYEVSITAIY 1728
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWtppPDGNGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77
VWA_2 pfam13519
von Willebrand factor type A domain;
441-548 8.47e-12

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 63.85  E-value: 8.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   441 IVFLVDGSYSI-----GIANFVKVRAFLEVLAKSFeispNRVQISLVQYSRDPHTEFTLKEfnRVEDIIKAINTFPYRGG 515
Cdd:pfam13519    1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSL----PGDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|...
gi 568960715   516 STNTGKAMTYVREKIfvpnKGSRSNVPKVMILI 548
Cdd:pfam13519   75 GTNLAAALQLARAAL----KHRRKNQPRRIVLI 103
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1628-1990 8.98e-12

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 70.80  E-value: 8.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1628 TQYTVSVSAVYDEGTSPPATAYD-TTRRVP--APTNLQFTEVTPESFRGTWD-HGASDVSLYRITWAPVGNpDKMETILN 1703
Cdd:COG3401   203 TTYYYRVAATDTGGESAPSNEVSvTTPTTPpsAPTGLTATADTPGSVTLSWDpVTESDATGYRVYRSNSGD-GPFTKVAT 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1704 GDENTLVFENLNPNTPYEVSITAIYPDESESeDLSGTERTLrliplTTQAPKSGPRNLQVYNATSNSLTVKWDPASG-RV 1782
Cdd:COG3401   282 VTTTSYTDTGLTNGTTYYYRVTAVDAAGNES-APSNVVSVT-----TDLTPPAAPSGLTATAVGSSSITLSWTASSDaDV 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1783 QKYRItYQPSTGEGNEQTITVGGRQNSVLLQKLKPDTPYTITVYSQYPDGEGGRMTGRGKTKPLNTVRNLRVYDPSTSSL 1862
Cdd:COG3401   356 TGYNV-YRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVP 434

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1863 SVRWDHAEGNP--RQYKLFYAPTSGGPEELVPIPGNTNYAILRNLQP-DTPYTITVVPVYTEGDGGRTSDTGRTLVRGLA 1939
Cdd:COG3401   435 LTDVAGATAAAsaASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTtDTTTANLSVTTGSLVGGSGASSVTNSVSVIGA 514

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568960715 1940 RNIQVYNPTPNSLDVRWDPAPGPVQQYR--IVYSPVAGTRPSESIVVPGNTRT 1990
Cdd:COG3401   515 SAAAAVGGAPDGTPNVTGASPVTVGASTgdVLITDLVSLTTSASSSVSGAGLG 567
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 440-617 9.36e-12

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: 66.57  E-value: 9.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  440 DIVFLVDGSYSIGIANFVK-VRAFLEVLAKSFEISPNRVQISLVQYS---RDpHTEFTLKEFNRVEDIIKAINTFP--YR 513
Cdd:cd01473     2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAeknRD-VVPFSDEERYDKNELLKKINDLKnsYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  514 -GGSTNTGKAMTYVREKIFvPNKGSRSNVPKVMILITDGKSSDA----FRDPAIKLRNSDVEIFAVGVKDAVRSELEAIA 588
Cdd:cd01473    81 sGGETYIVEALKYGLKNYT-KHGNRRKDAPKVTMLFTDGNDTSAskkeLQDISLLYKEENVKLLVVGVGAASENKLKLLA 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 568960715  589 --SPPAETHVFTVE-DFDAFQRISFELTQSIC 617
Cdd:cd01473   160 gcDINNDNCPNVIKtEWNNLNGISKFLTDKIC 191
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 335-420 9.70e-12

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 63.67  E-value: 9.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  335 EPPSNLVVTELSSKYIRLSWDPSP---SAVTGYKILLTPMAAGSRHHALSVGPQTTTLNVRDLTADTEYQISVFAMKGLT 411
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                  ....*....
gi 568960715  412 SSEPTSVME 420
Cdd:cd00063    82 ESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 815-896 1.10e-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: 63.28  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  815 GNPRDLRVSDATTSTLKLSWSRAP---GKVKQYLVTYTPAAGGETQEVTV-RGDTTTTMLRKLKEGTQYDLSVTALYASG 890
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                  ....*.
gi 568960715  891 AGEALS 896
Cdd:cd00063    82 ESPPSE 87
fn3 pfam00041
Fibronectin type III domain;
1476-1548 1.30e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 62.82  E-value: 1.30e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960715  1476 PVVSLNIYDVGPTTMHVQWQPV----GGATGYTVSYQPTRSPEgtKPKEMRVGPTVNDVQLTGLLPNTEYEVTVQAV 1548
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgnGPITGYEVEYRPKNSGE--PWNEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 2120-2195 1.32e-11

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: 62.63  E-value: 1.32e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   2120 PPQNIHIFDEWYTRFRVSWDPSP-----SPVLGYKIVYKPVGSNEPMEAFVGEVTSYTLHNLNPSTTYDVSVYAQYDSGL 2194
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 568960715   2195 S 2195
Cdd:smart00060   83 G 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1474-1563 1.46e-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: 62.90  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1474 PVPVVSLNIYDVGPTTMHVQWQPV----GGATGYTVSYQPTRSPEGTKPKemRVGPTVNDVQLTGLLPNTEYEVTVQAVL 1549
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPeddgGPITGYVVEYREKGSGDWKEVE--VTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                          90
                  ....*....|....
gi 568960715 1550 YDLTSEPAKAREVT 1563
Cdd:cd00063    79 GGGESPPSESVTVT 92
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1400-1780 1.57e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 70.03  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1400 SFRVSWTPPSDSVDRYKVEYYPVSGGKRQEFYVSRLDTST---VLKDLKPETDYVVNVYSVVEDEYSEPLKG----TEKT 1472
Cdd:COG3401   152 GANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTlvdGGGDIEPGTTYYYRVAATDTGGESAPSNEvsvtTPTT 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1473 LPVPVVSLNIYDVGPTTMHVQWQPV--GGATGYTVSyqptRSPEGTKPKEMRVGPTVNDVQLTGLLPNTEYEVTVQAVLY 1550
Cdd:COG3401   232 PPSAPTGLTATADTPGSVTLSWDPVteSDATGYRVY----RSNSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDA 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1551 D----LTSEPAKAREVTLPLPRPQDVKLRDVTHSTMNVVWEPVLGK-VRKYIVrYKTPDEEFKEVEVDRSRASTILKD-- 1623
Cdd:COG3401   308 AgnesAPSNVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAdVTGYNV-YRSTSGGGTYTKIAETVTTTSYTDtg 386

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1624 LSSQTQYTVSVSAVYDEGTSPPATAYDTTRRVPAPTNLQFTEVTPESFRGTWDHGASDVSLYRITWAPVGNPDKMETI-- 1701
Cdd:COG3401   387 LTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTgn 466

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1702 --LNGDENTLVFENLNPNTPYEVSITAIypDESESEDLSGTERTLRLIPLTTQAPKSGPRNLQVYNATSNSLTVKWDPAS 1779
Cdd:COG3401   467 avPFTTTSSTVTATTTDTTTANLSVTTG--SLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGD 544


                  .
gi 568960715 1780 G 1780
Cdd:COG3401   545 V 545
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1569-1652 1.85e-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: 62.51  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1569 PQDVKLRDVTHSTMNVVWEPVL---GKVRKYIVRYK-TPDEEFKEVEVDRSRA-STILKDLSSQTQYTVSVSAVYDEGTS 1643
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYReKGSGDWKEVEVTPGSEtSYTLTGLKPGTEYEFRVRAVNGGGES 83


                  ....*....
gi 568960715 1644 PPATAYDTT 1652
Cdd:cd00063    84 PPSESVTVT 92
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 139-312 2.56e-11

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: 66.89  E-value: 2.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  139 TDLVFLVDGSWSVGRNNfkyILDFIVALVSAF-DIGEEKTRVGVVQYSSDTRTEFNLNqyYRREDLLAAVKKIPYKGGnT 217
Cdd:COG1240    93 RDVVLVVDASGSMAAEN---RLEAAKGALLDFlDDYRPRDRVGLVAFGGEAEVLLPLT--RDREALKRALDELPPGGG-T 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  218 MTGDAIdYLVKNTFTESAGSRagfPKVAIIITDGK---SQDEVEIPARELRNIGVEVFSLGI--KAADAKELKQIASTps 292
Cdd:COG1240   167 PLGDAL-ALALELLKRADPAR---RKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVgtEAVDEGLLREIAEA-- 240

                         170       180
                  ....*....|....*....|.
gi 568960715  293 LN-HVFNVANFDAIVDIQNEI 312
Cdd:COG1240   241 TGgRYFRADDLSELAAIYREI 261
fn3 pfam00041
Fibronectin type III domain;
1849-1927 3.25e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.66  E-value: 3.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1849 VRNLRVYDPSTSSLSVRWDHAE---GNPRQYKLFYAPTSGGPEEL-VPIPGNTNYAILRNLQPDTPYTITVVPVYTEGDG 1924
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   ...
gi 568960715  1925 GRT 1927
Cdd:pfam00041   83 PPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 26-106 3.28e-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: 62.13  E-value: 3.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   26 DPPSDLNFKIIDENTVHMSWERPVD---PIVGYRITVDPTTDGPTKEF-TLAASTTETLLSDLIPETQYVVTITSYNEVE 101
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDdggPITGYVVEYREKGSGDWKEVeVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                  ....*
gi 568960715  102 ESVPV 106
Cdd:cd00063    82 ESPPS 86
fn3 pfam00041
Fibronectin type III domain;
2030-2107 4.02e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.28  E-value: 4.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  2030 PRNIRVFGETTNSLSVAW---DHADGPVQQYRIIYSPTVGDPIDEYTTVPGRRNNVILQPLQPDTPYKITVIAIYEDGDG 2106
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWtppPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   .
gi 568960715  2107 G 2107
Cdd:pfam00041   83 P 83
fn3 pfam00041
Fibronectin type III domain;
1567-1645 4.18e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 61.28  E-value: 4.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1567 PRPQDVKLRDVTHSTMNVVWEPVL---GKVRKYIVRYKTPDEE--FKEVEVDRSRASTILKDLSSQTQYTVSVSAVYDEG 1641
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGepWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 568960715  1642 TSPP 1645
Cdd:pfam00041   81 EGPP 84
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1854-2210 4.88e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 68.49  E-value: 4.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1854 VYDPSTSSLSVRWDHAEGNPRQ-YKLFYAPTSGGPEELVPIPGNTNYAILRNLQPDTPYTiTVVPVYTEGDGGRTSDTGR 1932
Cdd:COG3401    57 VAAGLSSGGGLGTGGRAGTTSGvAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDE-VPSPAVGTATTATAVAGGA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1933 TLVRGLARNIQVYNPTPNSLDVRWDPAPGPVQQYRIVYSPVAGTRPSESIVVPGNTRTVHLERLIPDTPYSVNIVALYSD 2012
Cdd:COG3401   136 ATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTG 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2013 GEGNPSPS----QGRTLPRSgPRNIRVFGETTNSLSVAWD-HADGPVQQYRIIYSPTVGDPIDEYTTVPGrrNNVILQPL 2087
Cdd:COG3401   216 GESAPSNEvsvtTPTTPPSA-PTGLTATADTPGSVTLSWDpVTESDATGYRVYRSNSGDGPFTKVATVTT--TSYTDTGL 292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2088 QPDTPYKITVIAIYEDGDGGH----LTGNGRTVGLLPPQNIHIFDEWYTRFRVSWDPSPSP-VLGYKIVYKPVGSNEPME 2162
Cdd:COG3401   293 TNGTTYYYRVTAVDAAGNESApsnvVSVTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAdVTGYNVYRSTSGGGTYTK 372

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 568960715 2163 -AFVGEVTSYTLHNLNPSTTYDVSVYAQYDSGLSVPLTDQGTTLYLNVT 2210
Cdd:COG3401   373 iAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAA 421
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 2028-2106 5.09e-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: 61.36  E-value: 5.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2028 SGPRNIRVFGETTNSLSVAWDHAD---GPVQQYRIIYSPTVGDPIDEYTTVPGRRNNVILQPLQPDTPYKITVIAIYEDG 2104
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                  ..
gi 568960715 2105 DG 2106
Cdd:cd00063    82 ES 83
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 440-611 7.78e-11

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: 63.85  E-value: 7.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  440 DIVFLVDGSYSIGIANFVKVRAFLEVLAK---SFEISPNrvqISLVQYSRDPHTEFTLKEF--NRVEDIIKAINTFPYR- 513
Cdd:cd01470     2 NIYIALDASDSIGEEDFDEAKNAIKTLIEkisSYEVSPR---YEIISYASDPKEIVSIRDFnsNDADDVIKRLEDFNYDd 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  514 ---GGSTNTGKAMTYVREKIFVPNKGSRSNVPK---VMILITDGKSS------------DAFRDPAIKLRNS-----DVE 570
Cdd:cd01470    79 hgdKTGTNTAAALKKVYERMALEKVRNKEAFNEtrhVIILFTDGKSNmggsplptvdkiKNLVYKNNKSDNPredylDVY 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568960715  571 IFAVGvKDAVRSELEAIAS-PPAETHVFTVEDFDAFQRiSFE 611
Cdd:cd01470   159 VFGVG-DDVNKEELNDLASkKDNERHFFKLKDYEDLQE-VFD 198
VWA_2 pfam13519
von Willebrand factor type A domain;
141-248 8.42e-11

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 61.15  E-value: 8.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   141 LVFLVDGSWS-----VGRNNFKYILDFIVALVSAFDIgeekTRVGVVQYSSDTRTEFNLNQyyRREDLLAAVKKIPYKGG 215
Cdd:pfam13519    1 LVFVLDTSGSmrngdYGPTRLEAAKDAVLALLKSLPG----DRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|...
gi 568960715   216 NTMTGDAIDYLVKNTFTEsagsRAGFPKVAIII 248
Cdd:pfam13519   75 GTNLAAALQLARAALKHR----RKNQPRRIVLI 103
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1386-1668 9.76e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 67.72  E-value: 9.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1386 EAPTNLVISERTHRSFRVSWTPPSDS-VDRYKVEYYPVSGGKRQEfyVSRL-DTSTVLKDLKPETDYVVNVYSV----VE 1459
Cdd:COG3401   234 SAPTGLTATADTPGSVTLSWDPVTESdATGYRVYRSNSGDGPFTK--VATVtTTSYTDTGLTNGTTYYYRVTAVdaagNE 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1460 DEYSEPLKGT-EKTLPVPVVSLNIYDVGPTTMHVQWQPV--GGATGYTVsyqpTRSPEGTKPKEmRVGPTVNDVQLT--G 1534
Cdd:COG3401   312 SAPSNVVSVTtDLTPPAAPSGLTATAVGSSSITLSWTASsdADVTGYNV----YRSTSGGGTYT-KIAETVTTTSYTdtG 386

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1535 LLPNTEYEVTVQAV----LYDLTSEPAKAREVTLP----LPRPQDVKLRDVTHSTMNVVWEPVLGKVRKYIVRYKTPDEE 1606
Cdd:COG3401   387 LTPGTTYYYKVTAVdaagNESAPSEEVSATTASAAsgesLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGN 466

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568960715 1607 FKEVEVDRSRASTILKDLSSQTQYTVSVSAVYDEGTSPPATAYDTTRRVPAPTNLQFTEVTP 1668
Cdd:COG3401   467 AVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTP 528
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1569-1643 1.10e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 60.32  E-value: 1.10e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   1569 PQDVKLRDVTHSTMNVVWEP-----VLGKVRKYIVRYKTPDEEFKEVEVDRSRASTILKDLSSQTQYTVSVSAVYDEGTS 1643
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPppddgITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1090-1176 1.14e-10

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 60.59  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1090 PRNLKTSDPTMSSFRVTWEPAP---GEVKGYKVTFHPTGDDRRLGELVLGPYDNTVVLEELRAGTTYRVNVFGMFDGGES 1166
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGES 83

                          90
                  ....*....|
gi 568960715 1167 LPLVGQEMTT 1176
Cdd:cd00063    84 PPSESVTVTT 93
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 140-317 1.36e-10

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: 62.91  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  140 DLVFLVDGSWSVGRNNFKyILDFIVALVSAFDigEEKTRVGVVQYSSDTRTEFNLNQYYRREDLLAAVKKIPYKGGNTMT 219
Cdd:cd01474     6 DLYFVLDKSGSVAANWIE-IYDFVEQLVDRFN--SPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTYI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  220 GDAIDYLVKNTFTESAGSRAgFPKVAIIITDGKSQDEV----EIPARELRNIGVEVFSLGIKAADAKELKQIASTPslNH 295
Cdd:cd01474    83 HEGLENANEQIFNRNGGGRE-TVSVIIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSK--EY 159

                         170       180
                  ....*....|....*....|...
gi 568960715  296 VFNV-ANFDAIVDIQNEIISQVC 317
Cdd:cd01474   160 VFPVtSGFQALSGIIESVVKKAC 182
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1002-1075 4.88e-10

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 58.66  E-value: 4.88e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568960715 1002 LRVDEETEHTMRVTWKAAP---GKVVNYRVVYRPQGGGR-QMVAKVPPTVTSTVLKRLQPQTTYDITVLPMYKTGEGK 1075
Cdd:cd00063     7 LRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1387-1457 6.25e-10

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 58.01  E-value: 6.25e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568960715   1387 APTNLVISERTHRSFRVSWTPP-SDSVDRYKVEY---YPVSGGKRQEFYVSRLDTSTVLKDLKPETDYVVNVYSV 1457
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPpDDGITGYIVGYrveYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 440-589 1.13e-09

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 62.00  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  440 DIVFLVDGSYSIGIANFVKVRAFLEVLAKSFeiSPNRvQISLVQYSRDPHTEFTLKEFNRVEDIIKAINTFPYRGGsTNT 519
Cdd:COG2425   120 PVVLCVDTSGSMAGSKEAAAKAAALALLRAL--RPNR-RFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFAGGG-TDI 195

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568960715  520 GKAMTYVREKIFVPNKGSRsnvpkVMILITDGK---SSDAFRDpAIKLRNSDVEIFAVGVKDAVRSELEAIAS 589
Cdd:COG2425   196 APALRAALELLEEPDYRNA-----DIVLITDGEagvSPEELLR-EVRAKESGVRLFTVAIGDAGNPGLLEALA 262
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 2324-2474 2.14e-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: 61.11  E-value: 2.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2324 ADIVFLTDASWSIGDDNFNKVVKfifNTVGAFDEVNPAGIQVSFVQYSDEVksEFKLNTYNDKALALGALQNIRYRGGnT 2403
Cdd:COG1240    93 RDVVLVVDASGSMAAENRLEAAK---GALLDFLDDYRPRDRVGLVAFGGEA--EVLLPLTRDREALKRALDELPPGGG-T 166

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568960715 2404 RTGKALtfikEKVLTWESGMRKNVPKVLVVVTDGR---SQDEVKKAAFVIQQSGFSVFVVGVAD--VDYNELANIA 2474
Cdd:COG1240   167 PLGDAL----ALALELLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTeaVDEGLLREIA 238
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 26-103 2.65e-09

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 56.08  E-value: 2.65e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715     26 DPPSDLNFKIIDENTVHMSWERPVDP-----IVGYRItVDPTTDGPTKEFTLAASTTETLLSDLIPETQYVVTITSYNEV 100
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDgitgyIVGYRV-EYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 568960715    101 EES 103
Cdd:smart00060   81 GEG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 815-892 3.45e-09

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 56.08  E-value: 3.45e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715    815 GNPRDLRVSDATTSTLKLSWSRAPGKVKQ-YLVTYTPA---AGGETQEVTVRGDTTTTMLRKLKEGTQYDLSVTALYASG 890
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEyreEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 568960715    891 AG 892
Cdd:smart00060   82 EG 83
fn3 pfam00041
Fibronectin type III domain;
906-986 7.17e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.11  E-value: 7.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   906 GSPQNLVTKDITDTSIGAYWTSAP---GMVRGYRVSWKSLYDDIEAGETTLPGDAIHTMIENLQPETKYKISVFATYSSG 982
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 568960715   983 EGEP 986
Cdd:pfam00041   81 EGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1849-1924 7.41e-09

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.20  E-value: 7.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1849 VRNLRVYDPSTSSLSVRWDHAE---GNPRQYKLFYAPT-SGGPEELVPIPGNTNYAILRNLQPDTPYTITVVPVYTEGDG 1924
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKgSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGES 83
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 1199-1377 7.42e-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: 58.10  E-value: 7.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1199 DIVLLVDGSWSIGRANFRT-VRSFISRIVEVFEIGPKRVQIALAQYSGDPRT--EWQLNAHRDKKSLLQAVANLP--YK- 1272
Cdd:cd01473     2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRDvvPFSDEERYDKNELLKKINDLKnsYRs 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1273 GGNTLTGMALNFIRQQSFKtQAGMRPRARKIGVLITDG----KSQDDVEAPSKKLKDEGVELFAIGIKNADEVELKMIAt 1348
Cdd:cd01473    82 GGETYIVEALKYGLKNYTK-HGNRRKDAPKVTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLA- 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568960715 1349 dpdDTHAYNV-------ADFESLSKIVDDLTINLCN 1377
Cdd:cd01473   160 ---GCDINNDncpnvikTEWNNLNGISKFLTDKICD 192
VWA_2 pfam13519
von Willebrand factor type A domain;
1200-1307 1.01e-08

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 55.38  E-value: 1.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1200 IVLLVDGSWSI-----GRANFRTVRSFISRIVEVFeigpKRVQIALAQYSGDPRTEWQLNahRDKKSLLQAVANLPYKGG 1274
Cdd:pfam13519    1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSL----PGDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|...
gi 568960715  1275 NTLTGMALNFIRQQSFKtqagMRPRARKIGVLI 1307
Cdd:pfam13519   75 GTNLAAALQLARAALKH----RRKNQPRRIVLI 103
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 906-988 1.12e-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: 54.81  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  906 GSPQNLVTKDITDTSIGAYWTSAP---GMVRGYRVSWKSLYDDIEAGETTLPGDAIHTMIENLQPETKYKISVFATYSSG 982
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGGG 81


                  ....*.
gi 568960715  983 EGEPVT 988
Cdd:cd00063    82 ESPPSE 87
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 336-413 1.41e-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: 54.16  E-value: 1.41e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715    336 PPSNLVVTELSSKYIRLSWDPSPSAVTGYKIL---LTPMAAGSRHHALSVGPQTTTLNVRDLTADTEYQISVFAMKGLTS 412
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVgyrVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 568960715    413 S 413
Cdd:smart00060   83 G 83
fn3 pfam00041
Fibronectin type III domain;
1089-1166 1.69e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.96  E-value: 1.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  1089 SPRNLKTSDPTMSSFRVTWEPAP---GEVKGYKVTFHPTGDDRRLGELVLGPYDNTVVLEELRAGTTYRVNVF---GMFD 1162
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQavnGGGE 81


                   ....
gi 568960715  1163 GGES 1166
Cdd:pfam00041   82 GPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1940-2015 1.80e-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: 1.80e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   1940 RNIQVYNPTPNSLDVRWDPAP-----GPVQQYRIVYSPVAGTrpSESIVVPGNTRTVHLERLIPDTPYSVNIVALYSDGE 2014
Cdd:smart00060    5 SNLRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYREEGSE--WKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 568960715   2015 G 2015
Cdd:smart00060   83 G 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 2028-2106 1.85e-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: 1.85e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   2028 SGPRNIRVFGETTNSLSVAWDHADGPVQQ-YRIIYSPTVGDPIDEYTTV--PGRRNNVILQPLQPDTPYKITVIAIYEDG 2104
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITgYIVGYRVEYREEGSEWKEVnvTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 568960715   2105 DG 2106
Cdd:smart00060   82 EG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1002-1074 2.99e-08

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.39  E-value: 2.99e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568960715   1002 LRVDEETEHTMRVTWKAAP-----GKVVNYRVVYRPQGGGRQMVaKVPPTVTSTVLKRLQPQTTYDITVLPMYKTGEG 1074
Cdd:smart00060    7 LRVTDVTSTSVTLSWEPPPddgitGYIVGYRVEYREEGSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
440-616 4.90e-08

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 55.70  E-value: 4.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  440 DIVFLVDGSYSIGIANFVKVRAFLEVLAKSFEISPN---RVQISLVQYSRDPHTeftLKEFNRVEDIikAINTFPYRGGs 516
Cdd:COG4245     7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYaleTVEVSVITFDGEAKV---LLPLTDLEDF--QPPDLSASGG- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  517 TNTGKAMTYVREKI-----FVPNKGSRSNVPkVMILITDGKSSD-AFRDPAIKLRNSD----VEIFAVGV-KDAVRSELE 585
Cdd:COG4245    81 TPLGAALELLLDLIerrvqKYTAEGKGDWRP-VVFLITDGEPTDsDWEAALQRLKDGEaakkANIFAIGVgPDADTEVLK 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 568960715  586 AIASPpaeTHVFTVEDFDAFQRIsFE-LTQSI 616
Cdd:COG4245   160 QLTDP---VRALDALDGLDFREF-FKwLSASV 187
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 906-984 6.53e-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: 52.23  E-value: 6.53e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715    906 GSPQNLVTKDITDTSIGAYWT-SAPGMVRGYRVSWKSLYDDIEAGETTLPGDAIHT--MIENLQPETKYKISVFATYSSG 982
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEpPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTsyTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 568960715    983 EG 984
Cdd:smart00060   82 EG 83
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1849-1924 8.10e-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: 51.85  E-value: 8.10e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   1849 VRNLRVYDPSTSSLSVRWDHAEGNPR-----QYKLFYAPTSGGPEELVPIPGNTNYaILRNLQPDTPYTITVVPVYTEGD 1923
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGItgyivGYRVEYREEGSEWKEVNVTPSSTSY-TLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 568960715   1924 G 1924
Cdd:smart00060   83 G 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1656-1728 8.33e-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: 52.50  E-value: 8.33e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960715 1656 PAPTNLQFTEVTPESFRGTWD---HGASDVSLYRITWAPVGNPDKME-TILNGDENTLVFENLNPNTPYEVSITAIY 1728
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTppeDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1197-1402 9.48e-08

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 57.67  E-value: 9.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1197 EADIVLLVDGSWSIGRANFRT-VRSFISRIVEVFEIGPKRVQIALAQYSGDPRTEWQL--NAHRDKKSLLQAV-----AN 1268
Cdd:PTZ00441   42 EVDLYLLVDGSGSIGYHNWIThVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLgsGASKDKEQALIIVkslrkTY 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1269 LPYkgGNTLTGMALNFIRQQsFKTQAGmRPRARKIGVLITDG--KSQDDVEAPSKKLKDEGVELFAIGIKNADEVELK-- 1344
Cdd:PTZ00441  122 LPY--GKTNMTDALLEVRKH-LNDRVN-RENAIQLVILMTDGipNSKYRALEESRKLKDRNVKLAVIGIGQGINHQFNrl 197

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568960715 1345 MIATDPDDTHA--YNVADFESLSKIVDDLTINLCNSVK-----GPGDLEAPTNLVISERTHRSFR 1402
Cdd:PTZ00441  198 LAGCRPREGKCkfYSDADWEEAKNLIKPFIAKVCTEVErtascGPWDEWTPCSVTCGKGTHSRSR 262
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2766-2898 2.08e-07

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 56.45  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2766 RGERGI---NGAVGPPGPRGDTGPPGPQGPPGPQGPNGLsiPGEQGRQGMKGDAGEPGLPGRTGTPGLPGPPGPMGPPGD 2842
Cdd:NF038329  119 KGEPGPagpAGPAGEQGPRGDRGETGPAGPAGPPGPQGE--RGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568960715 2843 RGFTGKDGAMGPRGPPGPPGSPGSPGVTGPSGKPGKP--GDHGRPGQSGLKGEKGDRG 2898
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDG 254
fn3 pfam00041
Fibronectin type III domain;
1002-1075 2.39e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.88  E-value: 2.39e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568960715  1002 LRVDEETEHTMRVTWKAAP---GKVVNYRVVYRPQGGGRQMVAK-VPPTVTSTVLKRLQPQTTYDITVLPMYKTGEGK 1075
Cdd:pfam00041    6 LTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEItVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGP 83
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 1195-1347 2.46e-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: 55.07  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1195 RAEADIVLLVDGSWSIGRANFRTVRSFISRIVEVFEigpKRVQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGG 1274
Cdd:COG2425   116 LLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALR---PNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFAGGG 192

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568960715 1275 NTLTG---MALNFIRQQSFktqagmrpRARKIgVLITDGKSQDDVEAPSKKL--KDEGVELFAIGIKNADEVEL-KMIA 1347
Cdd:COG2425   193 TDIAPalrAALELLEEPDY--------RNADI-VLITDGEAGVSPEELLREVraKESGVRLFTVAIGDAGNPGLlEALA 262
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2766-2898 4.84e-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: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2766 RGERGINGAVGPPGPRGDTGPPGPQGPPGPQGPNGLSIPGEQGRQGMKGDAGEPGLPGRTGTpglpgppgpmgppgdrgf 2845
Cdd:NF038329  194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGP------------------ 255

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568960715 2846 TGKDGAMGPRGPPGPPGSPGSPGVTGPSGKPGK---------PGDHGRPGQSGLKGEKGDRG 2898
Cdd:NF038329  256 AGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKdgqngkdglPGKDGKDGQNGKDGLPGKDG 317
VWA_2 pfam13519
von Willebrand factor type A domain;
2326-2434 7.26e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 49.98  E-value: 7.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  2326 IVFLTDASWSIGDD-----NFNKVVKFIFNTVGAFDEVnpagiQVSFVQYSDEVKSEFKLNTynDKALALGALQNIRYRG 2400
Cdd:pfam13519    1 LVFVLDTSGSMRNGdygptRLEAAKDAVLALLKSLPGD-----RVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKG 73

                           90       100       110
                   ....*....|....*....|....*....|....
gi 568960715  2401 GNTRTGKALtfikEKVLTWESGMRKNVPKVLVVV 2434
Cdd:pfam13519   74 GGTNLAAAL----QLARAALKHRRKNQPRRIVLI 103
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1089-1166 7.98e-07

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 49.15  E-value: 7.98e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   1089 SPRNLKTSDPTMSSFRVTWE-PAPGEVKGYKVTFHPTGDDRRLGELVL--GPYDNTVVLEELRAGTTYRVNVFGMFDGGE 1165
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEpPPDDGITGYIVGYRVEYREEGSEWKEVnvTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 568960715   1166 S 1166
Cdd:smart00060   83 G 83
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2767-2898 1.23e-06

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: 53.76  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2767 GERGINGAVGPPGPRGDTGPPGPQGPPGPQGPNGLSipGEQGRQGMKGDAGEPGLPGRTGTPGLPGPPGPMGPPGDRGFT 2846
Cdd:NF038329  144 GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD--GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA 221

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2847 GKDGAMGPRGPPGPPGSPGSPGV--------TGPSGKPGKPGDHGRPGQSGLKGEKGDRG 2898
Cdd:NF038329  222 GEDGPAGPAGDGQQGPDGDPGPTgedgpqgpDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1656-1728 1.49e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 48.38  E-value: 1.49e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568960715   1656 PAPTNLQFTEVTPESFRGTWDHGASDVSL-----YRITWAPVgNPDKMETILNGDENTLVFENLNPNTPYEVSITAIY 1728
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITgyivgYRVEYREE-GSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2767-2898 2.33e-06

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: 52.99  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2767 GERGINGAVGPPGPRGDtgppgpqgppgpqgpnglsiPGEQGRQGMKGDAGEPGLPGRTGTPGLPGPPGPMGPPGDRGFT 2846
Cdd:NF038329  117 GEKGEPGPAGPAGPAGE--------------------QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568960715 2847 GKDGAMGPRGPPGPPGSPGSPGVTGPSGKPGKPGDHGRPGQSGLKGEKGDRG 2898
Cdd:NF038329  177 GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG 228
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
650-941 4.50e-06

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 52.64  E-value: 4.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  650 AEWSPPGdNVFSYHVTYKDANGDdeVTVVEPASSTSVVLNNLRPETlYLVNVTAEYEDGF-SVPITGEETTAEVK----G 724
Cdd:COG4733   556 VSWDAPA-GAVAYEVEWRRDDGN--WVSVPRTSGTSFEVPGIYAGD-YEVRVRAINALGVsSAWAASSETTVTGKtappP 631

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  725 VPRNLKVTDeTTDSFKLTWSQAPG-RVLRYRIRYRPVSGGESKEV-STPANQRRKTLENLTPDTKYEISVIAEYSSGPGS 802
Cdd:COG4733   632 APTGLTATG-GLGGITLSWSFPVDaDTLRTEIRYSTTGDWASATVaQALYPGNTYTLAGLKAGQTYYYRARAVDRSGNVS 710

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  803 PLTGNA-ATEEVRGNPRDLRVSDATTSTLK-LSWSRAPGKV------------KQYLVTYTPAAGGETQEVTVRGDTTTT 868
Cdd:COG4733   711 AWWVSGqASADAAGILDAITGQILETELGQeLDAIIQNATVaevvaatvtdvtAQIDTAVLFAGVATAAAIGAEARVAAT 790

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568960715  869 MLRKLKEGTQYDLSVTALYASGAGEALSGKGSTLEERGSPQNLVTKDITDTSIGAYWTSAPGMVRGYRVSWKS 941
Cdd:COG4733   791 VAESATAAAATGTAADAAGDASGGVTAGTSGTTGAGDTAASTTRVAAAVVLAGVVVYGDAIIESGNTGDIVAT 863
fn3 pfam00041
Fibronectin type III domain;
2209-2284 1.30e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.87  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  2209 VTDLKTYQVGWDTFCVKWSP----HRAATSYRLKLSPADGTRG-QEITVRGSETSHCFTGLSPEAEYGVTVFVQTPNLEG 2283
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPppdgNGPITGYEVEYRPKNSGEPwNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEG 82


                   .
gi 568960715  2284 P 2284
Cdd:pfam00041   83 P 83
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 138-289 5.95e-05

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: 46.65  E-value: 5.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  138 WTDLVFLVDGSWSVGRNNFKYILDFIVALVSAFDIG------EEKTRVGVVQYSSDTRTEFNLNQYYRREDL----LAAV 207
Cdd:cd01477    19 WLDIVFVVDNSKGMTQGGLWQVRATISSLFGSSSQIgtdyddPRSTRVGLVTYNSNATVVADLNDLQSFDDLysqiQGSL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  208 KKIPYKGGNTM-TG-DAIDYLVKNTFtesAGSRAGFPKVAIIIT----DGKSQDEVEIpARELRNIGVEV----FSLGIK 277
Cdd:cd01477    99 TDVSSTNASYLdTGlQAAEQMLAAGK---RTSRENYKKVVIVFAsdynDEGSNDPRPI-AARLKSTGIAIitvaFTQDES 174

                         170
                  ....*....|..
gi 568960715  278 AADAKELKQIAS 289
Cdd:cd01477   175 SNLLDKLGKIAS 186
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2767-2893 1.22e-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: 42.10  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  2767 GERGINGAVGPPGPRGDtgppgpqgppgpqgpnglsiPGEQGRQGMKGDAGEPGLPGrtgtpglpgppgpmgppgdrgft 2846
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGP--------------------PGPPGPPGPPGPPGEPGPPG----------------------- 37

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 568960715  2847 gkdgamgprgppgPpgspgspgvtgpsgkPGKPGDHGRPGQSGLKGE 2893
Cdd:pfam01391   38 -------------P---------------PGPPGPPGPPGAPGAPGP 56
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 2325-2474 1.28e-04

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: 45.77  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2325 DIVFLTDASWSIGDDNFNKVV-----KFIFNTVGAFDEVNpAGI------QVSFVQYSDEvksefklNTYNDKAL--ALG 2391
Cdd:cd01473     2 DLTLILDESASIGYSNWRKDVipfteKIINNLNISKDKVH-VGIllfaekNRDVVPFSDE-------ERYDKNELlkKIN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2392 ALQNIRYRGGNTRTGKALTFIKEKVlTWESGMRKNVPKVLVVVTDGRSQDEVKKAAFVI----QQSGFSVFVVGVADVDY 2467
Cdd:cd01473    74 DLKNSYRSGGETYIVEALKYGLKNY-TKHGNRRKDAPKVTMLFTDGNDTSASKKELQDIsllyKEENVKLLVVGVGAASE 152


                  ....*..
gi 568960715 2468 NELANIA 2474
Cdd:cd01473   153 NKLKLLA 159
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2871-2899 1.46e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 1.46e-04
                           10        20
                   ....*....|....*....|....*....
gi 568960715  2871 GPSGKPGKPGDHGRPGQSGLKGEKGDRGD 2899
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGE 32
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 140-288 2.57e-04

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 45.86  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  140 DLVFLVDGSWSVGRNNFKYILDFIVALVSAFDigeEKTRVGVVQYSSDTRTEFNLNQYYRREDLLAAVKKIpYKGGNTMT 219
Cdd:COG2304    93 NLVFVIDVSGSMSGDKLELAKEAAKLLVDQLR---PGDRVSIVTFAGDARVLLPPTPATDRAKILAAIDRL-QAGGGTAL 168

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568960715  220 GDAIDyLVKNTFTESAgsRAGFPKVAIIITDGKSQDEVEIP------ARELRNIGVEVFSLGI-KAADAKELKQIA 288
Cdd:COG2304   169 GAGLE-LAYELARKHF--IPGRVNRVILLTDGDANVGITDPeellklAEEAREEGITLTTLGVgSDYNEDLLERLA 241
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 2208-2293 3.68e-04

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: 42.10  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2208 NVTDLKTYQVGWDTFCVKWSP----HRAATSYRLKLSPADGTRGQEITVRGSETSHC-FTGLSPEAEYGVTVFVQTPNLE 2282
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPpeddGGPITGYVVEYREKGSGDWKEVEVTPGSETSYtLTGLKPGTEYEFRVRAVNGGGE 82

                          90
                  ....*....|.
gi 568960715 2283 GPGVPIKEQTT 2293
Cdd:cd00063    83 SPPSESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
783-1184 4.68e-04

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 45.76  E-value: 4.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  783 TPDTKYEISVIAEYSSGPGSPLTGNAATEEVRGNPRDLRVSDATTSTLKLSWSrapgkvkqYLVTYTPAAGGETQEVTVR 862
Cdd:COG3401    32 SGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAV--------AAAPPTATGLTTLTGSGSV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  863 GDTTTTMLRKLKEGTQYDLSVTALYASGAGEALSGKGSTLEERGSPQNLVTKDITDTSIGAYWTSAPGMVRGYrvswksl 942
Cdd:COG3401   104 GGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSA------- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  943 YDDIEAGETTLPGDAIHTMIENLQPETKYKISVFATYSSGEGEP---VTGDATTELSQDSKILRVDEETEHTMRVTWKAA 1019
Cdd:COG3401   177 TAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPsneVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPV 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1020 PGK-VVNYRVVYRPQGGGR-QMVAKVppTVTSTVLKRLQPQTTYDITVLPMYKTG-EGKLRQGSGTTASRFK--SPRNLK 1094
Cdd:COG3401   257 TESdATGYRVYRSNSGDGPfTKVATV--TTTSYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTPpaAPSGLT 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1095 TSDPTMSSFRVTWEPAPGE-VKGYKV--TFHPTGDDRRLGELVLGpydNTVVLEELRAGTTYRVNVFGMFDGGESLPLVG 1171
Cdd:COG3401   335 ATAVGSSSITLSWTASSDAdVTGYNVyrSTSGGGTYTKIAETVTT---TSYTDTGLTPGTTYYYKVTAVDAAGNESAPSE 411

                         410
                  ....*....|...
gi 568960715 1172 QEMTTLSDTTVTP 1184
Cdd:COG3401   412 EVSATTASAASGE 424
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
1448-1810 8.65e-04

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 45.32  E-value: 8.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1448 TDYVVNVYSVVEDEYSEPLKGTekTLPVPVVSLNIYDV-----GPTTMHVQWQPVGGATGYTVSYqptRSPEGTKPKEMR 1522
Cdd:COG4733   509 VQHAPEKYAAIDAGAFDDVPPQ--WPPVNVTTSESLSVvaqgtAVTTLTVSWDAPAGAVAYEVEW---RRDDGNWVSVPR 583

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1523 VGPTVNDVQltgLLPNTEYEVTVQAV-LYDLTSEPAKAREVTL-----PLPRPQDVKLRDVTHSTmNVVWEPVLG-KVRK 1595
Cdd:COG4733   584 TSGTSFEVP---GIYAGDYEVRVRAInALGVSSAWAASSETTVtgktaPPPAPTGLTATGGLGGI-TLSWSFPVDaDTLR 659

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1596 YIVRY-KTPDEEFKEVEVDRSRAST-ILKDLSSQTQYTVSVSAVYDEGTSPPATAYDTTRRVPAPTNLQFTEVTPESFRG 1673
Cdd:COG4733   660 TEIRYsTTGDWASATVAQALYPGNTyTLAGLKAGQTYYYRARAVDRSGNVSAWWVSGQASADAAGILDAITGQILETELG 739

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1674 twdhGASDVSLYRITWAPVGNPDKMETILNGDENTLVFENLNPNTPYEVSITAIYPDESESEDLSGTE---------RTL 1744
Cdd:COG4733   740 ----QELDAIIQNATVAEVVAATVTDVTAQIDTAVLFAGVATAAAIGAEARVAATVAESATAAAATGTaadaagdasGGV 815

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568960715 1745 RLIPLTTQAPKSGPRNLQVYNATSNSLTVKwdpASGRVQKYRITYQPSTGEGNEQTITVGGRQNSV 1810
Cdd:COG4733   816 TAGTSGTTGAGDTAASTTRVAAAVVLAGVV---VYGDAIIESGNTGDIVATGDIASAAAGAVATTV 878
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
2028-2274 9.98e-04

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 44.61  E-value: 9.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2028 SGPRNIRVFGETTNSLSVAWDHADGPVQQYRIIYSPTVGDPIDEYTTVPGRRNNVILQPLQPDTPYKITVIAIYEDGDG- 2106
Cdd:COG3401   140 TYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESa 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2107 --GHLTGNGRTVGLLPPQNIHIFDEWYTRFRVSWDPSPSP-VLGYKIVYKPVGSNEPMEafVGEV--TSYTLHNLNPSTT 2181
Cdd:COG3401   220 psNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESdATGYRVYRSNSGDGPFTK--VATVttTSYTDTGLTNGTT 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 2182 YDVSVYAQYD----SGLSVPLTDQGTTLYLNV-TDLKTYQVGWDTFCVKW--SPHRAATSYRLKLSPADGTRGQEITVRG 2254
Cdd:COG3401   298 YYYRVTAVDAagneSAPSNVVSVTTDLTPPAApSGLTATAVGSSSITLSWtaSSDADVTGYNVYRSTSGGGTYTKIAETV 377

                         250       260
                  ....*....|....*....|
gi 568960715 2255 SETSHCFTGLSPEAEYGVTV 2274
Cdd:COG3401   378 TTTSYTDTGLTPGTTYYYKV 397
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 1198-1356 1.04e-03

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


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 42.65  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1198 ADIVLLVDGSWSIGRANFRTVRSFISRIVEvfEIGPKRvQIALAQYSGDPRTEWQLNAHRDKKSLLQAVANLPYKGGNTL 1277
Cdd:cd01465     1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVD--QLRPDD-RLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTAGGSTAG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1278 -TGMALNFirQQSfktQAGMRPRARKIGVLITDGK------SQDDVEAPSKKLKDEGVELFAIGI-KNADEVELKMIATD 1349
Cdd:cd01465    78 gAGIQLGY--QEA---QKHFVPGGVNRILLATDGDfnvgetDPDELARLVAQKRESGITLSTLGFgDNYNEDLMEAIADA 152


                  ....*..
gi 568960715 1350 PDDTHAY 1356
Cdd:cd01465   153 GNGNTAY 159
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
1199-1372 1.47e-03

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 42.60  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1199 DIVLLVDGSWS-----IGRANfRTVRSFISRIVEVfEIGPKRVQIALAQYSGDPRTewqlnaHRDKKSLLQ-AVANLPYk 1272
Cdd:COG4245     7 PVYLLLDTSGSmsgepIEALN-EGLQALIDELRQD-PYALETVEVSVITFDGEAKV------LLPLTDLEDfQPPDLSA- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1273 GGNTLTG----MALNFIRQQSFKTQAGMRPRARKIGVLITDGKSQD-DVEAPSKKLKD----EGVELFAIGI-KNADEVE 1342
Cdd:COG4245    78 SGGTPLGaaleLLLDLIERRVQKYTAEGKGDWRPVVFLITDGEPTDsDWEAALQRLKDgeaaKKANIFAIGVgPDADTEV 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 568960715 1343 LKMIAtdpDDTHAYNVADFESLSKIVDDLT 1372
Cdd:COG4245   158 LKQLT---DPVRALDALDGLDFREFFKWLS 184
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 243-306 3.06e-03

A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus; A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. This group includes proteins similar to PfpI from P. furiosus. and PH1704 from Pyrococcus horikoshii. These enzymes are ATP-independent intracellular proteases and may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For PH1704, it is believed that this Cys together with a different His in one monomer and Glu (from an adjacent monomer) forms a different catalytic triad from the typical GATase1domain. PfpI is homooligomeric. Protease activity is only found for oligomeric forms of PH1704.


Pssm-ID: 153228 [Multi-domain]  Cd Length: 165  Bit Score: 40.99  E-value: 3.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568960715  243 KVAIIITDGKSQDEVEIPARELRNIGVEVFSLGIKAADA----KELKQIASTPSLNHVfNVANFDAIV 306
Cdd:cd03134     1 KVAILAADGFEDVELTYPLYRLREAGAEVVVAGPEAGGEiqgkHGYDTVTVDLTIADV-DADDYDALV 67
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 2208-2283 3.21e-03

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: 39.13  E-value: 3.21e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715   2208 NVTDLKTYQVGWDTFCVKWSP--HRAATSYRLKLSPADGTRG---QEITVRGSETSHCFTGLSPEAEYGVTVFVQTPNLE 2282
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPppDDGITGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGE 82


                    .
gi 568960715   2283 G 2283
Cdd:smart00060   83 G 83
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2760-2823 4.47e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 4.47e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568960715  2760 PGAKGPRGERGINGAVGPPGPRGDtgppgpqgppgpqgpNGLsiPGEQGRQGMKGDAGEPGLPG 2823
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGPPGE---------------PGP--PGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2870-2898 5.56e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.47  E-value: 5.56e-03
                           10        20
                   ....*....|....*....|....*....
gi 568960715  2870 TGPSGKPGKPGDHGRPGQSGLKGEKGDRG 2898
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPG 37
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 440-590 6.52e-03

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: 40.48  E-value: 6.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  440 DIVFLVDGSYSIGIANFVKVRAFLEVLAKSFEI------SPNRVQISLVQYSRDPHTEFTLKEFNRVEDIIKAINTFPYR 513
Cdd:cd01477    21 DIVFVVDNSKGMTQGGLWQVRATISSLFGSSSQigtdydDPRSTRVGLVTYNSNATVVADLNDLQSFDDLYSQIQGSLTD 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  514 GGSTNTGKAMTYVREKIFVPNKG---SRSNVPKVMILIT----DGKSSDAfRDPAIKLRNSDVEIFAV-----GVKDAVr 581
Cdd:cd01477   101 VSSTNASYLDTGLQAAEQMLAAGkrtSRENYKKVVIVFAsdynDEGSNDP-RPIAARLKSTGIAIITVaftqdESSNLL- 178


                  ....*....
gi 568960715  582 SELEAIASP 590
Cdd:cd01477   179 DKLGKIASP 187
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
336-422 6.75e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 41.91  E-value: 6.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715  336 PPSNLVVTELSSKYIRLSWDPSPSA-VTGYKILLTPMAAGSrHHALSVGPQTTTLNVRDLTADTEYQISVFAM-KGLTSS 413
Cdd:COG3401   329 APSGLTATAVGSSSITLSWTASSDAdVTGYNVYRSTSGGGT-YTKIAETVTTTSYTDTGLTPGTTYYYKVTAVdAAGNES 407


                  ....*....
gi 568960715  414 EPTSVMEKT 422
Cdd:COG3401   408 APSEEVSAT 416
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 1199-1369 7.01e-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: 40.35  E-value: 7.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1199 DIVLLVDGSWSIGRANFRTVRSFISRIVE---VFEIGPkRVQIALaqYSGDP------RTEWQLNAHRDKKSLlqavANL 1269
Cdd:cd01470     2 NIYIALDASDSIGEEDFDEAKNAIKTLIEkisSYEVSP-RYEIIS--YASDPkeivsiRDFNSNDADDVIKRL----EDF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960715 1270 PYK----GGNTLTGMALNFI--RQQSFKTQAGMR-PRARKIGVLITDGKS-------------QDDV--EAPSKKLKDEG 1327
Cdd:cd01470    75 NYDdhgdKTGTNTAAALKKVyeRMALEKVRNKEAfNETRHVIILFTDGKSnmggsplptvdkiKNLVykNNKSDNPREDY 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568960715 1328 VELFAIGI-KNADEVELKMIATD-PDDTHAYNVADFESLSKIVD 1369
Cdd:cd01470   155 LDVYVFGVgDDVNKEELNDLASKkDNERHFFKLKDYEDLQEVFD 198
 
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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