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Conserved domains on  [gi|55743106|ref|NP_476508|]
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collagen alpha-3(VI) chain isoform 5 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1229-1393 7.26e-89

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: 286.91  E-value: 7.26e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1229 ADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPL 1308
Cdd:cd01481    1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1309 NTGKALEFVARNLFVKSAGSRIEDGVPQHLVLVLGGKSQDDVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDPRLVF 1388
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106 1389 TVREF 1393
Cdd:cd01481  161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 238-402 1.54e-85

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: 277.28  E-value: 1.54e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  238 RDIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSAL 317
Cdd:cd01481    1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  318 YTGSALDFVRNNLFTSSAGYRAAEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSSLVF 397
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106  398 IPAEF 402
Cdd:cd01481  161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 432-596 2.97e-84

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: 273.43  E-value: 2.97e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  432 RDIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGL 511
Cdd:cd01481    1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  512 NTGSALSYVYANHFTEAGGSRIREHVPQLLLLLTAGQSEDSYLQAANALTRAGILTFCVGASQANKAELEQIAFNPSLVY 591
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106  592 LMDDF 596
Cdd:cd01481  161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1026-1188 7.61e-83

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: 269.58  E-value: 7.61e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1026 RDVVFLIDGSQSAGP-EFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQI 1104
Cdd:cd01481    1 KDIVFLIDGSDNVGSgNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1105 NVGNALEYVSRNIFKRPLGSRIEEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTI-ARNADQEELVKISLSPEYVF 1183
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIgARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106 1184 SVSTF 1188
Cdd:cd01481  161 QVSDF 165
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 822-985 2.73e-70

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 actual alignment was detected with superfamily member cd01481:

Pssm-ID: 469594  Cd Length: 165  Bit Score: 233.37  E-value: 2.73e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  822 KDVVFLLDGSEGVRS-GFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTP 900
Cdd:cd01481    1 KDIVFLIDGSDNVGSgNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  901 NTGAALEFVLRNILVSSAGSRITEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPDFAV 980
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106  981 AIPTF 985
Cdd:cd01481  161 QVSDF 165
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 35-199 2.14e-66

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 actual alignment was detected with superfamily member cd01481:

Pssm-ID: 469594  Cd Length: 165  Bit Score: 222.58  E-value: 2.14e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   35 ADIIFLIDGSNNTGSVNFAVILDFLVNLLEKLPIGTQQIRVGVVQFSDEPRTMFSLDTYSTKAQVLGAVKALGFAGGELA 114
Cdd:cd01481    1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  115 NIGLALDFVVENHFTRAGGSRVEEGVPQVLVLISAGPSSDEIRYGVVALKQASVFSFGLGAQAASRAELQHIATDDNLVF 194
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106  195 TVPEF 199
Cdd:cd01481  161 QVSDF 165
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 630-793 4.33e-60

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 actual alignment was detected with superfamily member cd01481:

Pssm-ID: 469594  Cd Length: 165  Bit Score: 204.48  E-value: 4.33e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  630 RDILFLFDGSANL-VGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKAL 708
Cdd:cd01481    1 KDIVFLIDGSDNVgSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  709 NLGYALDYAQRYIFVKSAGSRIEDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPAFIL 788
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106  789 AAESL 793
Cdd:cd01481  161 QVSDF 165
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1829-2165 1.24e-46

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: 175.48  E-value: 1.24e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1829 KCSGQRGDRGPIGSIGPKGIPGEDGYRGYPGDeggpgergppgvngtQGFQGCPGQRGVKGSRGFPGEKGEVGEIGLDGL 1908
Cdd:NF038329  114 KGDGEKGEPGPAGPAGPAGEQGPRGDRGETGP---------------AGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1909 DGEDGDKGLPgssGEKGNPGRRGDKGPRGEKGERGdvgirgdpgnpgqdsqERGPKGETGDLGPMGVPGrdgvPGGPGET 1988
Cdd:NF038329  179 DGEAGAKGPA---GEKGPQGPRGETGPAGEQGPAG----------------PAGPDGEAGPAGEDGPAG----PAGDGQQ 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1989 GKnggfgrrgppgakgnKGGPGQPGFEGEQGTRgaqgpagpagppgliGEQGisgprgsggaagapgergRTGPLGRKGE 2068
Cdd:NF038329  236 GP---------------DGDPGPTGEDGPQGPD---------------GPAG------------------KDGPRGDRGE 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  2069 PGEPGPKGGIGNRGPRGETGDDGRDG-VGSEGRRGKKGERGFPGYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGP----- 2142
Cdd:NF038329  268 AGPDGPDGKDGERGPVGPAGKDGQNGkDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPktpev 347

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 55743106  2143 -------------PGIVGQKGDPGyPGPAGPKgNRG 2165
Cdd:NF038329  348 pqkpdtaphtpktPQIPGQSKDVT-PAPQNPS-NRG 381
VWA pfam00092
von Willebrand factor type A domain;
1433-1605 4.99e-45

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 161.67  E-value: 4.99e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1433 DIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRHAN 1512
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1513 TKVGLEHLRVNHFVPEAGSRLDqrVPQIAFVITGGKSVE-DAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIASNSA--T 1589
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPG--APKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|....*.
gi 55743106   1590 AFRVGNVQELSELSEQ 1605
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
Kunitz_collagen_alpha3_VI cd22629
Kunitz-type domain from the alpha3 chain of human type VI collagen, and similar proteins; This ...
 2904-2956 2.29e-38

Kunitz-type domain from the alpha3 chain of human type VI collagen, and similar proteins; This model includes the Kunitz-type domain from the alpha3 chain of type VI collagen (collagen alpha 3(VI) chain), encoded by COL6A3 gene. Collagen VI is a widely expressed member of the triple helix-containing protein superfamily of collagens and forms beaded microfibrils that anchor large interstitial structures. Immediately after fibril formation, the Kunitz domain can be cleaved off. Mutations in the alpha1, alpha2, and alpha3 chains of collagen VI cause myopathies ranging from the severe Ullrich congenital muscular dystrophy to the milder Bethlem myopathy, including intermediate forms. Early onset isolated dystonia, a neurological disease, has been shown to be caused by mutations in the alpha3 chain. Findings also indicated potential associations between COL6A3 polymorphisms and lung cancer risk. This domain is similar to that of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


:

Pssm-ID: 438672  Cd Length: 53  Bit Score: 137.89  E-value: 2.29e-38
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2904 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22629    1 DICKLPKDEGTCRDFVLKWYYDPETKSCARFWYGGCGGNENRFDSQEECEKVC 53
VWA pfam00092
von Willebrand factor type A domain;
2413-2600 1.43e-31

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 123.15  E-value: 1.43e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   2413 DMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDpkasqhFARVAVVQHApsesvDNasmppVKVEFSLTDYGSKEKL 2492
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPD------GTRVGLVQYS-----SD-----VRTEFPLNDYSSKEEL 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   2493 VDFLSRGMTQLQGTRALGSAIEYTIENVFESAPNPRDL--KIVVLMLTGEVPEQQLEEaqrVILQAKCKGYFFVVLGIGr 2570
Cdd:pfam00092   65 LSAVDNLRYLGGGTTNTGKALKYALENLFSSAAGARPGapKVVVLLTDGRSQDGDPEE---VARELKSAGVTVFAVGVG- 140

                          170       180       190
                   ....*....|....*....|....*....|
gi 55743106   2571 KVNIKEVYTFASEPNDVFFKLVDKSTELNE 2600
Cdd:pfam00092  141 NADDEELRKIASEPGEGHVFTVSDFEALED 170
VWA pfam00092
von Willebrand factor type A domain;
2196-2374 2.77e-22

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 96.19  E-value: 2.77e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   2196 ELAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIaesnCPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQVaLT 2275
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDI----GPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRY-LG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   2276 SKQQSLETAMSFVARNTFKRVRNG-FLMRKVAVFFSNTPTrASPQLREAVLKLSDAGITPLFL-TRQEDRQLINALQiNN 2353
Cdd:pfam00092   76 GGTTNTGKALKYALENLFSSAAGArPGAPKVVVLLTDGRS-QDGDPEEVARELKSAGVTVFAVgVGNADDEELRKIA-SE 153

                          170       180
                   ....*....|....*....|.
gi 55743106   2354 TAVGHALVLPAGRDLTDFLEN 2374
Cdd:pfam00092  154 PGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1632-1788 4.02e-09

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: 58.23  E-value: 4.02e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    1632 DVILGFDGSRDqnvfVAQKGFESKVDAILNRISQMHRvscsggRSPTVRVSVVAnTPSGPVEAFDFDEYQ--PEMLEKFR 1709
Cdd:smart00327    1 DVVFLLDGSGS----MGGNRFELAKEFVLKLVEQLDI------GPDGDRVGLVT-FSDDARVLFPLNDSRskDALLEALA 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    1710 NMRsqhpYVLTEDT---------LKVYLNKFRQSSPDSVKVVIHFTDGADGDLA-DLHRASENLRQEGVRaLILVGLERV 1779
Cdd:smart00327   70 SLS----YKLGGGTnlgaalqyaLENLFSKSAGSRRGAPKVVILITDGESNDGPkDLLKAAKELKRSGVK-VFVVGVGND 144


                    ....*....
gi 55743106    1780 VNLERLMHL 1788
Cdd:smart00327  145 VDEEELKKL 153
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 2787-2855 1.53e-03

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: 40.17  E-value: 1.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2787 REVQVFEITENSAKLHWERAEPPGP----YFYDLTVTSAHDQSLVLKQNLTVTDRVIGGLLAGQTYHVAVVCY 2855
Cdd:cd00063    5 TNLRVTDVTSTSVTLSWTPPEDDGGpitgYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
 
Name Accession Description Interval E-value
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1229-1393 7.26e-89

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: 286.91  E-value: 7.26e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1229 ADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPL 1308
Cdd:cd01481    1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1309 NTGKALEFVARNLFVKSAGSRIEDGVPQHLVLVLGGKSQDDVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDPRLVF 1388
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106 1389 TVREF 1393
Cdd:cd01481  161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 238-402 1.54e-85

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: 277.28  E-value: 1.54e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  238 RDIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSAL 317
Cdd:cd01481    1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  318 YTGSALDFVRNNLFTSSAGYRAAEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSSLVF 397
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106  398 IPAEF 402
Cdd:cd01481  161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 432-596 2.97e-84

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: 273.43  E-value: 2.97e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  432 RDIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGL 511
Cdd:cd01481    1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  512 NTGSALSYVYANHFTEAGGSRIREHVPQLLLLLTAGQSEDSYLQAANALTRAGILTFCVGASQANKAELEQIAFNPSLVY 591
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106  592 LMDDF 596
Cdd:cd01481  161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1026-1188 7.61e-83

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: 269.58  E-value: 7.61e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1026 RDVVFLIDGSQSAGP-EFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQI 1104
Cdd:cd01481    1 KDIVFLIDGSDNVGSgNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1105 NVGNALEYVSRNIFKRPLGSRIEEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTI-ARNADQEELVKISLSPEYVF 1183
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIgARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106 1184 SVSTF 1188
Cdd:cd01481  161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 822-985 2.73e-70

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: 233.37  E-value: 2.73e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  822 KDVVFLLDGSEGVRS-GFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTP 900
Cdd:cd01481    1 KDIVFLIDGSDNVGSgNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  901 NTGAALEFVLRNILVSSAGSRITEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPDFAV 980
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106  981 AIPTF 985
Cdd:cd01481  161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 35-199 2.14e-66

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: 222.58  E-value: 2.14e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   35 ADIIFLIDGSNNTGSVNFAVILDFLVNLLEKLPIGTQQIRVGVVQFSDEPRTMFSLDTYSTKAQVLGAVKALGFAGGELA 114
Cdd:cd01481    1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  115 NIGLALDFVVENHFTRAGGSRVEEGVPQVLVLISAGPSSDEIRYGVVALKQASVFSFGLGAQAASRAELQHIATDDNLVF 194
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106  195 TVPEF 199
Cdd:cd01481  161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 630-793 4.33e-60

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: 204.48  E-value: 4.33e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  630 RDILFLFDGSANL-VGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKAL 708
Cdd:cd01481    1 KDIVFLIDGSDNVgSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  709 NLGYALDYAQRYIFVKSAGSRIEDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPAFIL 788
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106  789 AAESL 793
Cdd:cd01481  161 QVSDF 165
VWA pfam00092
von Willebrand factor type A domain;
433-605 5.26e-55

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 190.18  E-value: 5.26e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    433 DIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGLN 512
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    513 TGSALSYVYANHFTEAGGSriREHVPQLLLLLTAGQSED-SYLQAANALTRAGILTFCVGASQANKAELEQIAFNPS--L 589
Cdd:pfam00092   81 TGKALKYALENLFSSAAGA--RPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|....*.
gi 55743106    590 VYLMDDFSSLPALPQQ 605
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
1230-1402 3.06e-54

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 187.87  E-value: 3.06e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1230 DIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPLN 1309
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1310 TGKALEFVARNLFVKSAGSRIedGVPQHLVLVLGGKSQD-DVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDP--RL 1386
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARP--GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPgeGH 158

                          170
                   ....*....|....*.
gi 55743106   1387 VFTVREFRELPNIEER 1402
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
1027-1197 1.89e-51

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 179.78  E-value: 1.89e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1027 DVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQIN 1105
Cdd:pfam00092    1 DIVFLLDGSGSIGGDnFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1106 VGNALEYVSRNIFKRPLGSRieEGVPQFLVLISSGKSDD-EVDDPAVELKQFGVAPFTIA-RNADQEELVKISLSP--EY 1181
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGvGNADDEELRKIASEPgeGH 158

                          170
                   ....*....|....*.
gi 55743106   1182 VFSVSTFRELPSLEQK 1197
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
239-406 8.98e-51

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 177.85  E-value: 8.98e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    239 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSALY 318
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    319 TGSALDFVRNNLFTSSAGYRaaEGIPKLLVLITGGKSLD-EISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSS--L 395
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|.
gi 55743106    396 VFIPAEFRAAP 406
Cdd:pfam00092  159 VFTVSDFEALE 169
VWA pfam00092
von Willebrand factor type A domain;
823-993 9.89e-51

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 177.85  E-value: 9.89e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    823 DVVFLLDGSEGVR-SGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPN 901
Cdd:pfam00092    1 DIVFLLDGSGSIGgDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    902 TGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGD-DVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPD--F 978
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|....*
gi 55743106    979 AVAIPTFRQLGTVQQ 993
Cdd:pfam00092  159 VFTVSDFEALEDLQD 173
VWA pfam00092
von Willebrand factor type A domain;
36-208 9.00e-48

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 169.38  E-value: 9.00e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     36 DIIFLIDGSNNTGSVNFAVILDFLVNLLEKLPIGTQQIRVGVVQFSDEPRTMFSLDTYSTKAQVLGAVKALGFAGGELAN 115
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    116 IGLALDFVVENHFTRAGGSRveEGVPQVLVLISAGPSSD-EIRYGVVALKQASVFSFGLGAQAASRAELQHIATDDN--L 192
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|....*.
gi 55743106    193 VFTVPEFRSFGDLQEK 208
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1829-2165 1.24e-46

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: 175.48  E-value: 1.24e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1829 KCSGQRGDRGPIGSIGPKGIPGEDGYRGYPGDeggpgergppgvngtQGFQGCPGQRGVKGSRGFPGEKGEVGEIGLDGL 1908
Cdd:NF038329  114 KGDGEKGEPGPAGPAGPAGEQGPRGDRGETGP---------------AGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1909 DGEDGDKGLPgssGEKGNPGRRGDKGPRGEKGERGdvgirgdpgnpgqdsqERGPKGETGDLGPMGVPGrdgvPGGPGET 1988
Cdd:NF038329  179 DGEAGAKGPA---GEKGPQGPRGETGPAGEQGPAG----------------PAGPDGEAGPAGEDGPAG----PAGDGQQ 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1989 GKnggfgrrgppgakgnKGGPGQPGFEGEQGTRgaqgpagpagppgliGEQGisgprgsggaagapgergRTGPLGRKGE 2068
Cdd:NF038329  236 GP---------------DGDPGPTGEDGPQGPD---------------GPAG------------------KDGPRGDRGE 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  2069 PGEPGPKGGIGNRGPRGETGDDGRDG-VGSEGRRGKKGERGFPGYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGP----- 2142
Cdd:NF038329  268 AGPDGPDGKDGERGPVGPAGKDGQNGkDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPktpev 347

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 55743106  2143 -------------PGIVGQKGDPGyPGPAGPKgNRG 2165
Cdd:NF038329  348 pqkpdtaphtpktPQIPGQSKDVT-PAPQNPS-NRG 381
VWA pfam00092
von Willebrand factor type A domain;
1433-1605 4.99e-45

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 161.67  E-value: 4.99e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1433 DIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRHAN 1512
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1513 TKVGLEHLRVNHFVPEAGSRLDqrVPQIAFVITGGKSVE-DAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIASNSA--T 1589
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPG--APKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|....*.
gi 55743106   1590 AFRVGNVQELSELSEQ 1605
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
631-802 1.56e-41

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 151.66  E-value: 1.56e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    631 DILFLFDGSANL-VGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKALN 709
Cdd:pfam00092    1 DIVFLLDGSGSIgGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    710 LGYALDYAQRYIFVKSAGSRIedGVLQFLVLLVAGRSSD-RVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPA--F 786
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARP--GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|....*.
gi 55743106    787 ILAAESLPKIGDLHPQ 802
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 433-591 2.18e-41

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: 151.07  E-value: 2.18e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     433 DIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGLN 512
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     513 TGSALSYVYANHFTEAGGSriREHVPQLLLLLTAGQSEDS---YLQAANALTRAGILTFCVGASQA-NKAELEQIAFNPS 588
Cdd:smart00327   81 LGAALQYALENLFSKSAGS--RRGAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158


                    ...
gi 55743106     589 LVY 591
Cdd:smart00327  159 GVY 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1432-1595 7.76e-41

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: 149.36  E-value: 7.76e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1432 ADIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGrha 1511
Cdd:cd01482    1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGG--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1512 NTKVG--LEHLRVNHFVPEAGSRLDqrVPQIAFVITGGKSVEDAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIAS--NS 1587
Cdd:cd01482   78 NTRTGkaLTHVREKNFTPDAGARPG--VPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASkpSE 155


                 ....*...
gi 55743106 1588 ATAFRVGN 1595
Cdd:cd01482  156 THVFNVAD 163
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1027-1194 6.13e-40

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: 147.22  E-value: 6.13e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    1027 DVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQIN 1105
Cdd:smart00327    1 DVVFLLDGSGSMGGNrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    1106 VGNALEYVSRNIFKRPLGSRieEGVPQFLVLISSGKSDD---EVDDPAVELKQFGVAPFTIA--RNADQEELVKISLSP- 1179
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGvgNDVDEEELKKLASAPg 158

                           170
                    ....*....|....*.
gi 55743106    1180 -EYVFSVSTFRELPSL 1194
Cdd:smart00327  159 gVYVFLPELLDLLIDL 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 239-411 5.15e-39

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: 144.52  E-value: 5.15e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     239 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSALY 318
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     319 TGSALDFVRNNLFTSSAGYRaaEGIPKLLVLITGGKSLD---EISQPAQELKRSSIMAFAIG-NKGADQAELEEIAFDSS 394
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGvGNDVDEEELKKLASAPG 158

                           170
                    ....*....|....*..
gi 55743106     395 LVFIPAEFRAAPLQGML 411
Cdd:smart00327  159 GVYVFLPELLDLLIDLL 175
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1230-1399 5.41e-39

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: 144.52  E-value: 5.41e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    1230 DIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPLN 1309
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    1310 TGKALEFVARNLFVKSAGSRieDGVPQHLVLVLGGKSQD---DVSRFAQVIRSSGIVSLGVG-DRNIDRTELQTITNDPR 1385
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGvGNDVDEEELKKLASAPG 158

                           170
                    ....*....|....*.
gi 55743106    1386 LV--FTVREFRELPNI 1399
Cdd:smart00327  159 GVyvFLPELLDLLIDL 174
Kunitz_collagen_alpha3_VI cd22629
Kunitz-type domain from the alpha3 chain of human type VI collagen, and similar proteins; This ...
 2904-2956 2.29e-38

Kunitz-type domain from the alpha3 chain of human type VI collagen, and similar proteins; This model includes the Kunitz-type domain from the alpha3 chain of type VI collagen (collagen alpha 3(VI) chain), encoded by COL6A3 gene. Collagen VI is a widely expressed member of the triple helix-containing protein superfamily of collagens and forms beaded microfibrils that anchor large interstitial structures. Immediately after fibril formation, the Kunitz domain can be cleaved off. Mutations in the alpha1, alpha2, and alpha3 chains of collagen VI cause myopathies ranging from the severe Ullrich congenital muscular dystrophy to the milder Bethlem myopathy, including intermediate forms. Early onset isolated dystonia, a neurological disease, has been shown to be caused by mutations in the alpha3 chain. Findings also indicated potential associations between COL6A3 polymorphisms and lung cancer risk. This domain is similar to that of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438672  Cd Length: 53  Bit Score: 137.89  E-value: 2.29e-38
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2904 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22629    1 DICKLPKDEGTCRDFVLKWYYDPETKSCARFWYGGCGGNENRFDSQEECEKVC 53
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 823-995 1.17e-35

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: 134.89  E-value: 1.17e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     823 DVVFLLDGSEGVR-SGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPN 901
Cdd:smart00327    1 DVVFLLDGSGSMGgNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     902 TGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGD---DVRNPSVVVKRGGAVPIGIGIGNA-DITEMQTISFIPD 977
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158

                           170
                    ....*....|....*...
gi 55743106     978 FaVAIPTFRQLGTVQQVI 995
Cdd:smart00327  159 G-VYVFLPELLDLLIDLL 175
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 36-209 6.40e-34

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: 129.88  E-value: 6.40e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106      36 DIIFLIDGSNNTGSVNFAVILDFLVNLLEKLPIGTQQIRVGVVQFSDEPRTMFSLDTYSTKAQVLGAVKALGFAGGELAN 115
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     116 IGLALDFVVENHFTRAGGSRveEGVPQVLVLISAGPSSDEIRYGVVALKQA-----SVFSFGLGaQAASRAELQHIATDD 190
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDGPKDLLKAAKELkrsgvKVFVVGVG-NDVDEEELKKLASAP 157

                           170
                    ....*....|....*....
gi 55743106     191 NLVFtVPEFRSFGDLQEKL 209
Cdd:smart00327  158 GGVY-VFLPELLDLLIDLL 175
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1433-1606 2.16e-32

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: 125.26  E-value: 2.16e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    1433 DIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRHAN 1512
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    1513 TKVGLEHLRVNHFVPEAGSRLDqrVPQIAFVITGGKS---VEDAQDVSLALTQRGVKVFAVGVRN-IDSEEVGKIASNSA 1588
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRG--APKVVILITDGESndgPKDLLKAAKELKRSGVKVFVVGVGNdVDEEELKKLASAPG 158

                           170
                    ....*....|....*...
gi 55743106    1589 TAFrVGNVQELSELSEQV 1606
Cdd:smart00327  159 GVY-VFLPELLDLLIDLL 175
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1904-2166 6.07e-32

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: 131.95  E-value: 6.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1904 GLDGLDGeDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVGIRGDPGNPGqdsqERGPKGETGDLGPMGVPGRDGVPG 1983
Cdd:NF038329  109 GLQQLKG-DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERG----EKGPAGPQGEAGPQGPAGKDGEAG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1984 gpgetgknggfgrrgppgAKGNKGGPGQPGFEGEqgtrgaqgpagpagppgligeqgisgprgsggaagapgergrTGPL 2063
Cdd:NF038329  184 ------------------AKGPAGEKGPQGPRGE------------------------------------------TGPA 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  2064 GRKGEPGEPGPKGGIGNRGPRGETGDDGRdgvgseGRRGKKGERGfpgypgpkgnpgepglngttgPKGIRGRRGNSGPP 2143
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGD------GQQGPDGDPG---------------------PTGEDGPQGPDGPA 256

                         250       260
                  ....*....|....*....|...
gi 55743106  2144 GIVGQKGDPGYPGPAGPKGNRGD 2166
Cdd:NF038329  257 GKDGPRGDRGEAGPDGPDGKDGE 279
VWA pfam00092
von Willebrand factor type A domain;
2413-2600 1.43e-31

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 123.15  E-value: 1.43e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   2413 DMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDpkasqhFARVAVVQHApsesvDNasmppVKVEFSLTDYGSKEKL 2492
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPD------GTRVGLVQYS-----SD-----VRTEFPLNDYSSKEEL 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   2493 VDFLSRGMTQLQGTRALGSAIEYTIENVFESAPNPRDL--KIVVLMLTGEVPEQQLEEaqrVILQAKCKGYFFVVLGIGr 2570
Cdd:pfam00092   65 LSAVDNLRYLGGGTTNTGKALKYALENLFSSAAGARPGapKVVVLLTDGRSQDGDPEE---VARELKSAGVTVFAVGVG- 140

                          170       180       190
                   ....*....|....*....|....*....|
gi 55743106   2571 KVNIKEVYTFASEPNDVFFKLVDKSTELNE 2600
Cdd:pfam00092  141 NADDEELRKIASEPGEGHVFTVSDFEALED 170
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1914-2165 4.85e-31

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: 129.25  E-value: 4.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1914 DKGLPGSSGEkgnpGRRGDKGPRGEKGERGDVGIRGDPGnpgqdsqERGPKGETGDLGPMGVPGRDGVPGGPGETGKngg 1993
Cdd:NF038329  107 DEGLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRG-------ETGPAGPAGPPGPQGERGEKGPAGPQGEAGP--- 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1994 fgrrgppgakgnkggpgqpgfegeqgtrgaqgpagpAGPPGLIGEQGisgprgsggaagAPGERGRTGPLGRKGEPGEPG 2073
Cdd:NF038329  173 ------------------------------------QGPAGKDGEAG------------AKGPAGEKGPQGPRGETGPAG 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  2074 PKGGIGNRGPRGETGDD------GRDGVGSEGRRGKKGERGFPGYPGPKGNPGE------PGLNGTTGPKGIRGRRGNSG 2141
Cdd:NF038329  205 EQGPAGPAGPDGEAGPAgedgpaGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKdgprgdRGEAGPDGPDGKDGERGPVG 284

                         250       260
                  ....*....|....*....|....
gi 55743106  2142 PPGIVGQKGDPGYPGPAGPKGNRG 2165
Cdd:NF038329  285 PAGKDGQNGKDGLPGKDGKDGQNG 308
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 631-786 3.32e-30

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: 119.10  E-value: 3.32e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     631 DILFLFDGSANLVGQ-FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKALN 709
Cdd:smart00327    1 DVVFLLDGSGSMGGNrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     710 LGYALDYAQRYIFVKSAGSRieDGVLQFLVLLVAGRSSD---RVDGPASNLKQSGVVPFIFQAKNA-DPAELEQIVLSPA 785
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158


                    .
gi 55743106     786 F 786
Cdd:smart00327  159 G 159
Kunitz_BPTI pfam00014
Kunitz/Bovine pancreatic trypsin inhibitor domain; Indicative of a protease inhibitor, usually ...
 2905-2956 4.52e-26

Kunitz/Bovine pancreatic trypsin inhibitor domain; Indicative of a protease inhibitor, usually a serine protease inhibitor. Structure is a disulfide rich alpha+beta fold. BPTI (bovine pancreatic trypsin inhibitor) is an extensively studied model structure. Certain family members are similar to the tick anticoagulant peptide (TAP). This is a highly selective inhibitor of factor Xa in the blood coagulation pathways. TAP molecules are highly dipolar, and are arranged to form a twisted two- stranded antiparallel beta-sheet followed by an alpha helix.


Pssm-ID: 425421  Cd Length: 53  Bit Score: 102.72  E-value: 4.52e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 55743106   2905 ICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:pfam00014    1 ICSLPPDSGPCKASIPRWYYNPTTGTCEPFTYGGCGGNANNFESLEECESTC 52
KU smart00131
BPTI/Kunitz family of serine protease inhibitors; Serine protease inhibitors. One member of ...
 2904-2956 9.36e-25

BPTI/Kunitz family of serine protease inhibitors; Serine protease inhibitors. One member of the family is encoded by an alternatively-spliced form of Alzheimer's amyloid beta-protein.


Pssm-ID: 197529  Cd Length: 53  Bit Score: 98.88  E-value: 9.36e-25
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 55743106    2904 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:smart00131    1 DVCLLPPDTGPCGGSIPRYYYDPETGTCEPFTYGGCGGNANNFESLEECERTC 53
VWA pfam00092
von Willebrand factor type A domain;
2196-2374 2.77e-22

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 96.19  E-value: 2.77e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   2196 ELAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIaesnCPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQVaLT 2275
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDI----GPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRY-LG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   2276 SKQQSLETAMSFVARNTFKRVRNG-FLMRKVAVFFSNTPTrASPQLREAVLKLSDAGITPLFL-TRQEDRQLINALQiNN 2353
Cdd:pfam00092   76 GGTTNTGKALKYALENLFSSAAGArPGAPKVVVLLTDGRS-QDGDPEEVARELKSAGVTVFAVgVGNADDEELRKIA-SE 153

                          170       180
                   ....*....|....*....|.
gi 55743106   2354 TAVGHALVLPAGRDLTDFLEN 2374
Cdd:pfam00092  154 PGEGHVFTVSDFEALEDLQDQ 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2197-2337 5.79e-22

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: 95.05  E-value: 5.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2197 LAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIAesncPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQvALTS 2276
Cdd:cd01450    3 IVFLLDGSESVGPENFEKVKDFIEKLVEKLDIG----PDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLK-YLGG 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55743106 2277 KQQSLETAMSFVARNTFKRVRNGFLMRKVAVFFSNTPTRASPQLREAVLKLSDAGITPLFL 2337
Cdd:cd01450   78 GGTNTGKALQYALEQLFSESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVV 138
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 2197-2372 4.36e-20

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: 90.21  E-value: 4.36e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    2197 LAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIaesnCPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQVALtS 2276
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDI----GPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKL-G 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    2277 KQQSLETAMSFVARNTFKRVRNGFLM-RKVAVFFSN-TPTRASPQLREAVLKLSDAGITP--LFLTRQEDRQLINALQIN 2352
Cdd:smart00327   77 GGTNLGAALQYALENLFSKSAGSRRGaPKVVILITDgESNDGPKDLLKAAKELKRSGVKVfvVGVGNDVDEEELKKLASA 156

                           170       180
                    ....*....|....*....|
gi 55743106    2353 NTAVGHALVLPAgRDLTDFL 2372
Cdd:smart00327  157 PGGVYVFLPELL-DLLIDLL 175
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2412-2589 8.97e-20

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: 88.89  E-value: 8.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2412 IDMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDPkasqhfARVAVVQHAPSesvdnasmppVKVEFSLTDYGSKEK 2491
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDK------TRVGLVQYSDD----------VRVEFSLNDYKSKDD 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2492 LVDFLsRGMTQLQGTR-ALGSAIEYTIENVF-ESAPNPRDLKIVVLMLTGEvpEQQLEEAQRVILQAKCKGYFFVVLGIG 2569
Cdd:cd01450   65 LLKAV-KNLKYLGGGGtNTGKALQYALEQLFsESNARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVG 141

                        170       180
                 ....*....|....*....|
gi 55743106 2570 rKVNIKEVYTFASEPNDVFF 2589
Cdd:cd01450  142 -PADEEELREIASCPSERHV 160
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 2413-2602 1.81e-19

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: 88.28  E-value: 1.81e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    2413 DMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDpkasqhFARVAVVQHApsesvDNasmppVKVEFSLTDYGSKEKL 2492
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPD------GDRVGLVTFS-----DD-----ARVLFPLNDSRSKDAL 64

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    2493 VDFLSRGMTQLQGTRALGSAIEYTIENVFESAPNPR-DLKIVVLMLTGEVPEQQLEEAQRVILQAKCKGYFFVVLGIGRK 2571
Cdd:smart00327   65 LEALASLSYKLGGGTNLGAALQYALENLFSKSAGSRrGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGND 144

                           170       180       190
                    ....*....|....*....|....*....|.
gi 55743106    2572 VNIKEVYTFASEPNDVFFKLVDKSTELNEEP 2602
Cdd:smart00327  145 VDEEELKKLASAPGGVYVFLPELLDLLIDLL 175
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2111-2165 3.12e-16

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: 74.84  E-value: 3.12e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 55743106   2111 GYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAGPKGNRG 2165
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1869-2159 2.71e-13

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 75.45  E-value: 2.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1869 PPGVNGTQGFQGCpgqrgvKGSRGFPGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVGIR 1948
Cdd:COG5164   11 PSDPGGVTTPAGS------QGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1949 GDPGN--PGQDSQERGPKGETGDLGPMGVPGRDGVPGGPGETGKNGGFGRRGPPGAKGNKGGPGQPGFEGEQGTRgaqgp 2026
Cdd:COG5164   85 QNQGGtrPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPP----- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2027 agpagppgliGEQGISGPRGSGGAAGAPGERGRTGPlGRKGEPGEPGPKGGIGNRGPRGETGDDGrdgvgsegrrgkkge 2106
Cdd:COG5164  160 ----------GDGGSTTPPGPGGSTTPPDDGGSTTP-PNKGETGTDIPTGGTPRQGPDGPVKKDD--------------- 213

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2107 rgfpgyPGPKGNPgEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAG 2159
Cdd:COG5164  214 ------KNGKGNP-PDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTA 259
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2102-2170 2.94e-12

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 71.86  E-value: 2.94e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55743106  2102 GKKGERGFPGYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAGPKGNRGDSIDQ 2170
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1010-1176 1.52e-10

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: 64.57  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1010 LQPVLQPLPSPGVGGKRDVVFLID--GSQSAGPEFQYVRTLIERLVDYLDvgfDTTRVAVIQFSDDPKVefLLNAHSSKD 1087
Cdd:COG1240   77 LALALAPLALARPQRGRDVVLVVDasGSMAAENRLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEV--LLPLTRDRE 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1088 EVQNAVQRLRPKGGRQInvGNALeYVSRNIFKrplgsRIEEGVPQFLVLISSGKSDDEVDDP---AVELKQFGVAPFTIA 1164
Cdd:COG1240  152 ALKRALDELPPGGGTPL--GDAL-ALALELLK-----RADPARRKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIG 223

                        170
                 ....*....|....*
gi 55743106 1165 ---RNADQEELVKIS 1176
Cdd:COG1240  224 vgtEAVDEGLLREIA 238
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1632-1788 4.02e-09

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: 58.23  E-value: 4.02e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    1632 DVILGFDGSRDqnvfVAQKGFESKVDAILNRISQMHRvscsggRSPTVRVSVVAnTPSGPVEAFDFDEYQ--PEMLEKFR 1709
Cdd:smart00327    1 DVVFLLDGSGS----MGGNRFELAKEFVLKLVEQLDI------GPDGDRVGLVT-FSDDARVLFPLNDSRskDALLEALA 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    1710 NMRsqhpYVLTEDT---------LKVYLNKFRQSSPDSVKVVIHFTDGADGDLA-DLHRASENLRQEGVRaLILVGLERV 1779
Cdd:smart00327   70 SLS----YKLGGGTnlgaalqyaLENLFSKSAGSRRGAPKVVILITDGESNDGPkDLLKAAKELKRSGVK-VFVVGVGND 144


                    ....*....
gi 55743106    1780 VNLERLMHL 1788
Cdd:smart00327  145 VDEEELKKL 153
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 338-584 1.17e-08

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: 58.80  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  338 RAAEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSSLVFIPAEFRAAPLQGMLPGLLAP 417
Cdd:COG1240    1 DLALALLALLLLLALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  418 LRTLSGTPEVHSnkRDIIFLLDGSANVGKTN-FPYVRDFVMNLVNSLDignDNIRVGLVQFSDTPVTEFSLnTYQtKSDI 496
Cdd:COG1240   81 LAPLALARPQRG--RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPL-TRD-REAL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  497 LGHLRQLQLQGGSglNTGSALSYVYaNHFTEAGGSRIRehvpqLLLLLTAGQ---SEDSYLQAANALTRAGILTFCV--G 571
Cdd:COG1240  154 KRALDELPPGGGT--PLGDALALAL-ELLKRADPARRK-----VIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIgvG 225

                        250
                 ....*....|...
gi 55743106  572 ASQANKAELEQIA 584
Cdd:COG1240  226 TEAVDEGLLREIA 238
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1213-1403 3.32e-08

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: 57.26  E-value: 3.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1213 LLASTRYPPPAVESDAADIVFLIDSSeG--VRPDGFAHIRDFVSRIVRRLnigPSKVRVGVVQFSNDVFPEFYLKTYRSQ 1290
Cdd:COG1240   77 LALALAPLALARPQRGRDVVLVVDAS-GsmAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTRDREA 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1291 apVLDAIRRLRLRGGSPLntGKALEfVARNLFvksagSRIEDGVPQHLVLVLGGK---SQDDVSRFAQVIRSSGI--VSL 1365
Cdd:COG1240  153 --LKRALDELPPGGGTPL--GDALA-LALELL-----KRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIriYTI 222

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 55743106 1366 GVGDRNIDRTELQTI---TNDPrlVFTVREFRELPNIEERI 1403
Cdd:COG1240  223 GVGTEAVDEGLLREIaeaTGGR--YFRADDLSELAAIYREI 261
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1411-1602 1.07e-07

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: 55.71  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1411 AATPAPPGVDTPPPSRPEKKKADIVFLLD--GSINfRRDSFQEVLRFVSEIVDTvYEDGDsiQVGLVQYNSDPtdeFFLK 1488
Cdd:COG1240   72 VLLLLLALALAPLALARPQRGRDVVLVVDasGSMA-AENRLEAAKGALLDFLDD-YRPRD--RVGLVAFGGEA---EVLL 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1489 DFST-KRQIIDAINKVVYKGGrhanT------KVGLEHLRvnhfvpeagsRLDQRVPQIAFVITGGK---SVEDAQDVSL 1558
Cdd:COG1240  145 PLTRdREALKRALDELPPGGG----TplgdalALALELLK----------RADPARRKVIVLLTDGRdnaGRIDPLEAAE 210

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 55743106 1559 ALTQRGVKVFAVGV--RNIDSEEVGKIASNS-ATAFRVGNVQELSEL 1602
Cdd:COG1240  211 LAAAAGIRIYTIGVgtEAVDEGLLREIAEATgGRYFRADDLSELAAI 257
PHA03169 PHA03169
hypothetical protein; Provisional
 1876-2013 7.13e-07

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 54.59  E-value: 7.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1876 QGFQGCPGQRGVKGSRGFPGEKGEVGEIGLD---------GLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVG 1946
Cdd:PHA03169   89 QGGPSGSGSESVGSPTPSPSGSAEELASGLSpentsgsspESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQ 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1947 IRG----DPGNPG----QDSQERGPKGETGDLGPMGV-----PGRDGVPGGPGETGKNGGFGRRGPPGAKGNKG-GPGQP 2012
Cdd:PHA03169  169 PSHedspEEPEPPtsepEPDSPGPPQSETPTSSPPPQsppdePGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEReGPPFP 248


                  .
gi 55743106  2013 G 2013
Cdd:PHA03169  249 G 249
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 171-390 3.31e-06

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: 51.48  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  171 FGLGAQAASRAELQHIATDDNLVFTVPEFRSFGDLQEKLLPYIVGVAQRHIVLKPPTIVTQVIEVNKRDIVFLVDGS-SA 249
Cdd:COG1240   26 LLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASgSM 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  250 LGLANFN----AIRDFIAKVIQRLEIGqdLIqvAVAQYADTVRPefyfnthPT--KREVITAVRKMKPLDGSALYTG--S 321
Cdd:COG1240  106 AAENRLEaakgALLDFLDDYRPRDRVG--LV--AFGGEAEVLLP-------LTrdREALKRALDELPPGGGTPLGDAlaL 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55743106  322 ALDFVRnnlftssagyRAAEGIPKLLVLITGGK---SLDEISQPAQELKRSSIMAFAI--GNKGADQAELEEIA 390
Cdd:COG1240  175 ALELLK----------RADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIgvGTEAVDEGLLREIA 238
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 1878-2160 1.36e-05

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 50.77  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1878 FQGCPGQrGVKGSRGFPGEKGEvgeigldgldGEDGDKGLPGSSGekGNPGRRGDKGPRGEKGERGdvgirgdPGNPGQD 1957
Cdd:cd21118  121 WQGSGGH-GAYGSQGGPGVQGH----------GIPGGTGGPWASG--GNYGTNSLGGSVGQGGNGG-------PLNYGTN 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1958 SQ----------ERGPKGETGDLGPmgvPGRDGVPGGpgetgknggfgrrgppgakGNKGGPGQPGFEGEQGTRGAQGPA 2027
Cdd:cd21118  181 SQgavaqpgygtVRGNNQNSGCTNP---PPSGSHESF-------------------SNSGGSSSSGSSGSQGSHGSNGQG 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2028 GPAGPpgliGEQGISGPRGSGGAAGAPGERGRTGPLGRKGEPGEPGPKGGIGNRGPRGETGDDGrdgvGSEGRRGKKger 2107
Cdd:cd21118  239 SSGSS----GGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSSGGSG----GSGGGNKPE--- 307

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 55743106 2108 gfPGYPGPK-GNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAGP 2160
Cdd:cd21118  308 --CNNPGNDvRMAGGGGSQGSKESSGSHGSNGGNGQAEAVGGLNTLNSDASTLP 359
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1631-1785 2.30e-05

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: 47.29  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1631 LDVILGFDGSRDqnvfVAQKGFESKVDAILNRISQMHrvscSGGRSptVRVSVVANTPSGPVEaFDFDEYQ--PEMLEKF 1708
Cdd:cd01450    1 LDIVFLLDGSES----VGPENFEKVKDFIEKLVEKLD----IGPDK--TRVGLVQYSDDVRVE-FSLNDYKskDDLLKAV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1709 RNMRSQ-HPYVLTEDTLKV---YLNKFRQSSPDSVKVVIHFTDGADGDLADLHRASENLRQEGVrALILVGLERVV--NL 1782
Cdd:cd01450   70 KNLKYLgGGGTNTGKALQYaleQLFSESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGI-KVFVVGVGPADeeEL 148


                 ...
gi 55743106 1783 ERL 1785
Cdd:cd01450  149 REI 151
VWA pfam00092
von Willebrand factor type A domain;
1632-1785 3.94e-04

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 43.80  E-value: 3.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1632 DVILGFDGSRDqnvfVAQKGFESKVDAILNRISQMhrvscsgGRSP-TVRVSVV--ANTPsgpVEAFDFDEYQ--PEMLE 1706
Cdd:pfam00092    1 DIVFLLDGSGS----IGGDNFEKVKEFLKKLVESL-------DIGPdGTRVGLVqySSDV---RTEFPLNDYSskEELLS 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1707 KFRNMRSQ-HPYVLTEDTLK-VYLNKFRQSS---PDSVKVVIHFTDGADGDLaDLHRASENLRQEGVRaLILVGLERVVN 1781
Cdd:pfam00092   67 AVDNLRYLgGGTTNTGKALKyALENLFSSAAgarPGAPKVVVLLTDGRSQDG-DPEEVARELKSAGVT-VFAVGVGNADD 144


                   ....*.
gi 55743106   1782 --LERL 1785
Cdd:pfam00092  145 eeLRKI 150
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 33-187 3.95e-04

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: 44.93  E-value: 3.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   33 DSADIIFLIDGSNNTGSVN-FAVILDFLVNLLEKLPigtQQIRVGVVQFSDEPRTMFSLdTYStKAQVLGAVKALGFAGG 111
Cdd:COG1240   91 RGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPL-TRD-REALKRALDELPPGGG 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  112 elANIGLALDFVVEnHFTRAGGSRveegvPQVLVLISAGPSSDEIRYGVVALKQAS-----VFSFGLGAQAASRAELQHI 186
Cdd:COG1240  166 --TPLGDALALALE-LLKRADPAR-----RKVIVLLTDGRDNAGRIDPLEAAELAAaagirIYTIGVGTEAVDEGLLREI 237


                 .
gi 55743106  187 A 187
Cdd:COG1240  238 A 238
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 814-973 5.76e-04

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: 44.54  E-value: 5.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  814 APAPVSGEKDVVFLLD--GSEGVRSGFPLLKEFVQRVVESLdvgQDRVRVAVVQYSDRTRPEFYLNSymNKQDVVNAVRQ 891
Cdd:COG1240   85 ALARPQRGRDVVLVVDasGSMAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTR--DREALKRALDE 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  892 LTLLGGpTPnTGAALEfvlrniLVSSAGSRITEGVPQLLIVLT---ADRSGDDVRNPSVVVKRGGA--VPIGIGIGNADI 966
Cdd:COG1240  160 LPPGGG-TP-LGDALA------LALELLKRADPARRKVIVLLTdgrDNAGRIDPLEAAELAAAAGIriYTIGVGTEAVDE 231


                 ....*..
gi 55743106  967 TEMQTIS 973
Cdd:COG1240  232 GLLREIA 238
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 2787-2855 1.53e-03

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: 40.17  E-value: 1.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2787 REVQVFEITENSAKLHWERAEPPGP----YFYDLTVTSAHDQSLVLKQNLTVTDRVIGGLLAGQTYHVAVVCY 2855
Cdd:cd00063    5 TNLRVTDVTSTSVTLSWTPPEDDGGpitgYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
 
Name Accession Description Interval E-value
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1229-1393 7.26e-89

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: 286.91  E-value: 7.26e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1229 ADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPL 1308
Cdd:cd01481    1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1309 NTGKALEFVARNLFVKSAGSRIEDGVPQHLVLVLGGKSQDDVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDPRLVF 1388
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106 1389 TVREF 1393
Cdd:cd01481  161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 238-402 1.54e-85

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: 277.28  E-value: 1.54e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  238 RDIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSAL 317
Cdd:cd01481    1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  318 YTGSALDFVRNNLFTSSAGYRAAEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSSLVF 397
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106  398 IPAEF 402
Cdd:cd01481  161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 432-596 2.97e-84

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: 273.43  E-value: 2.97e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  432 RDIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGL 511
Cdd:cd01481    1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  512 NTGSALSYVYANHFTEAGGSRIREHVPQLLLLLTAGQSEDSYLQAANALTRAGILTFCVGASQANKAELEQIAFNPSLVY 591
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106  592 LMDDF 596
Cdd:cd01481  161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1026-1188 7.61e-83

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: 269.58  E-value: 7.61e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1026 RDVVFLIDGSQSAGP-EFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQI 1104
Cdd:cd01481    1 KDIVFLIDGSDNVGSgNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1105 NVGNALEYVSRNIFKRPLGSRIEEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTI-ARNADQEELVKISLSPEYVF 1183
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIgARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106 1184 SVSTF 1188
Cdd:cd01481  161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 822-985 2.73e-70

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: 233.37  E-value: 2.73e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  822 KDVVFLLDGSEGVRS-GFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTP 900
Cdd:cd01481    1 KDIVFLIDGSDNVGSgNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  901 NTGAALEFVLRNILVSSAGSRITEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPDFAV 980
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106  981 AIPTF 985
Cdd:cd01481  161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 35-199 2.14e-66

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: 222.58  E-value: 2.14e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   35 ADIIFLIDGSNNTGSVNFAVILDFLVNLLEKLPIGTQQIRVGVVQFSDEPRTMFSLDTYSTKAQVLGAVKALGFAGGELA 114
Cdd:cd01481    1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  115 NIGLALDFVVENHFTRAGGSRVEEGVPQVLVLISAGPSSDEIRYGVVALKQASVFSFGLGAQAASRAELQHIATDDNLVF 194
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106  195 TVPEF 199
Cdd:cd01481  161 QVSDF 165
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1229-1393 3.18e-63

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: 213.24  E-value: 3.18e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1229 ADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGsPL 1308
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGG-GT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1309 NTGKALEFVARNLFVKSagSRIEDGVPQHLVLVLGGKSQDDVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDP--RL 1386
Cdd:cd01472   80 NTGKALKYVRENLFTEA--SGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPkeLY 157


                 ....*..
gi 55743106 1387 VFTVREF 1393
Cdd:cd01472  158 VFNVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 238-402 9.41e-62

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: 209.01  E-value: 9.41e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  238 RDIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLdGSAL 317
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYI-GGGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  318 YTGSALDFVRNNLFTSSAgyRAAEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIAFD--SSL 395
Cdd:cd01472   80 NTGKALKYVRENLFTEAS--GSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDpkELY 157


                 ....*..
gi 55743106  396 VFIPAEF 402
Cdd:cd01472  158 VFNVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1026-1188 1.63e-61

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: 208.24  E-value: 1.63e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1026 RDVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGrQI 1104
Cdd:cd01472    1 ADIVFLVDGSESIGLSnFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGG-GT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1105 NVGNALEYVSRNIFKRPlgSRIEEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTIA-RNADQEELVKISLSP--EY 1181
Cdd:cd01472   80 NTGKALKYVRENLFTEA--SGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGvKNADEEELKQIASDPkeLY 157


                 ....*..
gi 55743106 1182 VFSVSTF 1188
Cdd:cd01472  158 VFNVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 432-596 8.64e-61

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: 206.31  E-value: 8.64e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  432 RDIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGsGL 511
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGG-GT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  512 NTGSALSYVYANHFTEAggSRIREHVPQLLLLLTAGQSEDSYLQAANALTRAGILTFCVGASQANKAELEQIAFNP--SL 589
Cdd:cd01472   80 NTGKALKYVRENLFTEA--SGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPkeLY 157


                 ....*..
gi 55743106  590 VYLMDDF 596
Cdd:cd01472  158 VFNVADF 164
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 630-793 4.33e-60

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: 204.48  E-value: 4.33e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  630 RDILFLFDGSANL-VGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKAL 708
Cdd:cd01481    1 KDIVFLIDGSDNVgSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  709 NLGYALDYAQRYIFVKSAGSRIEDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPAFIL 788
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                 ....*
gi 55743106  789 AAESL 793
Cdd:cd01481  161 QVSDF 165
VWA pfam00092
von Willebrand factor type A domain;
433-605 5.26e-55

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 190.18  E-value: 5.26e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    433 DIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGLN 512
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    513 TGSALSYVYANHFTEAGGSriREHVPQLLLLLTAGQSED-SYLQAANALTRAGILTFCVGASQANKAELEQIAFNPS--L 589
Cdd:pfam00092   81 TGKALKYALENLFSSAAGA--RPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|....*.
gi 55743106    590 VYLMDDFSSLPALPQQ 605
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
1230-1402 3.06e-54

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 187.87  E-value: 3.06e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1230 DIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPLN 1309
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1310 TGKALEFVARNLFVKSAGSRIedGVPQHLVLVLGGKSQD-DVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDP--RL 1386
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARP--GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPgeGH 158

                          170
                   ....*....|....*.
gi 55743106   1387 VFTVREFRELPNIEER 1402
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 35-199 3.40e-52

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: 181.66  E-value: 3.40e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   35 ADIIFLIDGSNNTGSVNFAVILDFLVNLLEKLPIGTQQIRVGVVQFSDEPRTMFSLDTYSTKAQVLGAVKALGFAGGELa 114
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGT- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  115 NIGLALDFVVENHFTRAggSRVEEGVPQVLVLISAGPSSDEIRYGVVALKQASVFSFGLGAQAASRAELQHIATD--DNL 192
Cdd:cd01472   80 NTGKALKYVRENLFTEA--SGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDpkELY 157


                 ....*..
gi 55743106  193 VFTVPEF 199
Cdd:cd01472  158 VFNVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 822-976 4.08e-52

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: 181.27  E-value: 4.08e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  822 KDVVFLLDGSEGV-RSGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTp 900
Cdd:cd01472    1 ADIVFLVDGSESIgLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGT- 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55743106  901 NTGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIP 976
Cdd:cd01472   80 NTGKALKYVRENLFTEASGSR--EGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDP 153
VWA pfam00092
von Willebrand factor type A domain;
1027-1197 1.89e-51

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 179.78  E-value: 1.89e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1027 DVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQIN 1105
Cdd:pfam00092    1 DIVFLLDGSGSIGGDnFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1106 VGNALEYVSRNIFKRPLGSRieEGVPQFLVLISSGKSDD-EVDDPAVELKQFGVAPFTIA-RNADQEELVKISLSP--EY 1181
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGvGNADDEELRKIASEPgeGH 158

                          170
                   ....*....|....*.
gi 55743106   1182 VFSVSTFRELPSLEQK 1197
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
239-406 8.98e-51

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 177.85  E-value: 8.98e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    239 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSALY 318
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    319 TGSALDFVRNNLFTSSAGYRaaEGIPKLLVLITGGKSLD-EISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSS--L 395
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|.
gi 55743106    396 VFIPAEFRAAP 406
Cdd:pfam00092  159 VFTVSDFEALE 169
VWA pfam00092
von Willebrand factor type A domain;
823-993 9.89e-51

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 177.85  E-value: 9.89e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    823 DVVFLLDGSEGVR-SGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPN 901
Cdd:pfam00092    1 DIVFLLDGSGSIGgDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    902 TGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGD-DVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPD--F 978
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|....*
gi 55743106    979 AVAIPTFRQLGTVQQ 993
Cdd:pfam00092  159 VFTVSDFEALEDLQD 173
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 433-592 8.60e-48

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: 169.01  E-value: 8.60e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  433 DIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGLN 512
Cdd:cd01450    2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGTN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  513 TGSALSYVYANHFTEaggSRIREHVPQLLLLLTAGQSEDSY--LQAANALTRAGILTFCVGASQANKAELEQIAFNPSLV 590
Cdd:cd01450   82 TGKALQYALEQLFSE---SNARENVPKVIIVLTDGRSDDGGdpKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSER 158


                 ..
gi 55743106  591 YL 592
Cdd:cd01450  159 HV 160
VWA pfam00092
von Willebrand factor type A domain;
36-208 9.00e-48

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 169.38  E-value: 9.00e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     36 DIIFLIDGSNNTGSVNFAVILDFLVNLLEKLPIGTQQIRVGVVQFSDEPRTMFSLDTYSTKAQVLGAVKALGFAGGELAN 115
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    116 IGLALDFVVENHFTRAGGSRveEGVPQVLVLISAGPSSD-EIRYGVVALKQASVFSFGLGAQAASRAELQHIATDDN--L 192
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|....*.
gi 55743106    193 VFTVPEFRSFGDLQEK 208
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1829-2165 1.24e-46

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: 175.48  E-value: 1.24e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1829 KCSGQRGDRGPIGSIGPKGIPGEDGYRGYPGDeggpgergppgvngtQGFQGCPGQRGVKGSRGFPGEKGEVGEIGLDGL 1908
Cdd:NF038329  114 KGDGEKGEPGPAGPAGPAGEQGPRGDRGETGP---------------AGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1909 DGEDGDKGLPgssGEKGNPGRRGDKGPRGEKGERGdvgirgdpgnpgqdsqERGPKGETGDLGPMGVPGrdgvPGGPGET 1988
Cdd:NF038329  179 DGEAGAKGPA---GEKGPQGPRGETGPAGEQGPAG----------------PAGPDGEAGPAGEDGPAG----PAGDGQQ 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1989 GKnggfgrrgppgakgnKGGPGQPGFEGEQGTRgaqgpagpagppgliGEQGisgprgsggaagapgergRTGPLGRKGE 2068
Cdd:NF038329  236 GP---------------DGDPGPTGEDGPQGPD---------------GPAG------------------KDGPRGDRGE 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  2069 PGEPGPKGGIGNRGPRGETGDDGRDG-VGSEGRRGKKGERGFPGYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGP----- 2142
Cdd:NF038329  268 AGPDGPDGKDGERGPVGPAGKDGQNGkDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPktpev 347

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 55743106  2143 -------------PGIVGQKGDPGyPGPAGPKgNRG 2165
Cdd:NF038329  348 pqkpdtaphtpktPQIPGQSKDVT-PAPQNPS-NRG 381
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 239-402 1.33e-45

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: 162.84  E-value: 1.33e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  239 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMkPLDGSALY 318
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNL-PYKGGNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  319 TGSALDFVRNNLFTSSAGYRaaEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSSL--V 396
Cdd:cd01482   81 TGKALTHVREKNFTPDAGAR--PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSEthV 158


                 ....*.
gi 55743106  397 FIPAEF 402
Cdd:cd01482  159 FNVADF 164
VWA pfam00092
von Willebrand factor type A domain;
1433-1605 4.99e-45

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 161.67  E-value: 4.99e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1433 DIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRHAN 1512
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1513 TKVGLEHLRVNHFVPEAGSRLDqrVPQIAFVITGGKSVE-DAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIASNSA--T 1589
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPG--APKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|....*.
gi 55743106   1590 AFRVGNVQELSELSEQ 1605
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 239-394 3.10e-44

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: 158.61  E-value: 3.10e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  239 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSALY 318
Cdd:cd01450    2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGTN 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55743106  319 TGSALDFVRNNLFTSSagyRAAEGIPKLLVLITGGKSLD--EISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSS 394
Cdd:cd01450   82 TGKALQYALEQLFSES---NARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 35-199 9.57e-44

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: 157.45  E-value: 9.57e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   35 ADIIFLIDGSNNTGSVNFAVILDFLVNLLEKLPIGTQQIRVGVVQFSDEPRTMFSLDTYSTKAQVLGAVKALGFAGGeLA 114
Cdd:cd01482    1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGG-NT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  115 NIGLALDFVVENHFTRAGGSRveEGVPQVLVLISAGPSSDEIRYGVVALKQASVFSFGLGAQAASRAELQHIA--TDDNL 192
Cdd:cd01482   80 RTGKALTHVREKNFTPDAGAR--PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIAskPSETH 157


                 ....*..
gi 55743106  193 VFTVPEF 199
Cdd:cd01482  158 VFNVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 433-596 1.60e-43

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: 156.68  E-value: 1.60e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  433 DIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGsGLN 512
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGG-NTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  513 TGSALSYVYANHFTEAGGSriREHVPQLLLLLTAGQSEDSYLQAANALTRAGILTFCVGASQANKAELEQIAFNPSL--V 590
Cdd:cd01482   81 TGKALTHVREKNFTPDAGA--RPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSEthV 158


                 ....*.
gi 55743106  591 YLMDDF 596
Cdd:cd01482  159 FNVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1229-1393 2.94e-43

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: 156.29  E-value: 2.94e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1229 ADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPl 1308
Cdd:cd01482    1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1309 NTGKALEFVARNLFVKSAGSRieDGVPQHLVLVLGGKSQDDVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDPRL-- 1386
Cdd:cd01482   80 RTGKALTHVREKNFTPDAGAR--PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSEth 157


                 ....*..
gi 55743106 1387 VFTVREF 1393
Cdd:cd01482  158 VFNVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 630-784 5.58e-43

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: 155.46  E-value: 5.58e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  630 RDILFLFDGSANlVGQ--FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKtGKA 707
Cdd:cd01472    1 ADIVFLVDGSES-IGLsnFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYI-GGG 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55743106  708 LNLGYALDYAQRYIFVKSagSRIEDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSP 784
Cdd:cd01472   79 TNTGKALKYVRENLFTEA--SGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDP 153
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1027-1183 7.73e-43

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: 154.76  E-value: 7.73e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1027 DVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQIN 1105
Cdd:cd01450    2 DIVFLLDGSESVGPEnFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGTN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1106 VGNALEYVSRNIFKrplGSRIEEGVPQFLVLISSGKSDDEVD--DPAVELKQFGVAPFTIA-RNADQEELVKISLSP--E 1180
Cdd:cd01450   82 TGKALQYALEQLFS---ESNARENVPKVIIVLTDGRSDDGGDpkEAAAKLKDEGIKVFVVGvGPADEEELREIASCPseR 158


                 ...
gi 55743106 1181 YVF 1183
Cdd:cd01450  159 HVF 161
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1229-1384 9.56e-43

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: 154.37  E-value: 9.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1229 ADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPL 1308
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55743106 1309 NTGKALEFVARNLFVKsagSRIEDGVPQHLVLVLGGKSQD--DVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDP 1384
Cdd:cd01450   81 NTGKALQYALEQLFSE---SNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCP 155
VWA pfam00092
von Willebrand factor type A domain;
631-802 1.56e-41

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 151.66  E-value: 1.56e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    631 DILFLFDGSANL-VGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKALN 709
Cdd:pfam00092    1 DIVFLLDGSGSIgGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    710 LGYALDYAQRYIFVKSAGSRIedGVLQFLVLLVAGRSSD-RVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPA--F 786
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARP--GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158

                          170
                   ....*....|....*.
gi 55743106    787 ILAAESLPKIGDLHPQ 802
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 433-591 2.18e-41

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: 151.07  E-value: 2.18e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     433 DIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGLN 512
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     513 TGSALSYVYANHFTEAGGSriREHVPQLLLLLTAGQSEDS---YLQAANALTRAGILTFCVGASQA-NKAELEQIAFNPS 588
Cdd:smart00327   81 LGAALQYALENLFSKSAGS--RRGAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158


                    ...
gi 55743106     589 LVY 591
Cdd:smart00327  159 GVY 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1432-1595 7.76e-41

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: 149.36  E-value: 7.76e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1432 ADIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGrha 1511
Cdd:cd01482    1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGG--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1512 NTKVG--LEHLRVNHFVPEAGSRLDqrVPQIAFVITGGKSVEDAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIAS--NS 1587
Cdd:cd01482   78 NTRTGkaLTHVREKNFTPDAGARPG--VPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASkpSE 155


                 ....*...
gi 55743106 1588 ATAFRVGN 1595
Cdd:cd01482  156 THVFNVAD 163
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1027-1194 6.13e-40

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: 147.22  E-value: 6.13e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    1027 DVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQIN 1105
Cdd:smart00327    1 DVVFLLDGSGSMGGNrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    1106 VGNALEYVSRNIFKRPLGSRieEGVPQFLVLISSGKSDD---EVDDPAVELKQFGVAPFTIA--RNADQEELVKISLSP- 1179
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGvgNDVDEEELKKLASAPg 158

                           170
                    ....*....|....*.
gi 55743106    1180 -EYVFSVSTFRELPSL 1194
Cdd:smart00327  159 gVYVFLPELLDLLIDL 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 823-977 7.99e-40

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: 146.28  E-value: 7.99e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  823 DVVFLLDGSEGVRS-GFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPN 901
Cdd:cd01450    2 DIVFLLDGSESVGPeNFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGTN 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55743106  902 TGAALEFVLRNILVSSAGSritEGVPQLLIVLTADRS--GDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPD 977
Cdd:cd01450   82 TGKALQYALEQLFSESNAR---ENVPKVIIVLTDGRSddGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1027-1188 1.68e-39

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: 145.51  E-value: 1.68e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1027 DVVFLIDGSQSAG-PEFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQiN 1105
Cdd:cd01482    2 DIVFLVDGSWSIGrSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT-R 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1106 VGNALEYVSRNIFKRPLGSRieEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTIA-RNADQEELVKISLSP--EYV 1182
Cdd:cd01482   81 TGKALTHVREKNFTPDAGAR--PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGvKDADESELKMIASKPseTHV 158


                 ....*.
gi 55743106 1183 FSVSTF 1188
Cdd:cd01482  159 FNVADF 164
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 239-411 5.15e-39

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: 144.52  E-value: 5.15e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     239 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSALY 318
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     319 TGSALDFVRNNLFTSSAGYRaaEGIPKLLVLITGGKSLD---EISQPAQELKRSSIMAFAIG-NKGADQAELEEIAFDSS 394
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGvGNDVDEEELKKLASAPG 158

                           170
                    ....*....|....*..
gi 55743106     395 LVFIPAEFRAAPLQGML 411
Cdd:smart00327  159 GVYVFLPELLDLLIDLL 175
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1230-1399 5.41e-39

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: 144.52  E-value: 5.41e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    1230 DIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPLN 1309
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    1310 TGKALEFVARNLFVKSAGSRieDGVPQHLVLVLGGKSQD---DVSRFAQVIRSSGIVSLGVG-DRNIDRTELQTITNDPR 1385
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGvGNDVDEEELKKLASAPG 158

                           170
                    ....*....|....*.
gi 55743106    1386 LV--FTVREFRELPNI 1399
Cdd:smart00327  159 GVyvFLPELLDLLIDL 174
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 823-977 5.65e-39

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: 143.97  E-value: 5.65e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  823 DVVFLLDGSEGV-RSGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTpN 901
Cdd:cd01482    2 DIVFLVDGSWSIgRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT-R 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55743106  902 TGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPD 977
Cdd:cd01482   81 TGKALTHVREKNFTPDAGAR--PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPS 154
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1432-1593 1.19e-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: 142.85  E-value: 1.19e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1432 ADIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRHA 1511
Cdd:cd01481    1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1512 NTKVGLEHLRVNHFVPEAGSRLDQRVPQIAFVITGGKSVEDAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIASNSATAF 1591
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                 ..
gi 55743106 1592 RV 1593
Cdd:cd01481  161 QV 162
Kunitz_collagen_alpha3_VI cd22629
Kunitz-type domain from the alpha3 chain of human type VI collagen, and similar proteins; This ...
 2904-2956 2.29e-38

Kunitz-type domain from the alpha3 chain of human type VI collagen, and similar proteins; This model includes the Kunitz-type domain from the alpha3 chain of type VI collagen (collagen alpha 3(VI) chain), encoded by COL6A3 gene. Collagen VI is a widely expressed member of the triple helix-containing protein superfamily of collagens and forms beaded microfibrils that anchor large interstitial structures. Immediately after fibril formation, the Kunitz domain can be cleaved off. Mutations in the alpha1, alpha2, and alpha3 chains of collagen VI cause myopathies ranging from the severe Ullrich congenital muscular dystrophy to the milder Bethlem myopathy, including intermediate forms. Early onset isolated dystonia, a neurological disease, has been shown to be caused by mutations in the alpha3 chain. Findings also indicated potential associations between COL6A3 polymorphisms and lung cancer risk. This domain is similar to that of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438672  Cd Length: 53  Bit Score: 137.89  E-value: 2.29e-38
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2904 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22629    1 DICKLPKDEGTCRDFVLKWYYDPETKSCARFWYGGCGGNENRFDSQEECEKVC 53
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1432-1599 2.74e-38

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: 141.98  E-value: 2.74e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1432 ADIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGrha 1511
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGG--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1512 NTKVG--LEHLRVNHFVPEAGSRLDqrVPQIAFVITGGKSVEDAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIASnSAT 1589
Cdd:cd01472   78 GTNTGkaLKYVRENLFTEASGSREG--VPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIAS-DPK 154

                        170
                 ....*....|
gi 55743106 1590 AFRVGNVQEL 1599
Cdd:cd01472  155 ELYVFNVADF 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 35-191 8.67e-36

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: 134.73  E-value: 8.67e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   35 ADIIFLIDGSNNTGSVNFAVILDFLVNLLEKLPIGTQQIRVGVVQFSDEPRTMFSLDTYSTKAQVLGAVKALGFAGGELA 114
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55743106  115 NIGLALDFVVENHFTragGSRVEEGVPQVLVLISAGPSSDEIRYGVVA--LKQASVFSFGLGAQAASRAELQHIATDDN 191
Cdd:cd01450   81 NTGKALQYALEQLFS---ESNARENVPKVIIVLTDGRSDDGGDPKEAAakLKDEGIKVFVVGVGPADEEELREIASCPS 156
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 823-995 1.17e-35

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: 134.89  E-value: 1.17e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     823 DVVFLLDGSEGVR-SGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPN 901
Cdd:smart00327    1 DVVFLLDGSGSMGgNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     902 TGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGD---DVRNPSVVVKRGGAVPIGIGIGNA-DITEMQTISFIPD 977
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158

                           170
                    ....*....|....*...
gi 55743106     978 FaVAIPTFRQLGTVQQVI 995
Cdd:smart00327  159 G-VYVFLPELLDLLIDLL 175
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1432-1585 3.67e-34

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 130.10  E-value: 3.67e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1432 ADIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRHA 1511
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55743106 1512 NTKVGLEHLRVNHFVPeagSRLDQRVPQIAFVITGGKS--VEDAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIAS 1585
Cdd:cd01450   81 NTGKALQYALEQLFSE---SNARENVPKVIIVLTDGRSddGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIAS 153
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 36-209 6.40e-34

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: 129.88  E-value: 6.40e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106      36 DIIFLIDGSNNTGSVNFAVILDFLVNLLEKLPIGTQQIRVGVVQFSDEPRTMFSLDTYSTKAQVLGAVKALGFAGGELAN 115
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     116 IGLALDFVVENHFTRAGGSRveEGVPQVLVLISAGPSSDEIRYGVVALKQA-----SVFSFGLGaQAASRAELQHIATDD 190
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDGPKDLLKAAKELkrsgvKVFVVGVG-NDVDEEELKKLASAP 157

                           170
                    ....*....|....*....
gi 55743106     191 NLVFtVPEFRSFGDLQEKL 209
Cdd:smart00327  158 GGVY-VFLPELLDLLIDLL 175
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 631-784 1.94e-33

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: 127.79  E-value: 1.94e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  631 DILFLFDGSANlVGQ--FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKAL 708
Cdd:cd01450    2 DIVFLLDGSES-VGPenFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55743106  709 NLGYALDYAQRYIFVKsagSRIEDGVLQFLVLLVAGRSSDRVDG--PASNLKQSGVVPFIFQAKNADPAELEQIVLSP 784
Cdd:cd01450   81 NTGKALQYALEQLFSE---SNARENVPKVIIVLTDGRSDDGGDPkeAAAKLKDEGIKVFVVGVGPADEEELREIASCP 155
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1433-1606 2.16e-32

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: 125.26  E-value: 2.16e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    1433 DIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRHAN 1512
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    1513 TKVGLEHLRVNHFVPEAGSRLDqrVPQIAFVITGGKS---VEDAQDVSLALTQRGVKVFAVGVRN-IDSEEVGKIASNSA 1588
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRG--APKVVILITDGESndgPKDLLKAAKELKRSGVKVFVVGVGNdVDEEELKKLASAPG 158

                           170
                    ....*....|....*...
gi 55743106    1589 TAFrVGNVQELSELSEQV 1606
Cdd:smart00327  159 GVY-VFLPELLDLLIDLL 175
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 433-606 4.57e-32

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: 126.35  E-value: 4.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  433 DIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQgGSGLN 512
Cdd:cd01475    4 DLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL-ETGTM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  513 TGSALSYVYANHFTEAGGSR-IREHVPQLLLLLTAGQSEDSYLQAANALTRAGILTFCVGASQANKAELEQIAFNPSL-- 589
Cdd:cd01475   83 TGLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLAdh 162

                        170
                 ....*....|....*..
gi 55743106  590 VYLMDDFSSLPALPQQL 606
Cdd:cd01475  163 VFYVEDFSTIEELTKKF 179
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1904-2166 6.07e-32

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: 131.95  E-value: 6.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1904 GLDGLDGeDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVGIRGDPGNPGqdsqERGPKGETGDLGPMGVPGRDGVPG 1983
Cdd:NF038329  109 GLQQLKG-DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERG----EKGPAGPQGEAGPQGPAGKDGEAG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1984 gpgetgknggfgrrgppgAKGNKGGPGQPGFEGEqgtrgaqgpagpagppgligeqgisgprgsggaagapgergrTGPL 2063
Cdd:NF038329  184 ------------------AKGPAGEKGPQGPRGE------------------------------------------TGPA 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  2064 GRKGEPGEPGPKGGIGNRGPRGETGDDGRdgvgseGRRGKKGERGfpgypgpkgnpgepglngttgPKGIRGRRGNSGPP 2143
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGD------GQQGPDGDPG---------------------PTGEDGPQGPDGPA 256

                         250       260
                  ....*....|....*....|...
gi 55743106  2144 GIVGQKGDPGYPGPAGPKGNRGD 2166
Cdd:NF038329  257 GKDGPRGDRGEAGPDGPDGKDGE 279
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1228-1407 9.49e-32

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: 125.19  E-value: 9.49e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1228 AADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLR-LRGGS 1306
Cdd:cd01475    2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEyLETGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1307 plNTGKALEFVARNLFVKSAGSR-IEDGVPQHLVLVLGGKSQDDVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDP- 1384
Cdd:cd01475   82 --MTGLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPl 159

                        170       180
                 ....*....|....*....|....
gi 55743106 1385 -RLVFTVREFRELPNIEERIMNSF 1407
Cdd:cd01475  160 aDHVFYVEDFSTIEELTKKFQGKI 183
VWA pfam00092
von Willebrand factor type A domain;
2413-2600 1.43e-31

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 123.15  E-value: 1.43e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   2413 DMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDpkasqhFARVAVVQHApsesvDNasmppVKVEFSLTDYGSKEKL 2492
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPD------GTRVGLVQYS-----SD-----VRTEFPLNDYSSKEEL 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   2493 VDFLSRGMTQLQGTRALGSAIEYTIENVFESAPNPRDL--KIVVLMLTGEVPEQQLEEaqrVILQAKCKGYFFVVLGIGr 2570
Cdd:pfam00092   65 LSAVDNLRYLGGGTTNTGKALKYALENLFSSAAGARPGapKVVVLLTDGRSQDGDPEE---VARELKSAGVTVFAVGVG- 140

                          170       180       190
                   ....*....|....*....|....*....|
gi 55743106   2571 KVNIKEVYTFASEPNDVFFKLVDKSTELNE 2600
Cdd:pfam00092  141 NADDEELRKIASEPGEGHVFTVSDFEALED 170
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 239-390 2.34e-31

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: 124.03  E-value: 2.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  239 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLdGSALY 318
Cdd:cd01475    4 DLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL-ETGTM 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55743106  319 TGSALDFVRNNLFTSSAGYR-AAEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIA 390
Cdd:cd01475   83 TGLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIA 155
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1914-2165 4.85e-31

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: 129.25  E-value: 4.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1914 DKGLPGSSGEkgnpGRRGDKGPRGEKGERGDVGIRGDPGnpgqdsqERGPKGETGDLGPMGVPGRDGVPGGPGETGKngg 1993
Cdd:NF038329  107 DEGLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRG-------ETGPAGPAGPPGPQGERGEKGPAGPQGEAGP--- 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1994 fgrrgppgakgnkggpgqpgfegeqgtrgaqgpagpAGPPGLIGEQGisgprgsggaagAPGERGRTGPLGRKGEPGEPG 2073
Cdd:NF038329  173 ------------------------------------QGPAGKDGEAG------------AKGPAGEKGPQGPRGETGPAG 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  2074 PKGGIGNRGPRGETGDD------GRDGVGSEGRRGKKGERGFPGYPGPKGNPGE------PGLNGTTGPKGIRGRRGNSG 2141
Cdd:NF038329  205 EQGPAGPAGPDGEAGPAgedgpaGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKdgprgdRGEAGPDGPDGKDGERGPVG 284

                         250       260
                  ....*....|....*....|....
gi 55743106  2142 PPGIVGQKGDPGYPGPAGPKGNRG 2165
Cdd:NF038329  285 PAGKDGQNGKDGLPGKDGKDGQNG 308
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 631-786 3.32e-30

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: 119.10  E-value: 3.32e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     631 DILFLFDGSANLVGQ-FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKALN 709
Cdd:smart00327    1 DVVFLLDGSGSMGGNrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     710 LGYALDYAQRYIFVKSAGSRieDGVLQFLVLLVAGRSSD---RVDGPASNLKQSGVVPFIFQAKNA-DPAELEQIVLSPA 785
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158


                    .
gi 55743106     786 F 786
Cdd:smart00327  159 G 159
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 631-785 1.22e-29

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: 117.00  E-value: 1.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  631 DILFLFDGSANlVGQ--FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKAl 708
Cdd:cd01482    2 DIVFLVDGSWS-IGRsnFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT- 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55743106  709 NLGYALDYAQRYIFVKSAGSRieDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPA 785
Cdd:cd01482   80 RTGKALTHVREKNFTPDAGAR--PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPS 154
Kunitz_collagen_alpha6_VI cd22630
Kunitz-type domain from the alpha6 chain of human type VI collagen, and similar proteins; This ...
 2904-2956 2.19e-29

Kunitz-type domain from the alpha6 chain of human type VI collagen, and similar proteins; This model includes the Kunitz-type domain from the alpha6 chain of type VI collagen (collagen alpha 6(VI) chain), encoded by COL6A6 gene, and similar proteins. Collagen VI is a widely expressed member of the triple helix-containing protein superfamily of collagens and forms beaded microfibrils that anchor large interstitial structures. Immediately after fibril formation, the Kunitz domain can be cleaved off. This domain is similar to that of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor) that shows an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438673  Cd Length: 55  Bit Score: 112.31  E-value: 2.19e-29
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2904 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22630    1 DACSLDQDEGECQNYVLKWYYDQEQKECSQFWYGGCGGNKNRFETQEECEALC 53
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 823-972 9.81e-28

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: 113.63  E-value: 9.81e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  823 DVVFLLDGSEGVR-SGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTpN 901
Cdd:cd01475    4 DLVFLIDSSRSVRpENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT-M 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55743106  902 TGAALEFVLRNILVSSAGSR-ITEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTI 972
Cdd:cd01475   83 TGLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREI 154
Kunitz_papilin_lacunin-like cd22639
Drosophila melanogaster Kunitz domain 1, Manduca sexta lacunin Kunitz domain 1, and simialr ...
 2906-2956 4.56e-27

Drosophila melanogaster Kunitz domain 1, Manduca sexta lacunin Kunitz domain 1, and simialr proteins; This model includes Drosophila melanogaster Kunitz domain 1 of papilin and Manduca sexta Kunitz domain 1 of lacunin, and similar proteins. D. melanogaster papilin is an essential extracellular matrix (ECM) protein that influences cell rearrangements. It may act by modulating metalloproteinase action during organogenesis and is able to non-competitively inhibit procollagen N-proteinase, an ADAMTS metalloproteinase. M. sexta lacunin is a large multidomain ECM containing several domains including several Kunitz-type protease inhibitors, thrombospondin type I, immunoglobulin-like and others. It exerts multiple effects on a variety of cell behaviors associated with the complex phenomenon of epithelial morphogenesis. These domains are similar to Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor) that shows an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438681  Cd Length: 52  Bit Score: 105.73  E-value: 4.56e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 55743106 2906 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22639    1 CSLPKDRGPCRNYTVKWYFDMAYGGCSRFWYGGCGGNGNRFDTEEECKAVC 51
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 432-584 1.37e-26

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: 108.42  E-value: 1.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  432 RDIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGL 511
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55743106  512 NTGSALSYVYANHFteaggSRIREHVPQLLLLLTAGQSEDSY---LQAANALTRAGILTFCVG-ASQANKAELEQIA 584
Cdd:cd00198   81 NIGAALRLALELLK-----SAKRPNARRVIILLTDGEPNDGPellAEAARELRKLGITVYTIGiGDDANEDELKEIA 152
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1027-1198 2.33e-26

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: 109.78  E-value: 2.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1027 DVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKgGRQIN 1105
Cdd:cd01475    4 DLVFLIDSSRSVRPEnFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL-ETGTM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1106 VGNALEYVSRNIFKRPLGSR-IEEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTIA-RNADQEELVKISLSP--EY 1181
Cdd:cd01475   83 TGLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGvGRADEEELREIASEPlaDH 162

                        170
                 ....*....|....*..
gi 55743106 1182 VFSVSTFRELPSLEQKL 1198
Cdd:cd01475  163 VFYVEDFSTIEELTKKF 179
Kunitz_BPTI pfam00014
Kunitz/Bovine pancreatic trypsin inhibitor domain; Indicative of a protease inhibitor, usually ...
 2905-2956 4.52e-26

Kunitz/Bovine pancreatic trypsin inhibitor domain; Indicative of a protease inhibitor, usually a serine protease inhibitor. Structure is a disulfide rich alpha+beta fold. BPTI (bovine pancreatic trypsin inhibitor) is an extensively studied model structure. Certain family members are similar to the tick anticoagulant peptide (TAP). This is a highly selective inhibitor of factor Xa in the blood coagulation pathways. TAP molecules are highly dipolar, and are arranged to form a twisted two- stranded antiparallel beta-sheet followed by an alpha helix.


Pssm-ID: 425421  Cd Length: 53  Bit Score: 102.72  E-value: 4.52e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 55743106   2905 ICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:pfam00014    1 ICSLPPDSGPCKASIPRWYYNPTTGTCEPFTYGGCGGNANNFESLEECESTC 52
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1430-1585 4.69e-26

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: 109.01  E-value: 4.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1430 KKADIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKgGR 1509
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL-ET 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55743106 1510 HANTKVGLEHLRVNHFVPEAGSR-LDQRVPQIAFVITGGKSVEDAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIAS 1585
Cdd:cd01475   80 GTMTGLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIAS 156
Kunitz_papilin cd22635
Kunitz domain of papilin, and similar proteins; This model includes the Kunitz domain found in ...
 2906-2956 1.59e-25

Kunitz domain of papilin, and similar proteins; This model includes the Kunitz domain found in human and mouse papilin, and similar proteins. Papilin is an extracellular matrix glycoprotein that has been found in many organisms to be involved in thin matrix layers during gastrulation, matrix associated with wandering, phagocytic hemocytes, basement membranes and space-filling matrix during Drosophila development. It is a multidomain protein that primarily occurs in basement membranes. Papilins interact with several extracellular matrix components and ADAMTS enzymes, influences cell rearrangements and may modulate metalloproteinases during organogenesis. Papilins exist in mammals and invertebrates as a set of related, though not necessarily identical proteins. Mammalian papilin contains a single Kunitz domain, while other papilins such as that from Caenorhabditis elegans, contains multiple Kunitz domains. These domains are similar to Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor) that shows an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438678  Cd Length: 52  Bit Score: 101.18  E-value: 1.59e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 55743106 2906 CKLPKDEGT-CRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22635    1 CLLDKDAGTvCGDYVQRWYYDPATGACNRFWYGGCGGNANRFATEAECLRTC 52
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1230-1399 2.34e-25

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: 105.13  E-value: 2.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1230 DIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPlN 1309
Cdd:cd01469    2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLT-N 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1310 TGKALEFVARNLFVKSAGSRieDGVPQHLVLVLGGKSQDDvSRFAQVIRSS---GIV--SLGVGD---RNIDRTELQTIT 1381
Cdd:cd01469   81 TATAIQYVVTELFSESNGAR--KDATKVLVVITDGESHDD-PLLKDVIPQAereGIIryAIGVGGhfqRENSREELKTIA 157

                        170       180
                 ....*....|....*....|
gi 55743106 1382 NDP--RLVFTVREFRELPNI 1399
Cdd:cd01469  158 SKPpeEHFFNVTDFAALKDI 177
Kunitz-type cd00109
Kunitz/Bovine pancreatic trypsin inhibitor (BPTI) domain; This family contains the Kunitz ...
 2906-2956 3.18e-25

Kunitz/Bovine pancreatic trypsin inhibitor (BPTI) domain; This family contains the Kunitz domain which is a common structural fold found in a family of reversible serine protease inhibitors. This domain is thought to have evolved over 500 million years and is ubiquitous in all kingdoms of life and has been incorporated into many different genes. In general, each domain is encoded by a single exon. Some genes encode proteins with a single Kunitz domain, e.g. bovine pancreatic trypsin inhibitor (BPTI), trophoblast Kunitz domain protein (TKDP), amyloid beta-protein precursor (ABPP), as well as Kunitz-type venom peptides such as dendrotoxin. Genes that encode multiple Kunitz domains include hepatocyte growth factor activator inhibitors HAI1 and HAI2 (two domains), tissue factor pathway inhibitor TFPI1 and TFPI2 (three domains) and Caenorhabditis elegans papilin (eleven domains). In addition, the Kunitz domain has been integrated into multi-domain proteins, e.g. the collagen alpha3(VI), alpha1(VII) and alpha1(XXVIII) chains, WFIKKN1 (containing WAP, Follistatin/Kazal, Immunoglobulin, two Kunitz and NTR domains) and papilin. Furthermore, each domain within a multi-Kunitz domain protein may exhibit different protease activity, such as for the three tandemly repeated domains within both tissue factor pathway inhibitors 1 and 2. The Kunitz domain is a representative of alpha/beta proteins with irregular secondary structure stabilized by three disulfide bonds and presenting three peptide loops that can be varied without introducing much destabilization to the scaffold. Protease inhibitors meet the scaffold criteria in that they are small, stable and capable of evolving the binding activity of exposed peptide loops through targeted randomization to construct combinatorial libraries. Kunitz domain-based scaffolds have been successfully utilized to construct and select a library of protease inhibitors with the potential for therapeutic application.


Pssm-ID: 438633  Cd Length: 51  Bit Score: 100.32  E-value: 3.18e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 55743106 2906 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd00109    1 CLLPPDPGPCRAYFPRWYYNSETGQCEEFIYGGCGGNANNFETKEECEATC 51
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1229-1389 3.89e-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: 104.02  E-value: 3.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1229 ADIVFLIDSSEGVRpDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDV--FPEFYLKTYRSQAPVLDAIRRLRLRGGS 1306
Cdd:cd01476    1 LDLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGrqRVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1307 PlNTGKALEFvARNLFVKSAGSRieDGVPQHLVLVLGGKSQDDVSRFAQVIRS---SGIVSLGVGDR-NIDRTELQTITN 1382
Cdd:cd01476   80 T-ATGAAIEV-ALQQLDPSEGRR--EGIPKVVVVLTDGRSHDDPEKQARILRAvpnIETFAVGTGDPgTVDTEELHSITG 155


                 ....*..
gi 55743106 1383 DPRLVFT 1389
Cdd:cd01476  156 NEDHIFT 162
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1026-1185 6.57e-25

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: 103.41  E-value: 6.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1026 RDVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQI 1104
Cdd:cd00198    1 ADIVFLLDVSGSMGGEkLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1105 NVGNALEYVSRNIFKRPLGSRieegvPQFLVLISSGKSDD---EVDDPAVELKQFGVAPFTIA--RNADQEELVKISLSP 1179
Cdd:cd00198   81 NIGAALRLALELLKSAKRPNA-----RRVIILLTDGEPNDgpeLLAEAARELRKLGITVYTIGigDDANEDELKEIADKT 155


                 ....*.
gi 55743106 1180 EYVFSV 1185
Cdd:cd00198  156 TGGAVF 161
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 35-209 6.94e-25

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: 105.54  E-value: 6.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   35 ADIIFLIDGSNNTGSVNFAVILDFLVNLLEKLPIGTQQIRVGVVQFSDEPRTMFSLDTYSTKAQVLGAVKALGF-AGGEL 113
Cdd:cd01475    3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYlETGTM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  114 AniGLALDFVVENHFTRAGGSR-VEEGVPQVLVLISAGPSSDEIRYGVVALKQASVFSFGLGAQAASRAELQHIATD--D 190
Cdd:cd01475   83 T--GLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEplA 160

                        170
                 ....*....|....*....
gi 55743106  191 NLVFTVPEFRSFGDLQEKL 209
Cdd:cd01475  161 DHVFYVEDFSTIEELTKKF 179
Kunitz_collagen_alpha1_XXVIII cd22628
Kunitz-type domain from the alpha1 chain of type XXVIII collagen, and similar proteins; This ...
 2906-2956 7.82e-25

Kunitz-type domain from the alpha1 chain of type XXVIII collagen, and similar proteins; This model includes the Kunitz-type domain from the alpha1 chain of type XXVIII collagen (collagen alpha-1(XXVIII) chain) and similar proteins. The zebrafish has four collagen XXVIII genes all of which are differentially expressed in the liver, thymus, muscle, intestine and skin; only the alpha1 chain contains the Kunitz domain which is often proteolytically processed. Mammals only contain the alpha1 collagen chain, expressed mostly in dorsal root ganglia and peripheral nerves. The Kunitz domain is found at the C-terminus, and is most related to Kunitz domains of papilin and alpha3(VI) collagen. This domain is similar to that of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor) that shows an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438671  Cd Length: 51  Bit Score: 99.28  E-value: 7.82e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 55743106 2906 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22628    1 CLEPLDPGPCREYVVKWYYDKQANSCAQFWYGGCEGNRNRFETEEECRKTC 51
KU smart00131
BPTI/Kunitz family of serine protease inhibitors; Serine protease inhibitors. One member of ...
 2904-2956 9.36e-25

BPTI/Kunitz family of serine protease inhibitors; Serine protease inhibitors. One member of the family is encoded by an alternatively-spliced form of Alzheimer's amyloid beta-protein.


Pssm-ID: 197529  Cd Length: 53  Bit Score: 98.88  E-value: 9.36e-25
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 55743106    2904 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:smart00131    1 DVCLLPPDTGPCGGSIPRYYYDPETGTCEPFTYGGCGGNANNFESLEECERTC 53
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 433-599 2.69e-24

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: 102.43  E-value: 2.69e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  433 DIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSgLN 512
Cdd:cd01469    2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGL-TN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  513 TGSALSYVYANHFTEAGGSriREHVPQLLLLLTAGQSEDSYL--QAANALTRAGILTFCVG---ASQANKA--ELEQIAF 585
Cdd:cd01469   81 TATAIQYVVTELFSESNGA--RKDATKVLVVITDGESHDDPLlkDVIPQAEREGIIRYAIGvggHFQRENSreELKTIAS 158

                        170
                 ....*....|....*.
gi 55743106  586 NPS--LVYLMDDFSSL 599
Cdd:cd01469  159 KPPeeHFFNVTDFAAL 174
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 239-389 8.24e-24

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: 100.89  E-value: 8.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  239 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSAlY 318
Cdd:cd01469    2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLT-N 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55743106  319 TGSALDFVRNNLFTSSAGYRaaEGIPKLLVLITGGKSLD--EISQPAQELKRSSIMAFAIGNKGADQAE--LEEI 389
Cdd:cd01469   81 TATAIQYVVTELFSESNGAR--KDATKVLVVITDGESHDdpLLKDVIPQAEREGIIRYAIGVGGHFQREnsREEL 153
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 35-196 8.85e-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: 100.33  E-value: 8.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   35 ADIIFLIDGSNNTGSVNFAVILDFLVNLLEKLPIGTQQIRVGVVQFSDEPRTMFSLDTYSTKAQVLGAVKALGFAGGELA 114
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  115 NIGLALDFVVENHFTRAGGSRveegvPQVLVLISAGPSSDEIRYGVVALKQA-----SVFSFGLGAQAASrAELQHIATD 189
Cdd:cd00198   81 NIGAALRLALELLKSAKRPNA-----RRVIILLTDGEPNDGPELLAEAARELrklgiTVYTIGIGDDANE-DELKEIADK 154


                 ....*..
gi 55743106  190 DNLVFTV 196
Cdd:cd00198  155 TTGGAVF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 822-952 4.84e-23

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: 98.24  E-value: 4.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  822 KDVVFLLDGSEGVRSGFPLLKEFVQRVVESLDVGQDRVRVAVVQYS--DRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPT 899
Cdd:cd01476    1 LDLLFVLDSSGSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106  900 pNTGAALEFVLrNILVSSAGSRitEGVPQLLIVLTADRSGDDVRNPSVVVKRG 952
Cdd:cd01476   81 -ATGAAIEVAL-QQLDPSEGRR--EGIPKVVVVLTDGRSHDDPEKQARILRAV 129
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1027-1194 6.55e-23

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: 98.20  E-value: 6.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1027 DVVFLIDGSQSAGP-EFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQiN 1105
Cdd:cd01469    2 DIVFVLDGSGSIYPdDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLT-N 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1106 VGNALEYVSRNIFKRPLGSRieEGVPQFLVLISSGKSDDEVDDPAV--ELKQFGVAPFTIA------RNADQEELVKISL 1177
Cdd:cd01469   81 TATAIQYVVTELFSESNGAR--KDATKVLVVITDGESHDDPLLKDVipQAEREGIIRYAIGvgghfqRENSREELKTIAS 158

                        170
                 ....*....|....*....
gi 55743106 1178 SP--EYVFSVSTFRELPSL 1194
Cdd:cd01469  159 KPpeEHFFNVTDFAALKDI 177
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 36-205 1.19e-22

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: 97.43  E-value: 1.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   36 DIIFLIDGSNNTGSVNFAVILDFLVNLLEKLPIGTQQIRVGVVQFSDEPRTMFSLDTYSTKAQVLGAVKALGFAGGeLAN 115
Cdd:cd01469    2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLG-LTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  116 IGLALDFVVENHFTRAGGSRveEGVPQVLVLISAGPSSDEIRYGVV--ALKQASVFSFGLGAQAA-----SRAELQHIAT 188
Cdd:cd01469   81 TATAIQYVVTELFSESNGAR--KDATKVLVVITDGESHDDPLLKDVipQAEREGIIRYAIGVGGHfqrenSREELKTIAS 158

                        170
                 ....*....|....*....
gi 55743106  189 D--DNLVFTVPEFRSFGDL 205
Cdd:cd01469  159 KppEEHFFNVTDFAALKDI 177
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1229-1384 1.84e-22

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: 96.48  E-value: 1.84e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1229 ADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPL 1308
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1309 NTGKALEFVARNLFvksagSRIEDGVPQHLVLVLGGKSQDD---VSRFAQVIRSSGI--VSLGVGDRNiDRTELQTITND 1383
Cdd:cd00198   81 NIGAALRLALELLK-----SAKRPNARRVIILLTDGEPNDGpelLAEAARELRKLGItvYTIGIGDDA-NEDELKEIADK 154


                 .
gi 55743106 1384 P 1384
Cdd:cd00198  155 T 155
Kunitz_TFPI2_1-like cd22616
Kunitz domain 1 (KD1) of tissue factor pathway inhibitor 2 (TFPI2) and similar proteins; This ...
 2903-2956 2.15e-22

Kunitz domain 1 (KD1) of tissue factor pathway inhibitor 2 (TFPI2) and similar proteins; This model represents the Kunitz-type domain 1 (KD1) of tissue factor pathway inhibitor 2 (TFPI2 or TFPI-2) and similar proteins. TFPI2 exhibits inhibitory activity primarily toward trypsin, plasmin, and factor VIIa (FVIIa)/tissue factor (TF) via its KD1. It is believed to be the major inhibitor of plasmin in the extracellular matrix (ECM) but has little inhibitory activity toward urokinase-type plasminogen activator, tissue-type plasminogen activator, or thrombin. TFPI2 specifically inhibits the proteases via the P1 arginine residue in KD1. The TFPI2 domains KD2 and KD3 appear to have no discernible inhibitory activity and may serve to bind to nearby proteins to localize TFPI2 in the ECM. Structure studies of KD1 complexed with proteases may help in the development of specific and potent KD1 domain protein that may have a large pharmacologic impact in preventing tumor metastasis, retinal degeneration, and degradation of collagen in the ECM. The structure of this domain is similar to that of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438659  Cd Length: 57  Bit Score: 92.30  E-value: 2.15e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 55743106 2903 TDICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22616    2 AEICLLPPDEGPCRALIPRYYYDRYTQTCREFSYGGCEGNANNFESLEDCEKTC 55
VWA pfam00092
von Willebrand factor type A domain;
2196-2374 2.77e-22

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 96.19  E-value: 2.77e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   2196 ELAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIaesnCPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQVaLT 2275
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDI----GPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRY-LG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   2276 SKQQSLETAMSFVARNTFKRVRNG-FLMRKVAVFFSNTPTrASPQLREAVLKLSDAGITPLFL-TRQEDRQLINALQiNN 2353
Cdd:pfam00092   76 GGTTNTGKALKYALENLFSSAAGArPGAPKVVVLLTDGRS-QDGDPEEVARELKSAGVTVFAVgVGNADDEELRKIA-SE 153

                          170       180
                   ....*....|....*....|.
gi 55743106   2354 TAVGHALVLPAGRDLTDFLEN 2374
Cdd:pfam00092  154 PGEGHVFTVSDFEALEDLQDQ 174
Kunitz_collagen_alpha6_VI-like cd22631
Kunitz-type domain from the alpha6 chain of fish type VI collagen, and similar proteins; This ...
 2906-2956 3.39e-22

Kunitz-type domain from the alpha6 chain of fish type VI collagen, and similar proteins; This model includes the Kunitz-type domain from the alpha6 chain of type VI collagen (collagen alpha 6(VI) chain) and similar proteins. Collagen VI is a widely expressed member of the triple helix-containing protein superfamily of collagens and forms beaded microfibrils that anchor large interstitial structures. Immediately after fibril formation, the Kunitz domain can be cleaved off. This domain is similar to that of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor) that shows an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438674 [Multi-domain]  Cd Length: 51  Bit Score: 91.52  E-value: 3.39e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 55743106 2906 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22631    1 CLLGQDAGSCQNYTMMWFFDSKQGRCSRFWYGGCGGNANRFETQEECENLC 51
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1433-1602 4.87e-22

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: 95.89  E-value: 4.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1433 DIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRhAN 1512
Cdd:cd01469    2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGL-TN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1513 TKVGLEHLRVNHFVPEAGSRLDqrVPQIAFVITGGKSVEDA--QDVSLALTQRGVKVFAVGV-----RNIDSEEVGKIAS 1585
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKD--ATKVLVVITDGESHDDPllKDVIPQAEREGIIRYAIGVgghfqRENSREELKTIAS 158

                        170
                 ....*....|....*....
gi 55743106 1586 NSATA--FRVGNVQELSEL 1602
Cdd:cd01469  159 KPPEEhfFNVTDFAALKDI 177
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2197-2337 5.79e-22

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: 95.05  E-value: 5.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2197 LAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIAesncPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQvALTS 2276
Cdd:cd01450    3 IVFLLDGSESVGPENFEKVKDFIEKLVEKLDIG----PDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLK-YLGG 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55743106 2277 KQQSLETAMSFVARNTFKRVRNGFLMRKVAVFFSNTPTRASPQLREAVLKLSDAGITPLFL 2337
Cdd:cd01450   78 GGTNTGKALQYALEQLFSESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVV 138
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 433-600 1.39e-21

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: 94.76  E-value: 1.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  433 DIIFLLDGSANVGKTN-FPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTY-----QTKSDILGHLRQLQLQ 506
Cdd:cd01471    2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPnstnkDLALNAIRALLSLYYP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  507 GGSgLNTGSALSYVYANHFTEAGGsriREHVPQLLLLLTAGQSEDSY--LQAANALTRAG--ILTFCVGASqANKAEleq 582
Cdd:cd01471   82 NGS-TNTTSALLVVEKHLFDTRGN---RENAPQLVIIMTDGIPDSKFrtLKEARKLRERGviIAVLGVGQG-VNHEE--- 153

                        170
                 ....*....|....*...
gi 55743106  583 iafNPSLVYLMDDFSSLP 600
Cdd:cd01471  154 ---NRSLVGCDPDDSPCP 168
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 823-977 1.58e-21

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: 94.34  E-value: 1.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  823 DVVFLLDGSEGVR-SGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTpN 901
Cdd:cd01469    2 DIVFVLDGSGSIYpDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLT-N 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  902 TGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGDDVRNPSVV--VKRGGAVPIGIGIGNA-----DITEMQTISF 974
Cdd:cd01469   81 TATAIQYVVTELFSESNGAR--KDATKVLVVITDGESHDDPLLKDVIpqAEREGIIRYAIGVGGHfqrenSREELKTIAS 158


                 ...
gi 55743106  975 IPD 977
Cdd:cd01469  159 KPP 161
Kunitz_papilin_mig6-like cd22637
Drosophila melanogaster Kunitz domains 5, 6, 7, and Caenorhabditis elegans Kunitz domain 5 of ...
 2906-2956 2.42e-21

Drosophila melanogaster Kunitz domains 5, 6, 7, and Caenorhabditis elegans Kunitz domain 5 of papilin, and similar domains; This model includes Kunitz domains from papilins with multiple Kunitz domains, such as Drosophila melanogaster Kunitz domains 5, 6, 7, and Caenorhabditis elegans Kunitz domain 5 of papilin, among others. Papilins are essential for embryonic development. D. melanogaster papilin is an essential extracellular matrix (ECM) protein that influences cell rearrangements. It may act by modulating metalloproteinases action during organogenesis and is able to non-competitively inhibit procollagen N-proteinase, an ADAMTS metalloproteinase. C. elegans papilin (also called abnormal cell migration protein 6) mig-6 encodes long (MIG-6L) and short (MIG-6S) isoforms of the extracellular matrix protein papilin, each required for distinct aspects of distal tip cell (DTC) migration and both isoforms have an N-terminal papilin cassette, lagrin repeats and six C-terminal Kunitz-type serine proteinase inhibitory domains. It plays a role in embryogenesis, the second phase of distal cell tip migration and is required for distribution of the metalloproteinase, mig-17, during organogenesis. These domains are similar to Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor) that shows an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438679  Cd Length: 51  Bit Score: 89.34  E-value: 2.42e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 55743106 2906 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22637    1 CDQPKDTGPCDNWVLKWYYDSKKGSCRQFYYGGCGGNDNRFDTEEECEARC 51
Kunitz_HAI1_2-like cd22624
Kunitz domain 2 of hepatocyte growth factor activator inhibitor-1 (HAI1); This model includes ...
 2906-2956 6.53e-21

Kunitz domain 2 of hepatocyte growth factor activator inhibitor-1 (HAI1); This model includes Kunitz domain 2 (KD2) of hepatocyte growth factor activator inhibitor type 1 (HAI-1 or HAI1, also known as Kunitz-type protease inhibitor 1), a membrane-bound multidomain protein essential to the integrity of the basement membrane during placental development. HAI-1 contains an extracellular region and several internal domains that include two Kunitz domains separated in sequence but spatially closed to each other, and their interdomain interactions have evolved to stimulate the inhibitory activity of an integrated Kunitz. While the Kunitz domain 1 (KD1) is the major inhibitory domain of HAI-1 and involved in auto-inhibition of the extracellular region via steric blockage of its active site in the HAI-1 compact tertiary structure, studies show that deletion of HAI-1 Kunitz domain 2 (KD2) and the extracellular region enhanced inhibition of matriptase. HAI-1 KD2 has been shown to have potent inhibitory activity against trypsin, but it cannot inhibit hepatocyte growth factor activator (HGFA), and matriptase. HAI-1 is also important in maintaining postnatal homeostasis in many tissues, including keratinization of the epidermis, hair development, colonic epithelium integrity, proliferation and cell fate of neural progenitor cells, and tissue injury and repair. The interaction between HAI-1 and matriptase is critical for tissue morphogenesis and cellular biology. HAI-1:matriptase ratio imbalance results in tumorigenesis; slight overexpression of matriptase relative to HAI-1 causes spontaneous squamous cell carcinoma, a phenotype that can be effectively reversed back to wild type by additional expression of HAI-1, indicating the need for a tight functional relationship between the two to maintain homeostasis. The structure of KD2 is similar to those of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438667  Cd Length: 61  Bit Score: 88.34  E-value: 6.53e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 55743106 2906 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22624    2 CTEPPVTGPCRASFTRWYYDPLSRKCHRFTYGGCDGNENNFETEDECMETC 52
Kunitz_collagen_alpha1_VII cd22627
Kunitz-type domain from the alpha1 chain of type VII collagen, and similar proteins; This ...
 2904-2956 7.55e-21

Kunitz-type domain from the alpha1 chain of type VII collagen, and similar proteins; This model includes the Kunitz-type domain from the alpha1 chain of type VII collagen (collagen alpha-1(VII) chain also called long-chain collagen or LC collagen) and similar proteins. LC collagen, encoded by the COL7A1 gene, is a stratified squamous epithelial basement membrane protein that forms anchoring fibrils which may contribute to epithelial basement membrane organization and adherence by interacting with extracellular matrix (ECM) proteins such as type IV collagen. So far, over 800 COL7A1 mutations have been reported, including missense, nonsense, splicing, insertion, and deletion mutations which to varying degrees leads to deficiency of type VII collagen. Epidermolysis bullosa acquisita (EBA) is an autoimmune acquired blistering skin disease resulting from autoantibodies to type VII collagen. The COL7A1 protein contains a Kunitz domain, the deactivation of which induces tumorigenesis. This domain is similar to that of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), that shows an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438670  Cd Length: 53  Bit Score: 88.07  E-value: 7.55e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2904 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22627    1 DPCLLPMDEGSCSDYTLLWYYHQKAGECRPFVYGGCGGNANRFSSKEDCELRC 53
Kunitz_amblin-like cd22638
Caenorhabditis elegans Kunitz domain 11 of papilin (also called abnormal cell migration ...
 2906-2956 9.80e-21

Caenorhabditis elegans Kunitz domain 11 of papilin (also called abnormal cell migration protein 6 or mig-6), Amblyomma hebraeum amblin domain 1, and similar proteins; This model includes Caenorhabditis elegans Kunitz domain 11 of papilin (also called abnormal cell migration protein 6 or mig-6) and domain 1 of Amblyomma hebraeum amblin, and similar proteins. C. elegans papilin (also called abnormal cell migration protein 6) mig-6 encodes long (MIG-6L) and short (MIG-6S) isoforms of the extracellular matrix protein papilin, each required for distinct aspects of distal tip cell (DTC) migration and both isoforms have an N-terminal papilin cassette, lagrin repeats and six C-terminal Kunitz-type serine proteinase inhibitory domains. It plays a role in embryogenesis, the second phase of distal cell tip migration and is required for distribution of the metalloproteinase, mig-17, during organogenesis. Amblin contains two Kunitz-like domains and specifically inhibits thrombin. These domains are similar to Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), that shows an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438680  Cd Length: 51  Bit Score: 87.44  E-value: 9.80e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 55743106 2906 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22638    1 CTLKPETGPCRAYIEKWYYDPSTQSCKTFIYGGCGGNGNRFDSEEDCQETC 51
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 238-390 1.04e-20

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: 91.47  E-value: 1.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  238 RDIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSAL 317
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55743106  318 YTGSALDFVRNNLFTssagyRAAEGIPKLLVLITGGKSLD---EISQPAQELKRSSIMAFAIG-NKGADQAELEEIA 390
Cdd:cd00198   81 NIGAALRLALELLKS-----AKRPNARRVIILLTDGEPNDgpeLLAEAARELRKLGITVYTIGiGDDANEDELKEIA 152
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 2197-2372 4.36e-20

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: 90.21  E-value: 4.36e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    2197 LAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIaesnCPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQVALtS 2276
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDI----GPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKL-G 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    2277 KQQSLETAMSFVARNTFKRVRNGFLM-RKVAVFFSN-TPTRASPQLREAVLKLSDAGITP--LFLTRQEDRQLINALQIN 2352
Cdd:smart00327   77 GGTNLGAALQYALENLFSKSAGSRRGaPKVVILITDgESNDGPKDLLKAAKELKRSGVKVfvVGVGNDVDEEELKKLASA 156

                           170       180
                    ....*....|....*....|
gi 55743106    2353 NTAVGHALVLPAgRDLTDFL 2372
Cdd:smart00327  157 PGGVYVFLPELL-DLLIDLL 175
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 823-973 5.34e-20

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: 89.55  E-value: 5.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  823 DVVFLLDGSEGVRSG-FPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPN 901
Cdd:cd00198    2 DIVFLLDVSGSMGGEkLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGTN 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55743106  902 TGAALEFVLRNILvssagSRITEGVPQLLIVLT---ADRSGDDVRNPSVVVKRGGAVPIGIGIGN-ADITEMQTIS 973
Cdd:cd00198   82 IGAALRLALELLK-----SAKRPNARRVIILLTdgePNDGPELLAEAARELRKLGITVYTIGIGDdANEDELKEIA 152
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2412-2589 8.97e-20

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: 88.89  E-value: 8.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2412 IDMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDPkasqhfARVAVVQHAPSesvdnasmppVKVEFSLTDYGSKEK 2491
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDK------TRVGLVQYSDD----------VRVEFSLNDYKSKDD 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2492 LVDFLsRGMTQLQGTR-ALGSAIEYTIENVF-ESAPNPRDLKIVVLMLTGEvpEQQLEEAQRVILQAKCKGYFFVVLGIG 2569
Cdd:cd01450   65 LLKAV-KNLKYLGGGGtNTGKALQYALEQLFsESNARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVG 141

                        170       180
                 ....*....|....*....|
gi 55743106 2570 rKVNIKEVYTFASEPNDVFF 2589
Cdd:cd01450  142 -PADEEELREIASCPSERHV 160
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 239-399 1.13e-19

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: 88.61  E-value: 1.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  239 DIVFLVDGSSALGlANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYA--DTVRPEFYFNTHPTKREVITAVRKMKPLDGSA 316
Cdd:cd01476    2 DLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  317 lYTGSALDFVrNNLFTSSAGYRaaEGIPKLLVLITGGKSLDEISQPAQELKR---SSIMAFAIGNKGA-DQAELEEIAFD 392
Cdd:cd01476   81 -ATGAAIEVA-LQQLDPSEGRR--EGIPKVVVVLTDGRSHDDPEKQARILRAvpnIETFAVGTGDPGTvDTEELHSITGN 156


                 ....*..
gi 55743106  393 SSLVFIP 399
Cdd:cd01476  157 EDHIFTD 163
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 2413-2602 1.81e-19

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: 88.28  E-value: 1.81e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    2413 DMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDpkasqhFARVAVVQHApsesvDNasmppVKVEFSLTDYGSKEKL 2492
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPD------GDRVGLVTFS-----DD-----ARVLFPLNDSRSKDAL 64

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    2493 VDFLSRGMTQLQGTRALGSAIEYTIENVFESAPNPR-DLKIVVLMLTGEVPEQQLEEAQRVILQAKCKGYFFVVLGIGRK 2571
Cdd:smart00327   65 LEALASLSYKLGGGTNLGAALQYALENLFSKSAGSRrGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGND 144

                           170       180       190
                    ....*....|....*....|....*....|.
gi 55743106    2572 VNIKEVYTFASEPNDVFFKLVDKSTELNEEP 2602
Cdd:smart00327  145 VDEEELKKLASAPGGVYVFLPELLDLLIDLL 175
Kunitz_actitoxin-like cd22633
Kunitz-type actitoxins such as Anemonia viridis U-actitoxin-Avd3l, and similar proteins; This ...
 2905-2956 2.27e-18

Kunitz-type actitoxins such as Anemonia viridis U-actitoxin-Avd3l, and similar proteins; This model includes the Kunitz-type actitoxins such as Anemonia viridis U-actitoxin-Avd3l (also called U-AITX-Avd3l or AsKC9), Anthopleura elegantissima KappaPI-actitoxin-Ael3a (also called KappaPI-AITX-Ael3a or Kunitz-type serine protease inhibitor APEKTx1) and Anthopleura aff. xanthogrammica PI-actitoxin-Axm2b (also called PI-AITX-Axm2b or Kunitz-type proteinase inhibitor AXPI-II). U-AITX-Avd3l and KappaPI-AITX-Ael3a are dual-function toxins that inhibit both the serine protease trypsin and voltage-gated potassium channels Kv1.2/KCNA2. These proteins are similar to Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor) that shows an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438676  Cd Length: 55  Bit Score: 81.04  E-value: 2.27e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 55743106 2905 ICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22633    4 ICLLPKDVGGCRARFPRYYYNSSTRRCEKFRYGGCGGNANNFHTLEECEKVC 55
Kunitz_boophilin_2-like cd22600
second Kunitz domain of Rhipicephalus microplus boophilin and similar proteins; This group ...
 2906-2958 4.50e-18

second Kunitz domain of Rhipicephalus microplus boophilin and similar proteins; This group includes venom serine protease inhibitors such as Rhipicephalus microplus and Ixodes scapularis boofilin, among others. Boophilin prevents blood clot formation to allow successful feeding and digestion through its inhibition activity of thrombin and other host anticoagulating factors like kallikrein, coagulation factor VII, or plasmin; it interacts with the host thrombin and trypsin. The structures of these domains are similar to those of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds. Rhipicephalus microplus boophilin contains two Kunitz domains; this model represents the second repeat.


Pssm-ID: 438643  Cd Length: 54  Bit Score: 80.16  E-value: 4.50e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2906 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVCAP 2958
Cdd:cd22600    2 CKPAAESGLCAAYLERWFFNVTTGACETFVYGGCGGNANNYKSQEECELACLR 54
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1027-1183 4.87e-18

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: 83.99  E-value: 4.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1027 DVVFLIDGSQSAGPEFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPK--VEFLLNAHSSKDEVQNAVQRLRPKGGrQI 1104
Cdd:cd01476    2 DLLFVLDSSGSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGG-TT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1105 NVGNALEYVSrNIFKRPLGSRieEGVPQFLVLISSGKSDDEVDDPAVELK-QFGVAPFTIAR----NADQEELVKISLSP 1179
Cdd:cd01476   81 ATGAAIEVAL-QQLDPSEGRR--EGIPKVVVVLTDGRSHDDPEKQARILRaVPNIETFAVGTgdpgTVDTEELHSITGNE 157


                 ....
gi 55743106 1180 EYVF 1183
Cdd:cd01476  158 DHIF 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1432-1590 1.14e-17

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: 82.61  E-value: 1.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1432 ADIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRHA 1511
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1512 NTKVGLEHLRVNHFvpeagSRLDQRVPQIAFVITGGKS---VEDAQDVSLALTQRGVKVFAVGVRN-IDSEEVGKIASNS 1587
Cdd:cd00198   81 NIGAALRLALELLK-----SAKRPNARRVIILLTDGEPndgPELLAEAARELRKLGITVYTIGIGDdANEDELKEIADKT 155


                 ...
gi 55743106 1588 ATA 1590
Cdd:cd00198  156 TGG 158
Kunitz_eppin cd22611
Kunitz domain of epididymal protease inhibitor eppin and similar proteins; This subfamily ...
 2904-2956 1.36e-17

Kunitz domain of epididymal protease inhibitor eppin and similar proteins; This subfamily includes the Kunitz inhibitor domain protein eppin (also called Cancer/testis antigen 71 or CT71, epididymal protease inhibitor, protease inhibitor WAP7, serine protease inhibitor-like with Kunitz and WAP domains 1, or WAP four-disulfide core domain protein 7) as well as WAP four-disulfide core domain proteins 6A and 6B in mice, and similar proteins. Eppin is a serine protease inhibitor that plays an essential role in male reproduction and fertility. It modulates the hydrolysis of seminal fluid protein semenogelin 1 (SEMG1) by the serine protease kallikrein-related peptidase 3 (KLK3, PSA), provides antimicrobial protection for spermatozoa in the ejaculate coagulum, and binds SEMG1, thereby inhibiting sperm motility. Thus, eppin could potentially be used as a target for male contraception. These domains are similar to Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor) that shows an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438654  Cd Length: 57  Bit Score: 78.99  E-value: 1.36e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2904 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22611    1 DVCSLPKESGPCMAYFPRWWYDKETNTCSKFIYGGCQGNNNNFQSEAICQNIC 53
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 631-784 2.30e-17

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: 83.59  E-value: 2.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  631 DILFLFDGSANLVGQ-FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMK-IKTGKAl 708
Cdd:cd01475    4 DLVFLIDSSRSVRPEnFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEyLETGTM- 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55743106  709 nLGYALDYAQRYIFVKSAGSR-IEDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSP 784
Cdd:cd01475   83 -TGLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEP 158
Kunitz_boophilin_1-like cd22599
first Kunitz domain of Rhipicephalus microplus boophilin and similar proteins; This group ...
 2905-2957 4.40e-17

first Kunitz domain of Rhipicephalus microplus boophilin and similar proteins; This group includes venom serine protease inhibitors such as Rhipicephalus microplus and Ixodes scapularis boofilin, among others. Boophilin prevents blood clot formation to allow successful feeding and digestion through its inhibition activity of thrombin and other host anticoagulating factors like kallikrein, coagulation factor VII, or plasmin; it interacts with the host thrombin and trypsin. The structures of these domains are similar to those of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds. Rhipicephalus microplus boophilin contains two Kunitz domains; this model represents the first repeat.


Pssm-ID: 438642  Cd Length: 61  Bit Score: 77.51  E-value: 4.40e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2905 ICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVCA 2957
Cdd:cd22599    5 ICRLPADEGICRALIPRFYFNTETGQCTEFIYGGCGGNENNFETIEECEKACG 57
Kunitz_SCI-I-like cd22634
chymotrypsin inhibitor SCI-I_III-like; This model includes the Kunitz-type chymotrypsin ...
 2905-2956 4.96e-17

chymotrypsin inhibitor SCI-I_III-like; This model includes the Kunitz-type chymotrypsin inhibitors SCI-III and SCI-I, and similar proteins in insects. SCI-III and SCI-I inhibit chymotrypsin, avoiding the accidental chymotrypsin-mediated activation of prophenoloxidase. This enzyme is required by the insect immune system to produce melanin which is used to engulf foreign objects. This subfamily also includes Kunitz-type male accessory gland peptide with protease inhibitory activity, synthesized and secreted by male accessory glands of Drosophila funebris; it may play a role as an acrosin inhibitor involved in reproduction. These proteins are similar to Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor) that shows an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438677  Cd Length: 57  Bit Score: 77.17  E-value: 4.96e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 55743106 2905 ICKLP-----KDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22634    1 ICGQPhslggGDGISCFAYIPSWSYNPDKNECEEFIYGGCGGNDNRFSTKAECEQKC 57
Kunitz_huwentoxin cd22598
Kunitz-type toxin huwentoxin-XI; This model contains Kunitz-type serine protease inhibitor ...
 2904-2957 7.46e-17

Kunitz-type toxin huwentoxin-XI; This model contains Kunitz-type serine protease inhibitor huwentoxin-XI, including U15-theraphotoxin-Hs1g (also called U15-TRTX-Hs1g or Huwentoxin HW11c39), and kappaPI-theraphotoxin-Hs1a (also called KappaPI-TRTX-Hs1a or Huwentoxin-HW11g8). Huwentoxin-XI is a bifunctional toxin that inhibits both serine proteases (trypsin) and voltage-gated potassium channels (Kv) via surfaces displayed on opposite faces of the toxin. The structures of these domains are similar to those of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438641  Cd Length: 53  Bit Score: 76.57  E-value: 7.46e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 55743106 2904 DICKLPKDEGTCRDFILKWYYDPNTksCARFWYGGCGGNENKFGSQKECEKVCA 2957
Cdd:cd22598    1 DTCRLPSDRGRCKASFERWYFNGRT--CAKFIYGGCGGNDNKFPTQEACMKRCA 52
Kunitz_TFPI1_2-like cd22614
Kunitz protease inhibitor (KPI) domain 2 (KPI-2 or K2) of tissue factor pathway inhibitor ...
 2904-2956 1.01e-16

Kunitz protease inhibitor (KPI) domain 2 (KPI-2 or K2) of tissue factor pathway inhibitor (TFPI); This model represents the second Kunitz-type domain (K2 or KPI-2) of tissue factor pathway inhibitor (TFPI or TFPI1), also known as extrinsic pathway inhibitor (EPI) or lipoprotein-associated coagulation inhibitor (LACI). TFPI down-regulates the extrinsic coagulation pathway via inhibition of activated factor X (FXa or Xa) and FVIIa (VIIa). It inhibits activated FXa via a "slow-tight binding mechanism", i.e. rapid formation of a loose FXa-TFPI complex that then slowly isomerizes to a tight FXa-TFPI* complex. Subsequent inhibition of FVIIa is facilitated by the presence of tissue factor (TF) and FXa, which together rapidly and efficiently form a quaternary FXa-TFPI-TF-FVIIa complex in which the activity of FXa and FVIIa are inhibited. TFPI consists of 3 Kunitz-type protease inhibitor (KPI) domains in a tandem arrangement; the K2 domain is exposed on functionally active TFPI pools in circulation in blood, in platelets, and attached to the endothelium. While the K1 (or KPI-1) domain of TFPI has been shown to bind and inhibit FVIIa, the K2 domain inhibits FXa by binding directly to the active site and forming a FXa:TFPI complex. A close interaction between the TFPI K2 domain and the FXa active site is essential for the FXa inhibitory action of TFPI and for the formation of an inactive TF/FVIIa/FXa/TFPI complex which then prevents FXa generation. Thus, blockage of K2 would prevent TFPI binding to both FXa and FVIIa/TF, and fully abolish TFPI inhibition of the coagulation cascade. The structure of the K2 domain is similar to those of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438657  Cd Length: 56  Bit Score: 76.20  E-value: 1.01e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2904 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22614    3 DFCFLEEDPGICRGLITRYFYNNQSKQCERFKYGGCLGNQNNFESLEECQNTC 55
Kunitz_TFPI1_TFPI2_3-like cd22615
Kunitz protease inhibitor (KPI) domain 3 (KPI-3 or K3) of tissue factor pathway inhibitor ...
 2905-2956 1.18e-16

Kunitz protease inhibitor (KPI) domain 3 (KPI-3 or K3) of tissue factor pathway inhibitor (TFPI) and TFPI2, and similar proteins; This model represents the third Kunitz-type domain (K3 or KPI-3) of tissue factor pathway inhibitor (TFPI or TFPI1), also known as extrinsic pathway inhibitor (EPI) or lipoprotein-associated coagulation inhibitor (LACI), and of TFPI2 (or TFPI-2). TFPI1 down-regulates the extrinsic coagulation pathway via inhibition of activated factor X (FXa or Xa) and FVIIa (VIIa). It inhibits activated FXa via a "slow-tight binding mechanism", i.e. rapid formation of a loose FXa-TFPI1 complex that then slowly isomerizes to a tight FXa-TFPI1* complex. Subsequent inhibition of FVIIa is facilitated by the presence of tissue factor (TF) and FXa, which together rapidly and efficiently form a quaternary FXa-TFPI1-TF-FVIIa complex in which the activity of FXa and FVIIa are inhibited. TFPI1 consists of 3 Kunitz-type protease inhibitor (KPI) domains in a tandem arrangement; while the K1 domain of TFPI has been shown to bind and inhibit FVIIa and the K2 domain similarly inhibits FXa, the K3 domain has no known inhibitory function. However, Protein S, which functions as a cofactor for TFPI to efficiently enhance TFPI inhibition of FXa and FXa activated TF-VIIa, is dependent on direct interactions with two important residues within K3, a Glutamate and an Arginine. This model also includes TFPI2 Kunitz domain 3 (KD3). TFPI2 exhibits inhibitory activity primarily toward trypsin, plasmin, and factor VIIa (FVIIa)/tissue factor (TF) via its KD1. It is believed to be the major inhibitor of plasmin in the extracellular matrix (ECM) but has little inhibitory activity toward urokinase-type plasminogen activator, tissue-type plasminogen activator, or thrombin. While TFPI2 specifically inhibits the proteases via the P1 arginine residue in KD1, domains KD2 and KD3 appear to have no discernible inhibitory activity and may serve to bind to nearby proteins to localize TFPI2 in the ECM. The structure of this domain is similar to that of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438658  Cd Length: 54  Bit Score: 76.18  E-value: 1.18e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 55743106 2905 ICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22615    3 FCLSPKDEGLCSASVTRYYYNSATKTCEPFNYTGCGGNNNNFTSKKDCLRVC 54
Kunitz_textilinin-like cd22594
venom Kunitz-type proteins such as textilinin, BF9 and PILP; This group includes toxins ...
 2906-2957 1.40e-16

venom Kunitz-type proteins such as textilinin, BF9 and PILP; This group includes toxins isolated from snake venoms, such as textilinin, vestiginin, spermatin, mulgin, venom basic protease inhibitor IX (BF9), and protease inhibitor-like protein (PILP), among others. Pseudonaja textilis textilinin-1 is a Kunitz-type serine protease inhibitor that binds to and blocks the activity of a range of serine proteases, including plasmin and trypsin. Ability of testilinin to inhibit plasmin, a protease involved in fibrinolysis, raises the possibility that it may be used as an alternative to aprotinin (Trasylol), which is a systemic antibleeding agent in surgery. Also included is the Bungarus fasciatus fraction IX (BF9), a chymotrypsin inhibitor that binds chymotrypsin but not trypsin. Protease inhibitor-like proteins PILP-1 and PILP-2 show weak binding and inhibition of matrix metalloproteinase-2 (MMP-2) and show an activity in inhibiting migration and invasion of neuroblastoma; they do not inhibit chymotrypsin or trypsin. The structures of these toxins are similar to those of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438637  Cd Length: 56  Bit Score: 75.82  E-value: 1.40e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 55743106 2906 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVCA 2957
Cdd:cd22594    5 CELPADPGPCNAYKPAFYYNPASHKCLEFIYGGCGGNANNFKTIDECHRTCA 56
Kunitz_bikunin_2-like cd22597
second Kunitz domain of bikunin and similar proteins; This subfamily includes the C-terminal ...
 2904-2956 2.52e-16

second Kunitz domain of bikunin and similar proteins; This subfamily includes the C-terminal domain of bikunin (also known as inter-alpha-trypsin inhibitor light chain (ITI-LC) or urinary trypsin inhibitor), a plasma protease inhibitor, that is associated with inflammation and stabilizes the extracellular matrix. Bikunin is encoded together with alpha-1-microglobulin (A1M) by an alpha-1-microglobulin/bikunin precursor (AMBP) gene that is tightly controlled by several hepatocyte-enriched nuclear (HEN) factors, and cleaved by a furin-like protease that releases the two mature molecules. Bikunin is a Kunitz-type serine protease inhibitor, found in vertebrate serum and urine, modified by a chondroitin sulfate (CS) chain. The structures of these toxins are similar to that of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds. Bikunin contains two Kunitz domains; this model represents the second repeat.


Pssm-ID: 438640  Cd Length: 55  Bit Score: 75.11  E-value: 2.52e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2904 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22597    2 AACRLPIVPGPCKGFVDLWAFDAVQGKCVPFSYGGCQGNGNKFYSEKECEEYC 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2111-2165 3.12e-16

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: 74.84  E-value: 3.12e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 55743106   2111 GYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAGPKGNRG 2165
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Kunitz_WFIKKN_2-like cd22606
second Kunitz domain of WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing proteins; ...
 2905-2956 5.97e-16

second Kunitz domain of WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing proteins; This subfamily includes WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing protein 1 (WFIKKN1, WFKN1), WFIKKN2 (WFKN2), and similar proteins. WFIKKN proteins are protease inhibitors that contain two distinct Kunitz-type protease inhibitor domains. They may have serine protease- and metalloprotease-inhibitor activity. This model represents the second Kunitz (KU2) domain, which has been shown to inhibit trypsin, but not chymotrypsin, elastase, plasmin, pancreatic kallikrein, lung tryptase, plasma kallikrein, thrombin, urokinase or tissue plasminogen activator. However, the inhibition constant of this domain for bovine trypsin is about five orders of magnitudes lower than that of bovine pancreatic trypsin inhibitor (BPTI) for trypsin. This could be due to unfavorable side-chain conformation of a tryptophan at P2' site which is incompatible with a trypsin complex; typical trypsin inhibitors of the Kunitz family feature a tyrosine residue or other less bulky residues at this site. The structure of KU2 is similar to those of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438649  Cd Length: 53  Bit Score: 73.93  E-value: 5.97e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 55743106 2905 ICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22606    1 ICSLPAVQGPCKAWEPRWAYNSLLKQCQSFVYGGCEGNENNFESKEACEDAC 52
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 433-587 1.13e-15

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: 77.05  E-value: 1.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  433 DIIFLLDGSANVGKTnFPYVRDFVMNLVNSLDIGNDNIRVGLVQFS--DTPVTEFSLNTYQTKSDILGHLRQLQLQGGSg 510
Cdd:cd01476    2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGT- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  511 LNTGSALSYVyANHFTEAGGSriREHVPQLLLLLTAGQSEDSYLQAANALTR-AGILTFCVGA---SQANKAELEQIAFN 586
Cdd:cd01476   80 TATGAAIEVA-LQQLDPSEGR--REGIPKVVVVLTDGRSHDDPEKQARILRAvPNIETFAVGTgdpGTVDTEELHSITGN 156


                 .
gi 55743106  587 P 587
Cdd:cd01476  157 E 157
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2108-2164 1.16e-15

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: 73.30  E-value: 1.16e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 55743106   2108 GFPGYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAGPKGNR 2164
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Kunitz_SmCI_3-like cd22603
third Kunitz domain of Carboxypeptidase Inhibitor SmCI and similar domains; This group ...
 2904-2956 1.43e-15

third Kunitz domain of Carboxypeptidase Inhibitor SmCI and similar domains; This group includes Sabellastarte magnifica carboxypeptidase inhibitor (SmCI), Bombyx mori cocoon shell-associated trypsin inhibitor (CSTI), Bombus terrestris Kunitz-type serine protease inhibitor Bt-KTI, and similar domains. SmCI is a tri-domain BPTI-Kunitz inhibitor capable of inhibiting serine proteases and A-like metallocarboxypeptidases. While the BPTI-Kunitz family of proteins includes voltage gated channel blockers and inhibitors of serine proteases, SmCI is the only BPTI-Kunitz protein capable of inhibiting metallocarboxypeptidases. Binding studies show that SmCI is able to bind three trypsin molecules under saturating conditions, but only one elastase interacts with the inhibitor. Additionally, SmCI can bind serine proteases and carboxypeptidases at the same time (at least in the ratio 1:1:1), thus becoming the first protease inhibitor that simultaneously blocks these two mechanistic classes of enzymes. CSTI and Bt-KTI are single Kunitz domain proteins that inhibit trypsin; in addition, Bt-KTI also inhibits plasmin. This model contains the third Kunitz domain of SmCI which has a structure similar to those of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438646  Cd Length: 53  Bit Score: 72.85  E-value: 1.43e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2904 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22603    1 EDCLLPSETGPCKGSFPRYYYDKETGKCKEFIYGGCQGNANNFETKEECERAC 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2105-2160 1.49e-15

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: 72.91  E-value: 1.49e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 55743106   2105 GERGFPGYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAGP 2160
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Kunitz_PPTI-like cd22608
Pseudocerastes persicus trypsin inhibitor (PPTI), Kunitz-type serine protease inhibitor ...
 2904-2956 3.88e-15

Pseudocerastes persicus trypsin inhibitor (PPTI), Kunitz-type serine protease inhibitor bitisilin, and similar proteins; This group contains Pseudocerastes persicus trypsin inhibitor (PPTI), Bitis gabonica Kunitz-type serine protease inhibitor bitisilin-1 (BG-11), -2 (BG-15) and -3 (two-Kunitz protease inhibitor), Oxyuranus scutellatus scutellatus taicatoxin, and serine protease inhibitor component (TSPI, also called venom protease inhibitor 1 or venom protease inhibitor 2), among others. PPTI from P. persicus venom shows inhibitory effect against trypsin proteolytic activity and has similarities to dendrotoxins (DTXs), with corresponding functionally important residues. Studies have shown the ability of PPTI to inhibit voltage-gated potassium channels, and consequently have dual functionality. Bitilisins 1, 2, and 3 are serine protease inhibitors expressed in snake venom glands; bitsilin-3 consists of two Kunitz protease inhibitor domains. Taicatoxin inhibits trypsin, tissue kallikrein, elastase, plasmin and factor Xa, and is also known to block the voltage-dependent L-type calcium channels from the heart, and the small conductance calcium-activated potassium channels (KCa) in chromaffin cells and in the brain. The structures of these Kunitz-type proteins are similar to other Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438651  Cd Length: 54  Bit Score: 71.56  E-value: 3.88e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2904 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22608    2 KFCYLPADPGPCKAYIPRFYYNSASNKCQQFIYGGCKGNANNFETKDECRYTC 54
Kunitz_conkunitzin cd22593
conkunitzin-S1 and -S2, and similar proteins; This model includes Kunitz-type conkunitzin-S1 ...
 2906-2956 5.32e-15

conkunitzin-S1 and -S2, and similar proteins; This model includes Kunitz-type conkunitzin-S1 (Cs1) and -S2 (Cs2). Conkunitzins are pore-modulating toxins that block voltage-dependent potassium channels (Kvs) by exploiting inherent slow inactivation to block K+ channels. Cs1 binds to the channel turrets and disrupts the structural water hydrogen-bonding network, exposing the peripheral water pockets of ion channels and triggering an asymmetric collapse of the pore. Conus bullatus conkunitzin-B1, expressed in the venom duct, specifically blocks voltage-activated potassium channels (Kv) of the Shaker family. Members of this subfamily contain 2 disulfide bonds instead of the 3 present in most Kunitz domain proteins.


Pssm-ID: 438636  Cd Length: 51  Bit Score: 71.10  E-value: 5.32e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 55743106 2906 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22593    1 CSLPLDEGSGNSSLTRWYYDPKKGQCKPFTYKGKGGNENNFLTKEDCEETC 51
Kunitz_ELP-like cd22632
early lactation protein (ELP), colostrum trypsin inhibitor (CTI), and similar proteins; This ...
 2904-2956 9.18e-15

early lactation protein (ELP), colostrum trypsin inhibitor (CTI), and similar proteins; This model includes the Kunitz-type proteins, colostrum trypsin inhibitor (CTI, also called colostrum BPI) and early lactation protein (ELP). In marsupials, the ELP gene is expressed in the mammary gland and the protein is secreted into milk during early lactation. Mature ELP shares approximately 55.4% similarity with the colostrum-specific bovine CTI protein. Marsupial ELP and eutherian CTI both have a single Kunitz domain and are secreted only during the early lactation phases, suggesting that this protein may have an important role in the immunologically immature young of these species. These proteins are similar to Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor) that shows an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438675  Cd Length: 55  Bit Score: 70.54  E-value: 9.18e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2904 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22632    2 SLCQLPPARGPCRSNILRYFYNSTSRECEPFIYGGCNGNANNFETVEMCLRTC 54
Kunitz_HAI1_1-like cd22623
Kunitz domain 1 of hepatocyte growth factor activator inhibitor-1 (HAI-1); This model includes ...
 2906-2959 1.13e-14

Kunitz domain 1 of hepatocyte growth factor activator inhibitor-1 (HAI-1); This model includes Kunitz domain 1 (KD1) of hepatocyte growth factor activator inhibitor type 1 (HAI1 or HAI-1, also known as Kunitz-type protease inhibitor 1), a membrane-bound multidomain protein essential to the integrity of the basement membrane during placental development. HAI-1 contains an extracellular region and several internal domains that include two Kunitz domains separated in sequence but spatially closed to each other, and their interdomain interactions have evolved to stimulate the inhibitory activity of an integrated Kunitz. KD1, the major inhibitory domain of HAI-1, is involved in auto-inhibition of the extracellular region via steric blockage of its active site in the HAI-1 compact tertiary structure; presence of the target protease causes changes in the HAI-1 structure to an extended conformation. HAI-1 has been shown to inhibit several serine proteases such as matripase, hepsin, trypsin, hepatocyte growth factor activator (HGFA), and prostasin. It is also important in maintaining postnatal homeostasis in many tissues, including keratinization of the epidermis, hair development, colonic epithelium integrity, proliferation and cell fate of neural progenitor cells, and tissue injury and repair. The interaction between HAI-1 and matriptase is critical for tissue morphogenesis and cellular biology. HAI-1:matriptase ratio imbalance results in tumorigenesis; slight overexpression of matriptase relative to HAI-1 causes spontaneous squamous cell carcinoma, a phenotype that can be effectively reversed back to wild type by additional expression of HAI-1, indicating the need for a tight functional relationship between the two to maintain homeostasis. The structures of these domains are similar to those of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438666  Cd Length: 59  Bit Score: 70.65  E-value: 1.13e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 55743106 2906 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVCAPV 2959
Cdd:cd22623    6 CLAPKKVGPCRGSFPRWHYNAASGKCEEFVFGGCKGNKNNYLSEEECLSACRGV 59
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 35-195 1.92e-14

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: 73.59  E-value: 1.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   35 ADIIFLIDGSNNTGSVnFAVILDFLVNLLEKLPIGTQQIRVGVVQFSDEPRTM--FSLDTYSTKAQVLGAVKALGFAGGe 112
Cdd:cd01476    1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRvrFNLPKHNDGEELLEKVDNLRFIGG- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  113 LANIGLALDFVVeNHFTRAGGSRveEGVPQVLVLISAGPSSDEIRYG---VVALKQASVFSFGLG-AQAASRAELQHIAT 188
Cdd:cd01476   79 TTATGAAIEVAL-QQLDPSEGRR--EGIPKVVVVLTDGRSHDDPEKQariLRAVPNIETFAVGTGdPGTVDTEELHSITG 155


                 ....*..
gi 55743106  189 DDNLVFT 195
Cdd:cd01476  156 NEDHIFT 162
Kunitz_TFPI1_1-like cd22613
Kunitz protease inhibitor (KPI) domain 1 (KPI-1 or K1) of tissue factor pathway inhibitor ...
 2905-2956 2.52e-14

Kunitz protease inhibitor (KPI) domain 1 (KPI-1 or K1) of tissue factor pathway inhibitor (TFPI); This model represents the first Kunitz-type domain (K1 or KPI-1) of tissue factor pathway inhibitor (TFPI or TFPI1), also known as extrinsic pathway inhibitor (EPI) or lipoprotein-associated coagulation inhibitor (LACI). TFPI down-regulates the extrinsic coagulation pathway via inhibition of activated factor X (FXa or Xa) and FVIIa (VIIa). It inhibits activated FXa via a "slow-tight binding mechanism", i.e. rapid formation of a loose FXa-TFPI complex that then slowly isomerizes to a tight FXa-TFPI* complex. Subsequent inhibition of FVIIa is facilitated by the presence of tissue factor (TF) and FXa, which together rapidly and efficiently form a quaternary FXa-TFPI-TF-FVIIa complex in which the activity of FXa and FVIIa are inhibited. TFPI consists of 3 Kunitz-type protease inhibitor (KPI) domains in a tandem arrangement; The K1 domain of TFPI has been shown to bind and inhibit FVIIa while the K2 domain similarly inhibits FXa. Small peptide blocking inhibition of FXa and TF-FVIIa by TFPI shows that domain K1 is not only important for FVIIa inhibition but also for FXa inhibition, i.e. for the transition of the loose to the tight FXa-TFPI complex. The structure of the K1 domain is similar to those of other Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438656  Cd Length: 55  Bit Score: 69.31  E-value: 2.52e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 55743106 2905 ICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22613    3 FCAFKADDGPCKAIMKRFFFNIFTRQCEEFIYGGCEGNENRFETLEECKKTC 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2099-2155 4.34e-14

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: 68.67  E-value: 4.34e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 55743106   2099 GRRGKKGERGFPGYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYP 2155
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Kunitz_BmTI-like cd22604
Kunitz-type serine protease inhibitor 6 (BmTI-6), A (BmTI-A), and similar proteins; This group ...
 2901-2956 4.61e-14

Kunitz-type serine protease inhibitor 6 (BmTI-6), A (BmTI-A), and similar proteins; This group includes Kunitz-type serine protease inhibitors 6 (BmTI-6) and A (BmTI-A), both of which inhibit bovine trypsin, bovine chymotrypsin, human plasmin, human plasma kallikrein and human neutrophil elastase, but not bovine thrombin, human factor Xa or porcine pancreatic kallikrein. They may play a role in blocking blood coagulation during the larvae fixation on cattle. This subfamily also includes Rhipicephalus microplus protease inhibitor carrapatin. These proteins are similar to Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor) that shows an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438647 [Multi-domain]  Cd Length: 56  Bit Score: 68.63  E-value: 4.61e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 55743106 2901 TETDICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22604    1 DFEKQCSPTADSGPCFAYFPMWWYNVKTGQCEEFIYGGCQGNDNRYETEEECEKTC 56
Kunitz_ABPP-like cd22607
Kunitz domain found in the amyloid-beta precursor protein (ABPP) subfamily; This subfamily ...
 2905-2956 6.00e-14

Kunitz domain found in the amyloid-beta precursor protein (ABPP) subfamily; This subfamily includes the amyloid-beta precursor protein (ABPP, also called APP, APPI, Alzheimer disease amyloid protein, amyloid-beta A4 protein, cerebral vascular amyloid peptide (CVAP), protease nexin II (PN2)), as well as amyloid-like protein 2 (APLP2, also called amyloid protein homolog or APPH), among others. ABPP/APPI is an inhibitor of serine proteases such as anionic and cationic trypsins. For example, APPI-4M is a variant that specifically inhibits Kallikrein (KLK)-related peptidase 6 (KLK6), which is highly upregulated in several types of cancer where its increased activity promotes cancer invasion and metastasis. Amyloid-like protein 2 (APLP2) inhibits trypsin, chymotrypsin, plasmin, factor XIA, and plasma and glandular kallikrein, and may play a role in the regulation of hemostasis. Proteins in this subfamily contain a single Kunitz domain, with a structure similar to those of other Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438650  Cd Length: 52  Bit Score: 68.22  E-value: 6.00e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 55743106 2905 ICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22607    1 VCSEQAETGPCRAMMPRWYFDVTEGKCAPFIYGGCGGNRNNFESEEYCMAVC 52
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 2412-2597 7.33e-14

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: 73.57  E-value: 7.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2412 IDMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDPkasqhfARVAVVQHAPSesvdnasmppVKVEFSLTDYGSKEK 2491
Cdd:cd01475    3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDA------TRVGLVQYSST----------VKQEFPLGRFKSKAD 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2492 LVDFLSRGMTQLQGTRAlGSAIEYTIENVFESA----PNPRDLKIVVLMLTGEVPEQQLEEAQRvilQAKCKGYFFVVLG 2567
Cdd:cd01475   67 LKRAVRRMEYLETGTMT-GLAIQYAMNNAFSEAegarPGSERVPRVGIVVTDGRPQDDVSEVAA---KARALGIEMFAVG 142

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 55743106 2568 IGRkVNIKEVYTFASEPND--VF----FKLVDKSTE 2597
Cdd:cd01475  143 VGR-ADEEELREIASEPLAdhVFyvedFSTIEELTK 177
Kunitz_HAI2_1-like cd22621
Kunitz-type domain 1 (KD1) of hepatocyte growth factor activator inhibitor type 2 (HAI-2), and ...
 2904-2956 8.30e-14

Kunitz-type domain 1 (KD1) of hepatocyte growth factor activator inhibitor type 2 (HAI-2), and similar proteins; This model includes the Kunitz domain 1 (KD1) of hepatocyte growth factor activator inhibitor type 2 (HAI-2 or HAI2, also known as placental bikunin or Kunitz-type protease inhibitor 2). HAI-2 is composed of two Kunitz domains that strongly inhibit many serine proteases with sub-nanomolar affinities. HAI-2 Kunitz domain 1 (KD1) has been found to be the domain responsible for inhibition of hepatocyte growth factor (HGF) activator; activated HGF/scatter factor (HGF/SF) binds to its receptor tyrosine kinase MET to induce dimerization and initiate phosphorylation cascades leading to comprehensive cellular changes that, in the deregulated context of cancer, drive malignant transformation and progression. HAI-2 has been found to be a natural tumor suppressor in renal cell carcinoma, breast cancer and prostate cancer; its loss leads to tumor growth and progression in part due to increased MET signaling. HAI-2 is also a specific substrate for mesotrypsin, which is up-regulated with progression in prostate cancers and shown to contribute to invasion and metastasis; these activities of mesotrypsin may in part be mediated through cleavage and inactivation of HAI-2, resulting in increases in HGF/SF activation and MET signaling. HAI-2 is a physiological inhibitor of hepsin and matriptase, two type II transmembrane serine proteases that, like HGF activator, can convert latent pro-HGF/SF into the two-chain active signaling heterodimer. The structures of these KD1 domains are similar to those of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438664  Cd Length: 53  Bit Score: 67.88  E-value: 8.30e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2904 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22621    1 DFCHLPKVVGRCRASFPRWWYNATSQSCQEFIFGGCKGNLNNFLSEQECLQKC 53
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 630-781 9.75e-14

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: 71.44  E-value: 9.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  630 RDILFLFDGSANLVGQ-FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKAL 708
Cdd:cd00198    1 ADIVFLLDVSGSMGGEkLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55743106  709 NLGYALDYAQRYIFvksagSRIEDGVLQFLVLLVAGRSSDRVDGP---ASNLKQSGVVPFIFQAKN-ADPAELEQIV 781
Cdd:cd00198   81 NIGAALRLALELLK-----SAKRPNARRVIILLTDGEPNDGPELLaeaARELRKLGITVYTIGIGDdANEDELKEIA 152
Kunitz_ixolaris_2 cd22626
Kunitz-type domain 2 (K2) of Ixolaris, and similar proteins; This model includes the second ...
 2906-2956 1.09e-13

Kunitz-type domain 2 (K2) of Ixolaris, and similar proteins; This model includes the second Kunitz-type domain (K2) of ixolaris from the venomous organism Conus striatus. Ixolaris is a potent tick salivary anticoagulant that binds coagulation factor Xa (FXa) and zymogen FX, and forms a quaternary tissue factor (TF)/FVIIa/FX(a)/Ixolaris inhibitory complex. It blocks TF-induced coagulation and PAR2 (proteinase-activated receptor 2) signaling, and prevents thrombosis, tumor growth, and immune activation. Ixolaris consists of 2 Kunitz domains (K1 and K2), both of which recognize the heparin-binding (pro)exosite (HBE) on FX. This model contains K2, an extraordinarily dynamic domain that encompasses several residues involved in FX binding. Its backbone plasticity is critical for ixolaris biological activity. This domain contains 2 disulfide bonds instead of the 3 typical of Kunitz domain proteins.


Pssm-ID: 438669  Cd Length: 51  Bit Score: 67.49  E-value: 1.09e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 55743106 2906 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22626    1 CSLELDYGVGKAYIPRWYFNTSNARCEMFIFGGIGGNKNNFETLEECKKTC 51
Kunitz_KTT cd22620
scorpion venom Kunitz-type toxin (KTT) such as LmKTT-1a, BmKTT-1, and BmKTT-2; This model ...
 2906-2958 1.83e-13

scorpion venom Kunitz-type toxin (KTT) such as LmKTT-1a, BmKTT-1, and BmKTT-2; This model includes scorpion Kunitz-type toxin (KTT) such as Lychas mucronatus LmKTT-1a (also called Delta-KTx 2.1 or SdPII), Mesobuthus martensii BmKTT-1 (also called Delta-KTx 2.4) and BmKTT-2 (also called Delta-KTx 3.1), all expressed by the venom gland. LmKTT-1a, BmKTT-1 and BmKTT-2 are all dual-function toxins that completely inhibit trypsin activity but have no effect on chymotrypsin or elastase. They also inhibit mKv1.3/KCNA3 potassium channel currents. The structures of these domains are similar to those of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor); however, they lack the conserved CysII-CysIV disulfide bond but contains 2 cysteine residues at the C-terminus that generate a new disulfide bond.


Pssm-ID: 438663  Cd Length: 58  Bit Score: 67.21  E-value: 1.83e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2906 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVCAP 2958
Cdd:cd22620    3 CQLPSDTGRGKASFTRYYYNEESGKCETFIYGGVGGNSNNFLTKEDCCKECAQ 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1869-2159 2.71e-13

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 75.45  E-value: 2.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1869 PPGVNGTQGFQGCpgqrgvKGSRGFPGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVGIR 1948
Cdd:COG5164   11 PSDPGGVTTPAGS------QGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1949 GDPGN--PGQDSQERGPKGETGDLGPMGVPGRDGVPGGPGETGKNGGFGRRGPPGAKGNKGGPGQPGFEGEQGTRgaqgp 2026
Cdd:COG5164   85 QNQGGtrPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPP----- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2027 agpagppgliGEQGISGPRGSGGAAGAPGERGRTGPlGRKGEPGEPGPKGGIGNRGPRGETGDDGrdgvgsegrrgkkge 2106
Cdd:COG5164  160 ----------GDGGSTTPPGPGGSTTPPDDGGSTTP-PNKGETGTDIPTGGTPRQGPDGPVKKDD--------------- 213

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2107 rgfpgyPGPKGNPgEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAG 2159
Cdd:COG5164  214 ------KNGKGNP-PDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTA 259
Kunitz_SmCI_1-like cd22601
first Kunitz domain of Carboxypeptidase Inhibitor SmCI and similar domains; This group ...
 2904-2957 2.99e-13

first Kunitz domain of Carboxypeptidase Inhibitor SmCI and similar domains; This group includes Sabellastarte magnifica carboxypeptidase inhibitor (SmCI), a tri-domain BPTI-Kunitz inhibitor capable of inhibiting serine proteases and A-like metallocarboxypeptidases. While the BPTI-Kunitz family of proteins includes voltage gated channel blockers and inhibitors of serine proteases, SmCI is the only BPTI-Kunitz protein capable of inhibiting metallocarboxypeptidases. Binding studies show that SmCI is able to bind three trypsin molecules under saturating conditions, but only one elastase interacts with the inhibitor. Additionally, SmCI can bind serine proteases and carboxypeptidases at the same time (at least in the ratio 1:1:1), thus becoming the first protease inhibitor that simultaneously blocks these two mechanistic classes of enzymes. This model contains the first Kunitz domain of SmCI, which has a structure similar to those of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438644  Cd Length: 55  Bit Score: 66.37  E-value: 2.99e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 55743106 2904 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVCA 2957
Cdd:cd22601    2 DVCDLPADRGPCTAYIPRWFYNKTTKKCEKFVYGGCQGNKNRFETKDDCLANCG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2096-2158 3.31e-13

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: 66.36  E-value: 3.31e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55743106   2096 GSEGRRGKKGERGFPGYPGPKGNPGEPglngttGPKGIRGRRGNSGPPGIVGQKGDPGYPGPA 2158
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPP------GPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Kunitz_HAI2_2-like cd22622
Kunitz-type domain 2 (KD2) of hepatocyte growth factor activator inhibitor type 2 (HAI-2), and ...
 2906-2956 3.60e-13

Kunitz-type domain 2 (KD2) of hepatocyte growth factor activator inhibitor type 2 (HAI-2), and similar proteins; This model includes Kunitz domain 2 (KD2) of hepatocyte growth factor activator inhibitor type 2 (HAI-2 or HAI2, also known as placental bikunin or Kunitz-type protease inhibitor 2). HAI-2 is composed of two Kunitz domains that strongly inhibit many serine proteases with sub-nanomolar affinities. It has been found to be a natural tumor suppressor in renal cell carcinoma, breast cancer and prostate cancer, the loss of which leads to tumor growth and progression attributable at least in part to increased MET signaling. HAI-2 is a specific substrate of mesotrypsin which is up-regulated with progression in prostate cancers and shown to contribute to invasion and metastasis; these activities of mesotrypsin may in part be mediated through cleavage and inactivation of HAI-2, resulting in increases in hetatocyte growth factor/scatter factor (HGF/SF) activation and MET signaling. HAI-2 is a physiological inhibitor of hepsin and matriptase, two type II transmembrane serine proteases that, like HGF activator, can convert latent pro-HGF/SF into the two-chain active signaling heterodimer. KD2 is similar to KD1, whose structure is similar to those of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438665  Cd Length: 53  Bit Score: 66.23  E-value: 3.60e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 55743106 2906 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22622    3 CAAPRVTGPCRAAFPRWYYDPESQSCKEFIYGGCRGNKNNYLSEEECMDRC 53
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 823-959 6.62e-13

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: 69.72  E-value: 6.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  823 DVVFLLDGSEGV-RSGFPLLKEFVQRVVESL------DVGQDRVRVAVVQYSDRTRPEF-YLNSYMNKQDVVNAVRQLTL 894
Cdd:cd01480    4 DITFVLDSSESVgLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLEY 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55743106  895 LGGPTpNTGAALEFVLRNILVSSAGsriteGVPQLLIVLTADRS-GDDVRNPSVVVKRGGAVPIGI 959
Cdd:cd01480   84 IGGGT-FTDCALKYATEQLLEGSHQ-----KENKFLLVITDGHSdGSPDGGIEKAVNEADHLGIKI 143
Kunitz_TFPI2_2-like cd22617
Kunitz domain 2 (KD2) of tissue factor pathway inhibitor 2 (TFPI2) and similar proteins; This ...
 2904-2956 7.33e-13

Kunitz domain 2 (KD2) of tissue factor pathway inhibitor 2 (TFPI2) and similar proteins; This model represents the Kunitz-type domain 2 (KD2) of tissue factor pathway inhibitor 2 (TFPI2 or TFPI-2) and similar proteins. TFPI2 exhibits inhibitory activity primarily toward trypsin, plasmin, and factor VIIa (FVIIa)/tissue factor (TF) via its KD1. It is believed to be the major inhibitor of plasmin in the extracellular matrix (ECM) but has little inhibitory activity toward urokinase-type plasminogen activator, tissue-type plasminogen activator, or thrombin. While TFPI2 specifically inhibits the proteases via the P1 arginine residue in KD1, domains KD2 and KD3 appear to have no discernible inhibitory activity and may serve to bind to nearby proteins to localize TFPI2 in the ECM. This domain is similar to that of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor) that shows an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438660  Cd Length: 54  Bit Score: 65.10  E-value: 7.33e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2904 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22617    2 KVCREVPDEGPCRALITRYFYNMTSMRCEEFTYGGCYGNGNNFRDKSSCISAC 54
Kunitz_dendrotoxin cd22595
dendrotoxins I, K, B and similar proteins; This group includes toxins isolated from snake ...
 2906-2956 8.51e-13

dendrotoxins I, K, B and similar proteins; This group includes toxins isolated from snake venoms, such as dendrotoxins (DTXs) I, K and B, mambaquaretin-1 (MQ-1) and calcicludine. The dendrotoxins have little or no anti-protease activity but have been shown to block certain subtypes of voltage dependent potassium channels in neurons. Dendroaspis angusticeps (green mamba) alpha-dendrotoxin is a neurotoxin that enhances acetylcholine release at neuromuscular junctions. Studies with cloned K(+) channels show that this toxin blocks Kv1.1, Kv1.2 and Kv1.6 channels in the nanomolar range, whereas Dendroaspis polylepis (black mamba) dendrotoxin K preferentially blocks Kv1.1 channels. Also, structural analogs of dendrotoxins have facilitated defining the molecular recognition properties of different types of K(+) channels, and therefore, dendrotoxins are widely used as probes for studying the function of K(+) channels in physiology and pathophysiology. The structures of these toxins are similar to that of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438638  Cd Length: 56  Bit Score: 65.15  E-value: 8.51e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 55743106 2906 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22595    4 CKLPVRPGPCKAFISAFYYNWKAKKCHPFTYSGCGGNANRFKTIEECRRTC 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1907-1966 8.70e-13

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: 65.21  E-value: 8.70e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1907 GLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVGIRGDPGNPGQDsqerGPKGE 1966
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP----GAPGP 56
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 2412-2603 1.01e-12

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: 68.92  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2412 IDMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMspDPKASQhfarVAVVQHAPSesvdnasmppVKVEFSLTDYGSKEK 2491
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDI--GPTKTQ----FGLVQYSES----------FRTEFTLNEYRTKEE 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2492 lVDFLSRGMTQLQGTRALGSAIEYTIENVF--ESAPNPRDLKIVVLMLTGEVPEQQLEEAqrVILQAKCKGYFFVVLGIG 2569
Cdd:cd01469   65 -PLSLVKHISQLLGLTNTATAIQYVVTELFseSNGARKDATKVLVVITDGESHDDPLLKD--VIPQAEREGIIRYAIGVG 141

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 55743106 2570 ----RKVNIKEVYTFASEPNDVFFKLVDkstelNEEPL 2603
Cdd:cd01469  142 ghfqRENSREELKTIASKPPEEHFFNVT-----DFAAL 174
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 433-599 1.15e-12

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: 68.95  E-value: 1.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  433 DIIFLLDGSANVGKTNFPYVRDFVMNLVNSL------DIGNDNIRVGLVQFSDTPVTEF-SLNTYQTKSDILGHLRQLQL 505
Cdd:cd01480    4 DITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLEY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  506 QGGsGLNTGSALSYVYanhfteaggSRIREHVPQL----LLLLTAGQS----EDSYLQAANALTRAGILTFCVGASQANK 577
Cdd:cd01480   84 IGG-GTFTDCALKYAT---------EQLLEGSHQKenkfLLVITDGHSdgspDGGIEKAVNEADHLGIKIFFVAVGSQNE 153

                        170       180
                 ....*....|....*....|..
gi 55743106  578 AELEQIAFNPSLVYLMDDFSSL 599
Cdd:cd01480  154 EPLSRIACDGKSALYRENFAEL 175
Kunitz_SmCI_2-like cd22602
second Kunitz domain of Carboxypeptidase Inhibitor SmCI and similar domains; This group ...
 2906-2956 1.55e-12

second Kunitz domain of Carboxypeptidase Inhibitor SmCI and similar domains; This group includes Sabellastarte magnifica carboxypeptidase inhibitor (SmCI), a tri-domain BPTI-Kunitz inhibitor capable of inhibiting serine proteases and A-like metallocarboxypeptidases. While the BPTI-Kunitz family of proteins includes voltage gated channel blockers and inhibitors of serine proteases, SmCI is the only BPTI-Kunitz protein capable of inhibiting metallocarboxypeptidases. Binding studies show that SmCI is able to bind three trypsin molecules under saturating conditions, but only one elastase interacts with the inhibitor. Additionally, SmCI can bind serine proteases and carboxypeptidases at the same time (at least in the ratio 1:1:1), thus becoming the first protease inhibitor that simultaneously blocks these two mechanistic classes of enzymes. This model contains the second Kunitz domain of SmCI, which has a structure similar to those of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438645  Cd Length: 51  Bit Score: 64.10  E-value: 1.55e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 55743106 2906 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22602    1 CSLPSKVGPCRVSARRWFHNPETEKCEVFIYGGCHGNANRFATETECQEVC 51
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 2102-2170 2.94e-12

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 71.86  E-value: 2.94e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55743106  2102 GKKGERGFPGYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAGPKGNRGDSIDQ 2170
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 823-962 2.99e-12

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: 67.80  E-value: 2.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  823 DVVFLLD--GSEGVRSGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSY--MNKQ---DVVNAVRQLTLL 895
Cdd:cd01471    2 DLYLLVDgsGSIGYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPnsTNKDlalNAIRALLSLYYP 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55743106  896 GGPTpNTGAALEFVlRNILVSSAGSRitEGVPQLLIVLTADRSGDDVRNPSVVVK---RGGAVP-IGIGIG 962
Cdd:cd01471   82 NGST-NTTSALLVV-EKHLFDTRGNR--ENAPQLVIIMTDGIPDSKFRTLKEARKlreRGVIIAvLGVGQG 148
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1901-1956 3.35e-12

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: 63.28  E-value: 3.35e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 55743106   1901 GEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVGIRGDPGNPGQ 1956
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1230-1368 5.73e-12

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: 67.03  E-value: 5.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1230 DIVFLIDSSEGV-RPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAP--VLDAIRRLR---LR 1303
Cdd:cd01471    2 DLYLLVDGSGSIgYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKdlALNAIRALLslyYP 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1304 GGSPlNTGKALEFVARNLFvKSAGSRieDGVPQhLVLVLGGKSQDDVSR---FAQVIRSSG--IVSLGVG 1368
Cdd:cd01471   82 NGST-NTTSALLVVEKHLF-DTRGNR--ENAPQ-LVIIMTDGIPDSKFRtlkEARKLRERGviIAVLGVG 146
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 239-383 1.01e-11

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: 66.25  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  239 DIVFLVDGSSALGLANFNAIRDFIAKVIQRL------EIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVIT-AVRKMKP 311
Cdd:cd01480    4 DITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTSLKeAVDNLEY 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55743106  312 LDGsALYTGSALDFVRNNLFTSSAGyraaeGIPKLLVLITGGKSLDE----ISQPAQELKRSSI--MAFAIGNKGADQ 383
Cdd:cd01480   84 IGG-GTFTDCALKYATEQLLEGSHQ-----KENKFLLVITDGHSDGSpdggIEKAVNEADHLGIkiFFVAVGSQNEEP 155
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1027-1196 1.05e-11

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: 66.25  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1027 DVVFLIDGSQSAGPE-FQYVRTLIERLVD------YLDVGFDTTRVAVIQFSDDPKVEF-LLNAHSSKDEVQNAVQRLRP 1098
Cdd:cd01480    4 DITFVLDSSESVGLQnFDITKNFVKRVAErflkdyYRKDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLEY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1099 KGGrQINVGNALEYVSRNIFKRPLGsrieeGVPQFLVLISSGKSDDEVD----DPAVELKQFGVAPFTIARNADQEE-LV 1173
Cdd:cd01480   84 IGG-GTFTDCALKYATEQLLEGSHQ-----KENKFLLVITDGHSDGSPDggieKAVNEADHLGIKIFFVAVGSQNEEpLS 157

                        170       180
                 ....*....|....*....|....*.
gi 55743106 1174 KIS---LSPEYVFSVSTFRELPSLEQ 1196
Cdd:cd01480  158 RIAcdgKSALYRENFAELLWSFFIDD 183
VWA_2 pfam13519
von Willebrand factor type A domain;
1028-1137 1.07e-11

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 63.47  E-value: 1.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1028 VVFLIDGSQSAGP------EFQYVRTLIERLVDYLDvgfdTTRVAVIQFSDDPKVEFLLNahSSKDEVQNAVQRLRPKGG 1101
Cdd:pfam13519    1 LVFVLDTSGSMRNgdygptRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 55743106   1102 rQINVGNALEYVSRNIFKRPlgsrieEGVPQFLVLI 1137
Cdd:pfam13519   75 -GTNLAAALQLARAALKHRR------KNQPRRIVLI 103
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 631-772 1.25e-11

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: 65.84  E-value: 1.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  631 DILFLFDGSANLV-GQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVK---RMKIKTGK 706
Cdd:cd01469    2 DIVFVLDGSGSIYpDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKhisQLLGLTNT 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55743106  707 ALnlgyALDYAQRYIFVKSAGSRieDGVLQFLVLLVAGRSSDRVDGPAsNLKQS---GVVPFI------FQAKNA 772
Cdd:cd01469   82 AT----AIQYVVTELFSESNGAR--KDATKVLVVITDGESHDDPLLKD-VIPQAereGIIRYAigvgghFQRENS 149
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1883-1938 1.38e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 61.74  E-value: 1.38e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 55743106   1883 GQRGVKGSRGFPGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGE 1938
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Kunitz_bikunin_1-like cd22596
first Kunitz domain of bikunin and similar proteins; This subfamily includes the N-terminal ...
 2904-2956 1.48e-11

first Kunitz domain of bikunin and similar proteins; This subfamily includes the N-terminal domain of bikunin (also known as inter-alpha-trypsin inhibitor light chain (ITI-LC) or urinary trypsin inhibitor), a plasma protease inhibitor, that is associated with inflammation and stabilizes the extracellular matrix. It is encoded together with alpha-1-microglobulin (A1M) by an alpha-1-microglobulin/bikunin precursor (AMBP) gene that is tightly controlled by several hepatocyte-enriched nuclear (HEN) factors, and cleaved by a furin-like protease that releases the two mature molecules. Bikunin is a Kunitz-type serine protease inhibitor, found in vertebrate serum and urine, modified by a chondroitin sulfate (CS) chain. The structures of these toxins are similar to that of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds. Bikunin contains two Kunitz domains; this model represents the first repeat.


Pssm-ID: 438639  Cd Length: 54  Bit Score: 61.50  E-value: 1.48e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2904 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22596    1 DSCKLPPDAGPCFGMIQRYFYNSSSMACQTFNYGGCLGNQNNFVTEKECLQTC 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1892-1946 2.10e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 61.36  E-value: 2.10e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 55743106   1892 GFPGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVG 1946
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1886-1942 3.97e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 60.59  E-value: 3.97e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 55743106   1886 GVKGSRGFPGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGER 1942
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1880-1936 5.07e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 60.20  E-value: 5.07e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 55743106   1880 GCPGQRGVKGSRGFPGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPR 1936
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1925-1990 6.28e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 59.81  E-value: 6.28e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55743106   1925 GNPGRRGDKGPRGEKGERGDVGIRGDPGNPGqdsqERGPkgetgdlgpmgvPGRDGVPGGPGETGK 1990
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPG----EPGP------------PGPPGPPGPPGPPGA 50
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 631-780 1.02e-10

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: 62.80  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  631 DILFLFDGSANLVGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVK--VESRFDEHQSKPEILNLVKRMKIKTGKAl 708
Cdd:cd01476    2 DLLFVLDSSGSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGTT- 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55743106  709 NLGYALDYAQRYiFVKSAGSRieDGVLQFLVLLVAGRSSDRVDGPASNLkQSGVVPFIFQAKNADP-----AELEQI 780
Cdd:cd01476   81 ATGAAIEVALQQ-LDPSEGRR--EGIPKVVVVLTDGRSHDDPEKQARIL-RAVPNIETFAVGTGDPgtvdtEELHSI 153
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1228-1400 1.04e-10

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: 63.17  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1228 AADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRL------NIGPSKVRVGVVQFSNDVFPEF-YLKTYRSQAPVLDAIRRL 1300
Cdd:cd01480    2 PVDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1301 R-LRGGSplNTGKALEFVARNLFVKSAGsriedGVPQHLVLVLGGKSQ----DDVSRFAQVIRSSGI--VSLGVGDRNID 1373
Cdd:cd01480   82 EyIGGGT--FTDCALKYATEQLLEGSHQ-----KENKFLLVITDGHSDgspdGGIEKAVNEADHLGIkiFFVAVGSQNEE 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 55743106 1374 RteLQTITNDP------RLVFTVREFRELPNIE 1400
Cdd:cd01480  155 P--LSRIACDGksalyrENFAELLWSFFIDDET 185
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 239-377 1.46e-10

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: 62.79  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  239 DIVFLVDGSSALGLAN-FNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTK-----REVITAVRKMkPL 312
Cdd:cd01471    2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTnkdlaLNAIRALLSL-YY 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  313 DGSALYTGSALDFVRNNLFTsSAGYRaaEGIPKLLVLITGGKSlDEISQP---AQELK-RSSIMA-FAIG 377
Cdd:cd01471   81 PNGSTNTTSALLVVEKHLFD-TRGNR--ENAPQLVIIMTDGIP-DSKFRTlkeARKLReRGVIIAvLGVG 146
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 2197-2337 1.50e-10

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: 62.25  E-value: 1.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2197 LAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIAesncPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQvaLTS 2276
Cdd:cd01472    3 IVFLVDGSESIGLSNFNLVKDFVKRVVERLDIG----PDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLR--YIG 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55743106 2277 KQQSLETAMSFVARNTFK---RVRNGFlmRKVAVFFsnTPTRASPQLREAVLKLSDAGITPLFL 2337
Cdd:cd01472   77 GGTNTGKALKYVRENLFTeasGSREGV--PKVLVVI--TDGKSQDDVEEPAVELKQAGIEVFAV 136
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1010-1176 1.52e-10

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: 64.57  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1010 LQPVLQPLPSPGVGGKRDVVFLID--GSQSAGPEFQYVRTLIERLVDYLDvgfDTTRVAVIQFSDDPKVefLLNAHSSKD 1087
Cdd:COG1240   77 LALALAPLALARPQRGRDVVLVVDasGSMAAENRLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEV--LLPLTRDRE 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1088 EVQNAVQRLRPKGGRQInvGNALeYVSRNIFKrplgsRIEEGVPQFLVLISSGKSDDEVDDP---AVELKQFGVAPFTIA 1164
Cdd:COG1240  152 ALKRALDELPPGGGTPL--GDAL-ALALELLK-----RADPARRKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIG 223

                        170
                 ....*....|....*
gi 55743106 1165 ---RNADQEELVKIS 1176
Cdd:COG1240  224 vgtEAVDEGLLREIA 238
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1927-2166 1.82e-10

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 66.21  E-value: 1.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1927 PGRRGDKGPRGEKGERGDVGIRGDPGNPGQDsqerGPKGETGDLGPmgvPGRDGVPGGPGETGKNGGFgrrgppgakGNK 2006
Cdd:COG5164    6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGST----RPAGNTGGTRP---AQNQGSTTPAGNTGGTRPA---------GNQ 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2007 GGPGQPGFEGEQGTrgaqgpagpagppglIGEQGisgprgsggAAGAPGERGRTGPLGRKGEPGEPGPKGGIgnrGPRGE 2086
Cdd:COG5164   70 GATGPAQNQGGTTP---------------AQNQG---------GTRPAGNTGGTTPAGDGGATGPPDDGGAT---GPPDD 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2087 TGDDGRDGVGSEGRRGKKGER-GFPGYPGPKGNPGEPGLNGTTGPKGIRGRRG--NSGPPGIVGQKGDPGYPGPAGPKGN 2163
Cdd:COG5164  123 GGSTTPPSGGSTTPPGDGGSTpPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTppDDGGSTTPPNKGETGTDIPTGGTPR 202


                 ...
gi 55743106 2164 RGD 2166
Cdd:COG5164  203 QGP 205
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2412-2589 2.07e-10

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: 61.81  E-value: 2.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2412 IDMAFILDSAETTTLFQFNEMKKYIAYLVRQLDmspdpkASQHFARVAVVQHApsesvDNAsmppvKVEFSLTDYGSKEK 2491
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLS------ASPPGDRVGLVTFG-----SNA-----RVVLPLTTDTDKAD 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2492 LVDFLSRGMTQLQGTRALGSAIEYTIENVFESAPNPRdlKIVVLMLTGEVPEQQLEEAQRVILQAKCKGYFFVVLGIGRK 2571
Cdd:cd00198   65 LLEAIDALKKGLGGGTNIGAALRLALELLKSAKRPNA--RRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDD 142

                        170
                 ....*....|....*...
gi 55743106 2572 VNIKEVYTFASEPNDVFF 2589
Cdd:cd00198  143 ANEDELKEIADKTTGGAV 160
Kunitz_SHPI cd22618
Stichodactyla helianthus Kunitz inhibitor protein ShPI-1, Heteractis crispa protease inhibitor ...
 2905-2956 4.14e-10

Stichodactyla helianthus Kunitz inhibitor protein ShPI-1, Heteractis crispa protease inhibitor stichotoxin-Hcr2e, and similar proteins; This model includes Kunitz inhibitor protein ShPI-1, the major protease inhibitor from the sea anemone Stichodactyla helianthus, as well as protease inhibitor stichotoxin-Hcr2e (also called PI- stichotoxin-Hcr2e, PI-SHTX-Hcr2e, or Kunitz-type serine protease inhibitor InhVJ) and HCRG1 from Heteractis crispa. ShPI-1 has an unusually broad specificity toward several serine proteases, including trypsin, chymotrypsin, human neutrophil elastase, kallikrein and plasmin, and can also bind aspartic and cysteine proteases, such as pepsin and papain, respectively. PI-SHTX-Hcr2e and HCRG1 inhibit trypsin and chymotrypsin, but do not inhibit the serine proteases plasmin, thrombin, kallikrein, the cysteine proteinase papain, and the aspartic protease pepsin. The structures of these domains are similar to those of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438661  Cd Length: 53  Bit Score: 57.55  E-value: 4.14e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 55743106 2905 ICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22618    1 ICSEPKVVGPCKAYFPRFYFDSETGKCTPFIYGGCGGNGNNFETLHACRAIC 52
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1432-1591 5.38e-10

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: 60.49  E-value: 5.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1432 ADIVFLLDGSINFRrDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTD--EFFLKDFSTKRQIIDAINKVVYKGGR 1509
Cdd:cd01476    1 LDLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1510 HAnTKVGLEhLRVNHFVPEAGSRldQRVPQIAFVITGGKSVEDAQDVSLAL-TQRGVKVFAVGVRNI---DSEEVGKIAS 1585
Cdd:cd01476   80 TA-TGAAIE-VALQQLDPSEGRR--EGIPKVVVVLTDGRSHDDPEKQARILrAVPNIETFAVGTGDPgtvDTEELHSITG 155


                 ....*.
gi 55743106 1586 NSATAF 1591
Cdd:cd01476  156 NEDHIF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 2413-2589 7.25e-10

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: 60.11  E-value: 7.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2413 DMAFILDSAETTTlFQFNEMKKYIAYLVRQLDMSPDPKasqhfaRVAVVQHapsesvdnASMPPVKVEFSLTDYGSKEKL 2492
Cdd:cd01476    2 DLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTAT------RVALITY--------SGRGRQRVRFNLPKHNDGEEL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2493 VDFLsRGMTQLQGTRALGSAIEYTIENVFESAP-NPRDLKIVVLMLTG---EVPEQQLEEAQRVilqakcKGYFFVVLGI 2568
Cdd:cd01476   67 LEKV-DNLRFIGGTTATGAAIEVALQQLDPSEGrREGIPKVVVVLTDGrshDDPEKQARILRAV------PNIETFAVGT 139

                        170       180
                 ....*....|....*....|...
gi 55743106 2569 G--RKVNIKEVYTFASEPNDVFF 2589
Cdd:cd01476  140 GdpGTVDTEELHSITGNEDHIFT 162
Kunitz_TKDP-like cd22609
trophoblast Kunitz domain protein (TKDP) and similar proteins; This model contains the ...
 2906-2956 8.11e-10

trophoblast Kunitz domain protein (TKDP) and similar proteins; This model contains the trophoblast Kunitz domain protein 1 (TKDP-1) and splice variant TKDP-4, among others, which are Kunitz inhibitor domain proteins. TKDP-1 is expressed in the trophectoderm which forms the outer epithelial layer of the trophoblast, and may play a role in mediating maternal-conceptus interactions in the immediate preimplantation period. However, it does not appear to have proteinase inhibitory activity. These domains are similar to those of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor) that shows an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438652  Cd Length: 52  Bit Score: 56.69  E-value: 8.11e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 55743106 2906 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22609    2 CLEPKVVGVCKASMTRYFYNAQTGHCEQFVYGGCGGNRNNFLTLEDCMKTC 52
VWA_2 pfam13519
von Willebrand factor type A domain;
824-933 1.07e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 58.07  E-value: 1.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    824 VVFLLDGSEGVRSG------FPLLKEFVQRVVESLDvgqdRVRVAVVQYSDRTRPEFYLNSymNKQDVVNAVRQLTLLGG 897
Cdd:pfam13519    1 LVFVLDTSGSMRNGdygptrLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 55743106    898 PTpNTGAALEFVLRNIlvssagSRITEGVPQLLIVL 933
Cdd:pfam13519   75 GT-NLAAALQLARAAL------KHRRKNQPRRIVLI 103
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 2412-2550 1.45e-09

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: 59.55  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2412 IDMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDPkasqhfARVAVVQHApsesvDNasmppVKVEFSLTDYGSKEk 2491
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDG------VRVGVVQYS-----DD-----PRTEFYLNTYRSKD- 63

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55743106 2492 lvDFLS--RGMTQLQGTRALGSAIEYTIENVFESAPNPRD--LKIVVLMLTG----EVPEQQLEEAQ 2550
Cdd:cd01472   64 --DVLEavKNLRYIGGGTNTGKALKYVRENLFTEASGSREgvPKVLVVITDGksqdDVEEPAVELKQ 128
Kunitz_BPTI cd22592
bovine pancreatic trypsin inhibitor; This model contains bovine pancreatic trypsin inhibitor ...
 2906-2956 2.07e-09

bovine pancreatic trypsin inhibitor; This model contains bovine pancreatic trypsin inhibitor (BPTI, also known as pancreatic Kunitz inhibitor, aprotinin, or trypsin-kallikrein inhibitor), a small protein that inhibits the action of the trypsin, and is thus a member of the serine protease family of inhibitors. This class of enzymes contains conserved cysteine residues that form 3 disulfide bonds to stabilize the three-dimensional structure. BPTI has a relatively broad specificity, inhibiting trypsin as well as chymotrypsin, and elastase-like serine (pro)enzymes capable of very different primary specificity. It reacts rapidly with serine proteases to form stable complexes, but the enzyme:inhibitor complex formation may involve several intermediates corresponding to discrete reaction steps. Furthermore, BPTI inhibits the nitric oxide synthase type-I and -II action, and impairs K+ transport by Ca2+-activated K+ channels. Clinically, BPTI is used in certain surgical interventions, such as cardiopulmonary surgery and orthotopic liver transplantation since it significantly reduces hemorrhagic complications.


Pssm-ID: 438635  Cd Length: 52  Bit Score: 55.34  E-value: 2.07e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 55743106 2906 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22592    2 CLEPPYTGPCKARIIRYFYNAKSGLCETFVYGGCRAKRNNFLSAEDCMRTC 52
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 2413-2588 2.08e-09

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: 58.87  E-value: 2.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2413 DMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDPkasqhfARVAVVQHApsesvDNasmppVKVEFSLTDYGSKEKL 2492
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDK------IRVAVVQFS-----DT-----PRPEFYLNTHSTKADV 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2493 VDFLSRgmTQLQGTRAL--GSAIEYTIENVFESAPNPRD----LKIVVLMLTGEvPEQQLEEAQRVILQAKckgyfFVVL 2566
Cdd:cd01481   66 LGAVRR--LRLRGGSQLntGSALDYVVKNLFTKSAGSRIeegvPQFLVLITGGK-SQDDVERPAVALKRAG-----IVPF 137

                        170       180
                 ....*....|....*....|...
gi 55743106 2567 GIGRK-VNIKEVYTFASEPNDVF 2588
Cdd:cd01481  138 AIGARnADLAELQQIAFDPSFVF 160
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1632-1788 4.02e-09

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: 58.23  E-value: 4.02e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    1632 DVILGFDGSRDqnvfVAQKGFESKVDAILNRISQMHRvscsggRSPTVRVSVVAnTPSGPVEAFDFDEYQ--PEMLEKFR 1709
Cdd:smart00327    1 DVVFLLDGSGS----MGGNRFELAKEFVLKLVEQLDI------GPDGDRVGLVT-FSDDARVLFPLNDSRskDALLEALA 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    1710 NMRsqhpYVLTEDT---------LKVYLNKFRQSSPDSVKVVIHFTDGADGDLA-DLHRASENLRQEGVRaLILVGLERV 1779
Cdd:smart00327   70 SLS----YKLGGGTnlgaalqyaLENLFSKSAGSRRGAPKVVILITDGESNDGPkDLLKAAKELKRSGVK-VFVVGVGND 144


                    ....*....
gi 55743106    1780 VNLERLMHL 1788
Cdd:smart00327  145 VDEEELKKL 153
Kunitz_B2B cd22619
Kunitz-type serine protease inhibitor subunit of beta 2-bungarotoxin, and similar proteins; ...
 2906-2956 4.83e-09

Kunitz-type serine protease inhibitor subunit of beta 2-bungarotoxin, and similar proteins; This model includes the Kunitz inhibitor subunit of beta 2-bungarotoxin, a presynaptic neurotoxin of the Bungarus multicinctus venom. Beta-bungarotoxin is a heterodimeric neurotoxin consisting of a phospholipase subunit linked by a disulfide bond to the Kunitz protease inhibitor subunit; the latter subunit is homologous to venom basic protease inhibitors but has no protease inhibitor activity and is non-toxic. The beta-bungarotoxin Kunitz subunit serves to guide the toxin to its site of action on the presynaptic membrane by virtue of a high-affinity interaction with a specific subclass of voltage-sensitive potassium channels. This subfamily also includes Kunitz-type serine protease inhibitor homolog beta-bungarotoxin B1 chain and protease inhibitor-like protein 1 (PILP-1). The B1 chain also has no protease inhibitor activity but blocks voltage-gated potassium channels, while PILP-1 inhibits trypsin. The structures of these domains are similar to those of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438662  Cd Length: 58  Bit Score: 54.49  E-value: 4.83e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 55743106 2906 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22619    7 CDKPPDTKRCKRVVRAFYYNPSAKTCLQFVYGGCNGNGNHFKSKALCRCHC 57
VWA_2 pfam13519
von Willebrand factor type A domain;
1231-1322 5.16e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 56.15  E-value: 5.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1231 IVFLIDSSEGVRPDG-----FAHIRDFVSRIVRRLNIgpskVRVGVVQFSNDVFPEFYLKtyRSQAPVLDAIRRLRLRGG 1305
Cdd:pfam13519    1 LVFVLDTSGSMRNGDygptrLEAAKDAVLALLKSLPG----DRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                           90
                   ....*....|....*..
gi 55743106   1306 SPlNTGKALEFVARNLF 1322
Cdd:pfam13519   75 GT-NLAAALQLARAALK 90
VWA_2 pfam13519
von Willebrand factor type A domain;
434-522 5.86e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 55.76  E-value: 5.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    434 IIFLLDGSA-----NVGKTNFPYVRDFVMNLVNSldigNDNIRVGLVQFSDTPVTEFSLNTyqTKSDILGHLRQLQLQGG 508
Cdd:pfam13519    1 LVFVLDTSGsmrngDYGPTRLEAAKDAVLALLKS----LPGDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90
                   ....*....|....
gi 55743106    509 sGLNTGSALSYVYA 522
Cdd:pfam13519   75 -GTNLAAALQLARA 87
Kunitz_WFIKKN_1-like cd22605
first Kunitz domain of WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing proteins; ...
 2907-2956 9.39e-09

first Kunitz domain of WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing proteins; This subfamily includes WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing protein 1 (WFIKKN1, WFKN1), WFIKKN2 (WFKN2), and similar proteins. WFIKKN proteins are protease inhibitors that contain two distinct Kunitz-type protease inhibitor domains. They may have serine protease- and metalloprotease-inhibitor activity. This model represents the first Kunitz domain that is similar to Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor) that shows an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438648  Cd Length: 52  Bit Score: 53.52  E-value: 9.39e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 55743106 2907 KLPkDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22605    4 KEP-DREDCGEEQVRWYFDAKRGNCFTFTYGGCDGNRNHFETYEECRLAC 52
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 338-584 1.17e-08

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: 58.80  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  338 RAAEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSSLVFIPAEFRAAPLQGMLPGLLAP 417
Cdd:COG1240    1 DLALALLALLLLLALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  418 LRTLSGTPEVHSnkRDIIFLLDGSANVGKTN-FPYVRDFVMNLVNSLDignDNIRVGLVQFSDTPVTEFSLnTYQtKSDI 496
Cdd:COG1240   81 LAPLALARPQRG--RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPL-TRD-REAL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  497 LGHLRQLQLQGGSglNTGSALSYVYaNHFTEAGGSRIRehvpqLLLLLTAGQ---SEDSYLQAANALTRAGILTFCV--G 571
Cdd:COG1240  154 KRALDELPPGGGT--PLGDALALAL-ELLKRADPARRK-----VIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIgvG 225

                        250
                 ....*....|...
gi 55743106  572 ASQANKAELEQIA 584
Cdd:COG1240  226 TEAVDEGLLREIA 238
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 35-152 2.25e-08

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: 56.62  E-value: 2.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   35 ADIIFLIDGSNNTGSVNFAVILDFLVNLLEKL------PIGTQQIRVGVVQFSDEPRTMFSLDTYSTKAQVLG-AVKALG 107
Cdd:cd01480    3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTSLKeAVDNLE 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 55743106  108 FAGGElANIGLALDFVVENHFTRAGGsrveeGVPQVLVLISAGPS 152
Cdd:cd01480   83 YIGGG-TFTDCALKYATEQLLEGSHQ-----KENKFLLVITDGHS 121
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 2199-2335 2.40e-08

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: 55.79  E-value: 2.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2199 FALDTSEGVNQDTFGRMRDVVLSIVNDLTIAesncPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQVaLTSKQ 2278
Cdd:cd01481    5 FLIDGSDNVGSGNFPAIRDFIERIVQSLDVG----PDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRL-RGGSQ 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55743106 2279 QSLETAMSFVARNTFK-----RVRNGFLMRKVAVffsnTPTRASPQLREAVLKLSDAGITPL 2335
Cdd:cd01481   80 LNTGSALDYVVKNLFTksagsRIEEGVPQFLVLI----TGGKSQDDVERPAVALKRAGIVPF 137
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1213-1403 3.32e-08

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: 57.26  E-value: 3.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1213 LLASTRYPPPAVESDAADIVFLIDSSeG--VRPDGFAHIRDFVSRIVRRLnigPSKVRVGVVQFSNDVFPEFYLKTYRSQ 1290
Cdd:COG1240   77 LALALAPLALARPQRGRDVVLVVDAS-GsmAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTRDREA 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1291 apVLDAIRRLRLRGGSPLntGKALEfVARNLFvksagSRIEDGVPQHLVLVLGGK---SQDDVSRFAQVIRSSGI--VSL 1365
Cdd:COG1240  153 --LKRALDELPPGGGTPL--GDALA-LALELL-----KRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIriYTI 222

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 55743106 1366 GVGDRNIDRTELQTI---TNDPrlVFTVREFRELPNIEERI 1403
Cdd:COG1240  223 GVGTEAVDEGLLREIaeaTGGR--YFRADDLSELAAIYREI 261
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 36-157 3.35e-08

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: 55.85  E-value: 3.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   36 DIIFLIDGSNNTGSVN-FAVILDFLVNLLEKLPIGTQQIRVGVVQFSDEPRTMFSLDTY-STKAQ----VLGAVKALGFA 109
Cdd:cd01471    2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPnSTNKDlalnAIRALLSLYYP 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 55743106  110 GGElANIGLALDFVVENHFTRAGGsrvEEGVPQVLVLISAGPSSDEIR 157
Cdd:cd01471   82 NGS-TNTTSALLVVEKHLFDTRGN---RENAPQLVIIMTDGIPDSKFR 125
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1433-1572 4.94e-08

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: 55.47  E-value: 4.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1433 DIVFLLDGSINFRR-DSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKD-FSTKRQ----IIDAINKVVYK 1506
Cdd:cd01471    2 DLYLLVDGSGSIGYsNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpNSTNKDlalnAIRALLSLYYP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55743106 1507 GGRhANTKVGLehLRVN-HFVPEAGSRldQRVPQIAFVITGGKSVEDAQDVSLA--LTQRGVKVFAVGV 1572
Cdd:cd01471   82 NGS-TNTTSAL--LVVEkHLFDTRGNR--ENAPQLVIIMTDGIPDSKFRTLKEArkLRERGVIIAVLGV 145
VWA_2 pfam13519
von Willebrand factor type A domain;
37-147 5.66e-08

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 53.06  E-value: 5.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106     37 IIFLIDGSN-----NTGSVNFAVILDFLVNLLEKLPIGtqqiRVGVVQFSDEPRTMFSLDtySTKAQVLGAVKALGFAGG 111
Cdd:pfam13519    1 LVFVLDTSGsmrngDYGPTRLEAAKDAVLALLKSLPGD----RVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 55743106    112 ElANIGLALDFVVENHFTRAGgsrveeGVPQVLVLI 147
Cdd:pfam13519   75 G-TNLAAALQLARAALKHRRK------NQPRRIVLI 103
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2061-2123 8.26e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.96  E-value: 8.26e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55743106   2061 GPLGRKGEPGEPGPKGGIGNRGPRGEtgddgrdgvgsegrrgkkgergfPGYPGPKGNPGEPG 2123
Cdd:pfam01391   16 GPPGPPGPPGPPGPPGEPGPPGPPGP-----------------------PGPPGPPGAPGAPG 55
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2197-2354 1.04e-07

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: 54.11  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2197 LAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIAesncPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQvALTS 2276
Cdd:cd00198    3 IVFLLDVSGSMGGEKLDKAKEALKALVSSLSAS----PPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALK-KGLG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2277 KQQSLETAMSFVARNTFKRVRNGflMRKVAVFFSN-TPTRASPQLREAVLKLSDAGIT--PLFLTRQEDRQLINALQINN 2353
Cdd:cd00198   78 GGTNIGAALRLALELLKSAKRPN--ARRVIILLTDgEPNDGPELLAEAARELRKLGITvyTIGIGDDANEDELKEIADKT 155


                 .
gi 55743106 2354 T 2354
Cdd:cd00198  156 T 156
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1411-1602 1.07e-07

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: 55.71  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1411 AATPAPPGVDTPPPSRPEKKKADIVFLLD--GSINfRRDSFQEVLRFVSEIVDTvYEDGDsiQVGLVQYNSDPtdeFFLK 1488
Cdd:COG1240   72 VLLLLLALALAPLALARPQRGRDVVLVVDasGSMA-AENRLEAAKGALLDFLDD-YRPRD--RVGLVAFGGEA---EVLL 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1489 DFST-KRQIIDAINKVVYKGGrhanT------KVGLEHLRvnhfvpeagsRLDQRVPQIAFVITGGK---SVEDAQDVSL 1558
Cdd:COG1240  145 PLTRdREALKRALDELPPGGG----TplgdalALALELLK----------RADPARRKVIVLLTDGRdnaGRIDPLEAAE 210

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 55743106 1559 ALTQRGVKVFAVGV--RNIDSEEVGKIASNS-ATAFRVGNVQELSEL 1602
Cdd:COG1240  211 LAAAAGIRIYTIGVgtEAVDEGLLREIAEATgGRYFRADDLSELAAI 257
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 433-611 1.27e-07

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


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 54.44  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  433 DIIFLLDGSANVGKtNFPYVRDFVMNLVNSLDigNDNIRVGLVQFSDTPVTEFSLNTYQTK-SDILGHLRQLQLQGGSGL 511
Cdd:cd01474    6 DLYFVLDKSGSVAA-NWIEIYDFVEQLVDRFN--SPGLRFSFITFSTRATKILPLTDDSSAiIKGLEVLKKVTPSGQTYI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  512 NTGsaLSYVYANHFTEAGGSRIREHVpqlLLLLTAGQ-SEDSYLQA---ANALTRAGILTFCVGASQANKAELEQIAFNP 587
Cdd:cd01474   83 HEG--LENANEQIFNRNGGGRETVSV---IIALTDGQlLLNGHKYPeheAKLSRKLGAIVYCVGVTDFLKSQLINIADSK 157

                        170       180
                 ....*....|....*....|....*
gi 55743106  588 SLVYLMDD-FSSLpalpQQLIQPLT 611
Cdd:cd01474  158 EYVFPVTSgFQAL----SGIIESVV 178
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1832-1902 1.40e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.18  E-value: 1.40e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55743106   1832 GQRGDRGPIGSIGPKGIPGEDGyrgypgdeggpgergPPGVNGTQGFQGCPGQRGVKGSRGFPGEKGEVGE 1902
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPG---------------PPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1853-1927 1.43e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.18  E-value: 1.43e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55743106   1853 GYRGYPGDeggpgergppgvngtqgfQGCPGQRGVKGSRGFPGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNP 1927
Cdd:pfam01391    1 GPPGPPGP------------------PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Kunitz_ixolaris_1 cd22625
Kunitz-type domain 1 (K1) of Ixolaris, and similar proteins; This model includes the first ...
 2906-2956 2.58e-07

Kunitz-type domain 1 (K1) of Ixolaris, and similar proteins; This model includes the first Kunitz-type domain (K1) of ixolaris from the venomous organism Conus striatus. Ixolaris is a potent tick salivary anticoagulant that binds coagulation factor Xa (FXa) and zymogen FX, and forms a quaternary tissue factor (TF)/FVIIa/FX(a)/Ixolaris inhibitory complex. It blocks TF-induced coagulation and PAR2 (proteinase-activated receptor 2) signaling, and prevents thrombosis, tumor growth, and immune activation. Ixolaris consists of 2 Kunitz domains (K1 and K2), both of which recognize the heparin-binding (pro)exosite (HBE) on FX. While K2 is an extraordinarily dynamic domain that encompasses several residues involved in FX binding, K1 domain keeps as a rigid platform supporting the conformational dynamic of the K2 domain, forming a salt bridge with FXa. The structure of this domain is similar to that of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438668  Cd Length: 53  Bit Score: 49.57  E-value: 2.58e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2906 CKLPKDEG-TCRDFILKWY-YDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22625    1 CTLPIQEItTCESQPTKRYgYNKKTQQCEEFLGTECGGGGNSFEEAKECWSSC 53
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1027-1144 5.99e-07

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: 52.39  E-value: 5.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1027 DVVFLIDGSQSAGPE--FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSS--KDEVQNAVQRLR----P 1098
Cdd:cd01471    2 DLYLLVDGSGSIGYSnwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNStnKDLALNAIRALLslyyP 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 55743106 1099 KGgrQINVGNALEYVSRNIFKRPlGSRieEGVPQFLVLISSGKSDD 1144
Cdd:cd01471   82 NG--STNTTSALLVVEKHLFDTR-GNR--ENAPQLVIIMTDGIPDS 122
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 1024-1210 6.34e-07

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


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 52.13  E-value: 6.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1024 GKRDVVFLIDGSQSAG---PE-FQYVRTLIERLVDyldvgfDTTRVAVIQFSDDPKVEFLLNAHSSKdEVQNA--VQRLR 1097
Cdd:cd01474    3 GHFDLYFVLDKSGSVAanwIEiYDFVEQLVDRFNS------PGLRFSFITFSTRATKILPLTDDSSA-IIKGLevLKKVT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1098 PKGgrQINVGNALEYVSRNIFKRPLGSRIEEGVpqfLVLISSGKSDDEV----DDPAVELKQFGVAPFTIA-RNADQEEL 1172
Cdd:cd01474   76 PSG--QTYIHEGLENANEQIFNRNGGGRETVSV---IIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGvTDFLKSQL 150

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 55743106 1173 VKISLSPEYVFSV-STFRELpsleQKLLTPITTLTSEQI 1210
Cdd:cd01474  151 INIADSKEYVFPVtSGFQAL----SGIIESVVKKACIEI 185
PHA03169 PHA03169
hypothetical protein; Provisional
 1876-2013 7.13e-07

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 54.59  E-value: 7.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1876 QGFQGCPGQRGVKGSRGFPGEKGEVGEIGLD---------GLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVG 1946
Cdd:PHA03169   89 QGGPSGSGSESVGSPTPSPSGSAEELASGLSpentsgsspESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQ 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1947 IRG----DPGNPG----QDSQERGPKGETGDLGPMGV-----PGRDGVPGGPGETGKNGGFGRRGPPGAKGNKG-GPGQP 2012
Cdd:PHA03169  169 PSHedspEEPEPPtsepEPDSPGPPQSETPTSSPPPQsppdePGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEReGPPFP 248


                  .
gi 55743106  2013 G 2013
Cdd:PHA03169  249 G 249
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 433-584 9.45e-07

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: 51.93  E-value: 9.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  433 DIIFLLDGSANVGKTNF-PYVRDFVMNLVNSLDIGNDNIRVGLVQFSD--TPVTEFSLNTYQTKSDILGHLRQLQ--LQG 507
Cdd:cd01473    2 DLTLILDESASIGYSNWrKDVIPFTEKIINNLNISKDKVHVGILLFAEknRDVVPFSDEERYDKNELLKKINDLKnsYRS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  508 GSGLNTGSALSYVYANHFteaGGSRIREHVPQLLLLLTAGQ---SEDSYLQAANAL-TRAGILTFCVGASQANKAELEQI 583
Cdd:cd01473   82 GGETYIVEALKYGLKNYT---KHGNRRKDAPKVTMLFTDGNdtsASKKELQDISLLyKEENVKLLVVGVGAASENKLKLL 158


                 .
gi 55743106  584 A 584
Cdd:cd01473  159 A 159
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 631-752 1.12e-06

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: 51.62  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  631 DILFLFDGSANlVG--QFPVVRDFLYKIIDELN----VKPE--GTRIAVAQYSDDVKVESRFDEH-QSKPEILNLVKRMK 701
Cdd:cd01480    4 DITFVLDSSES-VGlqNFDITKNFVKRVAERFLkdyyRKDPagSWRVGVVQYSDQQEVEAGFLRDiRNYTSLKEAVDNLE 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 55743106  702 IkTGKALNLGYALDYAQRYIFVKSAGsriedGVLQFLVLLVAGRSSDRVDG 752
Cdd:cd01480   83 Y-IGGGTFTDCALKYATEQLLEGSHQ-----KENKFLLVITDGHSDGSPDG 127
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 1228-1413 1.95e-06

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


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 50.97  E-value: 1.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1228 AADIVFLIDSSEGVRpDGFAHIRDFVSRIVRRLNigPSKVRVGVVQFSNDVFPEFYLKTYRSQ-APVLDAIRRLRLRGGS 1306
Cdd:cd01474    4 HFDLYFVLDKSGSVA-ANWIEIYDFVEQLVDRFN--SPGLRFSFITFSTRATKILPLTDDSSAiIKGLEVLKKVTPSGQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1307 PLntGKALEFVARNLFVKSAGSRIEDGVpqhLVLVLGGKSQDDV----SRFAQVIRSSGIVSLGVGDRNIDRTELQTITN 1382
Cdd:cd01474   81 YI--HEGLENANEQIFNRNGGGRETVSV---IIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGVTDFLKSQLINIAD 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 55743106 1383 DPRLVFTVRE-FRELpnieERIMNSFGPSAAT 1413
Cdd:cd01474  156 SKEYVFPVTSgFQAL----SGIIESVVKKACI 183
VWA_2 pfam13519
von Willebrand factor type A domain;
2197-2309 2.20e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 48.44  E-value: 2.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   2197 LAFALDTSEGVNQDTFGRMR-DVVLSIVNDLtiAESNcpRGARVAVVTYNNEVTTEIRFADSKRKsvLLDKIKNLQValT 2275
Cdd:pfam13519    1 LVFVLDTSGSMRNGDYGPTRlEAAKDAVLAL--LKSL--PGDRVGLVTFGDGPEVLIPLTKDRAK--ILRALRRLEP--K 72

                           90       100       110
                   ....*....|....*....|....*....|....
gi 55743106   2276 SKQQSLETAMSFvARNTFKRVRNGflMRKVAVFF 2309
Cdd:pfam13519   73 GGGTNLAAALQL-ARAALKHRRKN--QPRRIVLI 103
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 171-390 3.31e-06

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: 51.48  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  171 FGLGAQAASRAELQHIATDDNLVFTVPEFRSFGDLQEKLLPYIVGVAQRHIVLKPPTIVTQVIEVNKRDIVFLVDGS-SA 249
Cdd:COG1240   26 LLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASgSM 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  250 LGLANFN----AIRDFIAKVIQRLEIGqdLIqvAVAQYADTVRPefyfnthPT--KREVITAVRKMKPLDGSALYTG--S 321
Cdd:COG1240  106 AAENRLEaakgALLDFLDDYRPRDRVG--LV--AFGGEAEVLLP-------LTrdREALKRALDELPPGGGTPLGDAlaL 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55743106  322 ALDFVRnnlftssagyRAAEGIPKLLVLITGGK---SLDEISQPAQELKRSSIMAFAI--GNKGADQAELEEIA 390
Cdd:COG1240  175 ALELLK----------RADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIgvGTEAVDEGLLREIA 238
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 2413-2593 5.18e-06

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: 49.21  E-value: 5.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2413 DMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDPkasqhfARVAVVQHapseSVDnasmppVKVEFSLTDYGSKEKL 2492
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDG------VQVGLVQY----SDD------PRTEFDLNAYTSKEDV 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2493 VDFLSRgMTQLQGTRALGSAIEYTIENVF-ESAPNPRDLKIVVLMLTGEVPEQQLEEAQRVilqAKCKGYFFVVLGIgRK 2571
Cdd:cd01482   66 LAAIKN-LPYKGGNTRTGKALTHVREKNFtPDAGARPGVPKVVILITDGKSQDDVELPARV---LRNLGVNVFAVGV-KD 140

                        170       180
                 ....*....|....*....|..
gi 55743106 2572 VNIKEVYTFASEPNDVFFKLVD 2593
Cdd:cd01482  141 ADESELKMIASKPSETHVFNVA 162
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1432-1602 7.47e-06

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: 48.92  E-value: 7.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1432 ADIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDG------DSIQVGLVQYNSDPTDEF-FLKDFSTKRQIIDAINKVV 1504
Cdd:cd01480    3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYyrkdpaGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1505 Y-KGGRHANT--KVGLEHLRVnhfvpeaGSRLDQRvpQIAFVITGG-----------KSVEDAQDVslaltqrGVKVFAV 1570
Cdd:cd01480   83 YiGGGTFTDCalKYATEQLLE-------GSHQKEN--KFLLVITDGhsdgspdggieKAVNEADHL-------GIKIFFV 146

                        170       180       190
                 ....*....|....*....|....*....|..
gi 55743106 1571 GVRNIDSEEVGKIASNSATAFRVGNVQELSEL 1602
Cdd:cd01480  147 AVGSQNEEPLSRIACDGKSALYRENFAELLWS 178
VWA_2 pfam13519
von Willebrand factor type A domain;
240-339 1.27e-05

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 46.52  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    240 IVFLVDGS-----SALGLANFNAIRDFIAKVIQRLEIGQdliqVAVAQYADTVRPEFYFNTHPTKreVITAVRKMKPLDG 314
Cdd:pfam13519    1 LVFVLDTSgsmrnGDYGPTRLEAAKDAVLALLKSLPGDR----VGLVTFGDGPEVLIPLTKDRAK--ILRALRRLEPKGG 74

                           90       100
                   ....*....|....*....|....*
gi 55743106    315 SAlYTGSALDFVRNNLFTSSAGYRA 339
Cdd:pfam13519   75 GT-NLAAALQLARAALKHRRKNQPR 98
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 1878-2160 1.36e-05

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 50.77  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1878 FQGCPGQrGVKGSRGFPGEKGEvgeigldgldGEDGDKGLPGSSGekGNPGRRGDKGPRGEKGERGdvgirgdPGNPGQD 1957
Cdd:cd21118  121 WQGSGGH-GAYGSQGGPGVQGH----------GIPGGTGGPWASG--GNYGTNSLGGSVGQGGNGG-------PLNYGTN 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1958 SQ----------ERGPKGETGDLGPmgvPGRDGVPGGpgetgknggfgrrgppgakGNKGGPGQPGFEGEQGTRGAQGPA 2027
Cdd:cd21118  181 SQgavaqpgygtVRGNNQNSGCTNP---PPSGSHESF-------------------SNSGGSSSSGSSGSQGSHGSNGQG 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2028 GPAGPpgliGEQGISGPRGSGGAAGAPGERGRTGPLGRKGEPGEPGPKGGIGNRGPRGETGDDGrdgvGSEGRRGKKger 2107
Cdd:cd21118  239 SSGSS----GGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSSGGSG----GSGGGNKPE--- 307

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 55743106 2108 gfPGYPGPK-GNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAGP 2160
Cdd:cd21118  308 --CNNPGNDvRMAGGGGSQGSKESSGSHGSNGGNGQAEAVGGLNTLNSDASTLP 359
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 1026-1176 1.42e-05

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 49.71  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1026 RDVVFLIDGSQS-AGPEFQYVRTLIERLVDYLDvgfDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGrqI 1104
Cdd:COG2304   92 LNLVFVIDVSGSmSGDKLELAKEAAKLLVDQLR---PGDRVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQAGGG--T 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1105 NVGNALEYVsrniFKRPLGSRIEEGVPQfLVLISSGKSDDEVDDPAV------ELKQFGVAPFTIA--RNADQEELVKIS 1176
Cdd:COG2304  167 ALGAGLELA----YELARKHFIPGRVNR-VILLTDGDANVGITDPEEllklaeEAREEGITLTTLGvgSDYNEDLLERLA 241
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1631-1785 2.30e-05

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: 47.29  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1631 LDVILGFDGSRDqnvfVAQKGFESKVDAILNRISQMHrvscSGGRSptVRVSVVANTPSGPVEaFDFDEYQ--PEMLEKF 1708
Cdd:cd01450    1 LDIVFLLDGSES----VGPENFEKVKDFIEKLVEKLD----IGPDK--TRVGLVQYSDDVRVE-FSLNDYKskDDLLKAV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1709 RNMRSQ-HPYVLTEDTLKV---YLNKFRQSSPDSVKVVIHFTDGADGDLADLHRASENLRQEGVrALILVGLERVV--NL 1782
Cdd:cd01450   70 KNLKYLgGGGTNTGKALQYaleQLFSESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGI-KVFVVGVGPADeeEL 148


                 ...
gi 55743106 1783 ERL 1785
Cdd:cd01450  149 REI 151
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 2135-2167 8.33e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 8.33e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 55743106   2135 GRRGNSGPPGIVGQKGDPGYPGPAGPKGNRGDS 2167
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEP 33
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1980-2084 8.33e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 8.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1980 GVPGGPGETGknggfgrrgppgAKGNKGGPGQPGFEGEQGTRgaqgpagpagppgliGEqgisgprgsggaagapgergr 2059
Cdd:pfam01391    1 GPPGPPGPPG------------PPGPPGPPGPPGPPGPPGPP---------------GE--------------------- 32

                           90       100
                   ....*....|....*....|....*
gi 55743106   2060 TGPLGRKGEPGEPGPKGGIGNRGPR 2084
Cdd:pfam01391   33 PGPPGPPGPPGPPGPPGAPGAPGPP 57
Kunitz_MitTx cd22610
Micrurus tener tener Kunitz-type neurotoxin MitTx-alpha; Micrurus tener tener Kunitz-type ...
 2915-2956 2.15e-04

Micrurus tener tener Kunitz-type neurotoxin MitTx-alpha; Micrurus tener tener Kunitz-type neurotoxin MitTx-alpha is a subunit of the pain-inducing, heterodimeric polypeptide toxin that activates acid sensing ion channel a (ASIC1a) at nanomolar concentrations in a pH-independent manner. Acid sensing ion channels (ASICs) are sodium-selective, voltage-independent and amiloride-blockable ion channels that detect extracellular protons produced during inflammation or ischemic injury, and belong to the superfamily of degenerin/epithelial sodium channels. Subtype ASICa is expressed by primary afferent sensory neurons and is activated by MitTx. MitTx consists of two, non-covalently associated alpha and beta subunits that resemble Kunitz and phospholipase-A2 proteins, respectively, and together they function as a potent and selective ASIC1a agonist. The MitTx-alpha structures is similar to those of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438653  Cd Length: 59  Bit Score: 41.54  E-value: 2.15e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 55743106 2915 CRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2956
Cdd:cd22610   16 CGAFVDSYYFNRSRITCVHFFYGQCDVNQNHFTTMSECNRVC 57
PHA03169 PHA03169
hypothetical protein; Provisional
 1882-2116 2.16e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.50  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1882 PGQRGVKGSRGF------PGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVGiRGDPGNPG 1955
Cdd:PHA03169   33 AGRRRGTAARAAkpappaPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSP-TPSPSGSA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1956 QDSQERGPKGETGDLGPMGvPGRDGVPGGPGETGKNGGFGRRGPPGAKGNKGGPGQPGFEGEQGTRGaqgpagpagppgl 2035
Cdd:PHA03169  112 EELASGLSPENTSGSSPES-PASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEE------------- 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  2036 iGEQGISGPRGSGGAagapgergrtGPLGRKGEPGEPGPKGGIGNRGPRGETGD-----DGRDGVGSEGRRGKKGERGfP 2110
Cdd:PHA03169  178 -PEPPTSEPEPDSPG----------PPQSETPTSSPPPQSPPDEPGEPQSPTPQqapspNTQQAVEHEDEPTEPEREG-P 245


                  ....*.
gi 55743106  2111 GYPGPK 2116
Cdd:PHA03169  246 PFPGHR 251
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1974-2086 2.25e-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: 41.33  E-value: 2.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1974 GVPGRDGVPGGPgetgknggfgrrgppgakGNKGGPGQPGFEGEQGTRgaqgpagpagppgligeqgisgprgsggaaga 2053
Cdd:pfam01391    1 GPPGPPGPPGPP------------------GPPGPPGPPGPPGPPGPP-------------------------------- 30

                           90       100       110
                   ....*....|....*....|....*....|...
gi 55743106   2054 pgergrtGPLGRKGEPGEPGPKGGIGNRGPRGE 2086
Cdd:pfam01391   31 -------GEPGPPGPPGPPGPPGPPGAPGAPGP 56
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 2194-2333 2.45e-04

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: 45.07  E-value: 2.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2194 PTELAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIAesncPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQVA 2273
Cdd:cd01475    2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVG----PDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55743106 2274 LTSKQQSLetAMSFVARNTFK-----RVRNGFLMRKVAVFfsnTPTRASPQLREAVLKLSDAGIT 2333
Cdd:cd01475   78 ETGTMTGL--AIQYAMNNAFSeaegaRPGSERVPRVGIVV---TDGRPQDDVSEVAAKARALGIE 137
VWA pfam00092
von Willebrand factor type A domain;
1632-1785 3.94e-04

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 43.80  E-value: 3.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1632 DVILGFDGSRDqnvfVAQKGFESKVDAILNRISQMhrvscsgGRSP-TVRVSVV--ANTPsgpVEAFDFDEYQ--PEMLE 1706
Cdd:pfam00092    1 DIVFLLDGSGS----IGGDNFEKVKEFLKKLVESL-------DIGPdGTRVGLVqySSDV---RTEFPLNDYSskEELLS 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1707 KFRNMRSQ-HPYVLTEDTLK-VYLNKFRQSS---PDSVKVVIHFTDGADGDLaDLHRASENLRQEGVRaLILVGLERVVN 1781
Cdd:pfam00092   67 AVDNLRYLgGGTTNTGKALKyALENLFSSAAgarPGAPKVVVLLTDGRSQDG-DPEEVARELKSAGVT-VFAVGVGNADD 144


                   ....*.
gi 55743106   1782 --LERL 1785
Cdd:pfam00092  145 eeLRKI 150
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 33-187 3.95e-04

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: 44.93  E-value: 3.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   33 DSADIIFLIDGSNNTGSVN-FAVILDFLVNLLEKLPigtQQIRVGVVQFSDEPRTMFSLdTYStKAQVLGAVKALGFAGG 111
Cdd:COG1240   91 RGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPL-TRD-REALKRALDELPPGGG 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  112 elANIGLALDFVVEnHFTRAGGSRveegvPQVLVLISAGPSSDEIRYGVVALKQAS-----VFSFGLGAQAASRAELQHI 186
Cdd:COG1240  166 --TPLGDALALALE-LLKRADPAR-----RKVIVLLTDGRDNAGRIDPLEAAELAAaagirIYTIGVGTEAVDEGLLREI 237


                 .
gi 55743106  187 A 187
Cdd:COG1240  238 A 238
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 1432-1607 4.75e-04

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: 43.65  E-value: 4.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1432 ADIVFLLD--GSINfrrDSFQEVLRFVSEIVDTVYEDGdsIQVGLVQYNSDPTDEFFLKDFSTK-RQIIDAINKVVYKGG 1508
Cdd:cd01474    5 FDLYFVLDksGSVA---ANWIEIYDFVEQLVDRFNSPG--LRFSFITFSTRATKILPLTDDSSAiIKGLEVLKKVTPSGQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1509 RHANTkvGLEHLRVNHFVPEAGSRldqRVPQIAFVITGGKSVED----AQDVSLALTQRGVKVFAVGVRNIDSEEVGKIA 1584
Cdd:cd01474   80 TYIHE--GLENANEQIFNRNGGGR---ETVSVIIALTDGQLLLNghkyPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIA 154

                        170       180
                 ....*....|....*....|....
gi 55743106 1585 SNSATAFRV-GNVQELSELSEQVL 1607
Cdd:cd01474  155 DSKEYVFPVtSGFQALSGIIESVV 178
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 2412-2613 5.15e-04

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: 43.53  E-value: 5.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2412 IDMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDPKASQHFARVAVVQHAPSESVDNASMPpvkvefSLTDYGSKEK 2491
Cdd:cd01480    3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRKDPAGSWRVGVVQYSDQQEVEAGFLR------DIRNYTSLKE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2492 LVDflsrGMTQLQGTRALGSAIEYTIENVFESAPNPRdLKIVVLMLTGEV-------PEQQLEEAQRVILqakckGYFFV 2564
Cdd:cd01480   77 AVD----NLEYIGGGTFTDCALKYATEQLLEGSHQKE-NKFLLVITDGHSdgspdggIEKAVNEADHLGI-----KIFFV 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 55743106 2565 VlgIGRKVNikevytfasEPNDVFfkLVDKSTELNEEPlmrFGRLLPSF 2613
Cdd:cd01480  147 A--VGSQNE---------EPLSRI--ACDGKSALYREN---FAELLWSF 179
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 814-973 5.76e-04

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: 44.54  E-value: 5.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  814 APAPVSGEKDVVFLLD--GSEGVRSGFPLLKEFVQRVVESLdvgQDRVRVAVVQYSDRTRPEFYLNSymNKQDVVNAVRQ 891
Cdd:COG1240   85 ALARPQRGRDVVLVVDasGSMAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTR--DREALKRALDE 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  892 LTLLGGpTPnTGAALEfvlrniLVSSAGSRITEGVPQLLIVLT---ADRSGDDVRNPSVVVKRGGA--VPIGIGIGNADI 966
Cdd:COG1240  160 LPPGGG-TP-LGDALA------LALELLKRADPARRKVIVLLTdgrDNAGRIDPLEAAELAAAAGIriYTIGVGTEAVDE 231


                 ....*..
gi 55743106  967 TEMQTIS 973
Cdd:COG1240  232 GLLREIA 238
PHA03169 PHA03169
hypothetical protein; Provisional
 1922-2149 7.15e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 44.96  E-value: 7.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1922 GEKGNPGRRGDKGPRGEK---------GERGDVGIRGDPGNPGQDSQE-----RGPKGETGDLGPMGvPGRDGVPGGPGE 1987
Cdd:PHA03169   28 GTREQAGRRRGTAARAAKpappapttsGPQVRAVAEQGHRQTESDTETaeesrHGEKEERGQGGPSG-SGSESVGSPTPS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1988 TGKNGGFGRRGPPGAKGNKGGPGQPGFEGEQGTrgaqgpagpagppgligeqgisgprgsggaagapgERGRTGPlgrkG 2067
Cdd:PHA03169  107 PSGSAEELASGLSPENTSGSSPESPASHSPPPS-----------------------------------PPSHPGP----H 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  2068 EPGEPGPKGGIGNRGPRGETGDDGRDGV-------------GSEGRRGKKGERGFPGYPGPK--GNPGEPGLNGTTGPKG 2132
Cdd:PHA03169  148 EPAPPESHNPSPNQQPSSFLQPSHEDSPeepepptsepepdSPGPPQSETPTSSPPPQSPPDepGEPQSPTPQQAPSPNT 227

                         250       260       270
                  ....*....|....*....|....*....|....
gi 55743106  2133 IRG----------RRGNSGPPG-------IVGQK 2149
Cdd:PHA03169  228 QQAvehedeptepEREGPPFPGhrshsytVVGWK 261
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 2195-2332 7.92e-04

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: 42.66  E-value: 7.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2195 TELAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIAesncPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQV-- 2272
Cdd:cd01482    1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIG----PDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYkg 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55743106 2273 --ALTSKqqsletAMSFVARNTFK---RVRNGFlmRKVAVFFsnTPTRASPQLREAVLKLSDAGI 2332
Cdd:cd01482   77 gnTRTGK------ALTHVREKNFTpdaGARPGV--PKVVILI--TDGKSQDDVELPARVLRNLGV 131
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 2194-2271 8.13e-04

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: 43.14  E-value: 8.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2194 PTELAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIAESNCPR--GARVAVVTYNNEVTTEIRFADSKR-KSVLLDKIKNL 2270
Cdd:cd01480    2 PVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRKDPagSWRVGVVQYSDQQEVEAGFLRDIRnYTSLKEAVDNL 81


                 .
gi 55743106 2271 Q 2271
Cdd:cd01480   82 E 82
VWA_2 pfam13519
von Willebrand factor type A domain;
1434-1521 1.17e-03

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 40.74  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   1434 IVFLLDGS-----INFRRDSFQEVLRFVSEIVDTVYEDgdsiQVGLVQYNSDPTDEFFLKDfsTKRQIIDAINKVVYKGG 1508
Cdd:pfam13519    1 LVFVLDTSgsmrnGDYGPTRLEAAKDAVLALLKSLPGD----RVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90
                   ....*....|...
gi 55743106   1509 rHANTKVGLEHLR 1521
Cdd:pfam13519   75 -GTNLAAALQLAR 86
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 433-549 1.36e-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: 42.66  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  433 DIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTP-----VTEFSLNtyqTKSDILGHLRQLQLQ- 506
Cdd:cd01470    2 NIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPkeivsIRDFNSN---DADDVIKRLEDFNYDd 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 55743106  507 --GGSGLNTGSALSYVY----------ANHFteaggSRIReHVpqlLLLLTAGQS 549
Cdd:cd01470   79 hgDKTGTNTAAALKKVYermalekvrnKEAF-----NETR-HV---IILFTDGKS 124
VWA_2 pfam13519
von Willebrand factor type A domain;
632-722 1.45e-03

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 40.35  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106    632 ILFLFDGSANLVGQ------FPVVRDFLYKIIDELNvkpeGTRIAVAQYSDDVKVESRFDEHQSKpeILNLVKRMKIKTG 705
Cdd:pfam13519    1 LVFVLDTSGSMRNGdygptrLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLTKDRAK--ILRALRRLEPKGG 74

                           90
                   ....*....|....*..
gi 55743106    706 KAlNLGYALDYAQRYIF 722
Cdd:pfam13519   75 GT-NLAAALQLARAALK 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 2787-2855 1.53e-03

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: 40.17  E-value: 1.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55743106 2787 REVQVFEITENSAKLHWERAEPPGP----YFYDLTVTSAHDQSLVLKQNLTVTDRVIGGLLAGQTYHVAVVCY 2855
Cdd:cd00063    5 TNLRVTDVTSTSVTLSWTPPEDDGGpitgYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
Kunitz_ornithodorin_C-like cd22612
C-terminal Kunitz domain of inhibitor ornithodorin and similar proteins; The Kunitz inhibitor ...
 2913-2956 2.55e-03

C-terminal Kunitz domain of inhibitor ornithodorin and similar proteins; The Kunitz inhibitor ornithodorin is a highly selective and potent thrombin inhibitor isolated from blood sucking soft tick Ornithodoros moubata. Ornithodorin is a two-domain protein that resembles the tick anticoagulant peptide (TAP) isolated from the same organism, especially the N-terminal domain; this model contains the C-terminal domain. While the N-terminal domain binds to the active site of thrombin, this C-terminal domain binds at the fibrinogen recognition exosite. The structure of this domain is similar to those of Kunitz-type proteinase inhibitors such as BPTI (bovine pancreatic trypsin inhibitor), showing an alpha/beta fold with irregular secondary structure stabilized by three disulfide bonds.


Pssm-ID: 438655  Cd Length: 49  Bit Score: 38.03  E-value: 2.55e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 55743106 2913 GTCRDFILKWYYDPNTKSCARFWYGgCGGNENKFGSQKECEKVC 2956
Cdd:cd22612    7 TSCAEGAEITYYDSDSRTCKVLAAG-CPSGENAFESEIECQVAC 49
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 1229-1369 2.60e-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: 41.10  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1229 ADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIgpsKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPL 1308
Cdd:cd01465    1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRP---DDRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTAGGSTAG 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55743106 1309 NTG--KALEFVARNlFVKSAGSRI---EDGVPQHlvlvlGGKSQDDVSRFAQVIRSSGI--VSLGVGD 1369
Cdd:cd01465   78 GAGiqLGYQEAQKH-FVPGGVNRIllaTDGDFNV-----GETDPDELARLVAQKRESGItlSTLGFGD 139
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 1910-2167 3.30e-03

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 43.06  E-value: 3.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1910 GEDGDKGLPGSSGEKGN---PGRRGDKGPRGEKGERGDVGIRG--DPG-NPGQDSQERGPKGETGDLGPMGVPGRDGVpG 1983
Cdd:cd21118   70 GEEGGSTLGSRGDVFEHrlgEAARSLGNAGNEIGRQAEDIIRHgvDAVhNSWQGSGGHGAYGSQGGPGVQGHGIPGGT-G 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1984 GPGETGKNGGFGRRGPPGAKGNKGGP-----------GQPGFEGEQGTRGaqgpagpagppgligEQGIsgprgsggaag 2052
Cdd:cd21118  149 GPWASGGNYGTNSLGGSVGQGGNGGPlnygtnsqgavAQPGYGTVRGNNQ---------------NSGC----------- 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2053 apgergrTGPLGRKGEPGEpGPKGGIGNRGPRGETGDDGRDGVGSEGRRGKKGERGFPGypGPKGNPGEPGlnGTTGpkg 2132
Cdd:cd21118  203 -------TNPPPSGSHESF-SNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNG--SSSSNSGNSG--GSNG--- 267

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 55743106 2133 irGRRGNSGPPGIVGQKGDPGYPGPAGPKGNRGDS 2167
Cdd:cd21118  268 --GSSGNSGSGSGGSSSGGSNGWGGSSSSGGSGGS 300
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
1027-1191 4.82e-03

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 41.06  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1027 DVVFLIDGSQS-AGPEFQYV----RTLIERLVDYLDVGfDTTRVAVIQFSDDPKVEFLLnahSSKDEVQnaVQRLRPKGG 1101
Cdd:COG4245    7 PVYLLLDTSGSmSGEPIEALneglQALIDELRQDPYAL-ETVEVSVITFDGEAKVLLPL---TDLEDFQ--PPDLSASGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 1102 rqINVGNALEYVsRNIFKRPLGSRIEEGVPQF---LVLISSGK-SDDEVDDPAVELKQFGVAP----FTIA--RNADQEE 1171
Cdd:COG4245   81 --TPLGAALELL-LDLIERRVQKYTAEGKGDWrpvVFLITDGEpTDSDWEAALQRLKDGEAAKkaniFAIGvgPDADTEV 157

                        170       180
                 ....*....|....*....|...
gi 55743106 1172 LVKISlSPEYVFSVS---TFREL 1191
Cdd:COG4245  158 LKQLT-DPVRALDALdglDFREF 179
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 1883-1969 4.86e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.58  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1883 GQRGVKGSRGFPGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVGIRGDPGNPGQDSQERG 1962
Cdd:PRK12678  134 GEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGD 213


                  ....*..
gi 55743106  1963 PKGETGD 1969
Cdd:PRK12678  214 RREERGR 220
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 2195-2293 6.49e-03

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: 40.42  E-value: 6.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106 2195 TELAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIAESNCprgaRVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNL-QVA 2273
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKT----QFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHIsQLL 76

                         90       100
                 ....*....|....*....|
gi 55743106 2274 LTSKQQsleTAMSFVARNTF 2293
Cdd:cd01469   77 GLTNTA---TAIQYVVTELF 93
PTZ00146 PTZ00146
fibrillarin; Provisional
 2064-2122 7.55e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 41.26  E-value: 7.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 55743106  2064 GRKGEPGEPGPKGGIGNRGPRGETGddGRDGVGSEGRRGKKGERGFPGYPGPKGNPGEP 2122
Cdd:PTZ00146    5 GFGGGRGGGRGGGGGGGRGGGGRGG--GRGGGRGRGRGGGGGGRGGGGGGGPGKVIVVP 61
PHA03169 PHA03169
hypothetical protein; Provisional
 1831-1971 7.95e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.49  E-value: 7.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  1831 SGQRGDRGPIGSIGPKGIPGEDGYRGYPGDEGGPGERGPPGVNGTQGFQGCPGQrgvkGSRGFPGEKGEVGEIGLDGLDG 1910
Cdd:PHA03169   93 SGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGP----HEPAPPESHNPSPNQQPSSFLQ 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55743106  1911 EDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVGIRG--DPGNPGQDSQERGPKGETGDLG 1971
Cdd:PHA03169  169 PSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPpdEPGEPQSPTPQQAPSPNTQQAV 231
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 36-196 8.00e-03

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 39.99  E-value: 8.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106   36 DIIFLIDGSNNTGSVNF--AVIlDFLVNLLEKLPIGTQQIRVGVVQFSDEPRT--MFSLDTYSTKAQVLGAVKAL--GFA 109
Cdd:cd01473    2 DLTLILDESASIGYSNWrkDVI-PFTEKIINNLNISKDKVHVGILLFAEKNRDvvPFSDEERYDKNELLKKINDLknSYR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55743106  110 GGELANIGLALDFVVENhFTRAGGSRveEGVPQVLVLISAG---PSSDEIRYGVVAL-KQASVFSFGLGAQAASRAELQH 185
Cdd:cd01473   81 SGGETYIVEALKYGLKN-YTKHGNRR--KDAPKVTMLFTDGndtSASKKELQDISLLyKEENVKLLVVGVGAASENKLKL 157

                        170
                 ....*....|....*
gi 55743106  186 IA----TDDNLVFTV 196
Cdd:cd01473  158 LAgcdiNNDNCPNVI 172
 
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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