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Conserved domains on  [gi|657584108|ref|XP_008296193|]
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PREDICTED: collagen alpha-6(VI) chain isoform X3 [Stegastes partitus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 33-197 1.36e-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: 214.01  E-value: 1.36e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   33 ADIVFLIDGSSSIGISNFQEIRQFLRSVISGLDIGADKVRIGLAQYSDEPYQEFLLKDHMDKQSLLAAVDTFQYRTGGTE 112
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  113 TGEAIDFLMNQYFTEDAGSRAKqrVPQIAVVITDGDSTDDVAAPALRLRQHGVIMFAIGVGKANPTELEAIANRPPKRFM 192
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREG--VPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYV 158


                  ....*
gi 657584108  193 FTIDN 197
Cdd:cd01472   159 FNVAD 163
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 419-587 6.16e-57

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: 195.14  E-value: 6.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  419 ADIVFIVDESGSIGVANFQMVRTFLHSIISGLEISPTRVRVGIVMYNDrpaDQAQQVYLNTFNNKDELLKFIKILPYHGG 498
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSD---DPRTEFYLNTYRSKDDVLEAVKNLRYIGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  499 GTNTGAALKFARESVFIKERGSRKdkGVQQVAVVITDGESQDDVSQPAADLRRAGVTIYSVGVKNANKVQLVEMASHPPN 578
Cdd:cd01472    78 GTNTGKALKYVRENLFTEASGSRE--GVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKE 155


                  ....*....
gi 657584108  579 KHVFIVDSF 587
Cdd:cd01472   156 LYVFNVADF 164
VWA pfam00092
von Willebrand factor type A domain;
816-984 9.84e-48

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 168.99  E-value: 9.84e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   816 DLLFLIDSSGSIYPQDYNKMKDFMKSVISKSFIGQNEVHVGVMQFSTIQKLEFPLNRFYSKGEMSKAIDDMQQIGGGT-H 894
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   895 TGEAITDV-SQYFDSSRGGRPGLRQRLVVITDGEAQDV-VRGPAAALRAKGVVVYAIGVVDANTTQLLEISGSPD--RMY 970
Cdd:pfam00092   81 TGKALKYAlENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegHVF 160

                          170
                   ....*....|....
gi 657584108   971 AERDFDALKDLESQ 984
Cdd:pfam00092  161 TVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
1195-1362 1.99e-47

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 168.22  E-value: 1.99e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1195 DLVFLIDQSGSIASTDYSIMKKFTTELVNSFKVSEDLVRVGLAQFSSNFQNEFYLNQFYTEEAVSKHIFNMRQLGGGT-N 1273
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1274 IGLALDS-IREYFEASRGCRRsaGISQNLVLITDGESQD-DVEDAAERLRALGIEVFAIGIGNVHDLELLQITGTP--ER 1349
Cdd:pfam00092   81 TGKALKYaLENLFSSAAGARP--GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPgeGH 158

                          170
                   ....*....|...
gi 657584108  1350 LFTVENFGSLEKI 1362
Cdd:pfam00092  159 VFTVSDFEALEDL 171
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 629-790 4.97e-45

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: 160.86  E-value: 4.97e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  629 ADIFFLIDHSGSIYPTDFQDMKKFIIEFIHTFRISPQHVRLGVAKYADSPNLEFDLTDYSDAKSVEKAVEGIRQIGGGTE 708
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  709 TGRALAFMSPHFDRAMTTRGHKVPEYLVVITDGKSSDKVKVPAEQLRAQGVIVYSIGVKSADMEELREISGDPKRT--FF 786
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELyvFN 160


                  ....
gi 657584108  787 VNNF 790
Cdd:cd01472   161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
1003-1176 6.19e-45

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 161.29  E-value: 6.19e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1003 DIIFLVDGSTSITLAKFRNMQRFMESMVNQTTVGKDLTRFGVILYSNDPKSVFTLNQYSSKKEVVKAISNLR-SPFGDTY 1081
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRyLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1082 TGKALAYSLQ-FFDAQHGGRAalQVPQILMVITDGDATDrNSLVAPSVALRDHGVSVFSIGVEGANMTQLEIMAGYDRSK 1160
Cdd:pfam00092   81 TGKALKYALEnLFSSAAGARP--GAPKVVVLLTDGRSQD-GDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                          170
                   ....*....|....*..
gi 657584108  1161 -VFYVDNFEALETLYKN 1176
Cdd:pfam00092  158 hVFTVSDFEALEDLQDQ 174
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1591-1853 1.45e-43

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: 166.23  E-value: 1.45e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1591 GHEGIRGSRGLPGSKGVSGQKGYPGFPGEEGIAGDRGSPGPSGPQGVQGCSGRRGVKGFRGLRGNRGEDGEDGLDGVDGE 1670
Cdd:NF038329  132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1671 QGLTGADGGRGERGNPGNPGipgirgeaglKGQRGLRGDPGEPGADnnspgakGDSGNAGLPGLPGPDGRPGESGIVGNP 1750
Cdd:NF038329  212 AGPDGEAGPAGEDGPAGPAG----------DGQQGPDGDPGPTGED-------GPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1751 GQDGRRGSPgvkgaagepgaaglqGIPGASGPQGTRGVRGQPGPRgipglpgpqggpgsvggpgaagrrggnGQKGQPGD 1830
Cdd:NF038329  275 GKDGERGPV---------------GPAGKDGQNGKDGLPGKDGKD---------------------------GQNGKDGL 312

                         250       260
                  ....*....|....*....|...
gi 657584108 1831 PGDKGVPGPLGPRGMPGEDGRDG 1853
Cdd:NF038329  313 PGKDGKDGQPGKDGLPGKDGKDG 335
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 228-387 2.05e-35

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: 133.60  E-value: 2.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  228 ADIFFLVDS--GISQAEFQQVRSVLVRLTNQVNFGASAHRLGLAQYGQDIKVEFLLNAFQSKDEMQGGIKRFRqrrLQTN 305
Cdd:cd01481     1 KDIVFLIDGsdNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLR---LRGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  306 EPRNLGSALQYASANFFTSEAGSRADQGYRQYLVVLSGKDSDDEVFRQSRLIKSEGVTVVGM-SLGASMNEIRVISTAP- 383
Cdd:cd01481    78 SQLNTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIgARNADLAELQQIAFDPs 157


                  ....
gi 657584108  384 YAYQ 387
Cdd:cd01481   158 FVFQ 161
Kunitz_collagen_alpha6_VI-like cd22631
Kunitz-type domain from the alpha6 chain of fish type VI collagen, and similar proteins; This ...
 2512-2562 1.42e-34

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: 126.96  E-value: 1.42e-34
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22631     1 CLLGQDAGSCQNYTMMWFFDSKQGRCSRFWYGGCGGNANRFETQEECENLC 51
Kunitz_papilin cd22635
Kunitz domain of papilin, and similar proteins; This model includes the Kunitz domain found in ...
 2439-2490 1.17e-33

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: 124.30  E-value: 1.17e-33
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGIQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22635     1 CLLDKDAGTVCGDYVQRWYYDPATGACNRFWYGGCGGNANRFATEAECLRTC 52
VWA pfam00092
von Willebrand factor type A domain;
1956-2097 8.76e-19

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 86.17  E-value: 8.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1956 ELVFGLDMSDDVTPTAFERQRSALLALLEEINIaesnCPSGARVAVVGYSAYTKYLIRFQDYRRKTQLEDAVKNIALeRT 2035
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDI----GPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRY-LG 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657584108  2036 SNKRHLGAAMHFVAQNVFKRVRSGMV-MRKVAVFFSNGPSQEvNDIPGAVMEYRGLNIVPAVI 2097
Cdd:pfam00092   76 GGTTNTGKALKYALENLFSSAAGARPgAPKVVVLLTDGRSQD-GDPEEVARELKSAGVTVFAV 137
VWA pfam00092
von Willebrand factor type A domain;
2166-2338 2.78e-18

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 84.63  E-value: 2.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  2166 DLVMVADSSREIQADQYAGVQQLLGSVVEQLAVSPQprragnQARVAVVQQGGarSAKVEFNLQTYQNQELMRTHLTQKM 2245
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPD------GTRVGLVQYSS--DVRTEFPLNDYSSKEELLSAVDNLR 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  2246 RQQGGSSALGQTLDYTLkEVLLKAGQPSRKKALLAVV----GTSTAWEDQArlhyVSQKAKCEGVALFVVTVGDHYNRtQ 2321
Cdd:pfam00092   73 YLGGGTTNTGKALKYAL-ENLFSSAAGARPGAPKVVVlltdGRSQDGDPEE----VARELKSAGVTVFAVGVGNADDE-E 146

                          170
                   ....*....|....*..
gi 657584108  2322 VEELASLPLQQHLIHVS 2338
Cdd:pfam00092  147 LRKIASEPGEGHVFTVS 163
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1858-1924 1.04e-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: 53.27  E-value: 1.04e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657584108  1858 GRKGVKGDPGFPGYPGLLGEDGLQGPKGLPgrkgnrgrggnsgrsgesGISGDPGYAGHRGPRGLPG 1924
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPP------------------GEPGPPGPPGPPGPPGPPG 49
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1451-1555 2.17e-03

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: 41.29  E-value: 2.17e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   1451 LYDFNFEGYSEDVVQKVMTLS--LAEPTYFNTAMLKSFGQKFKAE--SRAGV-KVLLIFSDGLDDDVMK-LEQESELLRQ 1524
Cdd:smart00327   52 LFPLNDSRSKDALLEALASLSykLGGGTNLGAALQYALENLFSKSagSRRGApKVVILITDGESNDGPKdLLKAAKELKR 131

                            90       100       110
                    ....*....|....*....|....*....|.
gi 657584108   1525 SGISaLLTVALEGVRDIAQLQMVEFGRGFGY 1555
Cdd:smart00327  132 SGVK-VFVVGVGNDVDEEELKKLASAPGGVY 161
 
Name Accession Description Interval E-value
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 33-197 1.36e-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: 214.01  E-value: 1.36e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   33 ADIVFLIDGSSSIGISNFQEIRQFLRSVISGLDIGADKVRIGLAQYSDEPYQEFLLKDHMDKQSLLAAVDTFQYRTGGTE 112
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  113 TGEAIDFLMNQYFTEDAGSRAKqrVPQIAVVITDGDSTDDVAAPALRLRQHGVIMFAIGVGKANPTELEAIANRPPKRFM 192
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREG--VPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYV 158


                  ....*
gi 657584108  193 FTIDN 197
Cdd:cd01472   159 FNVAD 163
VWA pfam00092
von Willebrand factor type A domain;
34-206 2.62e-57

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 196.73  E-value: 2.62e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    34 DIVFLIDGSSSIGISNFQEIRQFLRSVISGLDIGADKVRIGLAQYSDEPYQEFLLKDHMDKQSLLAAVDTFQYRTGGT-E 112
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   113 TGEAIDFLMNQYFTEDAGSRAkqRVPQIAVVITDGDSTD-DVAAPALRLRQHGVIMFAIGVGKANPTELEAIANRPPKRF 191
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARP--GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGH 158

                          170
                   ....*....|....*
gi 657584108   192 MFTIDNYEALQRLTE 206
Cdd:pfam00092  159 VFTVSDFEALEDLQD 173
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 419-587 6.16e-57

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: 195.14  E-value: 6.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  419 ADIVFIVDESGSIGVANFQMVRTFLHSIISGLEISPTRVRVGIVMYNDrpaDQAQQVYLNTFNNKDELLKFIKILPYHGG 498
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSD---DPRTEFYLNTYRSKDDVLEAVKNLRYIGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  499 GTNTGAALKFARESVFIKERGSRKdkGVQQVAVVITDGESQDDVSQPAADLRRAGVTIYSVGVKNANKVQLVEMASHPPN 578
Cdd:cd01472    78 GTNTGKALKYVRENLFTEASGSRE--GVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKE 155


                  ....*....
gi 657584108  579 KHVFIVDSF 587
Cdd:cd01472   156 LYVFNVADF 164
VWA pfam00092
von Willebrand factor type A domain;
420-595 2.48e-54

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 187.87  E-value: 2.48e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   420 DIVFIVDESGSIGVANFQMVRTFLHSIISGLEISPTRVRVGIVMYNDrpaDQAQQVYLNTFNNKDELLKFIKILPYHGGG 499
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSS---DVRTEFPLNDYSSKEELLSAVDNLRYLGGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   500 T-NTGAALKFARESVFIKERGSRkdKGVQQVAVVITDGESQD-DVSQPAADLRRAGVTIYSVGVKNANKVQLVEMASHPP 577
Cdd:pfam00092   78 TtNTGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPG 155

                          170
                   ....*....|....*...
gi 657584108   578 NKHVFIVDSFAKLKSMEQ 595
Cdd:pfam00092  156 EGHVFTVSDFEALEDLQD 173
VWA pfam00092
von Willebrand factor type A domain;
816-984 9.84e-48

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 168.99  E-value: 9.84e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   816 DLLFLIDSSGSIYPQDYNKMKDFMKSVISKSFIGQNEVHVGVMQFSTIQKLEFPLNRFYSKGEMSKAIDDMQQIGGGT-H 894
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   895 TGEAITDV-SQYFDSSRGGRPGLRQRLVVITDGEAQDV-VRGPAAALRAKGVVVYAIGVVDANTTQLLEISGSPD--RMY 970
Cdd:pfam00092   81 TGKALKYAlENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegHVF 160

                          170
                   ....*....|....
gi 657584108   971 AERDFDALKDLESQ 984
Cdd:pfam00092  161 TVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
1195-1362 1.99e-47

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 168.22  E-value: 1.99e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1195 DLVFLIDQSGSIASTDYSIMKKFTTELVNSFKVSEDLVRVGLAQFSSNFQNEFYLNQFYTEEAVSKHIFNMRQLGGGT-N 1273
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1274 IGLALDS-IREYFEASRGCRRsaGISQNLVLITDGESQD-DVEDAAERLRALGIEVFAIGIGNVHDLELLQITGTP--ER 1349
Cdd:pfam00092   81 TGKALKYaLENLFSSAAGARP--GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPgeGH 158

                          170
                   ....*....|...
gi 657584108  1350 LFTVENFGSLEKI 1362
Cdd:pfam00092  159 VFTVSDFEALEDL 171
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 629-790 4.97e-45

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: 160.86  E-value: 4.97e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  629 ADIFFLIDHSGSIYPTDFQDMKKFIIEFIHTFRISPQHVRLGVAKYADSPNLEFDLTDYSDAKSVEKAVEGIRQIGGGTE 708
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  709 TGRALAFMSPHFDRAMTTRGHKVPEYLVVITDGKSSDKVKVPAEQLRAQGVIVYSIGVKSADMEELREISGDPKRT--FF 786
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELyvFN 160


                  ....
gi 657584108  787 VNNF 790
Cdd:cd01472   161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
1003-1176 6.19e-45

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 161.29  E-value: 6.19e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1003 DIIFLVDGSTSITLAKFRNMQRFMESMVNQTTVGKDLTRFGVILYSNDPKSVFTLNQYSSKKEVVKAISNLR-SPFGDTY 1081
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRyLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1082 TGKALAYSLQ-FFDAQHGGRAalQVPQILMVITDGDATDrNSLVAPSVALRDHGVSVFSIGVEGANMTQLEIMAGYDRSK 1160
Cdd:pfam00092   81 TGKALKYALEnLFSSAAGARP--GAPKVVVLLTDGRSQD-GDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                          170
                   ....*....|....*..
gi 657584108  1161 -VFYVDNFEALETLYKN 1176
Cdd:pfam00092  158 hVFTVSDFEALEDLQDQ 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 816-968 1.28e-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: 159.76  E-value: 1.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  816 DLLFLIDSSGSIYPQDYNKMKDFMKSVISKSFIGQNEVHVGVMQFSTIQKLEFPLNRFYSKGEMSKAIDDMQQIGG-GTH 894
Cdd:cd01450     2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGTN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657584108  895 TGEAITDVSQYFDSSRGGRPGLRQRLVVITDGEAQDV--VRGPAAALRAKGVVVYAIGVVDANTTQLLEISGSPDR 968
Cdd:cd01450    82 TGKALQYALEQLFSESNARENVPKVIIVLTDGRSDDGgdPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSE 157
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1194-1356 3.12e-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: 158.60  E-value: 3.12e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1194 ADLVFLIDQSGSIASTDYSIMKKFTTELVNSFKVSEDLVRVGLAQFSSNFQNEFYLNQFYTEEAVSKHIFNMRQLGGGTN 1273
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1274 IGLALDSIRE-YFEASRGCRRsaGISQNLVLITDGESQDDVEDAAERLRALGIEVFAIGIGNVHDLELLQITGTPER--L 1350
Cdd:cd01482    81 TGKALTHVREkNFTPDAGARP--GVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSEthV 158


                  ....*.
gi 657584108 1351 FTVENF 1356
Cdd:cd01482   159 FNVADF 164
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 420-590 6.78e-44

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 158.39  E-value: 6.78e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    420 DIVFIVDESGSIGVANFQMVRTFLHSIISGLEISPTRVRVGIVMYNDRPADqaqQVYLNTFNNKDELLKFIKILPYH-GG 498
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARV---LFPLNDSRSKDALLEALASLSYKlGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    499 GTNTGAALKFARESVFIKERGSRkdKGVQQVAVVITDGESQD---DVSQPAADLRRAGVTIYSVGVKNA-NKVQLVEMAS 574
Cdd:smart00327   78 GTNLGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLAS 155

                           170
                    ....*....|....*.
gi 657584108    575 HPPNKHVFIVDSFAKL 590
Cdd:smart00327  156 APGGVYVFLPELLDLL 171
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1591-1853 1.45e-43

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: 166.23  E-value: 1.45e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1591 GHEGIRGSRGLPGSKGVSGQKGYPGFPGEEGIAGDRGSPGPSGPQGVQGCSGRRGVKGFRGLRGNRGEDGEDGLDGVDGE 1670
Cdd:NF038329  132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1671 QGLTGADGGRGERGNPGNPGipgirgeaglKGQRGLRGDPGEPGADnnspgakGDSGNAGLPGLPGPDGRPGESGIVGNP 1750
Cdd:NF038329  212 AGPDGEAGPAGEDGPAGPAG----------DGQQGPDGDPGPTGED-------GPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1751 GQDGRRGSPgvkgaagepgaaglqGIPGASGPQGTRGVRGQPGPRgipglpgpqggpgsvggpgaagrrggnGQKGQPGD 1830
Cdd:NF038329  275 GKDGERGPV---------------GPAGKDGQNGKDGLPGKDGKD---------------------------GQNGKDGL 312

                         250       260
                  ....*....|....*....|...
gi 657584108 1831 PGDKGVPGPLGPRGMPGEDGRDG 1853
Cdd:NF038329  313 PGKDGKDGQPGKDGLPGKDGKDG 335
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 34-204 1.91e-43

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: 156.85  E-value: 1.91e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108     34 DIVFLIDGSSSIGISNFQEIRQFLRSVISGLDIGADKVRIGLAQYSDEPYQEFLLKDHMDKQSLLAAVDTFQYRTGG-TE 112
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGgTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    113 TGEAIDFLMNQYFTEDAGSRAkqRVPQIAVVITDGDSTD---DVAAPALRLRQHGVIMFAIGVGKA-NPTELEAIANRPP 188
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRR--GAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158

                           170
                    ....*....|....*.
gi 657584108    189 KRFMFTIDNYEALQRL 204
Cdd:smart00327  159 GVYVFLPELLDLLIDL 174
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1603-1887 6.62e-43

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: 164.31  E-value: 6.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1603 GSKGVSGQKGYPGFPGEEGIAGDRGSPGPSGPQGVQGCSGRRGVKGFRGLRGNRGEDGEDGLDGVDGEQGLTGADGGRGE 1682
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1683 RGNPGNPGIPGIRGEAGLKGQRGLRGDPGEPGadnnsPGAKGDSGNAGLPGlpgPDGRPGESGIVGNPGQDGRRGSPGvk 1762
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG-----PAGDGQQGPDGDPG---PTGEDGPQGPDGPAGKDGPRGDRG-- 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1763 gaagepgaaglqgipgasgPQGTRGVRGQPGPRgipglpgpqggpgsvggpgaagrrggngqkgqpGDPGDKGVPGPLGP 1842
Cdd:NF038329  267 -------------------EAGPDGPDGKDGER---------------------------------GPVGPAGKDGQNGK 294

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 657584108 1843 RGMPGEDGRDGY-GPAGRKGVKGDPGFPGYPGLLGEDGLQGPKGLP 1887
Cdd:NF038329  295 DGLPGKDGKDGQnGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
VWA pfam00092
von Willebrand factor type A domain;
630-794 7.37e-42

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 152.43  E-value: 7.37e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   630 DIFFLIDHSGSIYPTDFQDMKKFIIEFIHTFRISPQHVRLGVAKYADSPNLEFDLTDYSDAKSVEKAVEGIRQIGGGT-E 708
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   709 TGRALAF-MSPHFDRAMTTRGHkVPEYLVVITDGKSSDK-VKVPAEQLRAQGVIVYSIGVKSADMEELREISGDP--KRT 784
Cdd:pfam00092   81 TGKALKYaLENLFSSAAGARPG-APKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPgeGHV 159

                          170
                   ....*....|
gi 657584108   785 FFVNNFDALK 794
Cdd:pfam00092  160 FTVSDFEALE 169
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1002-1163 1.57e-41

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: 150.90  E-value: 1.57e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1002 ADIIFLVDGSTSITLAKFRNMQRFMESMVNQTTVGKDLTRFGVILYSNDPKSVFTLNQYSSKKEVVKAISNLRSPFGD-T 1080
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1081 YTGKALAYSLQFFDAQHGGRaaLQVPQILMVITDGDATDRNSLVAPSVALRDHGVSVFSIGVEGANMTQLEIMAGYDRSK 1160
Cdd:cd01450    81 NTGKALQYALEQLFSESNAR--ENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSER 158


                  ...
gi 657584108 1161 VFY 1163
Cdd:cd01450   159 HVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 816-978 4.78e-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: 144.13  E-value: 4.78e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    816 DLLFLIDSSGSIYPQDYNKMKDFMKSVISKSFIGQNEVHVGVMQFSTIQKLEFPLNRFYSKGEMSKAIDDMQQI-GGGTH 894
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    895 TGEAITDVSQY-FDSSRGGRPGLRQRLVVITDGEAQDV---VRGPAAALRAKGVVVYAIGVV-DANTTQLLEISGSPDRM 969
Cdd:smart00327   81 LGAALQYALENlFSKSAGSRRGAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGnDVDEEELKKLASAPGGV 160

                           170
                    ....*....|.
gi 657584108    970 YA--ERDFDAL 978
Cdd:smart00327  161 YVflPELLDLL 171
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1195-1364 1.55e-37

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: 139.90  E-value: 1.55e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   1195 DLVFLIDQSGSIASTDYSIMKKFTTELVNSFKVSEDLVRVGLAQFSSNFQNEFYLNQFYTEEAVSKHIFNMR-QLGGGTN 1273
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   1274 IGLALDSIREY-FEASRGCRRsaGISQNLVLITDGESQD---DVEDAAERLRALGIEVFAIGIGNVHDLELL-QITGTPE 1348
Cdd:smart00327   81 LGAALQYALENlFSKSAGSRR--GAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVDEEELkKLASAPG 158

                           170
                    ....*....|....*.
gi 657584108   1349 RLFTVENFGSLEKIKQ 1364
Cdd:smart00327  159 GVYVFLPELLDLLIDL 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1003-1173 7.74e-37

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: 137.97  E-value: 7.74e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   1003 DIIFLVDGSTSITLAKFRNMQRFMESMVNQTTVGKDLTRFGVILYSNDPKSVFTLNQYSSKKEVVKAISNLR-SPFGDTY 1081
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   1082 TGKALAYSLQ-FFDAQHGGRAalQVPQILMVITDGDATDRNSLVAPSV-ALRDHGVSVFSIGVEGA-NMTQLEIMAG-YD 1157
Cdd:smart00327   81 LGAALQYALEnLFSKSAGSRR--GAPKVVILITDGESNDGPKDLLKAAkELKRSGVKVFVVGVGNDvDEEELKKLASaPG 158

                           170
                    ....*....|....*.
gi 657584108   1158 RSKVFYVDNFEALETL 1173
Cdd:smart00327  159 GVYVFLPELLDLLIDL 174
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 228-387 2.05e-35

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: 133.60  E-value: 2.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  228 ADIFFLVDS--GISQAEFQQVRSVLVRLTNQVNFGASAHRLGLAQYGQDIKVEFLLNAFQSKDEMQGGIKRFRqrrLQTN 305
Cdd:cd01481     1 KDIVFLIDGsdNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLR---LRGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  306 EPRNLGSALQYASANFFTSEAGSRADQGYRQYLVVLSGKDSDDEVFRQSRLIKSEGVTVVGM-SLGASMNEIRVISTAP- 383
Cdd:cd01481    78 SQLNTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIgARNADLAELQQIAFDPs 157


                  ....
gi 657584108  384 YAYQ 387
Cdd:cd01481   158 FVFQ 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 630-798 6.36e-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: 132.58  E-value: 6.36e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    630 DIFFLIDHSGSIYPTDFQDMKKFIIEFIHTFRISPQHVRLGVAKYADSPNLEFDLTDYSDAKSVEKAVEGIRQI-GGGTE 708
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    709 TGRALAF-MSPHFDRAMTTRGHkVPEYLVVITDGKSSDK---VKVPAEQLRAQGVIVYSIGVKSA-DMEELREISGDPKR 783
Cdd:smart00327   81 LGAALQYaLENLFSKSAGSRRG-APKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 657584108    784 TFFVNNFDALKPIKD 798
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
Kunitz_collagen_alpha6_VI-like cd22631
Kunitz-type domain from the alpha6 chain of fish type VI collagen, and similar proteins; This ...
 2512-2562 1.42e-34

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: 126.96  E-value: 1.42e-34
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22631     1 CLLGQDAGSCQNYTMMWFFDSKQGRCSRFWYGGCGGNANRFETQEECENLC 51
Kunitz_papilin cd22635
Kunitz domain of papilin, and similar proteins; This model includes the Kunitz domain found in ...
 2439-2490 1.17e-33

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: 124.30  E-value: 1.17e-33
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGIQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22635     1 CLLDKDAGTVCGDYVQRWYYDPATGACNRFWYGGCGGNANRFATEAECLRTC 52
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1679-1924 3.20e-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: 132.72  E-value: 3.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1679 GRGERGNPGNPGIPGIRGEAGLKGQRGLRGDPGEpgadnnspgaKGDSGNAGLPGLPGPDGRPGESGIVGNPGQDGRRGs 1758
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGP----------AGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG- 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1759 pgvkgaagepgaagLQGIPGASGPQGTRGVRGQPGPRgipglpgpqggpgsvggpgaagrrggngqkGQPGDPGDKGVPG 1838
Cdd:NF038329  184 --------------AKGPAGEKGPQGPRGETGPAGEQ------------------------------GPAGPAGPDGEAG 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1839 PLGPRGMPGEDGRDGYGPAGRKGVKGDPGFPGYPGLLGEDGLQGPKGLPgrkgnrgrggnsgrsgesGISGDPGYAGHRG 1918
Cdd:NF038329  220 PAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA------------------GPDGPDGKDGERG 281


                  ....*.
gi 657584108 1919 PRGLPG 1924
Cdd:NF038329  282 PVGPAG 287
VWA pfam00092
von Willebrand factor type A domain;
229-383 1.58e-28

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 113.91  E-value: 1.58e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   229 DIFFLVDS--GISQAEFQQVRSVLVRLTNQVNFGASAHRLGLAQYGQDIKVEFLLNAFQSKDEMQGGIKRFRQrrlQTNE 306
Cdd:pfam00092    1 DIVFLLDGsgSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRY---LGGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   307 PRNLGSALQYASANFFTSEAGSRAdqGYRQYLVVLS-GKDSDDEVFRQSRLIKSEGVTV--VGMSlGASMNEIRVISTAP 383
Cdd:pfam00092   78 TTNTGKALKYALENLFSSAAGARP--GAPKVVVLLTdGRSQDGDPEEVARELKSAGVTVfaVGVG-NADDEELRKIASEP 154
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1693-1924 9.52e-26

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: 113.08  E-value: 9.52e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1693 GIRGEAGLKGQRGLRGDPGEpgadnnspgaKGDSGNAGLPGLPGPDGRPGESGIVGNPGQDGRRGspgvkgaagepgaag 1772
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGP----------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG--------------- 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1773 lqgipgasgPQGTRGVRGQPGPRGIPGLPGPQGGPGSVGGPGAAGRRGGNGQKGQPGDPGDKGVPGPL-----GPRGMPG 1847
Cdd:NF038329  172 ---------PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPG 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1848 EDGRDGY----GPAGRKGVKGDPGFPGYPGLLGEDGLQGPKGLPGRKGNRGRGGNSGRSGESGISGDPGYAGHRGPRGLP 1923
Cdd:NF038329  243 PTGEDGPqgpdGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322


                  .
gi 657584108 1924 G 1924
Cdd:NF038329  323 G 323
Kunitz_BPTI pfam00014
Kunitz/Bovine pancreatic trypsin inhibitor domain; Indicative of a protease inhibitor, usually ...
 2511-2562 3.69e-23

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: 94.25  E-value: 3.69e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 657584108  2511 ACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:pfam00014    1 ICSLPPDSGPCKASIPRWYYNPTTGTCEPFTYGGCGGNANNFESLEECESTC 52
KU smart00131
BPTI/Kunitz family of serine protease inhibitors; Serine protease inhibitors. One member of ...
 2510-2562 8.39e-23

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: 93.48  E-value: 8.39e-23
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 657584108   2510 DACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:smart00131    1 DVCLLPPDTGPCGGSIPRYYYDPETGTCEPFTYGGCGGNANNFESLEECERTC 53
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1593-1737 3.63e-22

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: 102.29  E-value: 3.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1593 EGIRGSRGLPGSKGVSGQKGYPGFPGEEGIAGDRGSPGPSGPqgvqgcsgrrgvkgfRGLRGNRGEDGEDGLDGVDGEQG 1672
Cdd:NF038329  232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP---------------DGKDGERGPVGPAGKDGQNGKDG 296

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657584108 1673 LTGADGGRGERgnpGNPGIPGIRGEAGLKGQRGLrgdPGEPGADnnspgakgdsgnaGLPGLPGP 1737
Cdd:NF038329  297 LPGKDGKDGQN---GKDGLPGKDGKDGQPGKDGL---PGKDGKD-------------GQPGKPAP 342
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 229-383 2.33e-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: 90.59  E-value: 2.33e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    229 DIFFLVD-SG-ISQAEFQQVRSVLVRLTNQVNFGASAHRLGLAQYGQDIKVEFLLNAFQSKDEMQGGIKRFRQRRLQTNe 306
Cdd:smart00327    1 DVVFLLDgSGsMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGT- 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    307 prNLGSALQYASANFFTSEAGSRAdqGYRQYLVVLS-GKDSDD--EVFRQSRLIKSEGVTV--VGMSLGASMNEIRVIST 381
Cdd:smart00327   80 --NLGAALQYALENLFSKSAGSRR--GAPKVVILITdGESNDGpkDLLKAAKELKRSGVKVfvVGVGNDVDEEELKKLAS 155


                    ..
gi 657584108    382 AP 383
Cdd:smart00327  156 AP 157
Kunitz_BPTI pfam00014
Kunitz/Bovine pancreatic trypsin inhibitor domain; Indicative of a protease inhibitor, usually ...
 2438-2491 5.86e-20

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: 85.39  E-value: 5.86e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 657584108  2438 RCQLDSDSGiQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTCV 2491
Cdd:pfam00014    1 ICSLPPDSG-PCKASIPRWYYNPTTGTCEPFTYGGCGGNANNFESLEECESTCR 53
KU smart00131
BPTI/Kunitz family of serine protease inhibitors; Serine protease inhibitors. One member of ...
 2438-2490 6.40e-19

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: 82.31  E-value: 6.40e-19
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 657584108   2438 RCQLDSDSGIqCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:smart00131    2 VCLLPPDTGP-CGGSIPRYYYDPETGTCEPFTYGGCGGNANNFESLEECERTC 53
VWA pfam00092
von Willebrand factor type A domain;
1956-2097 8.76e-19

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 86.17  E-value: 8.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1956 ELVFGLDMSDDVTPTAFERQRSALLALLEEINIaesnCPSGARVAVVGYSAYTKYLIRFQDYRRKTQLEDAVKNIALeRT 2035
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDI----GPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRY-LG 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657584108  2036 SNKRHLGAAMHFVAQNVFKRVRSGMV-MRKVAVFFSNGPSQEvNDIPGAVMEYRGLNIVPAVI 2097
Cdd:pfam00092   76 GGTTNTGKALKYALENLFSSAAGARPgAPKVVVLLTDGRSQD-GDPEEVARELKSAGVTVFAV 137
VWA pfam00092
von Willebrand factor type A domain;
2166-2338 2.78e-18

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 84.63  E-value: 2.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  2166 DLVMVADSSREIQADQYAGVQQLLGSVVEQLAVSPQprragnQARVAVVQQGGarSAKVEFNLQTYQNQELMRTHLTQKM 2245
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPD------GTRVGLVQYSS--DVRTEFPLNDYSSKEELLSAVDNLR 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  2246 RQQGGSSALGQTLDYTLkEVLLKAGQPSRKKALLAVV----GTSTAWEDQArlhyVSQKAKCEGVALFVVTVGDHYNRtQ 2321
Cdd:pfam00092   73 YLGGGTTNTGKALKYAL-ENLFSSAAGARPGAPKVVVlltdGRSQDGDPEE----VARELKSAGVTVFAVGVGNADDE-E 146

                          170
                   ....*....|....*..
gi 657584108  2322 VEELASLPLQQHLIHVS 2338
Cdd:pfam00092  147 LRKIASEPGEGHVFTVS 163
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2165-2335 1.34e-16

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: 79.26  E-value: 1.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 2165 VDLVMVADSSREIQADQYAGVQQLLGSVVEQLAVSPqprragNQARVAVVQQGGarSAKVEFNLQTYQNQELMRTHLtQK 2244
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGP------DKTRVGLVQYSD--DVRVEFSLNDYKSKDDLLKAV-KN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 2245 MRQQGGS-SALGQTLDYTLKEVLLKAGQPSR-KKALLAVVGTSTAWEDQARLhyVSQKAKCEGVALFVVTVGDHyNRTQV 2322
Cdd:cd01450    72 LKYLGGGgTNTGKALQYALEQLFSESNARENvPKVIIVLTDGRSDDGGDPKE--AAAKLKDEGIKVFVVGVGPA-DEEEL 148

                         170
                  ....*....|...
gi 657584108 2323 EELASLPLQQHLI 2335
Cdd:cd01450   149 REIASCPSERHVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 2166-2329 3.06e-16

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: 78.65  E-value: 3.06e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   2166 DLVMVADSSREIQADQYAGVQQLLGSVVEQLAVSPqprragNQARVAVVQQGGarSAKVEFNLQTYQNQELMRTHLtQKM 2245
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGP------DGDRVGLVTFSD--DARVLFPLNDSRSKDALLEAL-ASL 71

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   2246 RQQ-GGSSALGQTLDYTLKEVLLKA--GQPSRKKALLAVV-GTSTAWEDQARLhyVSQKAKCEGVALFVVTVGDHYNRTQ 2321
Cdd:smart00327   72 SYKlGGGTNLGAALQYALENLFSKSagSRRGAPKVVILITdGESNDGPKDLLK--AAKELKRSGVKVFVVGVGNDVDEEE 149


                    ....*...
gi 657584108   2322 VEELASLP 2329
Cdd:smart00327  150 LKKLASAP 157
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1957-2127 3.71e-16

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: 78.65  E-value: 3.71e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   1957 LVFGLDMSDDVTPTAFERQRSALLALLEEINIaesnCPSGARVAVVGYSAYTKYLIRFQDYRRKTQLEDAVKNIaLERTS 2036
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDI----GPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASL-SYKLG 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   2037 NKRHLGAAMHFVAQNVFKRVRSGMVM-RKVAVFFSNGPSQE-VNDIPGAVMEYRGLNIVPAVISLTNTPAIRQALAVDDT 2114
Cdd:smart00327   77 GGTNLGAALQYALENLFSKSAGSRRGaPKVVILITDGESNDgPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASA 156

                           170
                    ....*....|...
gi 657584108   2115 GNSIFTVLRRQQD 2127
Cdd:smart00327  157 PGGVYVFLPELLD 169
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1194-1362 4.63e-16

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 80.75  E-value: 4.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1194 ADLVFLIDQSGSIASTD-YSIMKKFTTELVNSFkVSEDlvRVGLAQFSSnfqnEFYLNQFYTE--EAVSKHIFNMrQLGG 1270
Cdd:COG1240    93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDY-RPRD--RVGLVAFGG----EAEVLLPLTRdrEALKRALDEL-PPGG 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1271 GTNIGLALDSIREYFEASRGCRRSAgisqnLVLITDGE---SQDDVEDAAERLRALGIEVFAIGIG-NVHDLELLQ---- 1342
Cdd:COG1240   165 GTPLGDALALALELLKRADPARRKV-----IVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGtEAVDEGLLReiae 239

                         170       180
                  ....*....|....*....|
gi 657584108 1343 ITGTpeRLFTVENFGSLEKI 1362
Cdd:COG1240   240 ATGG--RYFRADDLSELAAI 257
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 419-573 9.10e-16

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 79.98  E-value: 9.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  419 ADIVFIVDESGSIGVAN-FQMVRTFLHSIISGLeisPTRVRVGIVMYNDRPadqaqQVYLNTFNNKDELLKFIKILPYhG 497
Cdd:COG1240    93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEA-----EVLLPLTRDREALKRALDELPP-G 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  498 GGTNTGAALKFAREsvfikeRGSRKDKGVQQVAVVITDGE---SQDDVSQPAADLRRAGVTIYSVGV--KNANKVQLVEM 572
Cdd:COG1240   164 GGTPLGDALALALE------LLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVgtEAVDEGLLREI 237


                  .
gi 657584108  573 A 573
Cdd:COG1240   238 A 238
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1957-2101 6.39e-15

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: 74.64  E-value: 6.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1957 LVFGLDMSDDVTPTAFERQRSALLALLEEINIAesncPSGARVAVVGYSAYTKYLIRFQDYRRKTQLEDAVKNIaLERTS 2036
Cdd:cd01450     3 IVFLLDGSESVGPENFEKVKDFIEKLVEKLDIG----PDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNL-KYLGG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657584108 2037 NKRHLGAAMHFVAQNVFKRVRSGMVMRKVAVFFSNGPSQEVNDIPGAVMEYRGLNIVPAVISLTN 2101
Cdd:cd01450    78 GGTNTGKALQYALEQLFSESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVVGVGP 142
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1666-1724 1.80e-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: 69.83  E-value: 1.80e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 657584108  1666 GVDGEQGLTGADGGRGERGNPGNPGIPGIRGEAGLKGQRGLRGDPGEPGAdnnsPGAKG 1724
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA----PGAPG 55
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 811-963 3.27e-14

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 75.36  E-value: 3.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  811 KDIPGDLLFLIDSSGSIypQDYNKMkDFMKSVIsKSFIG--QNEVHVGVMQFSTIQKLEFPLNRfySKGEMSKAIDDMQq 888
Cdd:COG1240    89 PQRGRDVVLVVDASGSM--AAENRL-EAAKGAL-LDFLDdyRPRDRVGLVAFGGEAEVLLPLTR--DREALKRALDELP- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  889 IGGGTHTGEAITDVSQYFDSSRggrPGLRQRLVVITDGEAQDVVRGP---AAALRAKGVVVYAIGVVDA--NTTQLLEIS 963
Cdd:COG1240   162 PGGGTPLGDALALALELLKRAD---PARRKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEavDEGLLREIA 238
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 927-1177 2.46e-13

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 72.66  E-value: 2.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  927 EAQDVVRGPAAALRAKGVVVYAIGVVDANTTQLLEISGSPDRMYAERDFDALKDLESQVALELCDPERDCKKTEKADIIF 1006
Cdd:COG1240    18 LLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1007 LVDGSTS-ITLAKFRNMQRFMESMVNQTTVGkdlTRFGVILYSNDPKSV--FTlnqySSKKEVVKAISNLRsPFGDTYTG 1083
Cdd:COG1240    98 VVDASGSmAAENRLEAAKGALLDFLDDYRPR---DRVGLVAFGGEAEVLlpLT----RDREALKRALDELP-PGGGTPLG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1084 KALAYSLQFFDAQHGGRAAlqvpqILMVITDGDATD-RNSLVAPSVALRDHGVSVFSIGV--EGANMTQLEIMAGYDRSK 1160
Cdd:COG1240   170 DALALALELLKRADPARRK-----VIVLLTDGRDNAgRIDPLEAAELAAAAGIRIYTIGVgtEAVDEGLLREIAEATGGR 244

                         250
                  ....*....|....*..
gi 657584108 1161 VFYVDNFEALETLYKNI 1177
Cdd:COG1240   245 YFRADDLSELAAIYREI 261
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 625-796 6.73e-13

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 71.12  E-value: 6.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  625 QTDEADIFFLIDHSGSIYPTD-FQDMKKFIIEFIHTFRispQHVRLGVAKYADSPNLEFDLTdySDAKSVEKAVEGIrQI 703
Cdd:COG1240    89 PQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPLT--RDREALKRALDEL-PP 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  704 GGGTETGRALAFMSPHFDRAMTTRgHKVpeyLVVITDGKSSDKVKVP---AEQLRAQGVIVYSIGV--KSADMEELREIS 778
Cdd:COG1240   163 GGGTPLGDALALALELLKRADPAR-RKV---IVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVgtEAVDEGLLREIA 238

                         170       180
                  ....*....|....*....|..
gi 657584108  779 gdpKRT----FFVNNFDALKPI 796
Cdd:COG1240   239 ---EATggryFRADDLSELAAI 257
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 33-208 6.68e-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: 62.26  E-value: 6.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   33 ADIVFLIDGSSSIGISN-FQEIRQFLRSVISGLDigaDKVRIGLAQYSDEPYQEFLLKDhmDKQSLLAAVDTFQYRtGGT 111
Cdd:COG1240    93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPLTR--DREALKRALDELPPG-GGT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  112 ETGEAIdflmnqyftEDAGSRAKQRVPQ---IAVVITDGDSTDDVAAP---ALRLRQHGVIMFAIGVGKA--NPTELEAI 183
Cdd:COG1240   167 PLGDAL---------ALALELLKRADPArrkVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEavDEGLLREI 237

                         170       180
                  ....*....|....*....|....*
gi 657584108  184 ANRPPKRFmFTIDNYEALQRLTEGL 208
Cdd:COG1240   238 AEATGGRY-FRADDLSELAAIYREI 261
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1858-1924 1.04e-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: 53.27  E-value: 1.04e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657584108  1858 GRKGVKGDPGFPGYPGLLGEDGLQGPKGLPgrkgnrgrggnsgrsgesGISGDPGYAGHRGPRGLPG 1924
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPP------------------GEPGPPGPPGPPGPPGPPG 49
PHA03169 PHA03169
hypothetical protein; Provisional
 1577-1793 1.18e-08

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 59.98  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1577 VSDRECCNVMCKCSGHEGIR-GSRGLPGSKGVSGQKGYPGFPGEEGIAGDRGSPGPSGPQGVQGCSGRRGVKGFRGLRGN 1655
Cdd:PHA03169   13 HTLRSSCRGHCKRHGGTREQaGRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1656 RGE--DGEDGLDGVDGEQGLTGADGGRGERGNPGNPGIPGIRGEAGLKGQRGLRGDPGEPGADNNSPGAKGDSGNAGL-- 1731
Cdd:PHA03169   93 SGSgsESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPShe 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657584108 1732 ----PGlPGPDGRPGESGIVGNPGQDGRRGSPGVKGAAGepgaaglQGIPGASGPQGTRGVRGQPG 1793
Cdd:PHA03169  173 dspeEP-EPPTSEPEPDSPGPPQSETPTSSPPPQSPPDE-------PGEPQSPTPQQAPSPNTQQA 230
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 1483-1794 5.71e-06

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: 51.54  E-value: 5.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1483 LKSFGQKFKAESRAGVKVLLIFSDGLDDDVmklEQESELLRQSGISALLTvalEGVRDIAQLQMVEFGRGFGYRLPLSI- 1561
Cdd:cd21118    20 LHSGGEGTGAGESAGHGLGDAISHGIGEAV---GQGAKEAASSGIQNALG---QGHGEEGGSTLGSRGDVFEHRLGEAAr 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1562 GMPSVGSTILKQIDTVSDReccnvmckcsGHEGIRGSRGLPGSKGVSGQKGYPGFPGEeGIAGDRGSPGPSG-PQGVQGC 1640
Cdd:cd21118    94 SLGNAGNEIGRQAEDIIRH----------GVDAVHNSWQGSGGHGAYGSQGGPGVQGH-GIPGGTGGPWASGgNYGTNSL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1641 SGRRGVKGFRG-------LRGNRGEDGEDGLDGVDGEQGLT-----GADGGRGERGNPGNPGIPGIRGEAGLKGQRGLRG 1708
Cdd:cd21118   163 GGSVGQGGNGGplnygtnSQGAVAQPGYGTVRGNNQNSGCTnpppsGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGS 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1709 DPGEPGADNNSpGAKGDSGNAGlpglpgpDGRPGESGIVGNPGQDGRRGSPGVkgaagepgaaglQGIPGASGPQGTRGV 1788
Cdd:cd21118   243 SGGQGNGGNNG-SSSSNSGNSG-------GSNGGSSGNSGSGSGGSSSGGSNG------------WGGSSSSGGSGGSGG 302


                  ....*.
gi 657584108 1789 RGQPGP 1794
Cdd:cd21118   303 GNKPEC 308
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1000-1165 6.16e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 48.42  E-value: 6.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1000 EKADIIFLVDGSTSITLAKFRNMQRFM-ESMVNQTTVGKDLTRFGVILYSNDPKSVFTLNQYSS--KKEVVKAISNLRS- 1075
Cdd:PTZ00441   41 EEVDLYLLVDGSGSIGYHNWITHVIPMlMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASkdKEQALIIVKSLRKt 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1076 --PFGDTYTGKALAYSLQFFDAQHGGRAALQvpqILMVITDGDATDRNSLVAPSVALRDHGVSVFSIGV-EGANMTQLEI 1152
Cdd:PTZ00441  121 ylPYGKTNMTDALLEVRKHLNDRVNRENAIQ---LVILMTDGIPNSKYRALEESRKLKDRNVKLAVIGIgQGINHQFNRL 197

                         170
                  ....*....|....*.
gi 657584108 1153 MAG---YDRSKVFYVD 1165
Cdd:PTZ00441  198 LAGcrpREGKCKFYSD 213
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1861-1926 1.06e-03

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 44.13  E-value: 1.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657584108 1861 GVKGDPGFPGYPGllgEDGLQGPKGLPGRKGNRGRGGNSGRSGESGISGDPGYAGHRGPRGLPGSK 1926
Cdd:NF038329  117 GEKGEPGPAGPAG---PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD 179
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1451-1555 2.17e-03

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: 41.29  E-value: 2.17e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   1451 LYDFNFEGYSEDVVQKVMTLS--LAEPTYFNTAMLKSFGQKFKAE--SRAGV-KVLLIFSDGLDDDVMK-LEQESELLRQ 1524
Cdd:smart00327   52 LFPLNDSRSKDALLEALASLSykLGGGTNLGAALQYALENLFSKSagSRRGApKVVILITDGESNDGPKdLLKAAKELKR 131

                            90       100       110
                    ....*....|....*....|....*....|.
gi 657584108   1525 SGISaLLTVALEGVRDIAQLQMVEFGRGFGY 1555
Cdd:smart00327  132 SGVK-VFVVGVGNDVDEEELKKLASAPGGVY 161
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1454-1547 8.26e-03

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: 39.58  E-value: 8.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1454 FNFEGYS--EDVVQKVMTLSL--AEPTYFNTAMLKSFGQKF-KAESRAGV-KVLLIFSDGLDDDVMKLEQESELLRQSGI 1527
Cdd:cd01450    54 FSLNDYKskDDLLKAVKNLKYlgGGGTNTGKALQYALEQLFsESNARENVpKVIIVLTDGRSDDGGDPKEAAAKLKDEGI 133

                          90       100
                  ....*....|....*....|
gi 657584108 1528 SaLLTVALeGVRDIAQLQMV 1547
Cdd:cd01450   134 K-VFVVGV-GPADEEELREI 151
 
Name Accession Description Interval E-value
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 33-197 1.36e-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: 214.01  E-value: 1.36e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   33 ADIVFLIDGSSSIGISNFQEIRQFLRSVISGLDIGADKVRIGLAQYSDEPYQEFLLKDHMDKQSLLAAVDTFQYRTGGTE 112
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  113 TGEAIDFLMNQYFTEDAGSRAKqrVPQIAVVITDGDSTDDVAAPALRLRQHGVIMFAIGVGKANPTELEAIANRPPKRFM 192
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREG--VPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYV 158


                  ....*
gi 657584108  193 FTIDN 197
Cdd:cd01472   159 FNVAD 163
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 33-198 1.04e-62

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: 211.76  E-value: 1.04e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   33 ADIVFLIDGSSSIGISNFQEIRQFLRSVISGLDIGADKVRIGLAQYSDEPYQEFLLKDHMDKQSLLAAVDTFQYRTGGTE 112
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  113 TGEAIDFLMNQYFTEDAGSRAkqRVPQIAVVITDGDSTDDVAAPALRLRQHGVIMFAIGVGKANPTELEAIANRPPKRFM 192
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARP--GVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHV 158


                  ....*.
gi 657584108  193 FTIDNY 198
Cdd:cd01482   159 FNVADF 164
VWA pfam00092
von Willebrand factor type A domain;
34-206 2.62e-57

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 196.73  E-value: 2.62e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    34 DIVFLIDGSSSIGISNFQEIRQFLRSVISGLDIGADKVRIGLAQYSDEPYQEFLLKDHMDKQSLLAAVDTFQYRTGGT-E 112
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   113 TGEAIDFLMNQYFTEDAGSRAkqRVPQIAVVITDGDSTD-DVAAPALRLRQHGVIMFAIGVGKANPTELEAIANRPPKRF 191
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARP--GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGH 158

                          170
                   ....*....|....*
gi 657584108   192 MFTIDNYEALQRLTE 206
Cdd:pfam00092  159 VFTVSDFEALEDLQD 173
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 419-587 6.16e-57

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: 195.14  E-value: 6.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  419 ADIVFIVDESGSIGVANFQMVRTFLHSIISGLEISPTRVRVGIVMYNDrpaDQAQQVYLNTFNNKDELLKFIKILPYHGG 498
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSD---DPRTEFYLNTYRSKDDVLEAVKNLRYIGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  499 GTNTGAALKFARESVFIKERGSRKdkGVQQVAVVITDGESQDDVSQPAADLRRAGVTIYSVGVKNANKVQLVEMASHPPN 578
Cdd:cd01472    78 GTNTGKALKYVRENLFTEASGSRE--GVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKE 155


                  ....*....
gi 657584108  579 KHVFIVDSF 587
Cdd:cd01472   156 LYVFNVADF 164
VWA pfam00092
von Willebrand factor type A domain;
420-595 2.48e-54

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 187.87  E-value: 2.48e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   420 DIVFIVDESGSIGVANFQMVRTFLHSIISGLEISPTRVRVGIVMYNDrpaDQAQQVYLNTFNNKDELLKFIKILPYHGGG 499
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSS---DVRTEFPLNDYSSKEELLSAVDNLRYLGGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   500 T-NTGAALKFARESVFIKERGSRkdKGVQQVAVVITDGESQD-DVSQPAADLRRAGVTIYSVGVKNANKVQLVEMASHPP 577
Cdd:pfam00092   78 TtNTGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPG 155

                          170
                   ....*....|....*...
gi 657584108   578 NKHVFIVDSFAKLKSMEQ 595
Cdd:pfam00092  156 EGHVFTVSDFEALEDLQD 173
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 419-587 5.24e-54

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: 186.72  E-value: 5.24e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  419 ADIVFIVDESGSIGVANFQMVRTFLHSIISGLEISPTRVRVGIVMYNDRPAdqaQQVYLNTFNNKDELLKFIKILPYHGG 498
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPR---TEFDLNAYTSKEDVLAAIKNLPYKGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  499 GTNTGAALKFARESVFIKERGSRKdkGVQQVAVVITDGESQDDVSQPAADLRRAGVTIYSVGVKNANKVQLVEMASHPPN 578
Cdd:cd01482    78 NTRTGKALTHVREKNFTPDAGARP--GVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSE 155


                  ....*....
gi 657584108  579 KHVFIVDSF 587
Cdd:cd01482   156 THVFNVADF 164
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 33-198 5.15e-51

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 178.29  E-value: 5.15e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   33 ADIVFLIDGSSSIGISNFQEIRQFLRSVISGLDIGADKVRIGLAQYSDEPYQEFLLKDHMDKQSLLAAVDTFQYRTG-GT 111
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGsQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  112 ETGEAIDFLMNQYFTEDAGSRAKQRVPQIAVVITDGDSTDDVAAPALRLRQHGVIMFAIGVGKANPTELEAIANRPpkRF 191
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP--SF 158


                  ....*..
gi 657584108  192 MFTIDNY 198
Cdd:cd01481   159 VFQVSDF 165
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 33-193 9.85e-50

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: 174.40  E-value: 9.85e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   33 ADIVFLIDGSSSIGISNFQEIRQFLRSVISGLDIGADKVRIGLAQYSDEPYQEFLLKDHMDKQSLLAAVDTFQYRTG-GT 111
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  112 ETGEAIDFLMNQYFTEdagSRAKQRVPQIAVVITDGDSTD--DVAAPALRLRQHGVIMFAIGVGKANPTELEAIANRPPK 189
Cdd:cd01450    81 NTGKALQYALEQLFSE---SNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSE 157


                  ....
gi 657584108  190 RFMF 193
Cdd:cd01450   158 RHVF 161
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 419-582 1.47e-49

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: 174.02  E-value: 1.47e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  419 ADIVFIVDESGSIGVANFQMVRTFLHSIISGLEISPTRVRVGIVMYNDRPADqaqQVYLNTFNNKDELLKFIKILPYHGG 498
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRV---EFSLNDYKSKDDLLKAVKNLKYLGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  499 -GTNTGAALKFARESVFIKergSRKDKGVQQVAVVITDGESQD--DVSQPAADLRRAGVTIYSVGVKNANKVQLVEMASH 575
Cdd:cd01450    78 gGTNTGKALQYALEQLFSE---SNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASC 154


                  ....*..
gi 657584108  576 PPNKHVF 582
Cdd:cd01450   155 PSERHVF 161
VWA pfam00092
von Willebrand factor type A domain;
816-984 9.84e-48

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 168.99  E-value: 9.84e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   816 DLLFLIDSSGSIYPQDYNKMKDFMKSVISKSFIGQNEVHVGVMQFSTIQKLEFPLNRFYSKGEMSKAIDDMQQIGGGT-H 894
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   895 TGEAITDV-SQYFDSSRGGRPGLRQRLVVITDGEAQDV-VRGPAAALRAKGVVVYAIGVVDANTTQLLEISGSPD--RMY 970
Cdd:pfam00092   81 TGKALKYAlENLFSSAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegHVF 160

                          170
                   ....*....|....
gi 657584108   971 AERDFDALKDLESQ 984
Cdd:pfam00092  161 TVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
1195-1362 1.99e-47

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 168.22  E-value: 1.99e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1195 DLVFLIDQSGSIASTDYSIMKKFTTELVNSFKVSEDLVRVGLAQFSSNFQNEFYLNQFYTEEAVSKHIFNMRQLGGGT-N 1273
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1274 IGLALDS-IREYFEASRGCRRsaGISQNLVLITDGESQD-DVEDAAERLRALGIEVFAIGIGNVHDLELLQITGTP--ER 1349
Cdd:pfam00092   81 TGKALKYaLENLFSSAAGARP--GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPgeGH 158

                          170
                   ....*....|...
gi 657584108  1350 LFTVENFGSLEKI 1362
Cdd:pfam00092  159 VFTVSDFEALEDL 171
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 33-213 8.36e-46

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 165.64  E-value: 8.36e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   33 ADIVFLIDGSSSIGISNFQEIRQFLRSVISGLDIGADKVRIGLAQYSDEPYQEFLLKDHMDKQSLLAAVDTFQYRTGGTE 112
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  113 TGEAIDFLMNQYFTEDAGSR-AKQRVPQIAVVITDGDSTDDVAAPALRLRQHGVIMFAIGVGKANPTELEAIANRPPKRF 191
Cdd:cd01475    83 TGLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPLADH 162

                         170       180
                  ....*....|....*....|..
gi 657584108  192 MFTIDNYEALQRLTEGLLQTVC 213
Cdd:cd01475   163 VFYVEDFSTIEELTKKFQGKIC 184
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 629-790 4.97e-45

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: 160.86  E-value: 4.97e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  629 ADIFFLIDHSGSIYPTDFQDMKKFIIEFIHTFRISPQHVRLGVAKYADSPNLEFDLTDYSDAKSVEKAVEGIRQIGGGTE 708
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  709 TGRALAFMSPHFDRAMTTRGHKVPEYLVVITDGKSSDKVKVPAEQLRAQGVIVYSIGVKSADMEELREISGDPKRT--FF 786
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELyvFN 160


                  ....
gi 657584108  787 VNNF 790
Cdd:cd01472   161 VADF 164
VWA pfam00092
von Willebrand factor type A domain;
1003-1176 6.19e-45

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 161.29  E-value: 6.19e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1003 DIIFLVDGSTSITLAKFRNMQRFMESMVNQTTVGKDLTRFGVILYSNDPKSVFTLNQYSSKKEVVKAISNLR-SPFGDTY 1081
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRyLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1082 TGKALAYSLQ-FFDAQHGGRAalQVPQILMVITDGDATDrNSLVAPSVALRDHGVSVFSIGVEGANMTQLEIMAGYDRSK 1160
Cdd:pfam00092   81 TGKALKYALEnLFSSAAGARP--GAPKVVVLLTDGRSQD-GDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEG 157

                          170
                   ....*....|....*..
gi 657584108  1161 -VFYVDNFEALETLYKN 1176
Cdd:pfam00092  158 hVFTVSDFEALEDLQDQ 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 816-968 1.28e-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: 159.76  E-value: 1.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  816 DLLFLIDSSGSIYPQDYNKMKDFMKSVISKSFIGQNEVHVGVMQFSTIQKLEFPLNRFYSKGEMSKAIDDMQQIGG-GTH 894
Cdd:cd01450     2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGTN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657584108  895 TGEAITDVSQYFDSSRGGRPGLRQRLVVITDGEAQDV--VRGPAAALRAKGVVVYAIGVVDANTTQLLEISGSPDR 968
Cdd:cd01450    82 TGKALQYALEQLFSESNARENVPKVIIVLTDGRSDDGgdPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSE 157
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1194-1356 3.12e-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: 158.60  E-value: 3.12e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1194 ADLVFLIDQSGSIASTDYSIMKKFTTELVNSFKVSEDLVRVGLAQFSSNFQNEFYLNQFYTEEAVSKHIFNMRQLGGGTN 1273
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1274 IGLALDSIRE-YFEASRGCRRsaGISQNLVLITDGESQDDVEDAAERLRALGIEVFAIGIGNVHDLELLQITGTPER--L 1350
Cdd:cd01482    81 TGKALTHVREkNFTPDAGARP--GVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSEthV 158


                  ....*.
gi 657584108 1351 FTVENF 1356
Cdd:cd01482   159 FNVADF 164
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 420-590 6.78e-44

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 158.39  E-value: 6.78e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    420 DIVFIVDESGSIGVANFQMVRTFLHSIISGLEISPTRVRVGIVMYNDRPADqaqQVYLNTFNNKDELLKFIKILPYH-GG 498
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARV---LFPLNDSRSKDALLEALASLSYKlGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    499 GTNTGAALKFARESVFIKERGSRkdKGVQQVAVVITDGESQD---DVSQPAADLRRAGVTIYSVGVKNA-NKVQLVEMAS 574
Cdd:smart00327   78 GTNLGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLAS 155

                           170
                    ....*....|....*.
gi 657584108    575 HPPNKHVFIVDSFAKL 590
Cdd:smart00327  156 APGGVYVFLPELLDLL 171
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1591-1853 1.45e-43

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: 166.23  E-value: 1.45e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1591 GHEGIRGSRGLPGSKGVSGQKGYPGFPGEEGIAGDRGSPGPSGPQGVQGCSGRRGVKGFRGLRGNRGEDGEDGLDGVDGE 1670
Cdd:NF038329  132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGP 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1671 QGLTGADGGRGERGNPGNPGipgirgeaglKGQRGLRGDPGEPGADnnspgakGDSGNAGLPGLPGPDGRPGESGIVGNP 1750
Cdd:NF038329  212 AGPDGEAGPAGEDGPAGPAG----------DGQQGPDGDPGPTGED-------GPQGPDGPAGKDGPRGDRGEAGPDGPD 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1751 GQDGRRGSPgvkgaagepgaaglqGIPGASGPQGTRGVRGQPGPRgipglpgpqggpgsvggpgaagrrggnGQKGQPGD 1830
Cdd:NF038329  275 GKDGERGPV---------------GPAGKDGQNGKDGLPGKDGKD---------------------------GQNGKDGL 312

                         250       260
                  ....*....|....*....|...
gi 657584108 1831 PGDKGVPGPLGPRGMPGEDGRDG 1853
Cdd:NF038329  313 PGKDGKDGQPGKDGLPGKDGKDG 335
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 34-204 1.91e-43

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: 156.85  E-value: 1.91e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108     34 DIVFLIDGSSSIGISNFQEIRQFLRSVISGLDIGADKVRIGLAQYSDEPYQEFLLKDHMDKQSLLAAVDTFQYRTGG-TE 112
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGgTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    113 TGEAIDFLMNQYFTEDAGSRAkqRVPQIAVVITDGDSTD---DVAAPALRLRQHGVIMFAIGVGKA-NPTELEAIANRPP 188
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRR--GAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158

                           170
                    ....*....|....*.
gi 657584108    189 KRFMFTIDNYEALQRL 204
Cdd:smart00327  159 GVYVFLPELLDLLIDL 174
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1194-1359 2.74e-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: 155.85  E-value: 2.74e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1194 ADLVFLIDQSGSIASTDYSIMKKFTTELVNSFKVSEDLVRVGLAQFSSNFQNEFYLNQFYTEEAVSKHIFNMRQLGGGTN 1273
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1274 IGLALDSIRE-YFEASrgCRRSAGISQNLVLITDGESQDDVEDAAERLRALGIEVFAIGIGNVHDLELLQITGTPERLFt 1352
Cdd:cd01472    81 TGKALKYVREnLFTEA--SGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELY- 157


                  ....*..
gi 657584108 1353 VENFGSL 1359
Cdd:cd01472   158 VFNVADF 164
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 419-602 6.19e-43

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: 157.16  E-value: 6.19e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  419 ADIVFIVDESGSIGVANFQMVRTFLHSIISGLEISPTRVRVGIVMYndrpADQAQQVY-LNTFNNKDELLKFIKILPYHG 497
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQY----SSTVKQEFpLGRFKSKADLKRAVRRMEYLE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  498 GGTNTGAALKFARESVFIKERGSRK-DKGVQQVAVVITDGESQDDVSQPAADLRRAGVTIYSVGVKNANKVQLVEMASHP 576
Cdd:cd01475    79 TGTMTGLAIQYAMNNAFSEAEGARPgSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEP 158

                         170       180
                  ....*....|....*....|....*.
gi 657584108  577 PNKHVFIVDSFAKLKSMEQSLQKILC 602
Cdd:cd01475   159 LADHVFYVEDFSTIEELTKKFQGKIC 184
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1603-1887 6.62e-43

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: 164.31  E-value: 6.62e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1603 GSKGVSGQKGYPGFPGEEGIAGDRGSPGPSGPQGVQGCSGRRGVKGFRGLRGNRGEDGEDGLDGVDGEQGLTGADGGRGE 1682
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1683 RGNPGNPGIPGIRGEAGLKGQRGLRGDPGEPGadnnsPGAKGDSGNAGLPGlpgPDGRPGESGIVGNPGQDGRRGSPGvk 1762
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAG-----PAGDGQQGPDGDPG---PTGEDGPQGPDGPAGKDGPRGDRG-- 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1763 gaagepgaaglqgipgasgPQGTRGVRGQPGPRgipglpgpqggpgsvggpgaagrrggngqkgqpGDPGDKGVPGPLGP 1842
Cdd:NF038329  267 -------------------EAGPDGPDGKDGER---------------------------------GPVGPAGKDGQNGK 294

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 657584108 1843 RGMPGEDGRDGY-GPAGRKGVKGDPGFPGYPGLLGEDGLQGPKGLP 1887
Cdd:NF038329  295 DGLPGKDGKDGQnGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 419-587 9.03e-43

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 154.40  E-value: 9.03e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  419 ADIVFIVDESGSIGVANFQMVRTFLHSIISGLEISPTRVRVGIVMYNDRPAdqaQQVYLNTFNNKDELLKFIKILPYHGG 498
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPR---PEFYLNTHSTKADVLGAVRRLRLRGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  499 -GTNTGAALKFARESVFIKERGSRKDKGVQQVAVVITDGESQDDVSQPAADLRRAGVTIYSVGVKNANKVQLVEMASHPp 577
Cdd:cd01481    78 sQLNTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDP- 156

                         170
                  ....*....|
gi 657584108  578 nKHVFIVDSF 587
Cdd:cd01481   157 -SFVFQVSDF 165
VWA pfam00092
von Willebrand factor type A domain;
630-794 7.37e-42

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 152.43  E-value: 7.37e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   630 DIFFLIDHSGSIYPTDFQDMKKFIIEFIHTFRISPQHVRLGVAKYADSPNLEFDLTDYSDAKSVEKAVEGIRQIGGGT-E 708
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   709 TGRALAF-MSPHFDRAMTTRGHkVPEYLVVITDGKSSDK-VKVPAEQLRAQGVIVYSIGVKSADMEELREISGDP--KRT 784
Cdd:pfam00092   81 TGKALKYaLENLFSSAAGARPG-APKVVVLLTDGRSQDGdPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPgeGHV 159

                          170
                   ....*....|
gi 657584108   785 FFVNNFDALK 794
Cdd:pfam00092  160 FTVSDFEALE 169
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1194-1382 1.53e-41

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 153.31  E-value: 1.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1194 ADLVFLIDQSGSIASTDYSIMKKFTTELVNSFKVSEDLVRVGLAQFSSNFQNEFYLNQFYTEEAVSKHIFNMRQLGGGTN 1273
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1274 IGLALD-SIREYFEASRGCR-RSAGISQNLVLITDGESQDDVEDAAERLRALGIEVFAIGIGNVHDLELLQITGTP--ER 1349
Cdd:cd01475    83 TGLAIQyAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPlaDH 162

                         170       180       190
                  ....*....|....*....|....*....|...
gi 657584108 1350 LFTVENFGSLEKIKQKVINTICkskPIRDPSAC 1382
Cdd:cd01475   163 VFYVEDFSTIEELTKKFQGKIC---VVPDLCAT 192
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1002-1163 1.57e-41

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: 150.90  E-value: 1.57e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1002 ADIIFLVDGSTSITLAKFRNMQRFMESMVNQTTVGKDLTRFGVILYSNDPKSVFTLNQYSSKKEVVKAISNLRSPFGD-T 1080
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1081 YTGKALAYSLQFFDAQHGGRaaLQVPQILMVITDGDATDRNSLVAPSVALRDHGVSVFSIGVEGANMTQLEIMAGYDRSK 1160
Cdd:cd01450    81 NTGKALQYALEQLFSESNAR--ENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSER 158


                  ...
gi 657584108 1161 VFY 1163
Cdd:cd01450   159 HVF 161
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 816-972 1.61e-41

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: 150.84  E-value: 1.61e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  816 DLLFLIDSSGSIYPQDYNKMKDFMKSVISKSFIGQNEVHVGVMQFSTIQKLEFPLNRFYSKGEMSKAIDDMQQIGGGTHT 895
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657584108  896 GEAITDVS-QYFDSSRGGRPGLRQRLVVITDGEAQDVVRGPAAALRAKGVVVYAIGVVDANTTQLLEISGSPDRMYAE 972
Cdd:cd01472    82 GKALKYVReNLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPKELYVF 159
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1194-1349 5.77e-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: 5.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1194 ADLVFLIDQSGSIASTDYSIMKKFTTELVNSFKVSEDLVRVGLAQFSSNFQNEFYLNQFYTEEAVSKHIFNMRQLGG-GT 1272
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657584108 1273 NIGLALDSIREYFEASRGCRRsaGISQNLVLITDGESQD--DVEDAAERLRALGIEVFAIGIGNVHDLELLQITGTPER 1349
Cdd:cd01450    81 NTGKALQYALEQLFSESNARE--NVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSE 157
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 629-790 7.14e-40

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: 146.28  E-value: 7.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  629 ADIFFLIDHSGSIYPTDFQDMKKFIIEFIHTFRISPQHVRLGVAKYADSPNLEFDLTDYSDAKSVEKAVEGIRQIGGGTE 708
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  709 TGRALAFMSPHFDRAMTTRGHKVPEYLVVITDGKSSDKVKVPAEQLRAQGVIVYSIGVKSADMEELREISGDPKRT--FF 786
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSEThvFN 160


                  ....
gi 657584108  787 VNNF 790
Cdd:cd01482   161 VADF 164
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 816-978 4.78e-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: 144.13  E-value: 4.78e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    816 DLLFLIDSSGSIYPQDYNKMKDFMKSVISKSFIGQNEVHVGVMQFSTIQKLEFPLNRFYSKGEMSKAIDDMQQI-GGGTH 894
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    895 TGEAITDVSQY-FDSSRGGRPGLRQRLVVITDGEAQDV---VRGPAAALRAKGVVVYAIGVV-DANTTQLLEISGSPDRM 969
Cdd:smart00327   81 LGAALQYALENlFSKSAGSRRGAPKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGnDVDEEELKKLASAPGGV 160

                           170
                    ....*....|.
gi 657584108    970 YA--ERDFDAL 978
Cdd:smart00327  161 YVflPELLDLL 171
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 629-787 1.10e-38

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: 142.82  E-value: 1.10e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  629 ADIFFLIDHSGSIYPTDFQDMKKFIIEFIHTFRISPQHVRLGVAKYADSPNLEFDLTDYSDAKSVEKAVEGIRQIGG-GT 707
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGgGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  708 ETGRALAFMSPHFDRAMTTRGhKVPEYLVVITDGKSSD--KVKVPAEQLRAQGVIVYSIGVKSADMEELREISGDPKRTF 785
Cdd:cd01450    81 NTGKALQYALEQLFSESNARE-NVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSERH 159


                  ..
gi 657584108  786 FV 787
Cdd:cd01450   160 VF 161
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1002-1170 1.38e-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: 142.37  E-value: 1.38e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1002 ADIIFLVDGSTSITLAKFRNMQRFMESMVNQTTVGKDLTRFGVILYSNDPKSVFTLNQYSSKKEVVKAISNLRSPFGDTY 1081
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1082 TGKALAYSLQFFdAQHGGRAALQVPQILMVITDGDATDRnsLVAPSVALRDHGVSVFSIGVEGANMTQLEIMAgyDRSKV 1161
Cdd:cd01472    81 TGKALKYVRENL-FTEASGSREGVPKVLVVITDGKSQDD--VEEPAVELKQAGIEVFAVGVKNADEEELKQIA--SDPKE 155


                  ....*....
gi 657584108 1162 FYVDNFEAL 1170
Cdd:cd01472   156 LYVFNVADF 164
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1195-1364 1.55e-37

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: 139.90  E-value: 1.55e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   1195 DLVFLIDQSGSIASTDYSIMKKFTTELVNSFKVSEDLVRVGLAQFSSNFQNEFYLNQFYTEEAVSKHIFNMR-QLGGGTN 1273
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   1274 IGLALDSIREY-FEASRGCRRsaGISQNLVLITDGESQD---DVEDAAERLRALGIEVFAIGIGNVHDLELL-QITGTPE 1348
Cdd:smart00327   81 LGAALQYALENlFSKSAGSRR--GAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDVDEEELkKLASAPG 158

                           170
                    ....*....|....*.
gi 657584108   1349 RLFTVENFGSLEKIKQ 1364
Cdd:smart00327  159 GVYVFLPELLDLLIDL 174
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1194-1356 3.29e-37

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: 138.61  E-value: 3.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1194 ADLVFLIDQSGSIASTDYSIMKKFTTELVNSFKVSEDLVRVGLAQFSSNFQNEFYLNQFYTEEAVSKHIFNMRQLGG-GT 1272
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGsQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1273 NIGLALDSIRE-YFEASRGCRRSAGISQNLVLITDGESQDDVEDAAERLRALGIEVFAIGIGNVHDLELLQITGTPERLF 1351
Cdd:cd01481    81 NTGSALDYVVKnLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                  ....*
gi 657584108 1352 TVENF 1356
Cdd:cd01481   161 QVSDF 165
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1003-1173 7.74e-37

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: 137.97  E-value: 7.74e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   1003 DIIFLVDGSTSITLAKFRNMQRFMESMVNQTTVGKDLTRFGVILYSNDPKSVFTLNQYSSKKEVVKAISNLR-SPFGDTY 1081
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   1082 TGKALAYSLQ-FFDAQHGGRAalQVPQILMVITDGDATDRNSLVAPSV-ALRDHGVSVFSIGVEGA-NMTQLEIMAG-YD 1157
Cdd:smart00327   81 LGAALQYALEnLFSKSAGSRR--GAPKVVILITDGESNDGPKDLLKAAkELKRSGVKVFVVGVGNDvDEEELKKLASaPG 158

                           170
                    ....*....|....*.
gi 657584108   1158 RSKVFYVDNFEALETL 1173
Cdd:smart00327  159 GVYVFLPELLDLLIDL 174
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 34-201 1.78e-36

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 137.10  E-value: 1.78e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   34 DIVFLIDGSSSIGISNFQEIRQFLRSVISGLDIGADKVRIGLAQYSDEPYQEFLLKDHMDKQSLLAAVDTFQYRTGGTET 113
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  114 GEAIDFLMNQYFTEDAGSRAKqrVPQIAVVITDGDSTDDVAAPAL--RLRQHGVIMFAIGVGKA--NPT---ELEAIANR 186
Cdd:cd01469    82 ATAIQYVVTELFSESNGARKD--ATKVLVVITDGESHDDPLLKDVipQAEREGIIRYAIGVGGHfqRENsreELKTIASK 159

                         170
                  ....*....|....*
gi 657584108  187 PPKRFMFTIDNYEAL 201
Cdd:cd01469   160 PPEEHFFNVTDFAAL 174
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1002-1167 1.11e-35

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: 134.34  E-value: 1.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1002 ADIIFLVDGSTSITLAKFRNMQRFMESMVNQTTVGKDLTRFGVILYSNDPKSVFTLNQYSSKKEVVKAISNLRSPFGDTY 1081
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1082 TGKALAYSLQ-FFDAQHGGRAalQVPQILMVITDGDATDrnSLVAPSVALRDHGVSVFSIGVEGANMTQLEIMAGY-DRS 1159
Cdd:cd01482    81 TGKALTHVREkNFTPDAGARP--GVPKVVILITDGKSQD--DVELPARVLRNLGVNVFAVGVKDADESELKMIASKpSET 156


                  ....*...
gi 657584108 1160 KVFYVDNF 1167
Cdd:cd01482   157 HVFNVADF 164
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 816-981 1.70e-35

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 134.02  E-value: 1.70e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  816 DLLFLIDSSGSIYPQDYNKMKDFMKSVISKSFIGQNEVHVGVMQFSTIQKLEFPLNRFYSKGEMSKAIDDMQQIGGGTHT 895
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  896 GEAI-TDVSQYFDSSRGGRPGLRQRLVVITDGEAQDVVRGPAA--ALRAKGVVVYAIGVVDA-NTTQLLE----ISGSPD 967
Cdd:cd01469    82 ATAIqYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDVipQAEREGIIRYAIGVGGHfQRENSREelktIASKPP 161

                         170
                  ....*....|....*.
gi 657584108  968 RMYAER--DFDALKDL 981
Cdd:cd01469   162 EEHFFNvtDFAALKDI 177
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 228-387 2.05e-35

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: 133.60  E-value: 2.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  228 ADIFFLVDS--GISQAEFQQVRSVLVRLTNQVNFGASAHRLGLAQYGQDIKVEFLLNAFQSKDEMQGGIKRFRqrrLQTN 305
Cdd:cd01481     1 KDIVFLIDGsdNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLR---LRGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  306 EPRNLGSALQYASANFFTSEAGSRADQGYRQYLVVLSGKDSDDEVFRQSRLIKSEGVTVVGM-SLGASMNEIRVISTAP- 383
Cdd:cd01481    78 SQLNTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIgARNADLAELQQIAFDPs 157


                  ....
gi 657584108  384 YAYQ 387
Cdd:cd01481   158 FVFQ 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 630-798 6.36e-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: 132.58  E-value: 6.36e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    630 DIFFLIDHSGSIYPTDFQDMKKFIIEFIHTFRISPQHVRLGVAKYADSPNLEFDLTDYSDAKSVEKAVEGIRQI-GGGTE 708
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    709 TGRALAF-MSPHFDRAMTTRGHkVPEYLVVITDGKSSDK---VKVPAEQLRAQGVIVYSIGVKSA-DMEELREISGDPKR 783
Cdd:smart00327   81 LGAALQYaLENLFSKSAGSRRG-APKVVILITDGESNDGpkdLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPGG 159

                           170
                    ....*....|....*
gi 657584108    784 TFFVNNFDALKPIKD 798
Cdd:smart00327  160 VYVFLPELLDLLIDL 174
Kunitz_collagen_alpha6_VI-like cd22631
Kunitz-type domain from the alpha6 chain of fish type VI collagen, and similar proteins; This ...
 2512-2562 1.42e-34

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: 126.96  E-value: 1.42e-34
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22631     1 CLLGQDAGSCQNYTMMWFFDSKQGRCSRFWYGGCGGNANRFETQEECENLC 51
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 816-975 2.14e-34

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: 130.48  E-value: 2.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  816 DLLFLIDSSGSIYPQDYNKMKDFMKSVISKSFIGQNEVHVGVMQFSTIQKLEFPLNRFYSKGEMSKAIDDMQQIGGGTHT 895
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  896 GEAITDVSQ-YFDSSRGGRPGLRQRLVVITDGEAQDVVRGPAAALRAKGVVVYAIGVVDANTTQLLEISGSPDRMYAER- 973
Cdd:cd01482    82 GKALTHVREkNFTPDAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSETHVFNv 161


                  ...
gi 657584108  974 -DF 975
Cdd:cd01482   162 aDF 164
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 814-996 6.88e-34

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: 131.35  E-value: 6.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  814 PGDLLFLIDSSGSIYPQDYNKMKDFMKSVISKSFIGQNEVHVGVMQFSTIQKLEFPLNRFYSKGEMSKAIDDMQQIGGGT 893
Cdd:cd01475     2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  894 HTGEAIT---DVSqyFDSSRGGRPGlRQR----LVVITDGEAQDVVRGPAAALRAKGVVVYAIGVVDANTTQLLEISGSP 966
Cdd:cd01475    82 MTGLAIQyamNNA--FSEAEGARPG-SERvprvGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEP 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 657584108  967 --DRMYAERDFDALKDLESQVALELCDPERDC 996
Cdd:cd01475   159 laDHVFYVEDFSTIEELTKKFQGKICVVPDLC 190
Kunitz_papilin cd22635
Kunitz domain of papilin, and similar proteins; This model includes the Kunitz domain found in ...
 2439-2490 1.17e-33

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: 124.30  E-value: 1.17e-33
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGIQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22635     1 CLLDKDAGTVCGDYVQRWYYDPATGACNRFWYGGCGGNANRFATEAECLRTC 52
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 629-808 4.20e-33

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: 129.04  E-value: 4.20e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  629 ADIFFLIDHSGSIYPTDFQDMKKFIIEFIHTFRISPQHVRLGVAKYADSPNLEFDLTDYSDAKSVEKAVEGIRQIGGGTE 708
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  709 TGRALAFMsphFDRAMT------TRGHKVPEYLVVITDGKSSDKVKVPAEQLRAQGVIVYSIGVKSADMEELREISGDP- 781
Cdd:cd01475    83 TGLAIQYA---MNNAFSeaegarPGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPl 159

                         170       180
                  ....*....|....*....|....*...
gi 657584108  782 -KRTFFVNNFDALKPIKDDIITDICSTD 808
Cdd:cd01475   160 aDHVFYVEDFSTIEELTKKFQGKICVVP 187
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 419-582 2.09e-32

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 124.60  E-value: 2.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  419 ADIVFIVDESGSIGVANFQMVRTFLHSIISGLEISPTRVRVGIVMYNDRPadqAQQVYLNTFNNKDELLKFIK-ILPYHG 497
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNA---RVVLPLTTDTDKADLLEAIDaLKKGLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  498 GGTNTGAALKFARESVFikergSRKDKGVQQVAVVITDGESQDD---VSQPAADLRRAGVTIYSVGVKN-ANKVQLVEMA 573
Cdd:cd00198    78 GGTNIGAALRLALELLK-----SAKRPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGDdANEDELKEIA 152


                  ....*....
gi 657584108  574 SHPPNKHVF 582
Cdd:cd00198   153 DKTTGGAVF 161
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 420-592 3.13e-32

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: 124.78  E-value: 3.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  420 DIVFIVDESGSIGVANFQMVRTFLHSIISGLEISPTRVRVGIVMYNDRPadqaQQVY-LNTFNNKDELLKFIKILPYHGG 498
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESF----RTEFtLNEYRTKEEPLSLVKHISQLLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  499 GTNTGAALKFARESVFIKERGSRKDkgVQQVAVVITDGESQDDVSQPAA--DLRRAGVTIYSVGV----KNANKVQ-LVE 571
Cdd:cd01469    78 LTNTATAIQYVVTELFSESNGARKD--ATKVLVVITDGESHDDPLLKDVipQAEREGIIRYAIGVgghfQRENSREeLKT 155

                         170       180
                  ....*....|....*....|.
gi 657584108  572 MASHPPNKHVFIVDSFAKLKS 592
Cdd:cd01469   156 IASKPPEEHFFNVTDFAALKD 176
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1679-1924 3.20e-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: 132.72  E-value: 3.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1679 GRGERGNPGNPGIPGIRGEAGLKGQRGLRGDPGEpgadnnspgaKGDSGNAGLPGLPGPDGRPGESGIVGNPGQDGRRGs 1758
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGP----------AGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG- 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1759 pgvkgaagepgaagLQGIPGASGPQGTRGVRGQPGPRgipglpgpqggpgsvggpgaagrrggngqkGQPGDPGDKGVPG 1838
Cdd:NF038329  184 --------------AKGPAGEKGPQGPRGETGPAGEQ------------------------------GPAGPAGPDGEAG 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1839 PLGPRGMPGEDGRDGYGPAGRKGVKGDPGFPGYPGLLGEDGLQGPKGLPgrkgnrgrggnsgrsgesGISGDPGYAGHRG 1918
Cdd:NF038329  220 PAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA------------------GPDGPDGKDGERG 281


                  ....*.
gi 657584108 1919 PRGLPG 1924
Cdd:NF038329  282 PVGPAG 287
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1002-1167 3.55e-32

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: 124.36  E-value: 3.55e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1002 ADIIFLVDGSTSITLAKFRNMQRFMESMVNQTTVGKDLTRFGVILYSNDPKSVFTLNQYSSKKEVVKAISNLRsPFGDT- 1080
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLR-LRGGSq 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1081 -YTGKALAY-SLQFFDAQHGGRAALQVPQILMVITDGDATDrnSLVAPSVALRDHGVSVFSIGVEGANMTQLEIMAgYDR 1158
Cdd:cd01481    80 lNTGSALDYvVKNLFTKSAGSRIEEGVPQFLVLITGGKSQD--DVERPAVALKRAGIVPFAIGARNADLAELQQIA-FDP 156


                  ....*....
gi 657584108 1159 SKVFYVDNF 1167
Cdd:cd01481   157 SFVFQVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 629-790 6.99e-32

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: 123.20  E-value: 6.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  629 ADIFFLIDHSGSIYPTDFQDMKKFIIEFIHTFRISPQHVRLGVAKYADSPNLEFDLTDYSDAKSVEKAVEGIRQIGG-GT 707
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGsQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  708 ETGRALAF-MSPHFDRAMTTRGHK-VPEYLVVITDGKSSDKVKVPAEQLRAQGVIVYSIGVKSADMEELREISGDPKRTF 785
Cdd:cd01481    81 NTGSALDYvVKNLFTKSAGSRIEEgVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160


                  ....*
gi 657584108  786 FVNNF 790
Cdd:cd01481   161 QVSDF 165
Kunitz_collagen_alpha6_VI cd22630
Kunitz-type domain from the alpha6 chain of human type VI collagen, and similar proteins; This ...
 2510-2563 9.65e-31

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: 116.16  E-value: 9.65e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 657584108 2510 DACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLCL 2563
Cdd:cd22630     1 DACSLDQDEGECQNYVLKWYYDQEQKECSQFWYGGCGGNKNRFETQEECEALCV 54
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 816-970 3.67e-30

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 118.27  E-value: 3.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  816 DLLFLIDSSGSIYPQdYNKMKDFMKSVISKSFIGQNEVHVGVMQFSTI--QKLEFPLNRFYSKGEMSKAIDDMQQIGGGT 893
Cdd:cd01476     2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRgrQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  894 HTGEAITDVSQYFDSSRGGRPGLRQRLVVITDGEAQDVVRGPAAALRA-KGVVVYAIGVVD---ANTTQLLEISGSPDRM 969
Cdd:cd01476    81 ATGAAIEVALQQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAvPNIETFAVGTGDpgtVDTEELHSITGNEDHI 160


                  .
gi 657584108  970 Y 970
Cdd:cd01476   161 F 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 629-787 3.96e-30

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 118.05  E-value: 3.96e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  629 ADIFFLIDHSGSIYPTDFQDMKKFIIEFIHTFRISPQHVRLGVAKYADSPNLEFDLTDYSDAKSVEKAVEGIR-QIGGGT 707
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkGLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  708 ETGRALAFMSPHFDRAMTTRGHKVpeyLVVITDGKSSD---KVKVPAEQLRAQGVIVYSIGVKS-ADMEELREISGDPKR 783
Cdd:cd00198    81 NIGAALRLALELLKSAKRPNARRV---IILLTDGEPNDgpeLLAEAARELRKLGITVYTIGIGDdANEDELKEIADKTTG 157


                  ....
gi 657584108  784 TFFV 787
Cdd:cd00198   158 GAVF 161
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 630-796 4.24e-30

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: 118.61  E-value: 4.24e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  630 DIFFLIDHSGSIYPTDFQDMKKFIIEFIHTFRISPQHVRLGVAKYADSPNLEFDLTDYSDAKSVEKAVEGIRQIGGGTET 709
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  710 GRAL------AFmspHFDRAMTTRGHKVpeyLVVITDGKSSDKVKVPA--EQLRAQGVIVYSIGV-----KSADMEELRE 776
Cdd:cd01469    82 ATAIqyvvteLF---SESNGARKDATKV---LVVITDGESHDDPLLKDviPQAEREGIIRYAIGVgghfqRENSREELKT 155

                         170       180
                  ....*....|....*....|..
gi 657584108  777 ISGDPKRTFF--VNNFDALKPI 796
Cdd:cd01469   156 IASKPPEEHFfnVTDFAALKDI 177
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 33-193 4.32e-30

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 118.05  E-value: 4.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   33 ADIVFLIDGSSSIGISNFQEIRQFLRSVISGLDIGADKVRIGLAQYSDEPYQEFLLKDHMDKQSLLAAVDTFQYRT-GGT 111
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLgGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  112 ETGEAIDFLMNQYFtedagSRAKQRVPQIAVVITDGDSTDD---VAAPALRLRQHGVIMFAIGVG-KANPTELEAIANRP 187
Cdd:cd00198    81 NIGAALRLALELLK-----SAKRPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGdDANEDELKEIADKT 155


                  ....*.
gi 657584108  188 PKRFMF 193
Cdd:cd00198   156 TGGAVF 161
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 228-383 2.31e-29

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: 116.17  E-value: 2.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  228 ADIFFLVDS--GISQAEFQQVRSVLVRLTNQVNFGASAHRLGLAQYGQDIKVEFLLNAFQSKDEMQGGIKRFRQRRLQTn 305
Cdd:cd01472     1 ADIVFLVDGseSIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGT- 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657584108  306 eprNLGSALQYASANFFTSEAGSRadQGYRQYLVVLSGKDSDDEVFRQSRLIKSEGVTVVGMSLG-ASMNEIRVISTAP 383
Cdd:cd01472    80 ---NTGKALKYVRENLFTEASGSR--EGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKnADEEELKQIASDP 153
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 816-975 3.94e-29

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: 115.50  E-value: 3.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  816 DLLFLIDSSGSIYPQDYNKMKDFMKSVISKSFIGQNEVHVGVMQFSTIQKLEFPLNRFYSKGEMSKAIDDMQQIGG-GTH 894
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGsQLN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  895 TGEAITDVSQ-YFDSSRGGR--PGLRQRLVVITDGEAQDVVRGPAAALRAKGVVVYAIGVVDANTTQLLEISGSPDRMYA 971
Cdd:cd01481    82 TGSALDYVVKnLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVFQ 161


                  ....
gi 657584108  972 ERDF 975
Cdd:cd01481   162 VSDF 165
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1002-1182 6.66e-29

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: 117.10  E-value: 6.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1002 ADIIFLVDGSTSITLAKFRNMQRFMESMVNQTTVGKDLTRFGVILYSNDPKSVFTLNQYSSKKEVVKAISNLRSPFGDTY 1081
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1082 TGKALAYSLQ--FFDAQhGGR-AALQVPQILMVITDGDATDRNSLVAPSValRDHGVSVFSIGVEGANMTQLEIMAGYDR 1158
Cdd:cd01475    83 TGLAIQYAMNnaFSEAE-GARpGSERVPRVGIVVTDGRPQDDVSEVAAKA--RALGIEMFAVGVGRADEEELREIASEPL 159

                         170       180
                  ....*....|....*....|....*
gi 657584108 1159 SK-VFYVDNFEALETLYKNITQVLC 1182
Cdd:cd01475   160 ADhVFYVEDFSTIEELTKKFQGKIC 184
VWA pfam00092
von Willebrand factor type A domain;
229-383 1.58e-28

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 113.91  E-value: 1.58e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   229 DIFFLVDS--GISQAEFQQVRSVLVRLTNQVNFGASAHRLGLAQYGQDIKVEFLLNAFQSKDEMQGGIKRFRQrrlQTNE 306
Cdd:pfam00092    1 DIVFLLDGsgSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRY---LGGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   307 PRNLGSALQYASANFFTSEAGSRAdqGYRQYLVVLS-GKDSDDEVFRQSRLIKSEGVTV--VGMSlGASMNEIRVISTAP 383
Cdd:pfam00092   78 TTNTGKALKYALENLFSSAAGARP--GAPKVVVLLTdGRSQDGDPEEVARELKSAGVTVfaVGVG-NADDEELRKIASEP 154
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1002-1163 2.11e-28

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 113.43  E-value: 2.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1002 ADIIFLVDGSTSITLAKFRNMQRFMESMVNQTTVGKDLTRFGVILYSNDPKSVFTLNQYSSKKEVVKAISNLR-SPFGDT 1080
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkGLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1081 YTGKALAYSLQFFDAQHGGRAalqvPQILMVITDGDATDRNSLVAPSVA-LRDHGVSVFSIGV-EGANMTQLEIMAGYDR 1158
Cdd:cd00198    81 NIGAALRLALELLKSAKRPNA----RRVIILLTDGEPNDGPELLAEAAReLRKLGITVYTIGIgDDANEDELKEIADKTT 156


                  ....*
gi 657584108 1159 SKVFY 1163
Cdd:cd00198   157 GGAVF 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 816-968 3.77e-28

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 112.66  E-value: 3.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  816 DLLFLIDSSGSIYPQDYNKMKDFMKSVISKSFIGQNEVHVGVMQFSTIQKLEFPLNRFYSKGEMSKAIDDMQ-QIGGGTH 894
Cdd:cd00198     2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkGLGGGTN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657584108  895 TGEAITDVSQYFDSSRggRPGLRQRLVVITDGEAQDVVRGP---AAALRAKGVVVYAIGV-VDANTTQLLEISGSPDR 968
Cdd:cd00198    82 IGAALRLALELLKSAK--RPNARRVIILLTDGEPNDGPELLaeaARELRKLGITVYTIGIgDDANEDELKEIADKTTG 157
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1003-1173 5.31e-28

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: 112.83  E-value: 5.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1003 DIIFLVDGSTSITLAKFRNMQRFMESMVNQTTVGKDLTRFGVILYSNDPKSVFTLNQYSSKKEVVKAISNLRSPFGDTYT 1082
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1083 GKALAYSL-QFFDAQHGGRAalQVPQILMVITDGDATD--RNSLVAPsvALRDHGVSVFSIGVEGA---NMTQLE---IM 1153
Cdd:cd01469    82 ATAIQYVVtELFSESNGARK--DATKVLVVITDGESHDdpLLKDVIP--QAEREGIIRYAIGVGGHfqrENSREElktIA 157

                         170       180
                  ....*....|....*....|
gi 657584108 1154 AGYDRSKVFYVDNFEALETL 1173
Cdd:cd01469   158 SKPPEEHFFNVTDFAALKDI 177
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1194-1342 5.89e-28

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 111.89  E-value: 5.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1194 ADLVFLIDQSGSIASTDYSIMKKFTTELVNSFKVSEDLVRVGLAQFSSNFQNEFYLNQFYTEEAVSKHI-FNMRQLGGGT 1272
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIdALKKGLGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657584108 1273 NIGLALDSIREYFEAsrgcRRSAGISQNLVLITDGESQDD---VEDAAERLRALGIEVFAIGIGNVHDLELLQ 1342
Cdd:cd00198    81 NIGAALRLALELLKS----AKRPNARRVIILLTDGEPNDGpelLAEAARELRKLGITVYTIGIGDDANEDELK 149
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 419-583 2.96e-27

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 110.18  E-value: 2.96e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  419 ADIVFIVDESGSIGvANFQMVRTFLHSIISGLEISPTRVRVGIVMYNDrPADQAQQVYLNTFNNKDELLKFIKILPYHGG 498
Cdd:cd01476     1 LDLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSG-RGRQRVRFNLPKHNDGEELLEKVDNLRFIGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  499 GTNTGAALKFAREsvfIKERGSRKDKGVQQVAVVITDGESQDDVSQPAADLRR-AGVTIYSVGVKNANKVQLVEMASHPP 577
Cdd:cd01476    79 TTATGAAIEVALQ---QLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAvPNIETFAVGTGDPGTVDTEELHSITG 155


                  ....*..
gi 657584108  578 N-KHVFI 583
Cdd:cd01476   156 NeDHIFT 162
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1194-1352 1.12e-26

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 108.26  E-value: 1.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1194 ADLVFLIDQSGSIASTdYSIMKKFTTELVNSFKVSEDLVRVGLAQFSSNFQN--EFYLNQFYTEEAVSKHIFNMRQLGGG 1271
Cdd:cd01476     1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1272 TNIGLALDSIREYFEASRGCRRsaGISQNLVLITDGESQDDVEDAAERLRAL-GIEVFAIGIGN---VHDLELLQITGTP 1347
Cdd:cd01476    80 TATGAAIEVALQQLDPSEGRRE--GIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGDpgtVDTEELHSITGNE 157


                  ....*
gi 657584108 1348 ERLFT 1352
Cdd:cd01476   158 DHIFT 162
Kunitz_collagen_alpha3_VI cd22629
Kunitz-type domain from the alpha3 chain of human type VI collagen, and similar proteins; This ...
 2510-2562 2.35e-26

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: 103.60  E-value: 2.35e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2510 DACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22629     1 DICKLPKDEGTCRDFVLKWYYDPETKSCARFWYGGCGGNENRFDSQEECEKVC 53
Kunitz_papilin_lacunin-like cd22639
Drosophila melanogaster Kunitz domain 1, Manduca sexta lacunin Kunitz domain 1, and simialr ...
 2512-2562 2.86e-26

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: 103.04  E-value: 2.86e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22639     1 CSLPKDRGPCRNYTVKWYFDMAYGGCSRFWYGGCGGNGNRFDTEEECKAVC 51
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1693-1924 9.52e-26

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: 113.08  E-value: 9.52e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1693 GIRGEAGLKGQRGLRGDPGEpgadnnspgaKGDSGNAGLPGLPGPDGRPGESGIVGNPGQDGRRGspgvkgaagepgaag 1772
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGP----------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG--------------- 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1773 lqgipgasgPQGTRGVRGQPGPRGIPGLPGPQGGPGSVGGPGAAGRRGGNGQKGQPGDPGDKGVPGPL-----GPRGMPG 1847
Cdd:NF038329  172 ---------PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPG 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1848 EDGRDGY----GPAGRKGVKGDPGFPGYPGLLGEDGLQGPKGLPGRKGNRGRGGNSGRSGESGISGDPGYAGHRGPRGLP 1923
Cdd:NF038329  243 PTGEDGPqgpdGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQP 322


                  .
gi 657584108 1924 G 1924
Cdd:NF038329  323 G 323
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 33-192 3.94e-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: 3.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   33 ADIVFLIDGSSSIGiSNFQEIRQFLRSVISGLDIGADKVRIGLAQYSDEPYQ--EFLLKDHMDKQSLLAAVDTFQYRTGG 110
Cdd:cd01476     1 LDLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  111 TETGEAIDFLMnQYFTEDAGsrAKQRVPQIAVVITDGDSTDDVAAPALRLR-QHGVIMFAIGVG---KANPTELEAIANR 186
Cdd:cd01476    80 TATGAAIEVAL-QQLDPSEG--RREGIPKVVVVLTDGRSHDDPEKQARILRaVPNIETFAVGTGdpgTVDTEELHSITGN 156


                  ....*.
gi 657584108  187 PPKRFM 192
Cdd:cd01476   157 EDHIFT 162
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1195-1362 1.26e-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: 102.82  E-value: 1.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1195 DLVFLIDQSGSIASTDYSIMKKFTTELVNSFKVSEDLVRVGLAQFSSNFQNEFYLNQFYTEEAVSKHIFNMRQLGGGTNI 1274
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1275 GLALDSIR-EYFEASRGCRRSAgiSQNLVLITDGESQDD-----VEDAAERlraLGIEVFAIGIGNVHDL-----ELLQI 1343
Cdd:cd01469    82 ATAIQYVVtELFSESNGARKDA--TKVLVVITDGESHDDpllkdVIPQAER---EGIIRYAIGVGGHFQRensreELKTI 156

                         170       180
                  ....*....|....*....|.
gi 657584108 1344 TGTP--ERLFTVENFGSLEKI 1362
Cdd:cd01469   157 ASKPpeEHFFNVTDFAALKDI 177
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 228-383 1.87e-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: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 101.98  E-value: 1.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  228 ADIFFLVDS--GISQAEFQQVRSVLVRLTNQVNFGASAHRLGLAQYGQDIKVEFLLNAFQSKDEMQGGIKRFRQRRLQTN 305
Cdd:cd01450     1 LDIVFLLDGseSVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  306 eprNLGSALQYASANFFTseaGSRADQGYRQYLVVLS-GKDSDDE-VFRQSRLIKSEGVTVVGMSLG-ASMNEIRVISTA 382
Cdd:cd01450    81 ---NTGKALQYALEQLFS---ESNARENVPKVIIVLTdGRSDDGGdPKEAAAKLKDEGIKVFVVGVGpADEEELREIASC 154


                  .
gi 657584108  383 P 383
Cdd:cd01450   155 P 155
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 629-786 6.26e-24

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 100.55  E-value: 6.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  629 ADIFFLIDHSGSIYPTdFQDMKKFIIEFIHTFRISPQHVRLGVAKYADSPN--LEFDLTDYSDAKSVEKAVEGIRQIGGG 706
Cdd:cd01476     1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  707 TETGRALAFMSPHFDRAMTTRgHKVPEYLVVITDGKSSDKVKVPAEQLRAQ-GVIVYSIGVK---SADMEELREISGDPK 782
Cdd:cd01476    80 TATGAAIEVALQQLDPSEGRR-EGIPKVVVVLTDGRSHDDPEKQARILRAVpNIETFAVGTGdpgTVDTEELHSITGNED 158


                  ....
gi 657584108  783 RTFF 786
Cdd:cd01476   159 HIFT 162
Kunitz_papilin cd22635
Kunitz domain of papilin, and similar proteins; This model includes the Kunitz domain found in ...
 2512-2562 9.08e-24

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: 96.18  E-value: 9.08e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2512 CFLSQDQGS-CQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22635     1 CLLDKDAGTvCGDYVQRWYYDPATGACNRFWYGGCGGNANRFATEAECLRTC 52
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 33-200 1.14e-23

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: 100.54  E-value: 1.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   33 ADIVFLIDGSSSIGISNFQEIRQFLRSVIS------GLDIGADKVRIGLAQYSDEPYQEF-LLKDHMDKQSLLAAVDTFQ 105
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAErflkdyYRKDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  106 YRTGGTETGEAIDFLMNQYFTedaGSRAKQRvpQIAVVITDGDS---TDDVAAPALRLRQH-GVIMFAIGVGKANPTELE 181
Cdd:cd01480    83 YIGGGTFTDCALKYATEQLLE---GSHQKEN--KFLLVITDGHSdgsPDGGIEKAVNEADHlGIKIFFVAVGSQNEEPLS 157

                         170       180
                  ....*....|....*....|....*....
gi 657584108  182 AIANRPPK----------RFMFTIDNYEA 200
Cdd:cd01480   158 RIACDGKSalyrenfaelLWSFFIDDETA 186
Kunitz-type cd00109
Kunitz/Bovine pancreatic trypsin inhibitor (BPTI) domain; This family contains the Kunitz ...
 2512-2562 2.39e-23

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: 94.92  E-value: 2.39e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd00109     1 CLLPPDPGPCRAYFPRWYYNSETGQCEEFIYGGCGGNANNFETKEECEATC 51
Kunitz_BPTI pfam00014
Kunitz/Bovine pancreatic trypsin inhibitor domain; Indicative of a protease inhibitor, usually ...
 2511-2562 3.69e-23

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: 94.25  E-value: 3.69e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 657584108  2511 ACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:pfam00014    1 ICSLPPDSGPCKASIPRWYYNPTTGTCEPFTYGGCGGNANNFESLEECESTC 52
KU smart00131
BPTI/Kunitz family of serine protease inhibitors; Serine protease inhibitors. One member of ...
 2510-2562 8.39e-23

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: 93.48  E-value: 8.39e-23
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 657584108   2510 DACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:smart00131    1 DVCLLPPDTGPCGGSIPRYYYDPETGTCEPFTYGGCGGNANNFESLEECERTC 53
Kunitz_collagen_alpha1_XXVIII cd22628
Kunitz-type domain from the alpha1 chain of type XXVIII collagen, and similar proteins; This ...
 2512-2562 1.29e-22

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: 92.73  E-value: 1.29e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22628     1 CLEPLDPGPCREYVVKWYYDKQANSCAQFWYGGCEGNRNRFETEEECRKTC 51
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1593-1737 3.63e-22

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: 102.29  E-value: 3.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1593 EGIRGSRGLPGSKGVSGQKGYPGFPGEEGIAGDRGSPGPSGPqgvqgcsgrrgvkgfRGLRGNRGEDGEDGLDGVDGEQG 1672
Cdd:NF038329  232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGP---------------DGKDGERGPVGPAGKDGQNGKDG 296

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657584108 1673 LTGADGGRGERgnpGNPGIPGIRGEAGLKGQRGLrgdPGEPGADnnspgakgdsgnaGLPGLPGP 1737
Cdd:NF038329  297 LPGKDGKDGQN---GKDGLPGKDGKDGQPGKDGL---PGKDGKD-------------GQPGKPAP 342
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 629-795 4.42e-22

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 95.92  E-value: 4.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  629 ADIFFLIDHSGSIYPTDFQDMKKFIIEFIHTFR------ISPQHVRLGVAKYADSPNLEF-DLTDYSDAKSVEKAVEGIR 701
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFLkdyyrkDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  702 QIGGGTETGRALAFMSphfDRAMTTRGHKVPEYLVVITDGKSS----DKVKVPAEQLRAQGVIVYSIGVKSADMEELREI 777
Cdd:cd01480    83 YIGGGTFTDCALKYAT---EQLLEGSHQKENKFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAVGSQNEEPLSRI 159

                         170
                  ....*....|....*...
gi 657584108  778 SGDPKRTFFVNNFDALKP 795
Cdd:cd01480   160 ACDGKSALYRENFAELLW 177
Kunitz_papilin_mig6-like cd22637
Drosophila melanogaster Kunitz domains 5, 6, 7, and Caenorhabditis elegans Kunitz domain 5 of ...
 2512-2562 3.08e-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: 88.95  E-value: 3.08e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22637     1 CDQPKDTGPCDNWVLKWYYDSKKGSCRQFYYGGCGGNDNRFDTEEECEARC 51
Kunitz_papilin_lacunin-like cd22639
Drosophila melanogaster Kunitz domain 1, Manduca sexta lacunin Kunitz domain 1, and simialr ...
 2439-2491 7.44e-21

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: 87.63  E-value: 7.44e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2439 CQLDSDSGIqCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTCV 2491
Cdd:cd22639     1 CSLPKDRGP-CRNYTVKWYFDMAYGGCSRFWYGGCGGNGNRFDTEEECKAVCV 52
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 229-383 2.33e-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: 90.59  E-value: 2.33e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    229 DIFFLVD-SG-ISQAEFQQVRSVLVRLTNQVNFGASAHRLGLAQYGQDIKVEFLLNAFQSKDEMQGGIKRFRQRRLQTNe 306
Cdd:smart00327    1 DVVFLLDgSGsMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGT- 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    307 prNLGSALQYASANFFTSEAGSRAdqGYRQYLVVLS-GKDSDD--EVFRQSRLIKSEGVTV--VGMSLGASMNEIRVIST 381
Cdd:smart00327   80 --NLGAALQYALENLFSKSAGSRR--GAPKVVILITdGESNDGpkDLLKAAKELKRSGVKVfvVGVGNDVDEEELKKLAS 155


                    ..
gi 657584108    382 AP 383
Cdd:smart00327  156 AP 157
Kunitz-type cd00109
Kunitz/Bovine pancreatic trypsin inhibitor (BPTI) domain; This family contains the Kunitz ...
 2439-2490 2.45e-20

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: 86.06  E-value: 2.45e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGiQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd00109     1 CLLPPDPG-PCRAYFPRWYYNSETGQCEEFIYGGCGGNANNFETKEECEATC 51
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 419-581 2.59e-20

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: 90.91  E-value: 2.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  419 ADIVFIVDESGSIGVANFQMVRTFLHSIIS------GLEISPTRVRVGIVMYNDRPadQAQQVYLNTFNNKDELLKFIKI 492
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAErflkdyYRKDPAGSWRVGVVQYSDQQ--EVEAGFLRDIRNYTSLKEAVDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  493 LPYHGGGTNTGAALKFARESVFIkerGSRkdKGVQQVAVVITDGESqdDVSQPAADLR------RAGVTIYSVGVKNANK 566
Cdd:cd01480    81 LEYIGGGTFTDCALKYATEQLLE---GSH--QKENKFLLVITDGHS--DGSPDGGIEKavneadHLGIKIFFVAVGSQNE 153

                         170
                  ....*....|....*
gi 657584108  567 VQLVEMASHPPNKHV 581
Cdd:cd01480   154 EPLSRIACDGKSALY 168
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 814-980 2.85e-20

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: 90.91  E-value: 2.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  814 PGDLLFLIDSSGSIYPQDYNKMKDFMKSVISKsFIGQN-------EVHVGVMQFSTIQKLEFPLNRFY-SKGEMSKAIDD 885
Cdd:cd01480     2 PVDITFVLDSSESVGLQNFDITKNFVKRVAER-FLKDYyrkdpagSWRVGVVQYSDQQEVEAGFLRDIrNYTSLKEAVDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  886 MQQIGGGTHTGEAITDVS-QYFDSSRGGRpglRQRLVVITDGEAQ--------DVVRGPAAAlrakGVVVYAIGVVDANT 956
Cdd:cd01480    81 LEYIGGGTFTDCALKYATeQLLEGSHQKE---NKFLLVITDGHSDgspdggieKAVNEADHL----GIKIFFVAVGSQNE 153

                         170       180
                  ....*....|....*....|....*....
gi 657584108  957 TQLLEISGSP-----DRMYAERDFDALKD 980
Cdd:cd01480   154 EPLSRIACDGksalyRENFAELLWSFFID 182
Kunitz_collagen_alpha6_VI-like cd22631
Kunitz-type domain from the alpha6 chain of fish type VI collagen, and similar proteins; This ...
 2439-2490 3.17e-20

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: 85.74  E-value: 3.17e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGiQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22631     1 CLLGQDAG-SCQNYTMMWFFDSKQGRCSRFWYGGCGGNANRFETQEECENLC 51
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 420-561 3.67e-20

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: 90.52  E-value: 3.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  420 DIVFIVDESGSIGVAN-FQMVRTFLHSIISGLEISPTRVRVGIVMYNdrpADQAQQVYLNTFN--NKDELLKFI---KIL 493
Cdd:cd01471     2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFS---TNAKELIRLSSPNstNKDLALNAIralLSL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  494 PYHGGGTNTGAALKFARESVFiKERGSRKDkgVQQVAVVITDGESQDDVS--QPAADLRRAGVTIYSVGV 561
Cdd:cd01471    79 YYPNGSTNTTSALLVVEKHLF-DTRGNREN--APQLVIIMTDGIPDSKFRtlKEARKLRERGVIIAVLGV 145
Kunitz_BPTI pfam00014
Kunitz/Bovine pancreatic trypsin inhibitor domain; Indicative of a protease inhibitor, usually ...
 2438-2491 5.86e-20

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: 85.39  E-value: 5.86e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 657584108  2438 RCQLDSDSGiQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTCV 2491
Cdd:pfam00014    1 ICSLPPDSG-PCKASIPRWYYNPTTGTCEPFTYGGCGGNANNFESLEECESTCR 53
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 228-383 1.80e-19

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: 87.73  E-value: 1.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  228 ADIFFLVDSG--ISQAEFQQVRSVLVRLTNQVNFGASAHRLGLAQYGQDIKVEFLLNAFQSKDEMQGGIKRFRQRRLQTN 305
Cdd:cd01482     1 ADIVFLVDGSwsIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  306 EprnlGSALQYASANFFTSEAGSRAdqGYRQYLVVLSGKDSDDEVFRQSRLIKSEGVTV--VGMSlGASMNEIRVISTAP 383
Cdd:cd01482    81 T----GKALTHVREKNFTPDAGARP--GVPKVVILITDGKSQDDVELPARVLRNLGVNVfaVGVK-DADESELKMIASKP 153
Kunitz_collagen_alpha6_VI cd22630
Kunitz-type domain from the alpha6 chain of human type VI collagen, and similar proteins; This ...
 2439-2491 2.29e-19

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: 83.42  E-value: 2.29e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2439 CQLDSDSGiQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTCV 2491
Cdd:cd22630     3 CSLDQDEG-ECQNYVLKWYYDQEQKECSQFWYGGCGGNKNRFETQEECEALCV 54
Kunitz_collagen_alpha1_VII cd22627
Kunitz-type domain from the alpha1 chain of type VII collagen, and similar proteins; This ...
 2510-2562 5.76e-19

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: 82.30  E-value: 5.76e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2510 DACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22627     1 DPCLLPMDEGSCSDYTLLWYYHQKAGECRPFVYGGCGGNANRFSSKEDCELRC 53
KU smart00131
BPTI/Kunitz family of serine protease inhibitors; Serine protease inhibitors. One member of ...
 2438-2490 6.40e-19

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: 82.31  E-value: 6.40e-19
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 657584108   2438 RCQLDSDSGIqCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:smart00131    2 VCLLPPDTGP-CGGSIPRYYYDPETGTCEPFTYGGCGGNANNFESLEECERTC 53
VWA pfam00092
von Willebrand factor type A domain;
1956-2097 8.76e-19

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 86.17  E-value: 8.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1956 ELVFGLDMSDDVTPTAFERQRSALLALLEEINIaesnCPSGARVAVVGYSAYTKYLIRFQDYRRKTQLEDAVKNIALeRT 2035
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDI----GPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRY-LG 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657584108  2036 SNKRHLGAAMHFVAQNVFKRVRSGMV-MRKVAVFFSNGPSQEvNDIPGAVMEYRGLNIVPAVI 2097
Cdd:pfam00092   76 GGTTNTGKALKYALENLFSSAAGARPgAPKVVVLLTDGRSQD-GDPEEVARELKSAGVTVFAV 137
Kunitz_collagen_alpha3_VI cd22629
Kunitz-type domain from the alpha3 chain of human type VI collagen, and similar proteins; This ...
 2439-2490 1.17e-18

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: 81.65  E-value: 1.17e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGiQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22629     3 CKLPKDEG-TCRDFVLKWYYDPETKSCARFWYGGCGGNENRFDSQEECEKVC 53
VWA pfam00092
von Willebrand factor type A domain;
2166-2338 2.78e-18

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 84.63  E-value: 2.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  2166 DLVMVADSSREIQADQYAGVQQLLGSVVEQLAVSPQprragnQARVAVVQQGGarSAKVEFNLQTYQNQELMRTHLTQKM 2245
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPD------GTRVGLVQYSS--DVRTEFPLNDYSSKEELLSAVDNLR 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  2246 RQQGGSSALGQTLDYTLkEVLLKAGQPSRKKALLAVV----GTSTAWEDQArlhyVSQKAKCEGVALFVVTVGDHYNRtQ 2321
Cdd:pfam00092   73 YLGGGTTNTGKALKYAL-ENLFSSAAGARPGAPKVVVlltdGRSQDGDPEE----VARELKSAGVTVFAVGVGNADDE-E 146

                          170
                   ....*....|....*..
gi 657584108  2322 VEELASLPLQQHLIHVS 2338
Cdd:pfam00092  147 LRKIASEPGEGHVFTVS 163
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1194-1359 3.20e-18

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 84.74  E-value: 3.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1194 ADLVFLIDQSGSIASTDYSIMKKFTTELVNSF------KVSEDLVRVGLAQFSSNFQNEFYLNQFYTE-EAVSKHIFNMR 1266
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNyTSLKEAVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1267 QLGGGTNIGLALDSIRE-YFEASRGCRRsagisQNLVLITDGESQ----DDVEDAAERLRALGIEVFAIGIGNVHDLELL 1341
Cdd:cd01480    83 YIGGGTFTDCALKYATEqLLEGSHQKEN-----KFLLVITDGHSDgspdGGIEKAVNEADHLGIKIFFVAVGSQNEEPLS 157

                         170
                  ....*....|....*...
gi 657584108 1342 QITGTPERLFTVENFGSL 1359
Cdd:cd01480   158 RIACDGKSALYRENFAEL 175
Kunitz_papilin_mig6-like cd22637
Drosophila melanogaster Kunitz domains 5, 6, 7, and Caenorhabditis elegans Kunitz domain 5 of ...
 2439-2490 3.93e-18

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: 80.09  E-value: 3.93e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGiQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22637     1 CDQPKDTG-PCDNWVLKWYYDSKKGSCRQFYYGGCGGNDNRFDTEEECEARC 51
Kunitz_collagen_alpha1_XXVIII cd22628
Kunitz-type domain from the alpha1 chain of type XXVIII collagen, and similar proteins; This ...
 2439-2490 2.19e-17

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: 77.71  E-value: 2.19e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGiQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22628     1 CLEPLDPG-PCREYVVKWYYDKQANSCAQFWYGGCEGNRNRFETEEECRKTC 51
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1002-1162 8.23e-17

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: 80.14  E-value: 8.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1002 ADIIFLVDGSTSiTLAKFRNMQRFMESMVNQTTVGKDLTRFGVILYSNDPKS--VFTLNQYSSKKEVVKAISNLRSPFGD 1079
Cdd:cd01476     1 LDLLFVLDSSGS-VRGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1080 TYTGKALAYSLQFFDAQHGGRAAlqVPQILMVITDGDATDrnSLVAPSVALRDH-GVSVFSIGV---EGANMTQLEIMAG 1155
Cdd:cd01476    80 TATGAAIEVALQQLDPSEGRREG--IPKVVVVLTDGRSHD--DPEKQARILRAVpNIETFAVGTgdpGTVDTEELHSITG 155


                  ....*..
gi 657584108 1156 YDRSKVF 1162
Cdd:cd01476   156 NEDHIFT 162
Kunitz_SCI-I-like cd22634
chymotrypsin inhibitor SCI-I_III-like; This model includes the Kunitz-type chymotrypsin ...
 2515-2562 8.31e-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: 76.40  E-value: 8.31e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 657584108 2515 SQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22634    10 GGDGISCFAYIPSWSYNPDKNECEEFIYGGCGGNDNRFSTKAECEQKC 57
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 816-951 1.03e-16

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 80.51  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  816 DLLFLIDSSGSI-YPQDYNKMKDFMKSVISKSFIGQNEVHVGVMQFSTIQKLEFPLNRFYS--KGEMSKAIDDMQQI--- 889
Cdd:cd01471     2 DLYLLVDGSGSIgYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNStnKDLALNAIRALLSLyyp 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657584108  890 GGGTHTGEAITDVSQYFDSSRGGRPGLRQRLVVITDGEAQDVVRG--PAAALRAKGVVVYAIGV 951
Cdd:cd01471    82 NGSTNTTSALLVVEKHLFDTRGNRENAPQLVIIMTDGIPDSKFRTlkEARKLRERGVIIAVLGV 145
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2165-2335 1.34e-16

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: 79.26  E-value: 1.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 2165 VDLVMVADSSREIQADQYAGVQQLLGSVVEQLAVSPqprragNQARVAVVQQGGarSAKVEFNLQTYQNQELMRTHLtQK 2244
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGP------DKTRVGLVQYSD--DVRVEFSLNDYKSKDDLLKAV-KN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 2245 MRQQGGS-SALGQTLDYTLKEVLLKAGQPSR-KKALLAVVGTSTAWEDQARLhyVSQKAKCEGVALFVVTVGDHyNRTQV 2322
Cdd:cd01450    72 LKYLGGGgTNTGKALQYALEQLFSESNARENvPKVIIVLTDGRSDDGGDPKE--AAAKLKDEGIKVFVVGVGPA-DEEEL 148

                         170
                  ....*....|...
gi 657584108 2323 EELASLPLQQHLI 2335
Cdd:cd01450   149 REIASCPSERHVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 2166-2329 3.06e-16

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: 78.65  E-value: 3.06e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   2166 DLVMVADSSREIQADQYAGVQQLLGSVVEQLAVSPqprragNQARVAVVQQGGarSAKVEFNLQTYQNQELMRTHLtQKM 2245
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGP------DGDRVGLVTFSD--DARVLFPLNDSRSKDALLEAL-ASL 71

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   2246 RQQ-GGSSALGQTLDYTLKEVLLKA--GQPSRKKALLAVV-GTSTAWEDQARLhyVSQKAKCEGVALFVVTVGDHYNRTQ 2321
Cdd:smart00327   72 SYKlGGGTNLGAALQYALENLFSKSagSRRGAPKVVILITdGESNDGPKDLLK--AAKELKRSGVKVFVVGVGNDVDEEE 149


                    ....*...
gi 657584108   2322 VEELASLP 2329
Cdd:smart00327  150 LKKLASAP 157
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 34-173 3.57e-16

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: 78.97  E-value: 3.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   34 DIVFLIDGSSSIGISN-FQEIRQFLRSVISGLDIGADKVRIGLAQYSDEPYQEFLLKDH--MDKQSLL---AAVDTFQYR 107
Cdd:cd01471     2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPnsTNKDLALnaiRALLSLYYP 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657584108  108 TGGTETGEAIDFLMNQYFtEDAGSRakQRVPQIAVVITDG--DSTDDVAAPALRLRQHGVIMFAIGVG 173
Cdd:cd01471    82 NGSTNTTSALLVVEKHLF-DTRGNR--ENAPQLVIIMTDGipDSKFRTLKEARKLRERGVIIAVLGVG 146
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1957-2127 3.71e-16

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: 78.65  E-value: 3.71e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   1957 LVFGLDMSDDVTPTAFERQRSALLALLEEINIaesnCPSGARVAVVGYSAYTKYLIRFQDYRRKTQLEDAVKNIaLERTS 2036
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDI----GPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASL-SYKLG 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   2037 NKRHLGAAMHFVAQNVFKRVRSGMVM-RKVAVFFSNGPSQE-VNDIPGAVMEYRGLNIVPAVISLTNTPAIRQALAVDDT 2114
Cdd:smart00327   77 GGTNLGAALQYALENLFSKSAGSRRGaPKVVILITDGESNDgPKDLLKAAKELKRSGVKVFVVGVGNDVDEEELKKLASA 156

                           170
                    ....*....|...
gi 657584108   2115 GNSIFTVLRRQQD 2127
Cdd:smart00327  157 PGGVYVFLPELLD 169
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 1194-1362 4.63e-16

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 80.75  E-value: 4.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1194 ADLVFLIDQSGSIASTD-YSIMKKFTTELVNSFkVSEDlvRVGLAQFSSnfqnEFYLNQFYTE--EAVSKHIFNMrQLGG 1270
Cdd:COG1240    93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDY-RPRD--RVGLVAFGG----EAEVLLPLTRdrEALKRALDEL-PPGG 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1271 GTNIGLALDSIREYFEASRGCRRSAgisqnLVLITDGE---SQDDVEDAAERLRALGIEVFAIGIG-NVHDLELLQ---- 1342
Cdd:COG1240   165 GTPLGDALALALELLKRADPARRKV-----IVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGtEAVDEGLLReiae 239

                         170       180
                  ....*....|....*....|
gi 657584108 1343 ITGTpeRLFTVENFGSLEKI 1362
Cdd:COG1240   240 ATGG--RYFRADDLSELAAI 257
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 419-605 5.57e-16

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: 78.32  E-value: 5.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  419 ADIVFIVDESGSIG---VANFQMVRTFLHSIISgleispTRVRVGIVMYndrpADQAQQVYLNTFNNKDE---LLKFIKI 492
Cdd:cd01474     5 FDLYFVLDKSGSVAanwIEIYDFVEQLVDRFNS------PGLRFSFITF----STRATKILPLTDDSSAIikgLEVLKKV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  493 LPyhGGGTNTGAALKFARESVFIKERGSRKdkgVQQVAVVITDGESQDDV----SQPAADLRRAGVTIYSVGVKNANKVQ 568
Cdd:cd01474    75 TP--SGQTYIHEGLENANEQIFNRNGGGRE---TVSVIIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGVTDFLKSQ 149

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 657584108  569 LVEMASHPpnKHVFIVDS-FAKLKSMEQSLQKILCYNI 605
Cdd:cd01474   150 LINIADSK--EYVFPVTSgFQALSGIIESVVKKACIEI 185
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 419-573 9.10e-16

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 79.98  E-value: 9.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  419 ADIVFIVDESGSIGVAN-FQMVRTFLHSIISGLeisPTRVRVGIVMYNDRPadqaqQVYLNTFNNKDELLKFIKILPYhG 497
Cdd:COG1240    93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDY---RPRDRVGLVAFGGEA-----EVLLPLTRDREALKRALDELPP-G 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  498 GGTNTGAALKFAREsvfikeRGSRKDKGVQQVAVVITDGE---SQDDVSQPAADLRRAGVTIYSVGV--KNANKVQLVEM 572
Cdd:COG1240   164 GGTPLGDALALALE------LLKRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVgtEAVDEGLLREI 237


                  .
gi 657584108  573 A 573
Cdd:COG1240   238 A 238
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1003-1159 1.05e-15

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: 77.43  E-value: 1.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1003 DIIFLVDGSTSITLA-KFRNMQRFMESMVNQTTVGKDLTRFGVILYSNDPKSVFTLNQYSS--KKEVVKAISNLRS---P 1076
Cdd:cd01471     2 DLYLLVDGSGSIGYSnWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNStnKDLALNAIRALLSlyyP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1077 FGDTYTGKALAYSLQFFDAQHGGRAalQVPQILMVITDGDATDRNSLVAPSVALRDHGVSVFSIGV-EGANMTQLEIMAG 1155
Cdd:cd01471    82 NGSTNTTSALLVVEKHLFDTRGNRE--NAPQLVIIMTDGIPDSKFRTLKEARKLRERGVIIAVLGVgQGVNHEENRSLVG 159


                  ....
gi 657584108 1156 YDRS 1159
Cdd:cd01471   160 CDPD 163
Kunitz_amblin-like cd22638
Caenorhabditis elegans Kunitz domain 11 of papilin (also called abnormal cell migration ...
 2512-2562 1.22e-15

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: 72.81  E-value: 1.22e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22638     1 CTLKPETGPCRAYIEKWYYDPSTQSCKTFIYGGCGGNGNRFDSEEDCQETC 51
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 2165-2338 1.54e-15

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: 77.01  E-value: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 2165 VDLVMVADSSREIQADQYAGVQQLLGSVVEQLAVSPQprragnQARVAVVQQGgaRSAKVEFNLQTYQNQELMRThLTQK 2244
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPT------KTQFGLVQYS--ESFRTEFTLNEYRTKEEPLS-LVKH 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 2245 MRQQGGSSALGQTLDYTLKEVLLKA--GQPSRKKALlaVVGTSTAWEDQARLHYVSQKAKCEGVALFVVTVGDHYNR-TQ 2321
Cdd:cd01469    72 ISQLLGLTNTATAIQYVVTELFSESngARKDATKVL--VVITDGESHDDPLLKDVIPQAEREGIIRYAIGVGGHFQReNS 149

                         170       180
                  ....*....|....*....|
gi 657584108 2322 VEEL---ASLPLQQHLIHVS 2338
Cdd:cd01469   150 REELktiASKPPEEHFFNVT 169
Kunitz_TFPI1_2-like cd22614
Kunitz protease inhibitor (KPI) domain 2 (KPI-2 or K2) of tissue factor pathway inhibitor ...
 2510-2562 1.95e-15

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: 72.34  E-value: 1.95e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2510 DACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22614     3 DFCFLEEDPGICRGLITRYFYNNQSKQCERFKYGGCLGNQNNFESLEECQNTC 55
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 816-979 2.49e-15

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


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 76.40  E-value: 2.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  816 DLLFLIDSSGSI---YPQDYNKMKDFMKSVISKsfigqnEVHVGVMQFSTIQKLEFPLNRFysKGEMSKAIDDMQQI--G 890
Cdd:cd01474     6 DLYFVLDKSGSVaanWIEIYDFVEQLVDRFNSP------GLRFSFITFSTRATKILPLTDD--SSAIIKGLEVLKKVtpS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  891 GGTHTGEAITDVS-QYFDSSRGGRpglRQRLVVI--TDGE-AQDVVRGP---AAALRAKGVVVYAIGVVDANTTQLLEIS 963
Cdd:cd01474    78 GQTYIHEGLENANeQIFNRNGGGR---ETVSVIIalTDGQlLLNGHKYPeheAKLSRKLGAIVYCVGVTDFLKSQLINIA 154

                         170
                  ....*....|....*..
gi 657584108  964 GSPDRMYAERD-FDALK 979
Cdd:cd01474   155 DSKEYVFPVTSgFQALS 171
Kunitz_amblin-like cd22638
Caenorhabditis elegans Kunitz domain 11 of papilin (also called abnormal cell migration ...
 2439-2490 3.83e-15

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: 71.65  E-value: 3.83e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGIqCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22638     1 CTLKPETGP-CRAYIEKWYYDPSTQSCKTFIYGGCGGNGNRFDSEEDCQETC 51
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 1002-1182 6.36e-15

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


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 75.24  E-value: 6.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1002 ADIIFLVDGSTSItLAKFRNMQRFMESMVNQTTvgKDLTRFGVILYSNDPKSVFTLNQYSskKEVVKAISNLRS--PFGD 1079
Cdd:cd01474     5 FDLYFVLDKSGSV-AANWIEIYDFVEQLVDRFN--SPGLRFSFITFSTRATKILPLTDDS--SAIIKGLEVLKKvtPSGQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1080 TYTGKALAY-SLQFFDAQHGGRaalQVPQILMVITDGDATDRNSLVAPSVA--LRDHGVSVFSIGVEGANMTQLEIMAGy 1156
Cdd:cd01474    80 TYIHEGLENaNEQIFNRNGGGR---ETVSVIIALTDGQLLLNGHKYPEHEAklSRKLGAIVYCVGVTDFLKSQLINIAD- 155

                         170       180
                  ....*....|....*....|....*..
gi 657584108 1157 DRSKVFYVDN-FEALETLYKNITQVLC 1182
Cdd:cd01474   156 SKEYVFPVTSgFQALSGIIESVVKKAC 182
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1957-2101 6.39e-15

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: 74.64  E-value: 6.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1957 LVFGLDMSDDVTPTAFERQRSALLALLEEINIAesncPSGARVAVVGYSAYTKYLIRFQDYRRKTQLEDAVKNIaLERTS 2036
Cdd:cd01450     3 IVFLLDGSESVGPENFEKVKDFIEKLVEKLDIG----PDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNL-KYLGG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657584108 2037 NKRHLGAAMHFVAQNVFKRVRSGMVMRKVAVFFSNGPSQEVNDIPGAVMEYRGLNIVPAVISLTN 2101
Cdd:cd01450    78 GGTNTGKALQYALEQLFSESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVVGVGP 142
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 1195-1343 9.18e-15

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 77.03  E-value: 9.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1195 DLVFLIDQSGSIASTDYSIMKKFTTELVNSFKVSEdlvRVGLAQFSSNFQNEFYLNQFYTEEAVSKHIFnMRQLGGGTNI 1274
Cdd:COG2425   120 PVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNR---RFGVILFDTEVVEDLPLTADDGLEDAIEFLS-GLFAGGGTDI 195

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657584108 1275 GLALDSIREYFEASRGCRRSagisqnLVLITDGESQDDVEDAAERLRA--LGIEVFAIGIGNVHDLELLQI 1343
Cdd:COG2425   196 APALRAALELLEEPDYRNAD------IVLITDGEAGVSPEELLREVRAkeSGVRLFTVAIGDAGNPGLLEA 260
Kunitz_textilinin-like cd22594
venom Kunitz-type proteins such as textilinin, BF9 and PILP; This group includes toxins ...
 2439-2491 1.06e-14

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: 70.42  E-value: 1.06e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2439 CQLDSDSGiQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTCV 2491
Cdd:cd22594     5 CELPADPG-PCNAYKPAFYYNPASHKCLEFIYGGCGGNANNFKTIDECHRTCA 56
Kunitz_bikunin_2-like cd22597
second Kunitz domain of bikunin and similar proteins; This subfamily includes the C-terminal ...
 2510-2562 1.10e-14

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: 70.49  E-value: 1.10e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2510 DACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22597     2 AACRLPIVPGPCKGFVDLWAFDAVQGKCVPFSYGGCQGNGNKFYSEKECEEYC 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1666-1724 1.80e-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: 69.83  E-value: 1.80e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 657584108  1666 GVDGEQGLTGADGGRGERGNPGNPGIPGIRGEAGLKGQRGLRGDPGEPGAdnnsPGAKG 1724
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA----PGAPG 55
Kunitz_boophilin_1-like cd22599
first Kunitz domain of Rhipicephalus microplus boophilin and similar proteins; This group ...
 2512-2562 2.11e-14

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: 69.81  E-value: 2.11e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22599     6 CRLPADEGICRALIPRFYFNTETGQCTEFIYGGCGGNENNFETIEECEKAC 56
Kunitz_boophilin_2-like cd22600
second Kunitz domain of Rhipicephalus microplus boophilin and similar proteins; This group ...
 2511-2563 2.83e-14

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: 68.99  E-value: 2.83e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2511 ACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLCL 2563
Cdd:cd22600     1 GCKPAAESGLCAAYLERWFFNVTTGACETFVYGGCGGNANNYKSQEECELACL 53
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 811-963 3.27e-14

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 75.36  E-value: 3.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  811 KDIPGDLLFLIDSSGSIypQDYNKMkDFMKSVIsKSFIG--QNEVHVGVMQFSTIQKLEFPLNRfySKGEMSKAIDDMQq 888
Cdd:COG1240    89 PQRGRDVVLVVDASGSM--AAENRL-EAAKGAL-LDFLDdyRPRDRVGLVAFGGEAEVLLPLTR--DREALKRALDELP- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  889 IGGGTHTGEAITDVSQYFDSSRggrPGLRQRLVVITDGEAQDVVRGP---AAALRAKGVVVYAIGVVDA--NTTQLLEIS 963
Cdd:COG1240   162 PGGGTPLGDALALALELLKRAD---PARRKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEavDEGLLREIA 238
Kunitz_collagen_alpha1_VII cd22627
Kunitz-type domain from the alpha1 chain of type VII collagen, and similar proteins; This ...
 2438-2490 3.80e-14

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: 68.81  E-value: 3.80e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2438 RCQLDSDSGiQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22627     2 PCLLPMDEG-SCSDYTLLWYYHQKAGECRPFVYGGCGGNANRFSSKEDCELRC 53
Kunitz_eppin cd22611
Kunitz domain of epididymal protease inhibitor eppin and similar proteins; This subfamily ...
 2510-2566 5.54e-14

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: 68.20  E-value: 5.54e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 657584108 2510 DACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLCLTKS 2566
Cdd:cd22611     1 DVCSLPKESGPCMAYFPRWWYDKETNTCSKFIYGGCQGNNNNFQSEAICQNICKKKR 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1657-1713 6.36e-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: 68.29  E-value: 6.36e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 657584108  1657 GEDGEDGLDGVDGEQGLTGADGGRGERGNPGNPGIPGIRGEAGLKGQRGLRGDPGEP 1713
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1627-1683 8.35e-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: 67.90  E-value: 8.35e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 657584108  1627 GSPGPSGPQGVQGCSGRRGVKGFRGLRGNRGEDGEDGLDGVDGEQGLTGADGGRGER 1683
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Kunitz_SmCI_3-like cd22603
third Kunitz domain of Carboxypeptidase Inhibitor SmCI and similar domains; This group ...
 2510-2562 9.62e-14

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: 67.46  E-value: 9.62e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2510 DACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22603     1 EDCLLPSETGPCKGSFPRYYYDKETGKCKEFIYGGCQGNANNFETKEECERAC 53
Kunitz_TFPI2_1-like cd22616
Kunitz domain 1 (KD1) of tissue factor pathway inhibitor 2 (TFPI2) and similar proteins; This ...
 2510-2562 1.01e-13

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: 67.65  E-value: 1.01e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2510 DACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22616     3 EICLLPPDEGPCRALIPRYYYDRYTQTCREFSYGGCEGNANNFESLEDCEKTC 55
Kunitz_WFIKKN_2-like cd22606
second Kunitz domain of WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing proteins; ...
 2511-2562 1.24e-13

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: 67.38  E-value: 1.24e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2511 ACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22606     1 ICSLPAVQGPCKAWEPRWAYNSLLKQCQSFVYGGCEGNENNFESKEACEDAC 52
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 629-805 1.70e-13

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: 71.39  E-value: 1.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  629 ADIFFLIDHSGSIyPTDFQDMKKFIIEFIHTFrISPQhVRLGVAKYADSPNLEFDLTDYSdaKSVEKAVEGIRQI--GGG 706
Cdd:cd01474     5 FDLYFVLDKSGSV-AANWIEIYDFVEQLVDRF-NSPG-LRFSFITFSTRATKILPLTDDS--SAIIKGLEVLKKVtpSGQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  707 TETGRALAFMSPHFdRAMTTRGHKVPEYLVVITDGKSSDKVKVPAEQ----LRAQGVIVYSIGVKSADMEELREISGDPK 782
Cdd:cd01474    80 TYIHEGLENANEQI-FNRNGGGRETVSVIIALTDGQLLLNGHKYPEHeaklSRKLGAIVYCVGVTDFLKSQLINIADSKE 158

                         170       180
                  ....*....|....*....|....
gi 657584108  783 RTFFVNN-FDALKPIKDDIITDIC 805
Cdd:cd01474   159 YVFPVTSgFQALSGIIESVVKKAC 182
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 420-574 2.44e-13

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 72.79  E-value: 2.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  420 DIVFIVDESGSIGVANFQMVRTFLhsiISGLEISPTRVRVGIVMYNDRPadqAQQVYLNTFNNKDELLKFIKILPyHGGG 499
Cdd:COG2425   120 PVVLCVDTSGSMAGSKEAAAKAAA---LALLRALRPNRRFGVILFDTEV---VEDLPLTADDGLEDAIEFLSGLF-AGGG 192

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657584108  500 TNTGAALKFARESvfIKERGSRKDkgvqqVAVVITDGESQDDVSQ--PAADLRRAGVTIYSVGVKNANKVQLVEMAS 574
Cdd:COG2425   193 TDIAPALRAALEL--LEEPDYRNA-----DIVLITDGEAGVSPEEllREVRAKESGVRLFTVAIGDAGNPGLLEALA 262
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 927-1177 2.46e-13

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 72.66  E-value: 2.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  927 EAQDVVRGPAAALRAKGVVVYAIGVVDANTTQLLEISGSPDRMYAERDFDALKDLESQVALELCDPERDCKKTEKADIIF 1006
Cdd:COG1240    18 LLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1007 LVDGSTS-ITLAKFRNMQRFMESMVNQTTVGkdlTRFGVILYSNDPKSV--FTlnqySSKKEVVKAISNLRsPFGDTYTG 1083
Cdd:COG1240    98 VVDASGSmAAENRLEAAKGALLDFLDDYRPR---DRVGLVAFGGEAEVLlpLT----RDREALKRALDELP-PGGGTPLG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1084 KALAYSLQFFDAQHGGRAAlqvpqILMVITDGDATD-RNSLVAPSVALRDHGVSVFSIGV--EGANMTQLEIMAGYDRSK 1160
Cdd:COG1240   170 DALALALELLKRADPARRK-----VIVLLTDGRDNAgRIDPLEAAELAAAAGIRIYTIGVgtEAVDEGLLREIAEATGGR 244

                         250
                  ....*....|....*..
gi 657584108 1161 VFYVDNFEALETLYKNI 1177
Cdd:COG1240   245 YFRADDLSELAAIYREI 261
Kunitz_PPTI-like cd22608
Pseudocerastes persicus trypsin inhibitor (PPTI), Kunitz-type serine protease inhibitor ...
 2512-2562 2.90e-13

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: 66.17  E-value: 2.90e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22608     4 CYLPADPGPCKAYIPRFYYNSASNKCQQFIYGGCKGNANNFETKDECRYTC 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1594-1648 2.97e-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: 2.97e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 657584108  1594 GIRGSRGLPGSKGVSGQKGYPGFPGEEGIAGDRGSPGPSGPQGVQGCSGRRGVKG 1648
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Kunitz_BmTI-like cd22604
Kunitz-type serine protease inhibitor 6 (BmTI-6), A (BmTI-A), and similar proteins; This group ...
 2510-2562 3.51e-13

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: 65.93  E-value: 3.51e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2510 DACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22604     4 KQCSPTADSGPCFAYFPMWWYNVKTGQCEEFIYGGCQGNDNRYETEEECEKTC 56
Kunitz_boophilin_2-like cd22600
second Kunitz domain of Rhipicephalus microplus boophilin and similar proteins; This group ...
 2439-2490 4.19e-13

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: 65.91  E-value: 4.19e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGIqCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22600     2 CKPAAESGL-CAAYLERWFFNVTTGACETFVYGGCGGNANNYKSQEECELAC 52
Kunitz_textilinin-like cd22594
venom Kunitz-type proteins such as textilinin, BF9 and PILP; This group includes toxins ...
 2512-2562 4.29e-13

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: 65.80  E-value: 4.29e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22594     5 CELPADPGPCNAYKPAFYYNPASHKCLEFIYGGCGGNANNFKTIDECHRTC 55
Kunitz_huwentoxin cd22598
Kunitz-type toxin huwentoxin-XI; This model contains Kunitz-type serine protease inhibitor ...
 2510-2562 4.41e-13

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: 65.78  E-value: 4.41e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2510 DACFLSQDQGSCQNYSMMWFFDTeqNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22598     1 DTCRLPSDRGRCKASFERWYFNG--RTCAKFIYGGCGGNDNKFPTQEACMKRC 51
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 630-784 5.01e-13

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: 69.72  E-value: 5.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  630 DIFFLIDHSGSI-YPTDFQDMKKFIIEFIHTFRISPQHVRLGVAKYADSPNLEFDLTDY--SDAKSVEKAVEGIRQI--- 703
Cdd:cd01471     2 DLYLLVDGSGSIgYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPnsTNKDLALNAIRALLSLyyp 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  704 GGGTETGRALAFMSPH-FDRAMtTRGHkVPEYLVVITDGKSSDK---VKVpAEQLRAQGVIVYSIGVKSA-DMEELREIS 778
Cdd:cd01471    82 NGSTNTTSALLVVEKHlFDTRG-NREN-APQLVIIMTDGIPDSKfrtLKE-ARKLRERGVIIAVLGVGQGvNHEENRSLV 158


                  ....*.
gi 657584108  779 GDPKRT 784
Cdd:cd01471   159 GCDPDD 164
Kunitz_TFPI1_1-like cd22613
Kunitz protease inhibitor (KPI) domain 1 (KPI-1 or K1) of tissue factor pathway inhibitor ...
 2512-2563 5.40e-13

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: 65.45  E-value: 5.40e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLCL 2563
Cdd:cd22613     4 CAFKADDGPCKAIMKRFFFNIFTRQCEEFIYGGCEGNENRFETLEECKKTCI 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1600-1661 6.68e-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: 6.68e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657584108  1600 GLPGSKGVSGQKGYPGFPGEEGIAGDRGSPGPSGPQGVqgcsgrRGVKGFRGLRGNRGEDGE 1661
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGP------PGPPGPPGPPGAPGAPGP 56
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 625-796 6.73e-13

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 71.12  E-value: 6.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  625 QTDEADIFFLIDHSGSIYPTD-FQDMKKFIIEFIHTFRispQHVRLGVAKYADSPNLEFDLTdySDAKSVEKAVEGIrQI 703
Cdd:COG1240    89 PQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPLT--RDREALKRALDEL-PP 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  704 GGGTETGRALAFMSPHFDRAMTTRgHKVpeyLVVITDGKSSDKVKVP---AEQLRAQGVIVYSIGV--KSADMEELREIS 778
Cdd:COG1240   163 GGGTPLGDALALALELLKRADPAR-RKV---IVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVgtEAVDEGLLREIA 238

                         170       180
                  ....*....|....*....|..
gi 657584108  779 gdpKRT----FFVNNFDALKPI 796
Cdd:COG1240   239 ---EATggryFRADDLSELAAI 257
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1663-1722 7.23e-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: 7.23e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1663 GLDGVDGEQGLTGADGGRGERGNPGNPGIPGIRGEAGLKGQRGLRGDPGEPGAdnnsPGA 1722
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA----PGP 56
Kunitz_HAI1_2-like cd22624
Kunitz domain 2 of hepatocyte growth factor activator inhibitor-1 (HAI1); This model includes ...
 2519-2562 9.91e-13

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: 64.85  E-value: 9.91e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 657584108 2519 GSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22624     9 GPCRASFTRWYYDPLSRKCHRFTYGGCDGNENNFETEDECMETC 52
VWA_2 pfam13519
von Willebrand factor type A domain;
817-923 1.09e-12

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 66.16  E-value: 1.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   817 LLFLIDSSGSIYPQDYNK-----MKDFMKSVISKsfigQNEVHVGVMQFSTIQKLEFPLNRfySKGEMSKAIDDMQQIGG 891
Cdd:pfam13519    1 LVFVLDTSGSMRNGDYGPtrleaAKDAVLALLKS----LPGDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|..
gi 657584108   892 GTHTGEAITDVSQYFDSSRGGRPglrQRLVVI 923
Cdd:pfam13519   75 GTNLAAALQLARAALKHRRKNQP---RRIVLI 103
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1002-1170 1.14e-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: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1002 ADIIFLVDGSTSITLAKFRNMQRFMESMVNQT------TVGKDLTRFGVILYSNDPKSVFTLNQ-YSSKKEVVKAISNLR 1074
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRdIRNYTSLKEAVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1075 SPFGDTYTGKALAYSLQFFdaQHGGRAAlqVPQILMVITDGDA-TDRNSLVAPSVALRDH-GVSVFSIGVEGANMTQLEI 1152
Cdd:cd01480    83 YIGGGTFTDCALKYATEQL--LEGSHQK--ENKFLLVITDGHSdGSPDGGIEKAVNEADHlGIKIFFVAVGSQNEEPLSR 158

                         170
                  ....*....|....*...
gi 657584108 1153 MAgYDRSKVFYVDNFEAL 1170
Cdd:cd01480   159 IA-CDGKSALYRENFAEL 175
Kunitz_SmCI_1-like cd22601
first Kunitz domain of Carboxypeptidase Inhibitor SmCI and similar domains; This group ...
 2510-2562 1.16e-12

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: 64.45  E-value: 1.16e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2510 DACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22601     2 DVCDLPADRGPCTAYIPRWFYNKTTKKCEKFVYGGCQGNKNRFETKDDCLANC 54
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 1003-1183 1.37e-12

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 68.88  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1003 DIIFLVDGSTSITLAKFRN-MQRFMESMVNQTTVGKDLTRFGVILYSNDPKSVFTLNQYSS--KKEVVKAISNLRSPF-- 1077
Cdd:cd01473     2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERydKNELLKKINDLKNSYrs 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1078 -GDTYTGKALAYSLQFFdAQHGGRaALQVPQILMVITDGDATDRNSLVAPSVAL--RDHGVSVFSIGVEGANMTQLEIMA 1154
Cdd:cd01473    82 gGETYIVEALKYGLKNY-TKHGNR-RKDAPKVTMLFTDGNDTSASKKELQDISLlyKEENVKLLVVGVGAASENKLKLLA 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 657584108 1155 GYDRSKV----FYVDNFEALETLYKNITQVLCN 1183
Cdd:cd01473   160 GCDINNDncpnVIKTEWNNLNGISKFLTDKICD 192
Kunitz_actitoxin-like cd22633
Kunitz-type actitoxins such as Anemonia viridis U-actitoxin-Avd3l, and similar proteins; This ...
 2512-2562 1.83e-12

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: 64.09  E-value: 1.83e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22633     5 CLLPKDVGGCRARFPRYYYNSSTRRCEKFRYGGCGGNANNFHTLEECEKVC 55
Kunitz_bikunin_2-like cd22597
second Kunitz domain of bikunin and similar proteins; This subfamily includes the C-terminal ...
 2437-2490 4.67e-12

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: 62.79  E-value: 4.67e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 657584108 2437 ARCQLDSDSGiQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22597     2 AACRLPIVPG-PCKGFVDLWAFDAVQGKCVPFSYGGCQGNGNKFYSEKECEEYC 54
Kunitz_SCI-I-like cd22634
chymotrypsin inhibitor SCI-I_III-like; This model includes the Kunitz-type chymotrypsin ...
 2439-2490 5.75e-12

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: 62.53  E-value: 5.75e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 657584108 2439 CQL----DSDSGIQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22634     2 CGQphslGGGDGISCFAYIPSWSYNPDKNECEEFIYGGCGGNDNRFSTKAECEQKC 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1727-1795 5.79e-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: 62.51  E-value: 5.79e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657584108  1727 GNAGLPGLPGPDGRPGESGIVGNPGQDGRRGSPGvkgaagepgaagLQGIPGASGPQGTRGVRGQPGPR 1795
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPG------------PPGPPGPPGPPGPPGAPGAPGPP 57
Kunitz_WFIKKN_1-like cd22605
first Kunitz domain of WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing proteins; ...
 2512-2562 6.43e-12

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: 62.38  E-value: 6.43e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22605     2 CLKEPDREDCGEEQVRWYFDAKRGNCFTFTYGGCDGNRNHFETYEECRLAC 52
Kunitz_dendrotoxin cd22595
dendrotoxins I, K, B and similar proteins; This group includes toxins isolated from snake ...
 2439-2491 7.52e-12

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: 62.46  E-value: 7.52e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2439 CQLDSDSGiQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTCV 2491
Cdd:cd22595     4 CKLPVRPG-PCKAFISAFYYNWKAKKCHPFTYSGCGGNANRFKTIEECRRTCV 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1711-1782 7.83e-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: 62.13  E-value: 7.83e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657584108  1711 GEPGAdnnsPGAKGDSGNAGLPGLPGPDGRPGESGIVGNPGQDGRRGSPGvkgaagepgaagLQGIPGASGP 1782
Cdd:pfam01391    1 GPPGP----PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG------------PPGAPGAPGP 56
Kunitz_boophilin_1-like cd22599
first Kunitz domain of Rhipicephalus microplus boophilin and similar proteins; This group ...
 2439-2492 1.00e-11

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: 62.11  E-value: 1.00e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 657584108 2439 CQLDSDSGIqCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTCVA 2492
Cdd:cd22599     6 CRLPADEGI-CRALIPRFYFNTETGQCTEFIYGGCGGNENNFETIEECEKACGA 58
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 2165-2333 1.06e-11

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: 65.33  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 2165 VDLVMVADSSREIQADQYAGVQQLLGSVVEQLAVSPqprragNQARVAVVQQGGarSAKVEFNLQTYQNQELMRTHLtQK 2244
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGP------DGVRVGVVQYSD--DPRTEFYLNTYRSKDDVLEAV-KN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 2245 MRQQGGSSALGQTLDYTLKEVLLKAGQPS---RKKALLAVVGTSTaweDQARLHyvSQKAKCEGVALFVVTVGDHyNRTQ 2321
Cdd:cd01472    72 LRYIGGGTNTGKALKYVRENLFTEASGSRegvPKVLVVITDGKSQ---DDVEEP--AVELKQAGIEVFAVGVKNA-DEEE 145

                         170
                  ....*....|..
gi 657584108 2322 VEELASLPLQQH 2333
Cdd:cd01472   146 LKQIASDPKELY 157
Kunitz_SmCI_3-like cd22603
third Kunitz domain of Carboxypeptidase Inhibitor SmCI and similar domains; This group ...
 2439-2490 1.10e-11

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: 61.68  E-value: 1.10e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGIqCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22603     3 CLLPSETGP-CKGSFPRYYYDKETGKCKEFIYGGCQGNANNFETKEECERAC 53
Kunitz_conkunitzin cd22593
conkunitzin-S1 and -S2, and similar proteins; This model includes Kunitz-type conkunitzin-S1 ...
 2512-2562 1.11e-11

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: 61.47  E-value: 1.11e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22593     1 CSLPLDEGSGNSSLTRWYYDPKKGQCKPFTYKGKGGNENNFLTKEDCEETC 51
Kunitz_huwentoxin cd22598
Kunitz-type toxin huwentoxin-XI; This model contains Kunitz-type serine protease inhibitor ...
 2439-2490 1.44e-11

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: 61.55  E-value: 1.44e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGiQCADFVQVWFFDKHigACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22598     3 CRLPSDRG-RCKASFERWYFNGR--TCAKFIYGGCGGNDNKFPTQEACMKRC 51
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 229-383 1.73e-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: 65.07  E-value: 1.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  229 DIFFLVD-SG-ISQAEFQQVRSVLVRLTNQVNFGASAHRLGLAQYGQDIKVEFLLNAFQSKDEMQGGIKRFRQRRLQTNE 306
Cdd:cd01469     2 DIVFVLDgSGsIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  307 prnlGSALQYASANFFTSEAGSRADqGYRQYLVVLSGKDSDDE----VFRQSrliKSEGVTVVGMSLG------ASMNEI 376
Cdd:cd01469    82 ----ATAIQYVVTELFSESNGARKD-ATKVLVVITDGESHDDPllkdVIPQA---EREGIIRYAIGVGghfqreNSREEL 153


                  ....*..
gi 657584108  377 RVISTAP 383
Cdd:cd01469   154 KTIASKP 160
Kunitz_TFPI1_2-like cd22614
Kunitz protease inhibitor (KPI) domain 2 (KPI-2 or K2) of tissue factor pathway inhibitor ...
 2439-2490 2.29e-11

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: 60.79  E-value: 2.29e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGIqCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22614     5 CFLEEDPGI-CRGLITRYFYNNQSKQCERFKYGGCLGNQNNFESLEECQNTC 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1651-1715 2.36e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 60.97  E-value: 2.36e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657584108  1651 GLRGNRGEDGEDGLDGVDGEQGLTGADGGRGERGNPGNPGIPgirgeaglkGQRGLRGDPGEPGA 1715
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPP---------GPPGPPGAPGAPGP 56
VWA_2 pfam13519
von Willebrand factor type A domain;
633-738 2.69e-11

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 62.31  E-value: 2.69e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   633 FLIDHSGSIYPTD-----FQDMKKFIIEFIHTFRispqHVRLGVAKYADSPNLEFDLTDysDAKSVEKAVEGIRQIGGGT 707
Cdd:pfam13519    3 FVLDTSGSMRNGDygptrLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGGGT 76

                           90       100       110
                   ....*....|....*....|....*....|.
gi 657584108   708 ETGRALAFMSphfdRAMTTRGHKVPEYLVVI 738
Cdd:pfam13519   77 NLAAALQLAR----AALKHRRKNQPRRIVLI 103
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 1194-1371 2.89e-11

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: 64.84  E-value: 2.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1194 ADLVFLIDQSGSIASTDYSIMKkFTTELVNSFKVSEdlVRVGLAQFSSNFQNEFYLNQFytEEAVSKHIFNMRQL--GGG 1271
Cdd:cd01474     5 FDLYFVLDKSGSVAANWIEIYD-FVEQLVDRFNSPG--LRFSFITFSTRATKILPLTDD--SSAIIKGLEVLKKVtpSGQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1272 TNIGLALDSIRE-YFEASRGCRRSAGIsqnLVLITDGESQDDV----EDAAERLRALGIEVFAIGIGNVHDLELLQITGT 1346
Cdd:cd01474    80 TYIHEGLENANEqIFNRNGGGRETVSV---IIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADS 156

                         170       180
                  ....*....|....*....|....*.
gi 657584108 1347 PERLFTV-ENFGSLEKIKQKVINTIC 1371
Cdd:cd01474   157 KEYVFPVtSGFQALSGIIESVVKKAC 182
Kunitz_ABPP-like cd22607
Kunitz domain found in the amyloid-beta precursor protein (ABPP) subfamily; This subfamily ...
 2512-2562 2.97e-11

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: 60.52  E-value: 2.97e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2512 CFLSQDQGSCQnySMM--WFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22607     2 CSEQAETGPCR--AMMprWYFDVTEGKCAPFIYGGCGGNRNNFESEEYCMAVC 52
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 228-385 5.05e-11

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: 65.10  E-value: 5.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  228 ADIFFLVDSGIS--QAEFQQVRSVLVRLTNQVNFGASAHRLGLAQYGQDIKVEFLLNAFQSKDEMQGGIKRFRQRRLQTN 305
Cdd:cd01475     3 TDLVFLIDSSRSvrPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  306 EprnlGSALQYASANFFTSEAGSR--ADQGYRQYLVVLSGKDSDD--EVFRQSRlikSEGVTVVGMSLG-ASMNEIRVIS 380
Cdd:cd01475    83 T----GLAIQYAMNNAFSEAEGARpgSERVPRVGIVVTDGRPQDDvsEVAAKAR---ALGIEMFAVGVGrADEEELREIA 155


                  ....*
gi 657584108  381 TAPYA 385
Cdd:cd01475   156 SEPLA 160
Kunitz_ELP-like cd22632
early lactation protein (ELP), colostrum trypsin inhibitor (CTI), and similar proteins; This ...
 2512-2562 5.91e-11

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: 59.75  E-value: 5.91e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22632     4 CQLPPARGPCRSNILRYFYNSTSRECEPFIYGGCNGNANNFETVEMCLRTC 54
Kunitz_SmCI_1-like cd22601
first Kunitz domain of Carboxypeptidase Inhibitor SmCI and similar domains; This group ...
 2439-2490 6.08e-11

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: 59.82  E-value: 6.08e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGiQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22601     4 CDLPADRG-PCTAYIPRWFYNKTTKKCEKFVYGGCQGNKNRFETKDDCLANC 54
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 420-569 6.37e-11

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: 63.88  E-value: 6.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  420 DIVFIVDESGSIGVANFQM-VRTFLHSIISGLEISPTRVRVGIVMYNDRPADqaqqvyLNTFN-----NKDELLKFIKIL 493
Cdd:cd01473     2 DLTLILDESASIGYSNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRD------VVPFSdeeryDKNELLKKINDL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  494 PYH---GGGTNTGAALKFARESvFIKERGSRKDkgVQQVAVVITDG----ESQDDVSQPAADLRRAGVTIYSVGVKNANK 566
Cdd:cd01473    76 KNSyrsGGETYIVEALKYGLKN-YTKHGNRRKD--APKVTMLFTDGndtsASKKELQDISLLYKEENVKLLVVGVGAASE 152


                  ...
gi 657584108  567 VQL 569
Cdd:cd01473   153 NKL 155
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1195-1333 6.64e-11

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: 63.56  E-value: 6.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1195 DLVFLIDQSGSIA-STDYSIMKKFTTELVNSFKVSEDLVRVGLAQFSSNFQNEFYLNQFY-----TEEAVSKHIFNMRQL 1268
Cdd:cd01471     2 DLYLLVDGSGSIGySNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNstnkdLALNAIRALLSLYYP 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657584108 1269 GGGTNIGLALDSIREYFEASRGCRRSAgiSQNLVLITDGESQDDVE--DAAERLRALGIEVFAIGIG 1333
Cdd:cd01471    82 NGSTNTTSALLVVEKHLFDTRGNRENA--PQLVIIMTDGIPDSKFRtlKEARKLRERGVIIAVLGVG 146
VWA_2 pfam13519
von Willebrand factor type A domain;
35-144 9.24e-11

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 60.77  E-value: 9.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108    35 IVFLIDGSSSI-----GISNFQEIRQFLRSVISGLDIgadkVRIGLAQYSDEPYQEFLLKDhmDKQSLLAAVDTFQYRTG 109
Cdd:pfam13519    1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSLPG----DRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 657584108   110 GTETGEAIDFLMNQYFTEDAGsrakqrVPQIAVVI 144
Cdd:pfam13519   75 GTNLAAALQLARAALKHRRKN------QPRRIVLI 103
Kunitz_ixolaris_2 cd22626
Kunitz-type domain 2 (K2) of Ixolaris, and similar proteins; This model includes the second ...
 2512-2562 1.01e-10

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: 59.01  E-value: 1.01e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22626     1 CSLELDYGVGKAYIPRWYFNTSNARCEMFIFGGIGGNKNNFETLEECKKTC 51
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1957-2119 1.04e-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: 62.58  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1957 LVFGLDMSDDVTPTAFERQRSALLALLEEIniaeSNCPSGARVAVVGYSAYTKYLIRFQDYRRKTQLEDAVKNIALERTS 2036
Cdd:cd00198     3 IVFLLDVSGSMGGEKLDKAKEALKALVSSL----SASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 2037 NkRHLGAAMHFVAQNVFKRVRSGmvMRKVAVFFSNG-PSQEVNDIPGAVMEYRGLNIVPAVISLTNTPAIRQ--ALAVDD 2113
Cdd:cd00198    79 G-TNIGAALRLALELLKSAKRPN--ARRVIILLTDGePNDGPELLAEAARELRKLGITVYTIGIGDDANEDElkEIADKT 155


                  ....*.
gi 657584108 2114 TGNSIF 2119
Cdd:cd00198   156 TGGAVF 161
Kunitz_BmTI-like cd22604
Kunitz-type serine protease inhibitor 6 (BmTI-6), A (BmTI-A), and similar proteins; This group ...
 2439-2490 1.10e-10

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: 59.00  E-value: 1.10e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGIqCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22604     6 CSPTADSGP-CFAYFPMWWYNVKTGQCEEFIYGGCQGNDNRYETEEECEKTC 56
Kunitz_SHPI cd22618
Stichodactyla helianthus Kunitz inhibitor protein ShPI-1, Heteractis crispa protease inhibitor ...
 2519-2562 1.11e-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: 59.09  E-value: 1.11e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 657584108 2519 GSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22618     9 GPCKAYFPRFYFDSETGKCTPFIYGGCGGNGNNFETLHACRAIC 52
Kunitz_SmCI_2-like cd22602
second Kunitz domain of Carboxypeptidase Inhibitor SmCI and similar domains; This group ...
 2439-2490 1.16e-10

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: 58.71  E-value: 1.16e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGiQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22602     1 CSLPSKVG-PCRVSARRWFHNPETEKCEVFIYGGCHGNANRFATETECQEVC 51
Kunitz_HAI2_2-like cd22622
Kunitz-type domain 2 (KD2) of hepatocyte growth factor activator inhibitor type 2 (HAI-2), and ...
 2510-2562 1.17e-10

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: 58.91  E-value: 1.17e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2510 DACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22622     1 EYCAAPRVTGPCRAAFPRWYYDPESQSCKEFIYGGCRGNKNNYLSEEECMDRC 53
Kunitz_ELP-like cd22632
early lactation protein (ELP), colostrum trypsin inhibitor (CTI), and similar proteins; This ...
 2439-2490 1.32e-10

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: 58.60  E-value: 1.32e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGiQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22632     4 CQLPPARG-PCRSNILRYFYNSTSRECEPFIYGGCNGNANNFETVEMCLRTC 54
Kunitz_SmCI_2-like cd22602
second Kunitz domain of Carboxypeptidase Inhibitor SmCI and similar domains; This group ...
 2512-2562 1.41e-10

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: 58.71  E-value: 1.41e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22602     1 CSLPSKVGPCRVSARRWFHNPETEKCEVFIYGGCHGNANRFATETECQEVC 51
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1775-1867 1.59e-10

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: 58.66  E-value: 1.59e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1775 GIPGASGPQGTRGVRGQPGPRgipglpgpqggpgsvggpgaagrrggngqkGQPGDPGDKGVPGPLGPRGMPgedgrdgy 1854
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPP------------------------------GPPGPPGPPGEPGPPGPPGPP-------- 42

                           90
                   ....*....|...
gi 657584108  1855 GPAGRKGVKGDPG 1867
Cdd:pfam01391   43 GPPGPPGAPGAPG 55
Kunitz_TFPI2_1-like cd22616
Kunitz domain 1 (KD1) of tissue factor pathway inhibitor 2 (TFPI2) and similar proteins; This ...
 2439-2490 1.63e-10

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: 58.40  E-value: 1.63e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGIqCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22616     5 CLLPPDEGP-CRALIPRYYYDRYTQTCREFSYGGCEGNANNFESLEDCEKTC 55
Kunitz_dendrotoxin cd22595
dendrotoxins I, K, B and similar proteins; This group includes toxins isolated from snake ...
 2511-2563 1.87e-10

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: 58.22  E-value: 1.87e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2511 ACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLCL 2563
Cdd:cd22595     3 FCKLPVRPGPCKAFISAFYYNWKAKKCHPFTYSGCGGNANRFKTIEECRRTCV 55
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2165-2335 2.00e-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: 2.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 2165 VDLVMVADSSREIQADQYAGVQQLLGSVVEQLAVSPQprragnQARVAVVQQGGarSAKVEFNLQTYQNQELMRTHLTQK 2244
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPP------GDRVGLVTFGS--NARVVLPLTTDTDKADLLEAIDAL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 2245 MRQQGGSSALGQTLDYTLkEVLLKAGQPSRKKALLAVV-GTSTawEDQARLHYVSQKAKCEGVALFVVTVGDHYNRTQVE 2323
Cdd:cd00198    73 KKGLGGGTNIGAALRLAL-ELLKSAKRPNARRVIILLTdGEPN--DGPELLAEAARELRKLGITVYTIGIGDDANEDELK 149

                         170
                  ....*....|..
gi 657584108 2324 ELASLPLQQHLI 2335
Cdd:cd00198   150 EIADKTTGGAVF 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 2166-2337 2.93e-10

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: 61.15  E-value: 2.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 2166 DLVMVADSSREIQADQYAGVQQLLGSVVEQLAVSPqprragNQARVAVVQQGGarSAKVEFNLQTYQNQELMRTHLtQKM 2245
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGP------DGVQVGLVQYSD--DPRTEFDLNAYTSKEDVLAAI-KNL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 2246 RQQGGSSALGQTLDYTLKEVLLKAgQPSRKKA-LLAVVGTSTAWEDQARLhyVSQKAKCEGVALFVVTVGDHyNRTQVEE 2324
Cdd:cd01482    73 PYKGGNTRTGKALTHVREKNFTPD-AGARPGVpKVVILITDGKSQDDVEL--PARVLRNLGVNVFAVGVKDA-DESELKM 148

                         170
                  ....*....|...
gi 657584108 2325 LASLPLQQHLIHV 2337
Cdd:cd01482   149 IASKPSETHVFNV 161
Kunitz_TFPI1_1-like cd22613
Kunitz protease inhibitor (KPI) domain 1 (KPI-1 or K1) of tissue factor pathway inhibitor ...
 2439-2491 3.59e-10

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: 57.36  E-value: 3.59e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2439 CQLDSDSGiQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTCV 2491
Cdd:cd22613     4 CAFKADDG-PCKAIMKRFFFNIFTRQCEEFIYGGCEGNENRFETLEECKKTCI 55
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
1197-1370 3.88e-10

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 61.86  E-value: 3.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1197 VFLIDQSGSIASTDYSIMKKFTTELVNSFKVSEDL---VRVGLAQFSSNFQ--------NEFYLNQFYTeeavskhifnm 1265
Cdd:COG4245     9 YLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYAletVEVSVITFDGEAKvllpltdlEDFQPPDLSA----------- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1266 rqlGGGTNIGLALDSIREYFEASRGCRRSAGISQN---LVLITDGESQD-DVEDAAERLRAL----GIEVFAIGIGNVHD 1337
Cdd:COG4245    78 ---SGGTPLGAALELLLDLIERRVQKYTAEGKGDWrpvVFLITDGEPTDsDWEAALQRLKDGeaakKANIFAIGVGPDAD 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 657584108 1338 LELLQITGTPERLFTVENFGSLEKIKQKVINTI 1370
Cdd:COG4245   155 TEVLKQLTDPVRALDALDGLDFREFFKWLSASV 187
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 1003-1150 6.67e-10

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 62.39  E-value: 6.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1003 DIIFLVDGSTS-----ITLAKFrNMQRFMESMVnqttvGKDltRFGVILYSNDPKSVFTLNQYSSKKEVVKAISNLRsPF 1077
Cdd:COG2425   120 PVVLCVDTSGSmagskEAAAKA-AALALLRALR-----PNR--RFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLF-AG 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657584108 1078 GDTYTGKALAYSLQFFDAQHGGRAalqvpqILMVITDGDATDRNSLVAPSVALRDHGVSVFSIGVEGANMTQL 1150
Cdd:COG2425   191 GGTDIAPALRAALELLEEPDYRNA------DIVLITDGEAGVSPEELLREVRAKESGVRLFTVAIGDAGNPGL 257
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 33-208 6.68e-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: 62.26  E-value: 6.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   33 ADIVFLIDGSSSIGISN-FQEIRQFLRSVISGLDigaDKVRIGLAQYSDEPYQEFLLKDhmDKQSLLAAVDTFQYRtGGT 111
Cdd:COG1240    93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPLTR--DREALKRALDELPPG-GGT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  112 ETGEAIdflmnqyftEDAGSRAKQRVPQ---IAVVITDGDSTDDVAAP---ALRLRQHGVIMFAIGVGKA--NPTELEAI 183
Cdd:COG1240   167 PLGDAL---------ALALELLKRADPArrkVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIGVGTEavDEGLLREI 237

                         170       180
                  ....*....|....*....|....*
gi 657584108  184 ANRPPKRFmFTIDNYEALQRLTEGL 208
Cdd:COG1240   238 AEATGGRY-FRADDLSELAAIYREI 261
Kunitz_actitoxin-like cd22633
Kunitz-type actitoxins such as Anemonia viridis U-actitoxin-Avd3l, and similar proteins; This ...
 2439-2490 7.13e-10

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: 56.77  E-value: 7.13e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGIQCADFVQvWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22633     5 CLLPKDVGGCRARFPR-YYYNSSTRRCEKFRYGGCGGNANNFHTLEECEKVC 55
Kunitz_bikunin_1-like cd22596
first Kunitz domain of bikunin and similar proteins; This subfamily includes the N-terminal ...
 2439-2490 7.23e-10

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: 56.49  E-value: 7.23e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGIqCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22596     3 CKLPPDAGP-CFGMIQRYFYNSSSMACQTFNYGGCLGNQNNFVTEKECLQTC 53
Kunitz_TFPI2_2-like cd22617
Kunitz domain 2 (KD2) of tissue factor pathway inhibitor 2 (TFPI2) and similar proteins; This ...
 2510-2562 7.27e-10

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: 56.62  E-value: 7.27e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2510 DACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22617     2 KVCREVPDEGPCRALITRYFYNMTSMRCEEFTYGGCYGNGNNFRDKSSCISAC 54
VWA_2 pfam13519
von Willebrand factor type A domain;
1196-1304 7.79e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 58.07  E-value: 7.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1196 LVFLIDQSGSIASTDY-----SIMKKFTTELVNSFKvsEDlvRVGLAQFSSNFQNEFYLNQFYteEAVSKHIFNMRQLGG 1270
Cdd:pfam13519    1 LVFVLDTSGSMRNGDYgptrlEAAKDAVLALLKSLP--GD--RVGLVTFGDGPEVLIPLTKDR--AKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|....
gi 657584108  1271 GTNIGLALDSIREYFEasrgcRRSAGISQNLVLI 1304
Cdd:pfam13519   75 GTNLAAALQLARAALK-----HRRKNQPRRIVLI 103
VWA_2 pfam13519
von Willebrand factor type A domain;
421-533 8.67e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 58.07  E-value: 8.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   421 IVFIVDESGSI-----GVANFQMVRTFLHSIISGLEisptRVRVGIVMYNDRPadqaqQVYLNTFNNKDELLKFIKILPY 495
Cdd:pfam13519    1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSLP----GDRVGLVTFGDGP-----EVLIPLTKDRAKILRALRRLEP 71

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 657584108   496 HGGGTNTGAALKFARESVFikergsRKDKGVQQVAVVI 533
Cdd:pfam13519   72 KGGGTNLAAALQLARAALK------HRRKNQPRRIVLI 103
Kunitz_HAI2_1-like cd22621
Kunitz-type domain 1 (KD1) of hepatocyte growth factor activator inhibitor type 2 (HAI-2), and ...
 2438-2490 1.61e-09

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: 55.56  E-value: 1.61e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2438 RCQLDSDSGiQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22621     2 FCHLPKVVG-RCRASFPRWWYNATSQSCQEFIFGGCKGNLNNFLSEQECLQKC 53
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
819-982 1.62e-09

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 59.94  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  819 FLIDSSGSIYPQDYNKMKDFMKSVIS---KSFIGQNEVHVGVMQFSTIQKLEFPL---NRFYskgemskaIDDMQqIGGG 892
Cdd:COG4245    10 LLLDTSGSMSGEPIEALNEGLQALIDelrQDPYALETVEVSVITFDGEAKVLLPLtdlEDFQ--------PPDLS-ASGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  893 THTGEAIT--------DVSQYfdsSRGGRPGLRQRLVVITDGEAQDV-VRGPAAALR----AKGVVVYAIGV-VDANTTQ 958
Cdd:COG4245    81 TPLGAALEllldlierRVQKY---TAEGKGDWRPVVFLITDGEPTDSdWEAALQRLKdgeaAKKANIFAIGVgPDADTEV 157

                         170       180
                  ....*....|....*....|....
gi 657584108  959 LLEISGspdrmyAERDFDALKDLE 982
Cdd:COG4245   158 LKQLTD------PVRALDALDGLD 175
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 1957-2101 1.73e-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: 59.16  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1957 LVFGLDMSDDVTPTAFERQRSALLALLEEINIAesncPSGARVAVVGYSAYTKYLIRFQDYRRKTQLEDAVKNIALeRTS 2036
Cdd:cd01472     3 IVFLVDGSESIGLSNFNLVKDFVKRVVERLDIG----PDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRY-IGG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657584108 2037 NKRhLGAAMHFVAQNVFK---RVRSGmvMRKVAVFFSNGPSQEvnDIPGAVMEYRGLNIVPAVISLTN 2101
Cdd:cd01472    78 GTN-TGKALKYVRENLFTeasGSREG--VPKVLVVITDGKSQD--DVEEPAVELKQAGIEVFAVGVKN 140
Kunitz_KTT cd22620
scorpion venom Kunitz-type toxin (KTT) such as LmKTT-1a, BmKTT-1, and BmKTT-2; This model ...
 2512-2566 1.89e-09

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: 55.65  E-value: 1.89e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLCLTKS 2566
Cdd:cd22620     3 CQLPSDTGRGKASFTRYYYNEESGKCETFIYGGVGGNSNNFLTKEDCCKECAQGS 57
Kunitz_PPTI-like cd22608
Pseudocerastes persicus trypsin inhibitor (PPTI), Kunitz-type serine protease inhibitor ...
 2439-2490 2.26e-09

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: 55.00  E-value: 2.26e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGIqCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22608     4 CYLPADPGP-CKAYIPRFYYNSASNKCQQFIYGGCKGNANNFETKDECRYTC 54
Kunitz_HAI1_2-like cd22624
Kunitz domain 2 of hepatocyte growth factor activator inhibitor-1 (HAI1); This model includes ...
 2456-2490 2.54e-09

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: 55.22  E-value: 2.54e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 657584108 2456 WFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22624    18 WYYDPLSRKCHRFTYGGCDGNENNFETEDECMETC 52
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 1194-1342 2.98e-09

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 60.89  E-value: 2.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1194 ADLVFLIDQSGSIASTDYSIMKKFTTELVNSFKvSEDlvRVGLAQFSSNFQnEFYLNQFYTE-EAVSKHIfNMRQLGGGT 1272
Cdd:COG2304    92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLR-PGD--RVSIVTFAGDAR-VLLPPTPATDrAKILAAI-DRLQAGGGT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1273 NIG----LALDSIREYFEASRGCRrsagisqnLVLITDGE------SQDDVEDAAERLRALGIEVFAIGIGNVHDLELLQ 1342
Cdd:COG2304   167 ALGagleLAYELARKHFIPGRVNR--------VILLTDGDanvgitDPEELLKLAEEAREEGITLTTLGVGSDYNEDLLE 238
Kunitz_WFIKKN_1-like cd22605
first Kunitz domain of WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing proteins; ...
 2439-2490 2.99e-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: 54.67  E-value: 2.99e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGiQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22605     2 CLKEPDRE-DCGEEQVRWYFDAKRGNCFTFTYGGCDGNRNHFETYEECRLAC 52
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 814-962 4.61e-09

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 59.69  E-value: 4.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  814 PGDLLFLIDSSGSiypqdynkMKDFmKSVISKSFI------GQNEVHVGVMQFSTIQKLEFPLNrfySKGEMSKAIDDMQ 887
Cdd:COG2425   118 EGPVVLCVDTSGS--------MAGS-KEAAAKAAAlallraLRPNRRFGVILFDTEVVEDLPLT---ADDGLEDAIEFLS 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  888 QI--GGGTHTGEAITDVSQYFDSSRGGRpglrQRLVVITDGEAQ----DVVRgpAAALRAKGVVVYAIGVVDANTTQLLE 961
Cdd:COG2425   186 GLfaGGGTDIAPALRAALELLEEPDYRN----ADIVLITDGEAGvspeELLR--EVRAKESGVRLFTVAIGDAGNPGLLE 259


                  .
gi 657584108  962 I 962
Cdd:COG2425   260 A 260
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 228-375 5.20e-09

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: 57.58  E-value: 5.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  228 ADIFFLVD-SG-ISQAEFQQVRSVLVRLTNQVNFGASAHRLGLAQYGQDIKVEFLLNAFQSKDEMQGGIKRFRQrrlQTN 305
Cdd:cd00198     1 ADIVFLLDvSGsMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK---GLG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657584108  306 EPRNLGSALQYASANFFtseagSRADQGYRQYLVVLS-GKDSDD--EVFRQSRLIKSEGVTVVGMSLGASMNE 375
Cdd:cd00198    78 GGTNIGAALRLALELLK-----SAKRPNARRVIILLTdGEPNDGpeLLAEAARELRKLGITVYTIGIGDDANE 145
Kunitz_TFPI1_TFPI2_3-like cd22615
Kunitz protease inhibitor (KPI) domain 3 (KPI-3 or K3) of tissue factor pathway inhibitor ...
 2512-2562 5.23e-09

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: 54.22  E-value: 5.23e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22615     4 CLSPKDEGLCSASVTRYYYNSATKTCEPFNYTGCGGNNNNFTSKKDCLRVC 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1790-1873 5.28e-09

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: 54.04  E-value: 5.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1790 GQPGPRGIpglpgpqggpgsvggpgaagrrggngqKGQPGDPGDKGVPGPLGPRGMPGEDGRDgyGPAGRKGVKGDPGFP 1869
Cdd:pfam01391    1 GPPGPPGP---------------------------PGPPGPPGPPGPPGPPGPPGPPGEPGPP--GPPGPPGPPGPPGAP 51


                   ....
gi 657584108  1870 GYPG 1873
Cdd:pfam01391   52 GAPG 55
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1955-2092 5.44e-09

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: 57.68  E-value: 5.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1955 TELVFGLDMSDDVTPTAFERQRSALLALLEEINIAesncPSGARVAVVGYSAYTKYLIRFQDYRRKTQLEDAVKNIALeR 2034
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIG----PDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPY-K 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2035 TSNKRhLGAAMHFVAQNVFK---RVRSGMvmRKVAVFFSNGPSQEVNDIPGAVMEYRGLNI 2092
Cdd:cd01482    76 GGNTR-TGKALTHVREKNFTpdaGARPGV--PKVVILITDGKSQDDVELPARVLRNLGVNV 133
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
34-185 5.45e-09

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 58.40  E-value: 5.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   34 DIVFLIDGSSSIGISNFQEIRQFLRSVISGL---DIGADKVRIGLAQYSDEPYQefllkdHMDkqslLAAVDTFQ----Y 106
Cdd:COG4245     7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELrqdPYALETVEVSVITFDGEAKV------LLP----LTDLEDFQppdlS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  107 RTGGTETGEAIDFLMNQYFTEDAGSRAKQRV--PQIAVVITDGDSTDDVAAPALR-----LRQHGVIMFAIGVG-KANPT 178
Cdd:COG4245    77 ASGGTPLGAALELLLDLIERRVQKYTAEGKGdwRPVVFLITDGEPTDSDWEAALQrlkdgEAAKKANIFAIGVGpDADTE 156


                  ....*..
gi 657584108  179 ELEAIAN 185
Cdd:COG4245   157 VLKQLTD 163
Kunitz_eppin cd22611
Kunitz domain of epididymal protease inhibitor eppin and similar proteins; This subfamily ...
 2439-2490 5.60e-09

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: 54.33  E-value: 5.60e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGiQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22611     3 CSLPKESG-PCMAYFPRWWYDKETNTCSKFIYGGCQGNNNNFQSEAICQNIC 53
Kunitz_ixolaris_2 cd22626
Kunitz-type domain 2 (K2) of Ixolaris, and similar proteins; This model includes the second ...
 2439-2490 5.61e-09

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: 54.00  E-value: 5.61e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGIQCADFVQvWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22626     1 CSLELDYGVGKAYIPR-WYFNTSNARCEMFIFGGIGGNKNNFETLEECKKTC 51
Kunitz_bikunin_1-like cd22596
first Kunitz domain of bikunin and similar proteins; This subfamily includes the N-terminal ...
 2510-2562 6.79e-09

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: 53.80  E-value: 6.79e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2510 DACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22596     1 DSCKLPPDAGPCFGMIQRYFYNSSSMACQTFNYGGCLGNQNNFVTEKECLQTC 53
Kunitz_SHPI cd22618
Stichodactyla helianthus Kunitz inhibitor protein ShPI-1, Heteractis crispa protease inhibitor ...
 2449-2490 6.87e-09

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: 53.70  E-value: 6.87e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 657584108 2449 CADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22618    11 CKAYFPRFYFDSETGKCTPFIYGGCGGNGNNFETLHACRAIC 52
Kunitz_BPTI cd22592
bovine pancreatic trypsin inhibitor; This model contains bovine pancreatic trypsin inhibitor ...
 2519-2562 8.29e-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: 53.41  E-value: 8.29e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 657584108 2519 GSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22592     9 GPCKARIIRYFYNAKSGLCETFVYGGCRAKRNNFLSAEDCMRTC 52
Kunitz_TFPI1_TFPI2_3-like cd22615
Kunitz protease inhibitor (KPI) domain 3 (KPI-3 or K3) of tissue factor pathway inhibitor ...
 2439-2490 8.87e-09

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: 53.45  E-value: 8.87e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGIqCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22615     4 CLSPKDEGL-CSASVTRYYYNSATKTCEPFNYTGCGGNNNNFTSKKDCLRVC 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1858-1924 1.04e-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: 53.27  E-value: 1.04e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657584108  1858 GRKGVKGDPGFPGYPGLLGEDGLQGPKGLPgrkgnrgrggnsgrsgesGISGDPGYAGHRGPRGLPG 1924
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPP------------------GEPGPPGPPGPPGPPGPPG 49
Kunitz_KTT cd22620
scorpion venom Kunitz-type toxin (KTT) such as LmKTT-1a, BmKTT-1, and BmKTT-2; This model ...
 2439-2494 1.16e-08

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: 53.34  E-value: 1.16e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 657584108 2439 CQLDSDSGIQCADFVQvWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTCVAHS 2494
Cdd:cd22620     3 CQLPSDTGRGKASFTR-YYYNEESGKCETFIYGGVGGNSNNFLTKEDCCKECAQGS 57
PHA03169 PHA03169
hypothetical protein; Provisional
 1577-1793 1.18e-08

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 59.98  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1577 VSDRECCNVMCKCSGHEGIR-GSRGLPGSKGVSGQKGYPGFPGEEGIAGDRGSPGPSGPQGVQGCSGRRGVKGFRGLRGN 1655
Cdd:PHA03169   13 HTLRSSCRGHCKRHGGTREQaGRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1656 RGE--DGEDGLDGVDGEQGLTGADGGRGERGNPGNPGIPGIRGEAGLKGQRGLRGDPGEPGADNNSPGAKGDSGNAGL-- 1731
Cdd:PHA03169   93 SGSgsESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPShe 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657584108 1732 ----PGlPGPDGRPGESGIVGNPGQDGRRGSPGVKGAAGepgaaglQGIPGASGPQGTRGVRGQPG 1793
Cdd:PHA03169  173 dspeEP-EPPTSEPEPDSPGPPQSETPTSSPPPQSPPDE-------PGEPQSPTPQQAPSPNTQQA 230
Kunitz_BPTI cd22592
bovine pancreatic trypsin inhibitor; This model contains bovine pancreatic trypsin inhibitor ...
 2456-2490 1.30e-08

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: 53.03  E-value: 1.30e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 657584108 2456 WFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22592    18 YFYNAKSGLCETFVYGGCRAKRNNFLSAEDCMRTC 52
Kunitz_HAI2_2-like cd22622
Kunitz-type domain 2 (KD2) of hepatocyte growth factor activator inhibitor type 2 (HAI-2), and ...
 2456-2490 1.53e-08

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: 52.74  E-value: 1.53e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 657584108 2456 WFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22622    19 WYYDPESQSCKEFIYGGCRGNKNNYLSEEECMDRC 53
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 34-184 1.65e-08

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 56.94  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   34 DIVFLIDGSSSIGISNFQ-EIRQFLRSVISGLDIGADKVRIGLAQYSDE--PYQEFLLKDHMDKQSLLAAVDTFQ--YRT 108
Cdd:cd01473     2 DLTLILDESASIGYSNWRkDVIPFTEKIINNLNISKDKVHVGILLFAEKnrDVVPFSDEERYDKNELLKKINDLKnsYRS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  109 GG-TETGEAIDFLMNQYFtedAGSRAKQRVPQIAVVITDG--DSTDDVAAP--ALRLRQHGVIMFAIGVGKANPTELEAI 183
Cdd:cd01473    82 GGeTYIVEALKYGLKNYT---KHGNRRKDAPKVTMLFTDGndTSASKKELQdiSLLYKEENVKLLVVGVGAASENKLKLL 158


                  .
gi 657584108  184 A 184
Cdd:cd01473   159 A 159
Kunitz_TKDP-like cd22609
trophoblast Kunitz domain protein (TKDP) and similar proteins; This model contains the ...
 2512-2562 2.31e-08

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: 52.45  E-value: 2.31e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2512 CFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22609     2 CLEPKVVGVCKASMTRYFYNAQTGHCEQFVYGGCGGNRNNFLTLEDCMKTC 52
Kunitz_ABPP-like cd22607
Kunitz domain found in the amyloid-beta precursor protein (ABPP) subfamily; This subfamily ...
 2439-2490 2.32e-08

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: 52.43  E-value: 2.32e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGiQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22607     2 CSEQAETG-PCRAMMPRWYFDVTEGKCAPFIYGGCGGNRNNFESEEYCMAVC 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1754-1848 2.41e-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: 52.50  E-value: 2.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1754 GRRGSPGvkgaagepgaagLQGIPGASGPQGTRGVRGQPGPRGIPglpgpqggpgsvggpgaagrrggngqkGQPGDPGD 1833
Cdd:pfam01391    1 GPPGPPG------------PPGPPGPPGPPGPPGPPGPPGPPGEP---------------------------GPPGPPGP 41

                           90
                   ....*....|....*
gi 657584108  1834 KGVPGPLGPRGMPGE 1848
Cdd:pfam01391   42 PGPPGPPGAPGAPGP 56
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 28-186 3.07e-08

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 57.38  E-value: 3.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   28 AKANMADIVFLIDGSSSIGISNFQEIRQFLrsvISGLDIGADKVRIGLAQYSDEPYQEFLLKDHMDKQSLLAAVDTFQyR 107
Cdd:COG2425   114 VPLLEGPVVLCVDTSGSMAGSKEAAAKAAA---LALLRALRPNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLF-A 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  108 TGGTETGEAIDfLMNQYFTEDAGSRAkqrvpqIAVVITDGDSTDDVAA--PALRLRQHGVIMFAIGVGKANPTELEAIAN 185
Cdd:COG2425   190 GGGTDIAPALR-AALELLEEPDYRNA------DIVLITDGEAGVSPEEllREVRAKESGVRLFTVAIGDAGNPGLLEALA 262


                  .
gi 657584108  186 R 186
Cdd:COG2425   263 D 263
Kunitz_TKDP-like cd22609
trophoblast Kunitz domain protein (TKDP) and similar proteins; This model contains the ...
 2449-2490 3.19e-08

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: 52.06  E-value: 3.19e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 657584108 2449 CADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22609    11 CKASMTRYFYNAQTGHCEQFVYGGCGGNRNNFLTLEDCMKTC 52
VWA_2 pfam13519
von Willebrand factor type A domain;
1004-1112 3.61e-08

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 53.45  E-value: 3.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1004 IIFLVDGSTSIT-----LAKFRNMQRFMESMVNQTtvgkDLTRFGVILYSNDPKSVFTLNqySSKKEVVKAISNLRSPFG 1078
Cdd:pfam13519    1 LVFVLDTSGSMRngdygPTRLEAAKDAVLALLKSL----PGDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|....
gi 657584108  1079 DTYTGKALAYSLQFFDaqhggRAALQVPQILMVI 1112
Cdd:pfam13519   75 GTNLAAALQLARAALK-----HRRKNQPRRIVLI 103
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 27-215 3.61e-08

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


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 55.59  E-value: 3.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   27 CAKAnmADIVFLIDGSSSIGiSNFQEIRQFLRSVISGLDigADKVRIGLAQYSDEPYQEFLLKDHMDKQSLLAAVDTFQY 106
Cdd:cd01474     1 CAGH--FDLYFVLDKSGSVA-ANWIEIYDFVEQLVDRFN--SPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  107 RTGGTETGEAIDFLMNQYFTEDAGSRakqRVPQIAVVITDGDSTDDV----AAPALRLRQHGVIMFAIGVGKANPTELEA 182
Cdd:cd01474    76 PSGQTYIHEGLENANEQIFNRNGGGR---ETVSVIIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGVTDFLKSQLIN 152

                         170       180       190
                  ....*....|....*....|....*....|...
gi 657584108  183 IANRPPKRFMFTiDNYEALQRLTEGLLQTVCIS 215
Cdd:cd01474   153 IADSKEYVFPVT-SGFQALSGIIESVVKKACIE 184
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 2165-2345 4.07e-08

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: 56.24  E-value: 4.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 2165 VDLVMVADSSREIQADQYAGVQQLLGSVVEQLAVSPqprragNQARVAVVQQGGarSAKVEFNLQTYQNQELMRTHLtQK 2244
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGP------DATRVGLVQYSS--TVKQEFPLGRFKSKADLKRAV-RR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 2245 MRQQGGSSALGQTLDYTLkEVLLKAGQPSRKKAL----LAVVGTSTawEDQARLHYVSQKAKCEGVALFVVTVGdhynRT 2320
Cdd:cd01475    74 MEYLETGTMTGLAIQYAM-NNAFSEAEGARPGSErvprVGIVVTDG--RPQDDVSEVAAKARALGIEMFAVGVG----RA 146

                         170       180
                  ....*....|....*....|....*...
gi 657584108 2321 QVEEL---ASLPLQQHLIHVSRLKAGEQ 2345
Cdd:cd01475   147 DEEELreiASEPLADHVFYVEDFSTIEE 174
Kunitz_HAI2_1-like cd22621
Kunitz-type domain 1 (KD1) of hepatocyte growth factor activator inhibitor type 2 (HAI-2), and ...
 2510-2562 4.10e-08

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: 51.71  E-value: 4.10e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2510 DACFLSQDQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22621     1 DFCHLPKVVGRCRASFPRWWYNATSQSCQEFIFGGCKGNLNNFLSEQECLQKC 53
Kunitz_conkunitzin cd22593
conkunitzin-S1 and -S2, and similar proteins; This model includes Kunitz-type conkunitzin-S1 ...
 2439-2490 5.22e-08

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: 51.07  E-value: 5.22e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGIQCADfVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22593     1 CSLPLDEGSGNSS-LTRWYYDPKKGQCKPFTYKGKGGNENNFLTKEDCEETC 51
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 2166-2315 6.21e-08

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: 54.33  E-value: 6.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 2166 DLVMVADSSREIQaDQYAGVQQLLGSVVEQLAVSPQPRRagnqarVAVVQQGGARSAKVEFNLQTYQNQELMRTHLtQKM 2245
Cdd:cd01476     2 DLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATR------VALITYSGRGRQRVRFNLPKHNDGEELLEKV-DNL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657584108 2246 RQQGGSSALGQTLDYTLKevLLKAGQPSRKKALLAVVGTSTAW-----EDQARLhYVSQKakceGVALFVVTVGD 2315
Cdd:cd01476    74 RFIGGTTATGAAIEVALQ--QLDPSEGRREGIPKVVVVLTDGRshddpEKQARI-LRAVP----NIETFAVGTGD 141
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
630-794 6.90e-08

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 54.93  E-value: 6.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  630 DIFFLIDHSGSIYPTDFQDMKKFIIEFIHTFRISPQH---VRLGVAKYADSPNLEFDLTDYSDAKsvekavegIRQI--G 704
Cdd:COG4245     7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYAletVEVSVITFDGEAKVLLPLTDLEDFQ--------PPDLsaS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  705 GGTETGRALAFMSPHFD-RAMTTRGHKVPEY---LVVITDGKSSDKVKVPA-----EQLRAQGVIVYSIGV-KSADMEEL 774
Cdd:COG4245    79 GGTPLGAALELLLDLIErRVQKYTAEGKGDWrpvVFLITDGEPTDSDWEAAlqrlkDGEAAKKANIFAIGVgPDADTEVL 158

                         170       180
                  ....*....|....*....|
gi 657584108  775 REISgDPKRTFFVNNFDALK 794
Cdd:COG4245   159 KQLT-DPVRALDALDGLDFR 177
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1736-1837 7.49e-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: 7.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  1736 GPDGRPGESGIVGNPGQDGRRGSPGvkgaagepgaaglqgIPGASGPQGTRGVRGQPGPRgipglpgpqggpgsvggpga 1815
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPG---------------PPGPPGEPGPPGPPGPPGPP-------------------- 45

                           90       100
                   ....*....|....*....|..
gi 657584108  1816 agrrggngqkGQPGDPGDKGVP 1837
Cdd:pfam01391   46 ----------GPPGAPGAPGPP 57
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
420-565 9.78e-08

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 54.55  E-value: 9.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  420 DIVFIVDESGSIGVANFQMVRTFLHSIISGLEISPT---RVRVGIVmyndrpadqaqqvylnTFNNKDELL-------KF 489
Cdd:COG4245     7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYaleTVEVSVI----------------TFDGEAKVLlpltdleDF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  490 -IKILPYhGGGTNTGAALKFARESVFI-KERGSRKDKGV-QQVAVVITDGESQD-DVSQPAADLRRA----GVTIYSVGV 561
Cdd:COG4245    71 qPPDLSA-SGGTPLGAALELLLDLIERrVQKYTAEGKGDwRPVVFLITDGEPTDsDWEAALQRLKDGeaakKANIFAIGV 149


                  ....*
gi 657584108  562 -KNAN 565
Cdd:COG4245   150 gPDAD 154
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 422-595 9.91e-08

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


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 54.60  E-value: 9.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  422 VFIV-DESGSIGVANFQMVRTFLHSII---SGLEISPtrvRVGIVMYNDRPADQAQQVYLNTfNNKDELLKFIKILPY-- 495
Cdd:cd01470     3 IYIAlDASDSIGEEDFDEAKNAIKTLIekiSSYEVSP---RYEIISYASDPKEIVSIRDFNS-NDADDVIKRLEDFNYdd 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  496 HGG--GTNTGAALKFARES-VFIKERGSRKDKGVQQVAVVITDGES-------------QDDV--SQPAADLRRAGVTIY 557
Cdd:cd01470    79 HGDktGTNTAAALKKVYERmALEKVRNKEAFNETRHVIILFTDGKSnmggsplptvdkiKNLVykNNKSDNPREDYLDVY 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 657584108  558 SVGV-KNANKVQLVEMASHPPN-KHVFivdsfaKLKSMEQ 595
Cdd:cd01470   159 VFGVgDDVNKEELNDLASKKDNeRHFF------KLKDYED 192
Kunitz_HAI1_1-like cd22623
Kunitz domain 1 of hepatocyte growth factor activator inhibitor-1 (HAI-1); This model includes ...
 2528-2562 1.03e-07

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: 50.62  E-value: 1.03e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 657584108 2528 WFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22623    22 WHYNAASGKCEEFVFGGCKGNKNNYLSEEECLSAC 56
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 2166-2329 1.29e-07

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: 53.48  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 2166 DLVMVADSSREIQADQYAGVQQLLGSVVEQLAVSPqprragNQARVAVVQQggARSAKVEFNLQTYQNQELMRTHLtQKM 2245
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGP------DKIRVAVVQF--SDTPRPEFYLNTHSTKADVLGAV-RRL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 2246 RQQGGSSA-LGQTLDYTLKEVLLKAGQPSRKKALLAVVGTSTAWEDQARLHYVSQKAKCEGVALFVVTVGDhYNRTQVEE 2324
Cdd:cd01481    73 RLRGGSQLnTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARN-ADLAELQQ 151


                  ....*
gi 657584108 2325 LASLP 2329
Cdd:cd01481   152 IAFDP 156
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 1002-1173 5.07e-07

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: 51.89  E-value: 5.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1002 ADIIFLVDGSTSITLAKFRNMQRFMESMVNQTtvgKDLTRFGVILYSNDPKSVFTLNQYSSKKEVVKAISNLRsPFGDT- 1080
Cdd:cd01465     1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVDQL---RPDDRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLT-AGGSTa 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1081 -YTGKALAYSLqffdAQHGGRAAlQVPQILMvITDGDA----TDRNSLVAPSVALRDHGVSVFSIGVEGANMTQL-EIMA 1154
Cdd:cd01465    77 gGAGIQLGYQE----AQKHFVPG-GVNRILL-ATDGDFnvgeTDPDELARLVAQKRESGITLSTLGFGDNYNEDLmEAIA 150

                         170       180
                  ....*....|....*....|
gi 657584108 1155 GYDRSKVFYVDNF-EALETL 1173
Cdd:cd01465   151 DAGNGNTAYIDNLaEARKVF 170
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 633-774 7.89e-07

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 53.18  E-value: 7.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  633 FLIDHSGSIYPTDFQDMKKFIIEFIHtfRISPQHvRLGVAKYADSPNLEFDLTDYSDAKSVEKAVEGIRQiGGGTETGRA 712
Cdd:COG2304    96 FVIDVSGSMSGDKLELAKEAAKLLVD--QLRPGD-RVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQA-GGGTALGAG 171

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657584108  713 L----AFMSPHFDRAMTTRghkvpeyLVVITDGKSSDKVKVP------AEQLRAQGVIVYSIGV----KSADMEEL 774
Cdd:COG2304   172 LelayELARKHFIPGRVNR-------VILLTDGDANVGITDPeellklAEEAREEGITLTTLGVgsdyNEDLLERL 240
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1954-2080 8.57e-07

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: 52.39  E-value: 8.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1954 PTELVFGLDMSDDVTPTAFERQRSALLALLEEINIAesncPSGARVAVVGYSAYTKYLIRFQDYRRKTQLEDAVKNIA-L 2032
Cdd:cd01475     2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVG----PDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEyL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 657584108 2033 ERTSnkrHLGAAMHFVAQNVFK-----RVRSGMVMRkVAVFFSNGPSQE-VNDI 2080
Cdd:cd01475    78 ETGT---MTGLAIQYAMNNAFSeaegaRPGSERVPR-VGIVVTDGRPQDdVSEV 127
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 814-961 1.28e-06

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 52.80  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  814 PGDLLFLIDSSGSiypQDYNKM---KDFMKSVISKsfIGQNEvHVGVMQFSTIQKLEFPLNRFYSKGEMSKAIDDMQQiG 890
Cdd:COG2304    91 PLNLVFVIDVSGS---MSGDKLelaKEAAKLLVDQ--LRPGD-RVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQA-G 163

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657584108  891 GGTHTGEAITDVSQYFdsSRGGRPGLRQRLVVITDGEA------QDVVRGPAAALRAKGVVVYAIGV-VDANtTQLLE 961
Cdd:COG2304   164 GGTALGAGLELAYELA--RKHFIPGRVNRVILLTDGDAnvgitdPEELLKLAEEAREEGITLTTLGVgSDYN-EDLLE 238
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 624-774 1.60e-06

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 51.99  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  624 VQTDEADIFFLIDHSGSIYPTDFQDMKKFIIEFIHTFRispQHVRLGVAKYADSPNLEFDLTDYsdaKSVEKAVEGIRQI 703
Cdd:COG2425   114 VPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALR---PNRRFGVILFDTEVVEDLPLTAD---DGLEDAIEFLSGL 187

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657584108  704 --GGGTETGRALAFMSPHFDRAMTTRGHkvpeyLVVITDGKSSDKVKVPAEQLRAQ--GVIVYSIGVKSADMEEL 774
Cdd:COG2425   188 faGGGTDIAPALRAALELLEEPDYRNAD-----IVLITDGEAGVSPEELLREVRAKesGVRLFTVAIGDAGNPGL 257
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 419-586 2.19e-06

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: 49.96  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  419 ADIVFIVDESGSIGVANFQMVRTFLHSIISGLEISPtrvRVGIVMYNDRpadqAQQVYLNT-FNNKDELLKFIKILPyHG 497
Cdd:cd01465     1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDD---RLAIVTYDGA----AETVLPATpVRDKAAILAAIDRLT-AG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  498 GGTNTGAALKFARESV---FIKERGSRkdkgvqqvAVVITDGE------SQDDVSQPAADLRRAGVTIYSVGVKNANKVQ 568
Cdd:cd01465    73 GSTAGGAGIQLGYQEAqkhFVPGGVNR--------ILLATDGDfnvgetDPDELARLVAQKRESGITLSTLGFGDNYNED 144

                         170
                  ....*....|....*...
gi 657584108  569 LVEMASHPPNKHVFIVDS 586
Cdd:cd01465   145 LMEAIADAGNGNTAYIDN 162
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1591-1629 2.20e-06

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: 46.72  E-value: 2.20e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 657584108  1591 GHEGIRGSRGLPGSKGVSGQKGYPGFPGEEGIAGDRGSP 1629
Cdd:pfam01391   19 GPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Kunitz_B2B cd22619
Kunitz-type serine protease inhibitor subunit of beta 2-bungarotoxin, and similar proteins; ...
 2517-2563 2.65e-06

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: 46.78  E-value: 2.65e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 657584108 2517 DQGSCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLCL 2563
Cdd:cd22619    12 DTKRCKRVVRAFYYNPSAKTCLQFVYGGCNGNGNHFKSKALCRCHCH 58
vWA_ORF176_type cd01457
VWA ORF176 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 1193-1320 2.73e-06

VWA ORF176 type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses. In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. The members of this subgroup are Eubacterial in origin and have a conserved MIDAS motif. Not much is known about the biochemistry of these.


Pssm-ID: 238734  Cd Length: 199  Bit Score: 50.57  E-value: 2.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1193 KADLVFLIDQSGSIASTD-------YSIMKKFTTELVNS-FKVSEDLVRVGLaqFSSNFQNEFYLNQfyteeAVSKHIFN 1264
Cdd:cd01457     2 NRDYTLLIDKSGSMAEADeakersrWEEAQESTRALARKcEEYDSDGITVYL--FSGDFRRYDNVNS-----SKVDQLFA 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657584108 1265 MRQLGGGTNI-GLALDSIREYFEasrgcRRSAG----ISQNLVLITDGESQDdvEDAAERL 1320
Cdd:cd01457    75 ENSPDGGTNLaAVLQDALNNYFQ-----RKENGatcpEGETFLVITDGAPDD--KDAVERV 128
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 33-199 3.58e-06

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 49.64  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   33 ADIVFLIDGSSSIGISNFQEIRQF--LRSVISGLDIGADKVRIGLAQYSDEPY-QEFLLKDHMDKQSLLAAVDTFQyrTG 109
Cdd:cd01467     3 RDIMIALDVSGSMLAQDFVKPSRLeaAKEVLSDFIDRRENDRIGLVVFAGAAFtQAPLTLDRESLKELLEDIKIGL--AG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  110 -GTETGEAIDFLMNQyFTEdagSRAKQRVpqiAVVITDGDSTDDVAAP--ALRL-RQHGVIMFAIGVGKANPTE------ 179
Cdd:cd01467    81 qGTAIGDAIGLAIKR-LKN---SEAKERV---IVLLTDGENNAGEIDPatAAELaKNKGVRIYTIGVGKSGSGPkpdgst 153

                         170       180
                  ....*....|....*....|....*.
gi 657584108  180 ------LEAIANRPPKRFMFTIDNYE 199
Cdd:cd01467   154 ildedsLVEIADKTGGRIFRALDGFE 179
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 228-371 3.60e-06

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: 49.32  E-value: 3.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  228 ADIFFLVD-SGISQAEFQQVRSVLVRLTNQVNFGASAHRLGLAQYGQDIK--VEFLLNAFQSKDEMQGGIKRFRQRRLQT 304
Cdd:cd01476     1 LDLLFVLDsSGSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657584108  305 neprNLGSALQYAsANFFTSEAGSRadQGYRQYLVVLSGKDSDDEVFRQSRLIKSegvtVVGMSLGA 371
Cdd:cd01476    81 ----ATGAAIEVA-LQQLDPSEGRR--EGIPKVVVVLTDGRSHDDPEKQARILRA----VPNIETFA 136
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 819-963 3.83e-06

VWA subfamily: 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. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 49.65  E-value: 3.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  819 FLIDSSGSIYPQDYNKMKD---FMKSVISKSFIGQNEVHVGVMQFSTIQKLEFPL---NRFYSKgemskaiddMQQIGGG 892
Cdd:cd01464     8 LLLDTSGSMAGEPIEALNQglqMLQSELRQDPYALESVEISVITFDSAARVIVPLtplESFQPP---------RLTASGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  893 THTGEAIT--------DVSqyfDSSRGGRPGLRQRLVVITDGEAQDVVRGPAAALRA----KGVVVyAIGV-VDANTTQL 959
Cdd:cd01464    79 TSMGAALElaldcidrRVQ---RYRADQKGDWRPWVFLLTDGEPTDDLTAAIERIKEardsKGRIV-ACAVgPKADLDTL 154


                  ....
gi 657584108  960 LEIS 963
Cdd:cd01464   155 KQIT 158
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 1483-1794 5.71e-06

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: 51.54  E-value: 5.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1483 LKSFGQKFKAESRAGVKVLLIFSDGLDDDVmklEQESELLRQSGISALLTvalEGVRDIAQLQMVEFGRGFGYRLPLSI- 1561
Cdd:cd21118    20 LHSGGEGTGAGESAGHGLGDAISHGIGEAV---GQGAKEAASSGIQNALG---QGHGEEGGSTLGSRGDVFEHRLGEAAr 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1562 GMPSVGSTILKQIDTVSDReccnvmckcsGHEGIRGSRGLPGSKGVSGQKGYPGFPGEeGIAGDRGSPGPSG-PQGVQGC 1640
Cdd:cd21118    94 SLGNAGNEIGRQAEDIIRH----------GVDAVHNSWQGSGGHGAYGSQGGPGVQGH-GIPGGTGGPWASGgNYGTNSL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1641 SGRRGVKGFRG-------LRGNRGEDGEDGLDGVDGEQGLT-----GADGGRGERGNPGNPGIPGIRGEAGLKGQRGLRG 1708
Cdd:cd21118   163 GGSVGQGGNGGplnygtnSQGAVAQPGYGTVRGNNQNSGCTnpppsGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGS 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1709 DPGEPGADNNSpGAKGDSGNAGlpglpgpDGRPGESGIVGNPGQDGRRGSPGVkgaagepgaaglQGIPGASGPQGTRGV 1788
Cdd:cd21118   243 SGGQGNGGNNG-SSSSNSGNSG-------GSNGGSSGNSGSGSGGSSSGGSNG------------WGGSSSSGGSGGSGG 302


                  ....*.
gi 657584108 1789 RGQPGP 1794
Cdd:cd21118   303 GNKPEC 308
Kunitz_WFIKKN_2-like cd22606
second Kunitz domain of WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing proteins; ...
 2456-2490 5.82e-06

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: 45.43  E-value: 5.82e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 657584108 2456 WFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22606    18 WAYNSLLKQCQSFVYGGCEGNENNFESKEACEDAC 52
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 1194-1365 8.93e-06

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 48.48  E-value: 8.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1194 ADLVFLIDQSGSIASTDYSIMKKFTT--ELVNSF--KVSEDlvRVGLAQFSsnfQNEFYLNQFYTEEAVSKHIFNMRQ-- 1267
Cdd:cd01467     3 RDIMIALDVSGSMLAQDFVKPSRLEAakEVLSDFidRREND--RIGLVVFA---GAAFTQAPLTLDRESLKELLEDIKig 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1268 -LGGGTNIGLALDSIREYFEASRGCRRSagisqnLVLITDGESQDDV---EDAAERLRALGIEVFAIGIGNvhdlELLQI 1343
Cdd:cd01467    78 lAGQGTAIGDAIGLAIKRLKNSEAKERV------IVLLTDGENNAGEidpATAAELAKNKGVRIYTIGVGK----SGSGP 147

                         170       180
                  ....*....|....*....|..
gi 657584108 1344 TGTPErlfTVENFGSLEKIKQK 1365
Cdd:cd01467   148 KPDGS---TILDEDSLVEIADK 166
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 35-189 1.44e-05

VWA subfamily: 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. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 47.72  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   35 IVFLIDGSSSIGISNFQEIRQFLRSVISGL---DIGADKVRIGLAQYSDEPYQEfllkdhmdkqSLLAAVDTFQYRT--- 108
Cdd:cd01464     6 IYLLLDTSGSMAGEPIEALNQGLQMLQSELrqdPYALESVEISVITFDSAARVI----------VPLTPLESFQPPRlta 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  109 -GGTETGEAIDFLMNQYFTEDAGSRAKQR---VPQIaVVITDGDSTDDVAAPALRLRQHG-----VIMFAIGVgKANPTE 179
Cdd:cd01464    76 sGGTSMGAALELALDCIDRRVQRYRADQKgdwRPWV-FLLTDGEPTDDLTAAIERIKEARdskgrIVACAVGP-KADLDT 153

                         170
                  ....*....|
gi 657584108  180 LEAIANRPPK 189
Cdd:cd01464   154 LKQITEGVPL 163
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 419-561 1.47e-05

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 48.09  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  419 ADIVFIVDESGSIG------VANFQMVRTFLHSIISGLEISptrvRVGIVMYNDRPADQA----QQVYLNtfnnkdELLK 488
Cdd:cd01467     3 RDIMIALDVSGSMLaqdfvkPSRLEAAKEVLSDFIDRREND----RIGLVVFAGAAFTQApltlDRESLK------ELLE 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657584108  489 FIKILpYHGGGTNTGAALKFARESVfikergsRKDKGVQQVAVVITDGESQDDVSQP--AADLRRA-GVTIYSVGV 561
Cdd:cd01467    73 DIKIG-LAGQGTAIGDAIGLAIKRL-------KNSEAKERVIVLLTDGENNAGEIDPatAAELAKNkGVRIYTIGV 140
Kunitz_ixolaris_1 cd22625
Kunitz-type domain 1 (K1) of Ixolaris, and similar proteins; This model includes the first ...
 2516-2562 1.49e-05

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: 44.56  E-value: 1.49e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 657584108 2516 QDQGSCQNYSM-MWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22625     6 QEITTCESQPTkRYGYNKKTQQCEEFLGTECGGGGNSFEEAKECWSSC 53
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 1195-1371 1.99e-05

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: 47.70  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1195 DLVFLIDQSGSIastDYSIMKK----FTTELVNSFKVSEDLVRVGLAQFSSnFQNEFylNQFYTEEAVSK---------- 1260
Cdd:cd01473     2 DLTLILDESASI---GYSNWRKdvipFTEKIINNLNISKDKVHVGILLFAE-KNRDV--VPFSDEERYDKnellkkindl 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1261 --HIFNmrqlGGGTNIGLALD-SIREYFEasRGCRRSAGISQNlVLITDG----ESQDDVEDAAERLRALGIEVFAIGIG 1333
Cdd:cd01473    76 knSYRS----GGETYIVEALKyGLKNYTK--HGNRRKDAPKVT-MLFTDGndtsASKKELQDISLLYKEENVKLLVVGVG 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 657584108 1334 --NVHDLELL---QITGTPERLFTVENFGSLEKIKQKVINTIC 1371
Cdd:cd01473   149 aaSENKLKLLagcDINNDNCPNVIKTEWNNLNGISKFLTDKIC 191
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 420-559 2.10e-05

VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. The members of this subgroup lack the MIDAS motif. This subgroup is found only in C. elegans and the members identified thus far are always found fused to a C-Lectin type domain. Biochemical function thus far has not be attributed to any of the members of this subgroup.


Pssm-ID: 238754 [Multi-domain]  Cd Length: 193  Bit Score: 47.80  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  420 DIVFIVDESGSIGVANFQMVRTFLHSIISGLEISPTR------VRVGIVMYNDRPADQAQ----QVYLNTFNNKDELLKF 489
Cdd:cd01477    21 DIVFVVDNSKGMTQGGLWQVRATISSLFGSSSQIGTDyddprsTRVGLVTYNSNATVVADlndlQSFDDLYSQIQGSLTD 100

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657584108  490 IKILPyhggGTNTGAALKFARESVFIKERGSRkdKGVQQVAVVIT---DGESQDDVSQPAADLRRAGVTIYSV 559
Cdd:cd01477   101 VSSTN----ASYLDTGLQAAEQMLAAGKRTSR--ENYKKVVIVFAsdyNDEGSNDPRPIAARLKSTGIAIITV 167
Kunitz_TFPI2_2-like cd22617
Kunitz domain 2 (KD2) of tissue factor pathway inhibitor 2 (TFPI2) and similar proteins; This ...
 2438-2490 2.23e-05

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: 43.91  E-value: 2.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2438 RCQLDSDSGIQCADFVQvWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22617     3 VCREVPDEGPCRALITR-YFYNMTSMRCEEFTYGGCYGNGNNFRDKSSCISAC 54
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 420-575 2.95e-05

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


Pssm-ID: 238739 [Multi-domain]  Cd Length: 152  Bit Score: 46.57  E-value: 2.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  420 DIVFIVDESGSIGVANFQMVRTFlhsIISGLEISPTR-VRVGIVMYNDR----PADQAQQVylntfnnkDELLKFIKILP 494
Cdd:cd01462     2 PVILLVDQSGSMYGAPEEVAKAV---ALALLRIALAEnRDTYLILFDSEfqtkIVDKTDDL--------EEPVEFLSGVQ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  495 YhGGGTNTGAALKFARESvfIKERGSRKdkgvqQVAVVITDG---ESQDDVSQPAADLRRAGVTIYSVGVKNANKVQLVE 571
Cdd:cd01462    71 L-GGGTDINKALRYALEL--IERRDPRK-----ADIVLITDGyegGVSDELLREVELKRSRVARFVALALGDHGNPGYDR 142


                  ....
gi 657584108  572 MASH 575
Cdd:cd01462   143 ISAE 146
Kunitz_HAI1_1-like cd22623
Kunitz domain 1 of hepatocyte growth factor activator inhibitor-1 (HAI-1); This model includes ...
 2456-2490 3.27e-05

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: 43.69  E-value: 3.27e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 657584108 2456 WFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22623    22 WHYNAASGKCEEFVFGGCKGNKNNYLSEEECLSAC 56
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 33-184 3.48e-05

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


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 46.50  E-value: 3.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   33 ADIVFLIDGSSSIGISNFQEIRQFLRSVISGLDigaDKVRIGLAQYSDE-----PYQEFllkdhMDKQSLLAAVDTFQyR 107
Cdd:cd01465     1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVDQLR---PDDRLAIVTYDGAaetvlPATPV-----RDKAAILAAIDRLT-A 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  108 TGGTETGEAIDfLMNQYFTEDAGSRAKQRVpqiaVVITDGDST------DDVAAPALRLRQHGVIMFAIGVGKA-NPTEL 180
Cdd:cd01465    72 GGSTAGGAGIQ-LGYQEAQKHFVPGGVNRI----LLATDGDFNvgetdpDELARLVAQKRESGITLSTLGFGDNyNEDLM 146


                  ....
gi 657584108  181 EAIA 184
Cdd:cd01465   147 EAIA 150
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 631-778 5.18e-05

VWA subfamily: 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. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 46.18  E-value: 5.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  631 IFFLIDHSGSIYPTDFQDMKKFIIEFIHTFRISP---QHVRLGVAKYADSPNLEFDLTDysdaksVEKAVEGIRQIGGGT 707
Cdd:cd01464     6 IYLLLDTSGSMAGEPIEALNQGLQMLQSELRQDPyalESVEISVITFDSAARVIVPLTP------LESFQPPRLTASGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  708 ETGRALAFMSPHFDRAMT-TRGHKVPEY---LVVITDGKSSDKVKVPAEQLRAQG-----VIVYSIGVKsADMEELREIS 778
Cdd:cd01464    80 SMGAALELALDCIDRRVQrYRADQKGDWrpwVFLLTDGEPTDDLTAAIERIKEARdskgrIVACAVGPK-ADLDTLKQIT 158
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1000-1165 6.16e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 48.42  E-value: 6.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1000 EKADIIFLVDGSTSITLAKFRNMQRFM-ESMVNQTTVGKDLTRFGVILYSNDPKSVFTLNQYSS--KKEVVKAISNLRS- 1075
Cdd:PTZ00441   41 EEVDLYLLVDGSGSIGYHNWITHVIPMlMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASkdKEQALIIVKSLRKt 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1076 --PFGDTYTGKALAYSLQFFDAQHGGRAALQvpqILMVITDGDATDRNSLVAPSVALRDHGVSVFSIGV-EGANMTQLEI 1152
Cdd:PTZ00441  121 ylPYGKTNMTDALLEVRKHLNDRVNRENAIQ---LVILMTDGIPNSKYRALEESRKLKDRNVKLAVIGIgQGINHQFNRL 197

                         170
                  ....*....|....*.
gi 657584108 1153 MAG---YDRSKVFYVD 1165
Cdd:PTZ00441  198 LAGcrpREGKCKFYSD 213
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 1195-1332 1.13e-04

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


Pssm-ID: 238739 [Multi-domain]  Cd Length: 152  Bit Score: 44.65  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1195 DLVFLIDQSGSIASTDYSIMKKFTTELVnsFKVSEDLVRVGLAQFSSNFQNEFYLNQFYTEEAVSkhiFNMR-QLGGGTN 1273
Cdd:cd01462     2 PVILLVDQSGSMYGAPEEVAKAVALALL--RIALAENRDTYLILFDSEFQTKIVDKTDDLEEPVE---FLSGvQLGGGTD 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657584108 1274 IGLALDSIREYFEaSRGCRRSagisqNLVLITDG---ESQDDV--EDAAERLRALGIEVFAIGI 1332
Cdd:cd01462    77 INKALRYALELIE-RRDPRKA-----DIVLITDGyegGVSDELlrEVELKRSRVARFVALALGD 134
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 420-578 1.27e-04

VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known.


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 44.69  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  420 DIVFIVDESGSIGVANFQMVRTFLHSIISGLEispTRVRVGIVMYNDRPAdQAQQVYLNTFNNKDELLKFIKILpYHGGG 499
Cdd:cd01466     2 DLVAVLDVSGSMAGDKLQLVKHALRFVISSLG---DADRLSIVTFSTSAK-RLSPLRRMTAKGKRSAKRVVDGL-QAGGG 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657584108  500 TNTGAALKFAresvfIKERGSRKDKGVQQVAVVITDGESQDDVSQPAADLrrAGVTIYSVGVKNANKVQLVEMASHPPN 578
Cdd:cd01466    77 TNVVGGLKKA-----LKVLGDRRQKNPVASIMLLSDGQDNHGAVVLRADN--APIPIHTFGLGASHDPALLAFIAEITG 148
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 1954-2075 1.31e-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: 45.07  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1954 PTELVFGLDMSDDVTPTAFERQRSALLALLEEINIAESNCPS--GARVAVVGYS-AYTKYLIRFQDYRRKTQLEDAVKNi 2030
Cdd:cd01480     2 PVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRKDPagSWRVGVVQYSdQQEVEAGFLRDIRNYTSLKEAVDN- 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 657584108 2031 aLERTSNKRHLGAAMHFVAQNVFKRVRSGmvMRKVAVFFSNGPSQ 2075
Cdd:cd01480    81 -LEYIGGGTFTDCALKYATEQLLEGSHQK--ENKFLLVITDGHSD 122
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 816-951 1.47e-04

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 45.01  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  816 DLLFLIDSSGSIYPQDYNKMK--DFMKSVISKsFIGQNEV-HVGVMQFSTIQKLEFPLNRFY-SKGEMSKAIDDMQqIGG 891
Cdd:cd01467     4 DIMIALDVSGSMLAQDFVKPSrlEAAKEVLSD-FIDRRENdRIGLVVFAGAAFTQAPLTLDReSLKELLEDIKIGL-AGQ 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657584108  892 GTHTGEAITDVSQYFDSSRGgrpglRQR-LVVITDGE--AQDVVRGPAAAL-RAKGVVVYAIGV 951
Cdd:cd01467    82 GTAIGDAIGLAIKRLKNSEA-----KERvIVLLTDGEnnAGEIDPATAAELaKNKGVRIYTIGV 140
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 1263-1344 1.49e-04

VWA subfamily: 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. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 45.02  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1263 FNMRQL--GGGTNIGLAL--------DSIREYFEASRGCRRSAgisqnLVLITDGESQDDVEDAAERLRALGIE---VFA 1329
Cdd:cd01464    68 FQPPRLtaSGGTSMGAALelaldcidRRVQRYRADQKGDWRPW-----VFLLTDGEPTDDLTAAIERIKEARDSkgrIVA 142

                          90
                  ....*....|....*.
gi 657584108 1330 IGIGNVHDLELL-QIT 1344
Cdd:cd01464   143 CAVGPKADLDTLkQIT 158
Kunitz_ixolaris_1 cd22625
Kunitz-type domain 1 (K1) of Ixolaris, and similar proteins; This model includes the first ...
 2439-2490 1.60e-04

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: 41.48  E-value: 1.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 657584108 2439 CQLDSDSGIQCADFVQVWF-FDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22625     1 CTLPIQEITTCESQPTKRYgYNKKTQQCEEFLGTECGGGGNSFEEAKECWSSC 53
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 816-991 1.70e-04

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 45.00  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  816 DLLFLIDSSGSIypQDYNKMKDFM---KSVISKSFIGQNEVHVGVMQFSTIQKLefpLNRF-----YSKGEMSKAIDDMQ 887
Cdd:cd01473     2 DLTLILDESASI--GYSNWRKDVIpftEKIINNLNISKDKVHVGILLFAEKNRD---VVPFsdeerYDKNELLKKINDLK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  888 Q---IGGGTHTGEAIT-DVSQYF--DSSRGGRPGLRqrlVVITDG--------EAQDVVRgpaaALRAKGVVVYAIGVVD 953
Cdd:cd01473    77 NsyrSGGETYIVEALKyGLKNYTkhGNRRKDAPKVT---MLFTDGndtsaskkELQDISL----LYKEENVKLLVVGVGA 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 657584108  954 ANTTQLLEISG-------SPDRMYAErdFDALKDLESQVALELCD 991
Cdd:cd01473   150 ASENKLKLLAGcdinndnCPNVIKTE--WNNLNGISKFLTDKICD 192
Kunitz_B2B cd22619
Kunitz-type serine protease inhibitor subunit of beta 2-bungarotoxin, and similar proteins; ...
 2439-2490 2.20e-04

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: 41.39  E-value: 2.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 657584108 2439 CQLDSDSGIqCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22619     7 CDKPPDTKR-CKRVVRAFYYNPSAKTCLQFVYGGCNGNGNHFKSKALCRCHC 57
Kunitz_MitTx cd22610
Micrurus tener tener Kunitz-type neurotoxin MitTx-alpha; Micrurus tener tener Kunitz-type ...
 2437-2490 2.57e-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: 41.16  E-value: 2.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 657584108 2437 ARCQLDSDSGIQCADFVQVWFFDKHIGACSPFWYGGCGGNANRFNTEHECFRTC 2490
Cdd:cd22610     4 AFCYEDPPFFQKCGAFVDSYYFNRSRITCVHFFYGQCDVNQNHFTTMSECNRVC 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 1590-1626 5.29e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 5.29e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 657584108  1590 SGHEGIRGSRGLPGSKGVSGQKGYPGFPGEEGIAGDR 1626
Cdd:pfam01391   21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 2165-2318 5.38e-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: 5.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 2165 VDLVMVADSSREIQADQYAGVQQLLGSVVEQLAVSPQPRRAGNQARVAVVQQGGARSAKVEFnLQTYQNQELMRTHLtQK 2244
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRKDPAGSWRVGVVQYSDQQEVEAGF-LRDIRNYTSLKEAV-DN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 657584108 2245 MRQQGGSSALGQTLDYTLKEVLLKAGQPSRKKALLAVVGTSTAWEDQARLHYVsQKAKCEGVALFVVTVGDHYN 2318
Cdd:cd01480    81 LEYIGGGTFTDCALKYATEQLLEGSHQKENKFLLVITDGHSDGSPDGGIEKAV-NEADHLGIKIFFVAVGSQNE 153
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1956-2101 9.37e-04

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: 42.31  E-value: 9.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1956 ELVFGLDMSDDVTPTAFERQRSALLALLEEINIAesncPSGARVAVVGYSAYTKYLIRFQDYRRKTQLEDAVKNIALeRT 2035
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVG----PDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRL-RG 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657584108 2036 SNKRHLGAAMHFVAQNVFK-----RVRSGMVmrKVAVFFSNGPSQEVNDIPGAVMEYRGlnIVPAVISLTN 2101
Cdd:cd01481    77 GSQLNTGSALDYVVKNLFTksagsRIEEGVP--QFLVLITGGKSQDDVERPAVALKRAG--IVPFAIGARN 143
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 229-399 9.67e-04

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: 42.76  E-value: 9.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  229 DIFFLVDSGIS---QAEFQQVRSVLVRLTNQVNFGASAHRLGLAQYGQDIKVEFLLNAFQSKDEMQGgikRFRQRRLQTN 305
Cdd:cd01471     2 DLYLLVDGSGSigySNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKDLA---LNAIRALLSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  306 -EPR---NLGSALQYASANFFTSeAGSRADQgyRQYLVVLSG--KDSDDEVFRQSRLIKSEGV--TVVGMSLGASMNEIR 377
Cdd:cd01471    79 yYPNgstNTTSALLVVEKHLFDT-RGNRENA--PQLVIIMTDgiPDSKFRTLKEARKLRERGViiAVLGVGQGVNHEENR 155

                         170       180       190
                  ....*....|....*....|....*....|
gi 657584108  378 VI-----STAP---YAYQSISNAVPVLKGI 399
Cdd:cd01471   156 SLvgcdpDDSPcplYLQSSWSEVQNVIKPF 185
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1861-1926 1.06e-03

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 44.13  E-value: 1.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657584108 1861 GVKGDPGFPGYPGllgEDGLQGPKGLPGRKGNRGRGGNSGRSGESGISGDPGYAGHRGPRGLPGSK 1926
Cdd:NF038329  117 GEKGEPGPAGPAG---PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKD 179
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 421-577 1.38e-03

VWA subfamily: 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. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 41.94  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  421 IVFIVDESGSIGVANFQMVRTFLHSIISGL---EISPTRVRVGIVMYndrpADQAQQVYLNTfnnkdELLKFI-KILPYh 496
Cdd:cd01464     6 IYLLLDTSGSMAGEPIEALNQGLQMLQSELrqdPYALESVEISVITF----DSAARVIVPLT-----PLESFQpPRLTA- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  497 GGGTNTGAALKFARESVFI-KERGSRKDKG-VQQVAVVITDGESQDDVSQPAADLRRAG-----VTIYSVGVKnANKVQL 569
Cdd:cd01464    76 SGGTSMGAALELALDCIDRrVQRYRADQKGdWRPWVFLLTDGEPTDDLTAAIERIKEARdskgrIVACAVGPK-ADLDTL 154


                  ....*...
gi 657584108  570 VEMASHPP 577
Cdd:cd01464   155 KQITEGVP 162
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 1195-1347 1.59e-03

VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known.


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 41.61  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1195 DLVFLIDQSGSIASTDYSIMKKFTTELVNSFKvseDLVRVGLAQFSSNFQNEFYLnQFYTEEA--VSKHIFNMRQLGGGT 1272
Cdd:cd01466     2 DLVAVLDVSGSMAGDKLQLVKHALRFVISSLG---DADRLSIVTFSTSAKRLSPL-RRMTAKGkrSAKRVVDGLQAGGGT 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657584108 1273 NIGLALDsireyfEASR--GCRRSAGISQNLVLITDGESQDDVEDAaeRLRALGIEVFAIGIGNVHDLELLQITGTP 1347
Cdd:cd01466    78 NVVGGLK------KALKvlGDRRQKNPVASIMLLSDGQDNHGAVVL--RADNAPIPIHTFGLGASHDPALLAFIAEI 146
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 1195-1342 1.99e-03

vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix.


Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 41.43  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1195 DLVFLIDQSGSIASTdySI------MKKFTTEL--VNSFKVSEdlvrvglaqFSSNFQNEFYLNQFYTEEAVSKHIFNMR 1266
Cdd:cd01461     4 EVVFVIDTSGSMSGT--KIeqtkeaLLTALKDLppGDYFNIIG---------FSDTVEEFSPSSVSATAENVAAAIEYVN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1267 QL--GGGTNIGLALDsireyfEASRGCRRSAGISQNLVLITDGESQDDVEDAAERLRALG--IEVFAIGIGNVHDLELLQ 1342
Cdd:cd01461    73 RLqaLGGTNMNDALE------AALELLNSSPGSVPQIILLTDGEVTNESQILKNVREALSgrIRLFTFGIGSDVNTYLLE 146
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1451-1555 2.17e-03

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: 41.29  E-value: 2.17e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   1451 LYDFNFEGYSEDVVQKVMTLS--LAEPTYFNTAMLKSFGQKFKAE--SRAGV-KVLLIFSDGLDDDVMK-LEQESELLRQ 1524
Cdd:smart00327   52 LFPLNDSRSKDALLEALASLSykLGGGTNLGAALQYALENLFSKSagSRRGApKVVILITDGESNDGPKdLLKAAKELKR 131

                            90       100       110
                    ....*....|....*....|....*....|.
gi 657584108   1525 SGISaLLTVALEGVRDIAQLQMVEFGRGFGY 1555
Cdd:smart00327  132 SGVK-VFVVGVGNDVDEEELKKLASAPGGVY 161
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 630-794 2.89e-03

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


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 41.50  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  630 DIFFLIDHSGSIYPTDFQDMKKFI---IEFIHTFRISPqhvRLGVAKYADSPNLEFDLTDY--SDAKSVEKAVE----GI 700
Cdd:cd01470     2 NIYIALDASDSIGEEDFDEAKNAIktlIEKISSYEVSP---RYEIISYASDPKEIVSIRDFnsNDADDVIKRLEdfnyDD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  701 RQIGGGTETGRALAFMSPHF--------DRAMTTRgHKVpeylVVITDGKSS---------DKVK------VPAEQLRAQ 757
Cdd:cd01470    79 HGDKTGTNTAAALKKVYERMalekvrnkEAFNETR-HVI----ILFTDGKSNmggsplptvDKIKnlvyknNKSDNPRED 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 657584108  758 GVIVYSIGV-KSADMEELREIS---GDPKRTFFVNNFDALK 794
Cdd:cd01470   154 YLDVYVFGVgDDVNKEELNDLAskkDNERHFFKLKDYEDLQ 194
Kunitz_MitTx cd22610
Micrurus tener tener Kunitz-type neurotoxin MitTx-alpha; Micrurus tener tener Kunitz-type ...
 2505-2562 3.32e-03

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: 38.08  E-value: 3.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 657584108 2505 SFISKDACFLSQdqgsCQNYSMMWFFDTEQNECARFWYGGCGGNENRFKTQEECENLC 2562
Cdd:cd22610     4 AFCYEDPPFFQK----CGAFVDSYYFNRSRITCVHFFYGQCDVNQNHFTTMSECNRVC 57
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 34-186 3.58e-03

VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known.


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 40.45  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108   34 DIVFLIDGSSSIGISNFQEIRQFLRSVISGLdigADKVRIGLAQYSDEPYQEFLLKdHMD---KQSLLAAVDTFQyRTGG 110
Cdd:cd01466     2 DLVAVLDVSGSMAGDKLQLVKHALRFVISSL---GDADRLSIVTFSTSAKRLSPLR-RMTakgKRSAKRVVDGLQ-AGGG 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657584108  111 TETGEAIDFLMNQYftedAGSRAKQRVPQIaVVITDGDSTDDVAapALRLRQHGVIMFAIGVGKAN-PTELEAIANR 186
Cdd:cd01466    77 TNVVGGLKKALKVL----GDRRQKNPVASI-MLLSDGQDNHGAV--VLRADNAPIPIHTFGLGASHdPALLAFIAEI 146
Kunitz_TAP-like cd21630
Tick anticoagulant peptide, and similar proteins; Tick anticoagulant peptide (TAP) is a ...
 2448-2490 4.93e-03

Tick anticoagulant peptide, and similar proteins; Tick anticoagulant peptide (TAP) is a competitive inhibitor of factor Xa, a serine protease that converts prothrombin into thrombin, which acts to convert fibrinogen into fibrin, the insoluble matrix of blood clots. TAP is one of the antihemostatic components evolved in the blood-feeding tick. This subfamily also includes the N-terminal Kunitz inhibitor domain of ornithodorin which binds to the active site of thrombin, while the C-terminal domain binds at the fibrinogen recognition exosite. The TAP structure 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: 438634  Cd Length: 60  Bit Score: 37.55  E-value: 4.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 657584108 2448 QC--ADFVQVWFFDKHiGACSPFWYGGCGGN-ANRFNTEHECFRTC 2490
Cdd:cd21630    15 ECdsEAWERRYFRNGK-GGCESFWYCDEEDTgANYFSSMEDCFNAC 59
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 815-947 6.25e-03

VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known.


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 39.68  E-value: 6.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108  815 GDLLFLIDSSGSIYPQDYNKMKDFMKSVISKsfIGQNEvHVGVMQFSTIQKLEFPLNRFYSKG--EMSKAIDDMQQiGGG 892
Cdd:cd01466     1 VDLVAVLDVSGSMAGDKLQLVKHALRFVISS--LGDAD-RLSIVTFSTSAKRLSPLRRMTAKGkrSAKRVVDGLQA-GGG 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 657584108  893 THTGEAITDVSQYFDSSRGGRPGlrQRLVVITDGEAQDVvrgpAAALRAKGVVVY 947
Cdd:cd01466    77 TNVVGGLKKALKVLGDRRQKNPV--ASIMLLSDGQDNHG----AVVLRADNAPIP 125
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1454-1547 8.26e-03

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: 39.58  E-value: 8.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657584108 1454 FNFEGYS--EDVVQKVMTLSL--AEPTYFNTAMLKSFGQKF-KAESRAGV-KVLLIFSDGLDDDVMKLEQESELLRQSGI 1527
Cdd:cd01450    54 FSLNDYKskDDLLKAVKNLKYlgGGGTNTGKALQYALEQLFsESNARENVpKVIIVLTDGRSDDGGDPKEAAAKLKDEGI 133

                          90       100
                  ....*....|....*....|
gi 657584108 1528 SaLLTVALeGVRDIAQLQMV 1547
Cdd:cd01450   134 K-VFVVGV-GPADEEELREI 151
 
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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