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Conserved domains on  [gi|240255535|ref|NP_476507|]
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collagen alpha-3(VI) chain isoform 4 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
828-992 3.24e-89

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


:

Pssm-ID: 238758  Cd Length: 165  Bit Score: 287.68  E-value: 3.24e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  828 ADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPL 907
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  908 NTGKALEFVARNLFVKSAGSRIEDGVPQHLVLVLGGKSQDDVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDPRLVF 987
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160

                  ....*
gi 240255535  988 TVREF 992
Cdd:cd01481   161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
37-201 6.28e-86

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: 278.05  E-value: 6.28e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   37 RDIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSAL 116
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  117 YTGSALDFVRNNLFTSSAGYRAAEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSSLVF 196
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160

                  ....*
gi 240255535  197 IPAEF 201
Cdd:cd01481   161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
625-787 3.60e-83

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


:

Pssm-ID: 238758  Cd Length: 165  Bit Score: 270.35  E-value: 3.60e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  625 RDVVFLIDGSQSAGP-EFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQI 703
Cdd:cd01481     1 KDIVFLIDGSDNVGSgNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  704 NVGNALEYVSRNIFKRPLGSRIEEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTI-ARNADQEELVKISLSPEYVF 782
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIgARNADLAELQQIAFDPSFVF 160

                  ....*
gi 240255535  783 SVSTF 787
Cdd:cd01481   161 QVSDF 165
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
421-584 1.46e-70

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


The actual alignment was detected with superfamily member cd01481:

Pssm-ID: 469594  Cd Length: 165  Bit Score: 234.14  E-value: 1.46e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  421 KDVVFLLDGSEGVRS-GFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTP 499
Cdd:cd01481     1 KDIVFLIDGSDNVGSgNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  500 NTGAALEFVLRNILVSSAGSRITEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPDFAV 579
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160

                  ....*
gi 240255535  580 AIPTF 584
Cdd:cd01481   161 QVSDF 165
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
229-392 2.30e-60

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


The actual alignment was detected with superfamily member cd01481:

Pssm-ID: 469594  Cd Length: 165  Bit Score: 204.87  E-value: 2.30e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  229 RDILFLFDGSANL-VGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKAL 307
Cdd:cd01481     1 KDIVFLIDGSDNVgSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  308 NLGYALDYAQRYIFVKSAGSRIEDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPAFIL 387
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160

                  ....*
gi 240255535  388 AAESL 392
Cdd:cd01481   161 QVSDF 165
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1428-1764 1.05e-45

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: 172.40  E-value: 1.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1428 KCSGQRGDRGPIGSIGPKGIPGEDGYRgypgdeggpgergppgvnGTQGFQGCPGQRGVKGSRGFPGEKGEVGEIGLDGL 1507
Cdd:NF038329  114 KGDGEKGEPGPAGPAGPAGEQGPRGDR------------------GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1508 DGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGdvgirgdpgnpgqdsqERGPKGETGDLGPMGVPGrdgvPGGPGET 1587
Cdd:NF038329  176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG----------------PAGPDGEAGPAGEDGPAG----PAGDGQQ 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1588 GKnggfgrrgppgakgnKGGPGQPGFEGEQGTRgaqgpagpagppgliGEQGisgprgsggaagapgergRTGPLGRKGE 1667
Cdd:NF038329  236 GP---------------DGDPGPTGEDGPQGPD---------------GPAG------------------KDGPRGDRGE 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1668 PGEPGPKGGIGNRGPRGETGDDGRDG-VGSEGRRGKKGERGFPGYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGP----- 1741
Cdd:NF038329  268 AGPDGPDGKDGERGPVGPAGKDGQNGkDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPktpev 347
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 240255535 1742 -------------PGIVGQKGDPGyPGPAGPKgNRG 1764
Cdd:NF038329  348 pqkpdtaphtpktPQIPGQSKDVT-PAPQNPS-NRG 381
VWA pfam00092
von Willebrand factor type A domain;
1032-1204 2.00e-45

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 162.44  E-value: 2.00e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1032 DIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRHAN 1111
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1112 TKVGLEHLRVNHFVPEAGSRLDqrVPQIAFVITGGKSVE-DAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIASNSA--T 1188
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPG--APKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158
                          170
                   ....*....|....*.
gi 240255535  1189 AFRVGNVQELSELSEQ 1204
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
Kunitz_collagen_alpha3_VI cd22629
Kunitz-type domain from the alpha3 chain of human type VI collagen, and similar proteins; This ...
2503-2555 1.98e-38

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


:

Pssm-ID: 438672  Cd Length: 53  Bit Score: 137.89  E-value: 1.98e-38
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2503 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22629     1 DICKLPKDEGTCRDFVLKWYYDPETKSCARFWYGGCGGNENRFDSQEECEKVC 53
VWA pfam00092
von Willebrand factor type A domain;
2012-2199 6.38e-32

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 123.92  E-value: 6.38e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  2012 DMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDpkasqhFARVAVVQHApsesvDNasmppVKVEFSLTDYGSKEKL 2091
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPD------GTRVGLVQYS-----SD-----VRTEFPLNDYSSKEEL 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  2092 VDFLSRGMTQLQGTRALGSAIEYTIENVFESAPNPRDL--KIVVLMLTGEVPEQQLEEaqrVILQAKCKGYFFVVLGIGr 2169
Cdd:pfam00092   65 LSAVDNLRYLGGGTTNTGKALKYALENLFSSAAGARPGapKVVVLLTDGRSQDGDPEE---VARELKSAGVTVFAVGVG- 140
                          170       180       190
                   ....*....|....*....|....*....|
gi 240255535  2170 KVNIKEVYTFASEPNDVFFKLVDKSTELNE 2199
Cdd:pfam00092  141 NADDEELRKIASEPGEGHVFTVSDFEALED 170
VWA pfam00092
von Willebrand factor type A domain;
1795-1973 1.36e-22

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 96.96  E-value: 1.36e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1795 ELAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIaesnCPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQVaLT 1874
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDI----GPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRY-LG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1875 SKQQSLETAMSFVARNTFKRVRNG-FLMRKVAVFFSNTPTrASPQLREAVLKLSDAGITPLFL-TRQEDRQLINALQiNN 1952
Cdd:pfam00092   76 GGTTNTGKALKYALENLFSSAAGArPGAPKVVVLLTDGRS-QDGDPEEVARELKSAGVTVFAVgVGNADDEELRKIA-SE 153
                          170       180
                   ....*....|....*....|.
gi 240255535  1953 TAVGHALVLPAGRDLTDFLEN 1973
Cdd:pfam00092  154 PGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
1231-1387 2.09e-09

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


:

Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 59.01  E-value: 2.09e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   1231 DVILGFDGSRDqnvfVAQKGFESKVDAILNRISQMHRvscsggRSPTVRVSVVAnTPSGPVEAFDFDEYQ--PEMLEKFR 1308
Cdd:smart00327    1 DVVFLLDGSGS----MGGNRFELAKEFVLKLVEQLDI------GPDGDRVGLVT-FSDDARVLFPLNDSRskDALLEALA 69
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   1309 NMRsqhpYVLTEDT---------LKVYLNKFRQSSPDSVKVVIHFTDGADGDLA-DLHRASENLRQEGVRaLILVGLERV 1378
Cdd:smart00327   70 SLS----YKLGGGTnlgaalqyaLENLFSKSAGSRRGAPKVVILITDGESNDGPkDLLKAAKELKRSGVK-VFVVGVGND 144

                    ....*....
gi 240255535   1379 VNLERLMHL 1387
Cdd:smart00327  145 VDEEELKKL 153
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2386-2454 1.34e-03

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


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.17  E-value: 1.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2386 REVQVFEITENSAKLHWERAEPPGP----YFYDLTVTSAHDQSLVLKQNLTVTDRVIGGLLAGQTYHVAVVCY 2454
Cdd:cd00063     5 TNLRVTDVTSTSVTLSWTPPEDDGGpitgYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
 
Name Accession Description Interval E-value
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
828-992 3.24e-89

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 287.68  E-value: 3.24e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  828 ADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPL 907
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  908 NTGKALEFVARNLFVKSAGSRIEDGVPQHLVLVLGGKSQDDVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDPRLVF 987
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160

                  ....*
gi 240255535  988 TVREF 992
Cdd:cd01481   161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
37-201 6.28e-86

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: 278.05  E-value: 6.28e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   37 RDIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSAL 116
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  117 YTGSALDFVRNNLFTSSAGYRAAEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSSLVF 196
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160

                  ....*
gi 240255535  197 IPAEF 201
Cdd:cd01481   161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
625-787 3.60e-83

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 270.35  E-value: 3.60e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  625 RDVVFLIDGSQSAGP-EFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQI 703
Cdd:cd01481     1 KDIVFLIDGSDNVGSgNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  704 NVGNALEYVSRNIFKRPLGSRIEEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTI-ARNADQEELVKISLSPEYVF 782
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIgARNADLAELQQIAFDPSFVF 160

                  ....*
gi 240255535  783 SVSTF 787
Cdd:cd01481   161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
421-584 1.46e-70

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 234.14  E-value: 1.46e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  421 KDVVFLLDGSEGVRS-GFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTP 499
Cdd:cd01481     1 KDIVFLIDGSDNVGSgNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  500 NTGAALEFVLRNILVSSAGSRITEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPDFAV 579
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160

                  ....*
gi 240255535  580 AIPTF 584
Cdd:cd01481   161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
229-392 2.30e-60

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 204.87  E-value: 2.30e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  229 RDILFLFDGSANL-VGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKAL 307
Cdd:cd01481     1 KDIVFLIDGSDNVgSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  308 NLGYALDYAQRYIFVKSAGSRIEDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPAFIL 387
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160

                  ....*
gi 240255535  388 AAESL 392
Cdd:cd01481   161 QVSDF 165
VWA pfam00092
von Willebrand factor type A domain;
829-1001 1.10e-54

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 189.02  E-value: 1.10e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   829 DIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPLN 908
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   909 TGKALEFVARNLFVKSAGSRIedGVPQHLVLVLGGKSQD-DVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDP--RL 985
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARP--GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPgeGH 158
                          170
                   ....*....|....*.
gi 240255535   986 VFTVREFRELPNIEER 1001
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
626-796 6.81e-52

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 180.93  E-value: 6.81e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   626 DVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQIN 704
Cdd:pfam00092    1 DIVFLLDGSGSIGGDnFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   705 VGNALEYVSRNIFKRPLGSRieEGVPQFLVLISSGKSDD-EVDDPAVELKQFGVAPFTIA-RNADQEELVKISLSP--EY 780
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGvGNADDEELRKIASEPgeGH 158
                          170
                   ....*....|....*.
gi 240255535   781 VFSVSTFRELPSLEQK 796
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
38-205 3.23e-51

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 179.01  E-value: 3.23e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    38 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSALY 117
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   118 TGSALDFVRNNLFTSSAGYRaaEGIPKLLVLITGGKSLD-EISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSS--L 194
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158
                          170
                   ....*....|.
gi 240255535   195 VFIPAEFRAAP 205
Cdd:pfam00092  159 VFTVSDFEALE 169
VWA pfam00092
von Willebrand factor type A domain;
422-592 3.49e-51

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 179.01  E-value: 3.49e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   422 DVVFLLDGSEGVR-SGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPN 500
Cdd:pfam00092    1 DIVFLLDGSGSIGgDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   501 TGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGD-DVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPD--F 577
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158
                          170
                   ....*....|....*
gi 240255535   578 AVAIPTFRQLGTVQQ 592
Cdd:pfam00092  159 VFTVSDFEALEDLQD 173
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1428-1764 1.05e-45

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: 172.40  E-value: 1.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1428 KCSGQRGDRGPIGSIGPKGIPGEDGYRgypgdeggpgergppgvnGTQGFQGCPGQRGVKGSRGFPGEKGEVGEIGLDGL 1507
Cdd:NF038329  114 KGDGEKGEPGPAGPAGPAGEQGPRGDR------------------GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1508 DGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGdvgirgdpgnpgqdsqERGPKGETGDLGPMGVPGrdgvPGGPGET 1587
Cdd:NF038329  176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG----------------PAGPDGEAGPAGEDGPAG----PAGDGQQ 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1588 GKnggfgrrgppgakgnKGGPGQPGFEGEQGTRgaqgpagpagppgliGEQGisgprgsggaagapgergRTGPLGRKGE 1667
Cdd:NF038329  236 GP---------------DGDPGPTGEDGPQGPD---------------GPAG------------------KDGPRGDRGE 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1668 PGEPGPKGGIGNRGPRGETGDDGRDG-VGSEGRRGKKGERGFPGYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGP----- 1741
Cdd:NF038329  268 AGPDGPDGKDGERGPVGPAGKDGQNGkDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPktpev 347
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 240255535 1742 -------------PGIVGQKGDPGyPGPAGPKgNRG 1764
Cdd:NF038329  348 pqkpdtaphtpktPQIPGQSKDVT-PAPQNPS-NRG 381
VWA pfam00092
von Willebrand factor type A domain;
1032-1204 2.00e-45

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 162.44  E-value: 2.00e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1032 DIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRHAN 1111
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1112 TKVGLEHLRVNHFVPEAGSRLDqrVPQIAFVITGGKSVE-DAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIASNSA--T 1188
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPG--APKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158
                          170
                   ....*....|....*.
gi 240255535  1189 AFRVGNVQELSELSEQ 1204
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
230-401 6.26e-42

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 152.43  E-value: 6.26e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   230 DILFLFDGSANL-VGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKALN 308
Cdd:pfam00092    1 DIVFLLDGSGSIgGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   309 LGYALDYAQRYIFVKSAGSRIedGVLQFLVLLVAGRSSD-RVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPA--F 385
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARP--GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158
                          170
                   ....*....|....*.
gi 240255535   386 ILAAESLPKIGDLHPQ 401
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
1031-1194 5.45e-41

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 149.36  E-value: 5.45e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1031 ADIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGrha 1110
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGG--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1111 NTKVG--LEHLRVNHFVPEAGSRLDqrVPQIAFVITGGKSVEDAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIAS--NS 1186
Cdd:cd01482    78 NTRTGkaLTHVREKNFTPDAGARPG--VPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASkpSE 155

                  ....*...
gi 240255535 1187 ATAFRVGN 1194
Cdd:cd01482   156 THVFNVAD 163
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
626-793 2.55e-40

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 147.99  E-value: 2.55e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    626 DVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQIN 704
Cdd:smart00327    1 DVVFLLDGSGSMGGNrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    705 VGNALEYVSRNIFKRPLGSRieEGVPQFLVLISSGKSDD---EVDDPAVELKQFGVAPFTIA--RNADQEELVKISLSP- 778
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGvgNDVDEEELKKLASAPg 158
                           170
                    ....*....|....*.
gi 240255535    779 -EYVFSVSTFRELPSL 793
Cdd:smart00327  159 gVYVFLPELLDLLIDL 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
829-998 2.19e-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: 145.29  E-value: 2.19e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    829 DIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPLN 908
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    909 TGKALEFVARNLFVKSAGSRieDGVPQHLVLVLGGKSQD---DVSRFAQVIRSSGIVSLGVG-DRNIDRTELQTITNDPR 984
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGvGNDVDEEELKKLASAPG 158
                           170
                    ....*....|....*.
gi 240255535    985 LV--FTVREFRELPNI 998
Cdd:smart00327  159 GVyvFLPELLDLLIDL 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
38-210 2.19e-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: 145.29  E-value: 2.19e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535     38 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSALY 117
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    118 TGSALDFVRNNLFTSSAGYRaaEGIPKLLVLITGGKSLD---EISQPAQELKRSSIMAFAIG-NKGADQAELEEIAFDSS 193
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGvGNDVDEEELKKLASAPG 158
                           170
                    ....*....|....*..
gi 240255535    194 LVFIPAEFRAAPLQGML 210
Cdd:smart00327  159 GVYVFLPELLDLLIDLL 175
Kunitz_collagen_alpha3_VI cd22629
Kunitz-type domain from the alpha3 chain of human type VI collagen, and similar proteins; This ...
2503-2555 1.98e-38

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


Pssm-ID: 438672  Cd Length: 53  Bit Score: 137.89  E-value: 1.98e-38
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2503 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22629     1 DICKLPKDEGTCRDFVLKWYYDPETKSCARFWYGGCGGNENRFDSQEECEKVC 53
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
422-594 4.82e-36

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: 135.66  E-value: 4.82e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    422 DVVFLLDGSEGVR-SGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPN 500
Cdd:smart00327    1 DVVFLLDGSGSMGgNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    501 TGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGD---DVRNPSVVVKRGGAVPIGIGIGNA-DITEMQTISFIPD 576
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158
                           170
                    ....*....|....*...
gi 240255535    577 FaVAIPTFRQLGTVQQVI 594
Cdd:smart00327  159 G-VYVFLPELLDLLIDLL 175
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
1032-1205 1.01e-32

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 126.03  E-value: 1.01e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   1032 DIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRHAN 1111
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   1112 TKVGLEHLRVNHFVPEAGSRLDqrVPQIAFVITGGKS---VEDAQDVSLALTQRGVKVFAVGVRN-IDSEEVGKIASNSA 1187
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRG--APKVVILITDGESndgPKDLLKAAKELKRSGVKVFVVGVGNdVDEEELKKLASAPG 158
                           170
                    ....*....|....*...
gi 240255535   1188 TAFrVGNVQELSELSEQV 1205
Cdd:smart00327  159 GVY-VFLPELLDLLIDLL 175
VWA pfam00092
von Willebrand factor type A domain;
2012-2199 6.38e-32

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 123.92  E-value: 6.38e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  2012 DMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDpkasqhFARVAVVQHApsesvDNasmppVKVEFSLTDYGSKEKL 2091
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPD------GTRVGLVQYS-----SD-----VRTEFPLNDYSSKEEL 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  2092 VDFLSRGMTQLQGTRALGSAIEYTIENVFESAPNPRDL--KIVVLMLTGEVPEQQLEEaqrVILQAKCKGYFFVVLGIGr 2169
Cdd:pfam00092   65 LSAVDNLRYLGGGTTNTGKALKYALENLFSSAAGARPGapKVVVLLTDGRSQDGDPEE---VARELKSAGVTVFAVGVG- 140
                          170       180       190
                   ....*....|....*....|....*....|
gi 240255535  2170 KVNIKEVYTFASEPNDVFFKLVDKSTELNE 2199
Cdd:pfam00092  141 NADDEELRKIASEPGEGHVFTVSDFEALED 170
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1503-1765 2.45e-31

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 130.03  E-value: 2.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1503 GLDGLDGeDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVGIRGDPGNPGqdsqERGPKGETGDLGPMGVPGRDGVPG 1582
Cdd:NF038329  109 GLQQLKG-DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERG----EKGPAGPQGEAGPQGPAGKDGEAG 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1583 gpgetgknggfgrrgppgAKGNKGGPGQPGFEGEqgtrgaqgpagpagppgligeqgisgprgsggaagapgergrTGPL 1662
Cdd:NF038329  184 ------------------AKGPAGEKGPQGPRGE------------------------------------------TGPA 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1663 GRKGEPGEPGPKGGIGNRGPRGETGDDGRdgvgseGRRGKKGERGfpgypgpkgnpgepglngttgPKGIRGRRGNSGPP 1742
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGD------GQQGPDGDPG---------------------PTGEDGPQGPDGPA 256
                         250       260
                  ....*....|....*....|...
gi 240255535 1743 GIVGQKGDPGYPGPAGPKGNRGD 1765
Cdd:NF038329  257 GKDGPRGDRGEAGPDGPDGKDGE 279
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
230-385 1.42e-30

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 119.87  E-value: 1.42e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    230 DILFLFDGSANLVGQ-FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKALN 308
Cdd:smart00327    1 DVVFLLDGSGSMGGNrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    309 LGYALDYAQRYIFVKSAGSRieDGVLQFLVLLVAGRSSD---RVDGPASNLKQSGVVPFIFQAKNA-DPAELEQIVLSPA 384
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158

                    .
gi 240255535    385 F 385
Cdd:smart00327  159 G 159
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1513-1764 1.65e-30

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: 127.33  E-value: 1.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1513 DKGLPGSSGEkgnpGRRGDKGPRGEKGERGDVGIRGDPGnpgqdsqERGPKGETGDLGPMGVPGRDGVPGGPGETGKngg 1592
Cdd:NF038329  107 DEGLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRG-------ETGPAGPAGPPGPQGERGEKGPAGPQGEAGP--- 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1593 fgrrgppgakgnkggpgqpgfegeqgtrgaqgpagpAGPPGLIGEQGisgprgsggaagAPGERGRTGPLGRKGEPGEPG 1672
Cdd:NF038329  173 ------------------------------------QGPAGKDGEAG------------AKGPAGEKGPQGPRGETGPAG 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1673 PKGGIGNRGPRGETGDD------GRDGVGSEGRRGKKGERGFPGYPGPKGNPGE------PGLNGTTGPKGIRGRRGNSG 1740
Cdd:NF038329  205 EQGPAGPAGPDGEAGPAgedgpaGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKdgprgdRGEAGPDGPDGKDGERGPVG 284
                         250       260
                  ....*....|....*....|....
gi 240255535 1741 PPGIVGQKGDPGYPGPAGPKGNRG 1764
Cdd:NF038329  285 PAGKDGQNGKDGLPGKDGKDGQNG 308
Kunitz_BPTI pfam00014
Kunitz/Bovine pancreatic trypsin inhibitor domain; Indicative of a protease inhibitor, usually ...
2504-2555 3.91e-26

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


Pssm-ID: 425421  Cd Length: 53  Bit Score: 102.72  E-value: 3.91e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 240255535  2504 ICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:pfam00014    1 ICSLPPDSGPCKASIPRWYYNPTTGTCEPFTYGGCGGNANNFESLEECESTC 52
KU smart00131
BPTI/Kunitz family of serine protease inhibitors; Serine protease inhibitors. One member of ...
2503-2555 8.09e-25

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


Pssm-ID: 197529  Cd Length: 53  Bit Score: 98.88  E-value: 8.09e-25
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 240255535   2503 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:smart00131    1 DVCLLPPDTGPCGGSIPRYYYDPETGTCEPFTYGGCGGNANNFESLEECERTC 53
VWA pfam00092
von Willebrand factor type A domain;
1795-1973 1.36e-22

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 96.96  E-value: 1.36e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1795 ELAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIaesnCPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQVaLT 1874
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDI----GPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRY-LG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1875 SKQQSLETAMSFVARNTFKRVRNG-FLMRKVAVFFSNTPTrASPQLREAVLKLSDAGITPLFL-TRQEDRQLINALQiNN 1952
Cdd:pfam00092   76 GGTTNTGKALKYALENLFSSAAGArPGAPKVVVLLTDGRS-QDGDPEEVARELKSAGVTVFAVgVGNADDEELRKIA-SE 153
                          170       180
                   ....*....|....*....|.
gi 240255535  1953 TAVGHALVLPAGRDLTDFLEN 1973
Cdd:pfam00092  154 PGEGHVFTVSDFEALEDLQDQ 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
1796-1936 2.93e-22

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 95.82  E-value: 2.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1796 LAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIAesncPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQvALTS 1875
Cdd:cd01450     3 IVFLLDGSESVGPENFEKVKDFIEKLVEKLDIG----PDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLK-YLGG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240255535 1876 KQQSLETAMSFVARNTFKRVRNGFLMRKVAVFFSNTPTRASPQLREAVLKLSDAGITPLFL 1936
Cdd:cd01450    78 GGTNTGKALQYALEQLFSESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVV 138
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
1796-1971 2.08e-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: 90.98  E-value: 2.08e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   1796 LAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIaesnCPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQVALtS 1875
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDI----GPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKL-G 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   1876 KQQSLETAMSFVARNTFKRVRNGFLM-RKVAVFFSN-TPTRASPQLREAVLKLSDAGITP--LFLTRQEDRQLINALQIN 1951
Cdd:smart00327   77 GGTNLGAALQYALENLFSKSAGSRRGaPKVVILITDgESNDGPKDLLKAAKELKRSGVKVfvVGVGNDVDEEELKKLASA 156
                           170       180
                    ....*....|....*....|
gi 240255535   1952 NTAVGHALVLPAgRDLTDFL 1971
Cdd:smart00327  157 PGGVYVFLPELL-DLLIDLL 175
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
2011-2188 4.20e-20

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 89.27  E-value: 4.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 2011 IDMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDPkasqhfARVAVVQHAPSesvdnasmppVKVEFSLTDYGSKEK 2090
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDK------TRVGLVQYSDD----------VRVEFSLNDYKSKDD 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 2091 LVDFLsRGMTQLQGTR-ALGSAIEYTIENVF-ESAPNPRDLKIVVLMLTGEvpEQQLEEAQRVILQAKCKGYFFVVLGIG 2168
Cdd:cd01450    65 LLKAV-KNLKYLGGGGtNTGKALQYALEQLFsESNARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVG 141
                         170       180
                  ....*....|....*....|
gi 240255535 2169 rKVNIKEVYTFASEPNDVFF 2188
Cdd:cd01450   142 -PADEEELREIASCPSERHV 160
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
2012-2201 1.05e-19

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 88.67  E-value: 1.05e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   2012 DMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDpkasqhFARVAVVQHApsesvDNasmppVKVEFSLTDYGSKEKL 2091
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPD------GDRVGLVTFS-----DD-----ARVLFPLNDSRSKDAL 64
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   2092 VDFLSRGMTQLQGTRALGSAIEYTIENVFESAPNPR-DLKIVVLMLTGEVPEQQLEEAQRVILQAKCKGYFFVVLGIGRK 2170
Cdd:smart00327   65 LEALASLSYKLGGGTNLGAALQYALENLFSKSAGSRrGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGND 144
                           170       180       190
                    ....*....|....*....|....*....|.
gi 240255535   2171 VNIKEVYTFASEPNDVFFKLVDKSTELNEEP 2201
Cdd:smart00327  145 VDEEELKKLASAPGGVYVFLPELLDLLIDLL 175
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1710-1764 7.29e-16

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 73.68  E-value: 7.29e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 240255535  1710 GYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAGPKGNRG 1764
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1468-1758 4.63e-13

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 74.30  E-value: 4.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1468 PPGVNGTQGFQGCpgqrgvKGSRGFPGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVGIR 1547
Cdd:COG5164    11 PSDPGGVTTPAGS------QGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1548 GDPGN--PGQDSQERGPKGETGDLGPMGVPGRDGVPGGPGETGKNGGFGRRGPPGAKGNKGGPGQPGFEGEQGTRgaqgp 1625
Cdd:COG5164    85 QNQGGtrPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPP----- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1626 agpagppgliGEQGISGPRGSGGAAGAPGERGRTGPlGRKGEPGEPGPKGGIGNRGPRGETGDDGrdgvgsegrrgkkge 1705
Cdd:COG5164   160 ----------GDGGSTTPPGPGGSTTPPDDGGSTTP-PNKGETGTDIPTGGTPRQGPDGPVKKDD--------------- 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535 1706 rgfpgyPGPKGNPgEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAG 1758
Cdd:COG5164   214 ------KNGKGNP-PDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTA 259
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1701-1769 4.28e-12

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 71.09  E-value: 4.28e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240255535 1701 GKKGERGFPGYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAGPKGNRGDSIDQ 1769
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
609-775 9.97e-11

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 64.96  E-value: 9.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  609 LQPVLQPLPSPGVGGKRDVVFLID--GSQSAGPEFQYVRTLIERLVDYLDvgfDTTRVAVIQFSDDPKVefLLNAHSSKD 686
Cdd:COG1240    77 LALALAPLALARPQRGRDVVLVVDasGSMAAENRLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEV--LLPLTRDRE 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  687 EVQNAVQRLRPKGGRQInvGNALeYVSRNIFKrplgsRIEEGVPQFLVLISSGKSDDEVDDP---AVELKQFGVAPFTIA 763
Cdd:COG1240   152 ALKRALDELPPGGGTPL--GDAL-ALALELLK-----RADPARRKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIG 223
                         170
                  ....*....|....*
gi 240255535  764 ---RNADQEELVKIS 775
Cdd:COG1240   224 vgtEAVDEGLLREIA 238
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
1231-1387 2.09e-09

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 59.01  E-value: 2.09e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   1231 DVILGFDGSRDqnvfVAQKGFESKVDAILNRISQMHRvscsggRSPTVRVSVVAnTPSGPVEAFDFDEYQ--PEMLEKFR 1308
Cdd:smart00327    1 DVVFLLDGSGS----MGGNRFELAKEFVLKLVEQLDI------GPDGDRVGLVT-FSDDARVLFPLNDSRskDALLEALA 69
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   1309 NMRsqhpYVLTEDT---------LKVYLNKFRQSSPDSVKVVIHFTDGADGDLA-DLHRASENLRQEGVRaLILVGLERV 1378
Cdd:smart00327   70 SLS----YKLGGGTnlgaalqyaLENLFSKSAGSRRGAPKVVILITDGESNDGPkDLLKAAKELKRSGVK-VFVVGVGND 144

                    ....*....
gi 240255535   1379 VNLERLMHL 1387
Cdd:smart00327  145 VDEEELKKL 153
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
812-1002 2.14e-08

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 57.64  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  812 LLASTRYPPPAVESDAADIVFLIDSSeG--VRPDGFAHIRDFVSRIVRRLnigPSKVRVGVVQFSNDVFPEFYLKTYRSQ 889
Cdd:COG1240    77 LALALAPLALARPQRGRDVVLVVDAS-GsmAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTRDREA 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  890 apVLDAIRRLRLRGGSPLntGKALEfVARNLFvksagSRIEDGVPQHLVLVLGGK---SQDDVSRFAQVIRSSGI--VSL 964
Cdd:COG1240   153 --LKRALDELPPGGGTPL--GDALA-LALELL-----KRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIriYTI 222
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 240255535  965 GVGDRNIDRTELQTI---TNDPrlVFTVREFRELPNIEERI 1002
Cdd:COG1240   223 GVGTEAVDEGLLREIaeaTGGR--YFRADDLSELAAIYREI 261
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
1010-1201 6.79e-08

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 56.49  E-value: 6.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1010 AATPAPPGVDTPPPSRPEKKKADIVFLLD--GSINfRRDSFQEVLRFVSEIVDTvYEDGDsiQVGLVQYNSDPtdeFFLK 1087
Cdd:COG1240    72 VLLLLLALALAPLALARPQRGRDVVLVVDasGSMA-AENRLEAAKGALLDFLDD-YRPRD--RVGLVAFGGEA---EVLL 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1088 DFST-KRQIIDAINKVVYKGGrhanT------KVGLEHLRvnhfvpeagsRLDQRVPQIAFVITGGK---SVEDAQDVSL 1157
Cdd:COG1240   145 PLTRdREALKRALDELPPGGG----TplgdalALALELLK----------RADPARRKVIVLLTDGRdnaGRIDPLEAAE 210
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 240255535 1158 ALTQRGVKVFAVGV--RNIDSEEVGKIASNS-ATAFRVGNVQELSEL 1201
Cdd:COG1240   211 LAAAAGIRIYTIGVgtEAVDEGLLREIAEATgGRYFRADDLSELAAI 257
PHA03169 PHA03169
hypothetical protein; Provisional
1475-1612 1.58e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 53.05  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1475 QGFQGCPGQRGVKGSRGFPGEKGEVGEIGLD---------GLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVG 1545
Cdd:PHA03169   89 QGGPSGSGSESVGSPTPSPSGSAEELASGLSpentsgsspESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQ 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1546 IRG----DPGNPG----QDSQERGPKGETGDLGPMGV-----PGRDGVPGGPGETGKNGGFGRRGPPGAKGNKG-GPGQP 1611
Cdd:PHA03169  169 PSHedspEEPEPPtsepEPDSPGPPQSETPTSSPPPQsppdePGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEReGPPFP 248

                  .
gi 240255535 1612 G 1612
Cdd:PHA03169  249 G 249
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
37-189 2.32e-06

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 51.48  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   37 RDIVFLVDGS-SALGLANFN----AIRDFIAKVIQRLEIGqdLIqvAVAQYADTVRPefyfnthPT--KREVITAVRKMK 109
Cdd:COG1240    93 RDVVLVVDASgSMAAENRLEaakgALLDFLDDYRPRDRVG--LV--AFGGEAEVLLP-------LTrdREALKRALDELP 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  110 PLDGSALYTG--SALDFVRnnlftssagyRAAEGIPKLLVLITGGK---SLDEISQPAQELKRSSIMAFAI--GNKGADQ 182
Cdd:COG1240   162 PGGGTPLGDAlaLALELLK----------RADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIgvGTEAVDE 231

                  ....*..
gi 240255535  183 AELEEIA 189
Cdd:COG1240   232 GLLREIA 238
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
1477-1759 1.30e-05

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


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 50.38  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1477 FQGCPGQrGVKGSRGFPGEKGEvgeigldgldGEDGDKGLPGSSGekGNPGRRGDKGPRGEKGERGdvgirgdPGNPGQD 1556
Cdd:cd21118   121 WQGSGGH-GAYGSQGGPGVQGH----------GIPGGTGGPWASG--GNYGTNSLGGSVGQGGNGG-------PLNYGTN 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1557 SQ----------ERGPKGETGDLGPmgvPGRDGVPGGpgetgknggfgrrgppgakGNKGGPGQPGFEGEQGTRGAQGPA 1626
Cdd:cd21118   181 SQgavaqpgygtVRGNNQNSGCTNP---PPSGSHESF-------------------SNSGGSSSSGSSGSQGSHGSNGQG 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1627 GPAGPpgliGEQGISGPRGSGGAAGAPGERGRTGPLGRKGEPGEPGPKGGIGNRGPRGETGDDGrdgvGSEGRRGKKger 1706
Cdd:cd21118   239 SSGSS----GGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSSGGSG----GSGGGNKPE--- 307
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240255535 1707 gfPGYPGPK-GNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAGP 1759
Cdd:cd21118   308 --CNNPGNDvRMAGGGGSQGSKESSGSHGSNGGNGQAEAVGGLNTLNSDASTLP 359
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
1230-1384 1.34e-05

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 47.67  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1230 LDVILGFDGSRDqnvfVAQKGFESKVDAILNRISQMHrvscSGGRSptVRVSVVANTPSGPVEaFDFDEYQ--PEMLEKF 1307
Cdd:cd01450     1 LDIVFLLDGSES----VGPENFEKVKDFIEKLVEKLD----IGPDK--TRVGLVQYSDDVRVE-FSLNDYKskDDLLKAV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1308 RNMRSQ-HPYVLTEDTLKV---YLNKFRQSSPDSVKVVIHFTDGADGDLADLHRASENLRQEGVrALILVGLERVV--NL 1381
Cdd:cd01450    70 KNLKYLgGGGTNTGKALQYaleQLFSESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGI-KVFVVGVGPADeeEL 148

                  ...
gi 240255535 1382 ERL 1384
Cdd:cd01450   149 REI 151
VWA pfam00092
von Willebrand factor type A domain;
1231-1384 2.35e-04

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 44.19  E-value: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1231 DVILGFDGSRDqnvfVAQKGFESKVDAILNRISQMhrvscsgGRSP-TVRVSVV--ANTPsgpVEAFDFDEYQ--PEMLE 1305
Cdd:pfam00092    1 DIVFLLDGSGS----IGGDNFEKVKEFLKKLVESL-------DIGPdGTRVGLVqySSDV---RTEFPLNDYSskEELLS 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1306 KFRNMRSQ-HPYVLTEDTLK-VYLNKFRQSS---PDSVKVVIHFTDGADGDLaDLHRASENLRQEGVRaLILVGLERVVN 1380
Cdd:pfam00092   67 AVDNLRYLgGGTTNTGKALKyALENLFSSAAgarPGAPKVVVLLTDGRSQDG-DPEEVARELKSAGVT-VFAVGVGNADD 144

                   ....*.
gi 240255535  1381 --LERL 1384
Cdd:pfam00092  145 eeLRKI 150
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
413-572 4.13e-04

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 44.54  E-value: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  413 APAPVSGEKDVVFLLD--GSEGVRSGFPLLKEFVQRVVESLdvgQDRVRVAVVQYSDRTRPEFYLNSymNKQDVVNAVRQ 490
Cdd:COG1240    85 ALARPQRGRDVVLVVDasGSMAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTR--DREALKRALDE 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  491 LTLLGGpTPnTGAALEfvlrniLVSSAGSRITEGVPQLLIVLT---ADRSGDDVRNPSVVVKRGGA--VPIGIGIGNADI 565
Cdd:COG1240   160 LPPGGG-TP-LGDALA------LALELLKRADPARRKVIVLLTdgrDNAGRIDPLEAAELAAAAGIriYTIGVGTEAVDE 231

                  ....*..
gi 240255535  566 TEMQTIS 572
Cdd:COG1240   232 GLLREIA 238
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2386-2454 1.34e-03

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.17  E-value: 1.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2386 REVQVFEITENSAKLHWERAEPPGP----YFYDLTVTSAHDQSLVLKQNLTVTDRVIGGLLAGQTYHVAVVCY 2454
Cdd:cd00063     5 TNLRVTDVTSTSVTLSWTPPEDDGGpitgYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
 
Name Accession Description Interval E-value
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
828-992 3.24e-89

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 287.68  E-value: 3.24e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  828 ADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPL 907
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  908 NTGKALEFVARNLFVKSAGSRIEDGVPQHLVLVLGGKSQDDVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDPRLVF 987
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160

                  ....*
gi 240255535  988 TVREF 992
Cdd:cd01481   161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
37-201 6.28e-86

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: 278.05  E-value: 6.28e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   37 RDIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSAL 116
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  117 YTGSALDFVRNNLFTSSAGYRAAEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSSLVF 196
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160

                  ....*
gi 240255535  197 IPAEF 201
Cdd:cd01481   161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
625-787 3.60e-83

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 270.35  E-value: 3.60e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  625 RDVVFLIDGSQSAGP-EFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQI 703
Cdd:cd01481     1 KDIVFLIDGSDNVGSgNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  704 NVGNALEYVSRNIFKRPLGSRIEEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTI-ARNADQEELVKISLSPEYVF 782
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIgARNADLAELQQIAFDPSFVF 160

                  ....*
gi 240255535  783 SVSTF 787
Cdd:cd01481   161 QVSDF 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
421-584 1.46e-70

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 234.14  E-value: 1.46e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  421 KDVVFLLDGSEGVRS-GFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTP 499
Cdd:cd01481     1 KDIVFLIDGSDNVGSgNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  500 NTGAALEFVLRNILVSSAGSRITEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPDFAV 579
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160

                  ....*
gi 240255535  580 AIPTF 584
Cdd:cd01481   161 QVSDF 165
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
828-992 1.65e-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: 1.65e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  828 ADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGsPL 907
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGG-GT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  908 NTGKALEFVARNLFVKSagSRIEDGVPQHLVLVLGGKSQDDVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDP--RL 985
Cdd:cd01472    80 NTGKALKYVRENLFTEA--SGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDPkeLY 157

                  ....*..
gi 240255535  986 VFTVREF 992
Cdd:cd01472   158 VFNVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
37-201 4.80e-62

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


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 209.78  E-value: 4.80e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   37 RDIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLdGSAL 116
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYI-GGGT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  117 YTGSALDFVRNNLFTSSAgyRAAEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIAFD--SSL 194
Cdd:cd01472    80 NTGKALKYVRENLFTEAS--GSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDpkELY 157

                  ....*..
gi 240255535  195 VFIPAEF 201
Cdd:cd01472   158 VFNVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
625-787 8.92e-62

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


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 209.01  E-value: 8.92e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  625 RDVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGrQI 703
Cdd:cd01472     1 ADIVFLVDGSESIGLSnFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGG-GT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  704 NVGNALEYVSRNIFKRPlgSRIEEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTIA-RNADQEELVKISLSP--EY 780
Cdd:cd01472    80 NTGKALKYVRENLFTEA--SGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGvKNADEEELKQIASDPkeLY 157

                  ....*..
gi 240255535  781 VFSVSTF 787
Cdd:cd01472   158 VFNVADF 164
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
229-392 2.30e-60

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 204.87  E-value: 2.30e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  229 RDILFLFDGSANL-VGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKAL 307
Cdd:cd01481     1 KDIVFLIDGSDNVgSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  308 NLGYALDYAQRYIFVKSAGSRIEDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPAFIL 387
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160

                  ....*
gi 240255535  388 AAESL 392
Cdd:cd01481   161 QVSDF 165
VWA pfam00092
von Willebrand factor type A domain;
829-1001 1.10e-54

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 189.02  E-value: 1.10e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   829 DIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPLN 908
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   909 TGKALEFVARNLFVKSAGSRIedGVPQHLVLVLGGKSQD-DVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDP--RL 985
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARP--GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPgeGH 158
                          170
                   ....*....|....*.
gi 240255535   986 VFTVREFRELPNIEER 1001
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
421-575 2.29e-52

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


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 182.04  E-value: 2.29e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  421 KDVVFLLDGSEGV-RSGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTp 499
Cdd:cd01472     1 ADIVFLVDGSESIgLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGT- 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240255535  500 NTGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIP 575
Cdd:cd01472    80 NTGKALKYVRENLFTEASGSR--EGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDP 153
VWA pfam00092
von Willebrand factor type A domain;
626-796 6.81e-52

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 180.93  E-value: 6.81e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   626 DVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQIN 704
Cdd:pfam00092    1 DIVFLLDGSGSIGGDnFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   705 VGNALEYVSRNIFKRPLGSRieEGVPQFLVLISSGKSDD-EVDDPAVELKQFGVAPFTIA-RNADQEELVKISLSP--EY 780
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGvGNADDEELRKIASEPgeGH 158
                          170
                   ....*....|....*.
gi 240255535   781 VFSVSTFRELPSLEQK 796
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
VWA pfam00092
von Willebrand factor type A domain;
38-205 3.23e-51

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 179.01  E-value: 3.23e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    38 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSALY 117
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   118 TGSALDFVRNNLFTSSAGYRaaEGIPKLLVLITGGKSLD-EISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSS--L 194
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158
                          170
                   ....*....|.
gi 240255535   195 VFIPAEFRAAP 205
Cdd:pfam00092  159 VFTVSDFEALE 169
VWA pfam00092
von Willebrand factor type A domain;
422-592 3.49e-51

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 179.01  E-value: 3.49e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   422 DVVFLLDGSEGVR-SGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPN 500
Cdd:pfam00092    1 DIVFLLDGSGSIGgDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   501 TGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGD-DVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPD--F 577
Cdd:pfam00092   81 TGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158
                          170
                   ....*....|....*
gi 240255535   578 AVAIPTFRQLGTVQQ 592
Cdd:pfam00092  159 VFTVSDFEALEDLQD 173
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
38-201 8.87e-46

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: 163.23  E-value: 8.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   38 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMkPLDGSALY 117
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNL-PYKGGNTR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  118 TGSALDFVRNNLFTSSAGYRaaEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSSL--V 195
Cdd:cd01482    81 TGKALTHVREKNFTPDAGAR--PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSEthV 158

                  ....*.
gi 240255535  196 FIPAEF 201
Cdd:cd01482   159 FNVADF 164
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1428-1764 1.05e-45

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: 172.40  E-value: 1.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1428 KCSGQRGDRGPIGSIGPKGIPGEDGYRgypgdeggpgergppgvnGTQGFQGCPGQRGVKGSRGFPGEKGEVGEIGLDGL 1507
Cdd:NF038329  114 KGDGEKGEPGPAGPAGPAGEQGPRGDR------------------GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1508 DGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGdvgirgdpgnpgqdsqERGPKGETGDLGPMGVPGrdgvPGGPGET 1587
Cdd:NF038329  176 AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAG----------------PAGPDGEAGPAGEDGPAG----PAGDGQQ 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1588 GKnggfgrrgppgakgnKGGPGQPGFEGEQGTRgaqgpagpagppgliGEQGisgprgsggaagapgergRTGPLGRKGE 1667
Cdd:NF038329  236 GP---------------DGDPGPTGEDGPQGPD---------------GPAG------------------KDGPRGDRGE 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1668 PGEPGPKGGIGNRGPRGETGDDGRDG-VGSEGRRGKKGERGFPGYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGP----- 1741
Cdd:NF038329  268 AGPDGPDGKDGERGPVGPAGKDGQNGkDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPktpev 347
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 240255535 1742 -------------PGIVGQKGDPGyPGPAGPKgNRG 1764
Cdd:NF038329  348 pqkpdtaphtpktPQIPGQSKDVT-PAPQNPS-NRG 381
VWA pfam00092
von Willebrand factor type A domain;
1032-1204 2.00e-45

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 162.44  E-value: 2.00e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1032 DIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRHAN 1111
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1112 TKVGLEHLRVNHFVPEAGSRLDqrVPQIAFVITGGKSVE-DAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIASNSA--T 1188
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPG--APKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158
                          170
                   ....*....|....*.
gi 240255535  1189 AFRVGNVQELSELSEQ 1204
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
38-193 1.15e-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: 1.15e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   38 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSALY 117
Cdd:cd01450     2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGTN 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240255535  118 TGSALDFVRNNLFTSSagyRAAEGIPKLLVLITGGKSLD--EISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSS 193
Cdd:cd01450    82 TGKALQYALEQLFSES---NARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
828-992 1.95e-43

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 156.29  E-value: 1.95e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  828 ADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPl 907
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  908 NTGKALEFVARNLFVKSAGSRieDGVPQHLVLVLGGKSQDDVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDPRL-- 985
Cdd:cd01482    80 RTGKALTHVREKNFTPDAGAR--PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPSEth 157

                  ....*..
gi 240255535  986 VFTVREF 992
Cdd:cd01482   158 VFNVADF 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
626-782 2.75e-43

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 155.91  E-value: 2.75e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  626 DVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQIN 704
Cdd:cd01450     2 DIVFLLDGSESVGPEnFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGTN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  705 VGNALEYVSRNIFKrplGSRIEEGVPQFLVLISSGKSDDEVD--DPAVELKQFGVAPFTIA-RNADQEELVKISLSP--E 779
Cdd:cd01450    82 TGKALQYALEQLFS---ESNARENVPKVIIVLTDGRSDDGGDpkEAAAKLKDEGIKVFVVGvGPADEEELREIASCPseR 158

                  ...
gi 240255535  780 YVF 782
Cdd:cd01450   159 HVF 161
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
229-383 3.08e-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: 3.08e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  229 RDILFLFDGSANlVGQ--FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKtGKA 306
Cdd:cd01472     1 ADIVFLVDGSES-IGLsnFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYI-GGG 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240255535  307 LNLGYALDYAQRYIFVKSagSRIEDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSP 383
Cdd:cd01472    79 TNTGKALKYVRENLFTEA--SGSREGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDP 153
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
828-983 3.83e-43

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 155.53  E-value: 3.83e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  828 ADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPL 907
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240255535  908 NTGKALEFVARNLFVKsagSRIEDGVPQHLVLVLGGKSQD--DVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDP 983
Cdd:cd01450    81 NTGKALQYALEQLFSE---SNARENVPKVIIVLTDGRSDDggDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCP 155
VWA pfam00092
von Willebrand factor type A domain;
230-401 6.26e-42

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 152.43  E-value: 6.26e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   230 DILFLFDGSANL-VGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKALN 308
Cdd:pfam00092    1 DIVFLLDGSGSIgGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   309 LGYALDYAQRYIFVKSAGSRIedGVLQFLVLLVAGRSSD-RVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPA--F 385
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARP--GAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGegH 158
                          170
                   ....*....|....*.
gi 240255535   386 ILAAESLPKIGDLHPQ 401
Cdd:pfam00092  159 VFTVSDFEALEDLQDQ 174
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
1031-1194 5.45e-41

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 149.36  E-value: 5.45e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1031 ADIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGrha 1110
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGG--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1111 NTKVG--LEHLRVNHFVPEAGSRLDqrVPQIAFVITGGKSVEDAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIAS--NS 1186
Cdd:cd01482    78 NTRTGkaLTHVREKNFTPDAGARPG--VPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASkpSE 155

                  ....*...
gi 240255535 1187 ATAFRVGN 1194
Cdd:cd01482   156 THVFNVAD 163
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
626-793 2.55e-40

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 147.99  E-value: 2.55e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    626 DVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQIN 704
Cdd:smart00327    1 DVVFLLDGSGSMGGNrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    705 VGNALEYVSRNIFKRPLGSRieEGVPQFLVLISSGKSDD---EVDDPAVELKQFGVAPFTIA--RNADQEELVKISLSP- 778
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGvgNDVDEEELKKLASAPg 158
                           170
                    ....*....|....*.
gi 240255535    779 -EYVFSVSTFRELPSL 793
Cdd:smart00327  159 gVYVFLPELLDLLIDL 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
422-576 3.26e-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: 147.05  E-value: 3.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  422 DVVFLLDGSEGVRS-GFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPN 500
Cdd:cd01450     2 DIVFLLDGSESVGPeNFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGTN 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240255535  501 TGAALEFVLRNILVSSAGSritEGVPQLLIVLTADRS--GDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPD 576
Cdd:cd01450    82 TGKALQYALEQLFSESNAR---ENVPKVIIVLTDGRSddGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
626-787 1.24e-39

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 145.51  E-value: 1.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  626 DVVFLIDGSQSAG-PEFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQiN 704
Cdd:cd01482     2 DIVFLVDGSWSIGrSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT-R 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  705 VGNALEYVSRNIFKRPLGSRieEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTIA-RNADQEELVKISLSP--EYV 781
Cdd:cd01482    81 TGKALTHVREKNFTPDAGAR--PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGvKDADESELKMIASKPseTHV 158

                  ....*.
gi 240255535  782 FSVSTF 787
Cdd:cd01482   159 FNVADF 164
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
829-998 2.19e-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: 145.29  E-value: 2.19e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    829 DIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPLN 908
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    909 TGKALEFVARNLFVKSAGSRieDGVPQHLVLVLGGKSQD---DVSRFAQVIRSSGIVSLGVG-DRNIDRTELQTITNDPR 984
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGvGNDVDEEELKKLASAPG 158
                           170
                    ....*....|....*.
gi 240255535    985 LV--FTVREFRELPNI 998
Cdd:smart00327  159 GVyvFLPELLDLLIDL 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
38-210 2.19e-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: 145.29  E-value: 2.19e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535     38 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSALY 117
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    118 TGSALDFVRNNLFTSSAGYRaaEGIPKLLVLITGGKSLD---EISQPAQELKRSSIMAFAIG-NKGADQAELEEIAFDSS 193
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGvGNDVDEEELKKLASAPG 158
                           170
                    ....*....|....*..
gi 240255535    194 LVFIPAEFRAAPLQGML 210
Cdd:smart00327  159 GVYVFLPELLDLLIDLL 175
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
422-576 4.08e-39

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 143.97  E-value: 4.08e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  422 DVVFLLDGSEGV-RSGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTpN 500
Cdd:cd01482     2 DIVFLVDGSWSIgRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT-R 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240255535  501 TGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPD 576
Cdd:cd01482    81 TGKALTHVREKNFTPDAGAR--PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPS 154
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
1031-1192 8.08e-39

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: 143.23  E-value: 8.08e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1031 ADIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRHA 1110
Cdd:cd01481     1 KDIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1111 NTKVGLEHLRVNHFVPEAGSRLDQRVPQIAFVITGGKSVEDAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIASNSATAF 1190
Cdd:cd01481    81 NTGSALDYVVKNLFTKSAGSRIEEGVPQFLVLITGGKSQDDVERPAVALKRAGIVPFAIGARNADLAELQQIAFDPSFVF 160

                  ..
gi 240255535 1191 RV 1192
Cdd:cd01481   161 QV 162
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
1031-1198 1.73e-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: 1.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1031 ADIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGrha 1110
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGG--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1111 NTKVG--LEHLRVNHFVPEAGSRLDqrVPQIAFVITGGKSVEDAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIASnSAT 1188
Cdd:cd01472    78 GTNTGkaLKYVRENLFTEASGSREG--VPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIAS-DPK 154
                         170
                  ....*....|
gi 240255535 1189 AFRVGNVQEL 1198
Cdd:cd01472   155 ELYVFNVADF 164
Kunitz_collagen_alpha3_VI cd22629
Kunitz-type domain from the alpha3 chain of human type VI collagen, and similar proteins; This ...
2503-2555 1.98e-38

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


Pssm-ID: 438672  Cd Length: 53  Bit Score: 137.89  E-value: 1.98e-38
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2503 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22629     1 DICKLPKDEGTCRDFVLKWYYDPETKSCARFWYGGCGGNENRFDSQEECEKVC 53
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
422-594 4.82e-36

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: 135.66  E-value: 4.82e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    422 DVVFLLDGSEGVR-SGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPN 500
Cdd:smart00327    1 DVVFLLDGSGSMGgNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    501 TGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGD---DVRNPSVVVKRGGAVPIGIGIGNA-DITEMQTISFIPD 576
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158
                           170
                    ....*....|....*...
gi 240255535    577 FaVAIPTFRQLGTVQQVI 594
Cdd:smart00327  159 G-VYVFLPELLDLLIDLL 175
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
1031-1184 1.59e-34

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 130.87  E-value: 1.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1031 ADIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRHA 1110
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240255535 1111 NTKVGLEHLRVNHFVPeagSRLDQRVPQIAFVITGGKS--VEDAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIAS 1184
Cdd:cd01450    81 NTGKALQYALEQLFSE---SNARENVPKVIIVLTDGRSddGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIAS 153
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
230-383 7.92e-34

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 128.95  E-value: 7.92e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  230 DILFLFDGSANlVGQ--FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKAL 307
Cdd:cd01450     2 DIVFLLDGSES-VGPenFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240255535  308 NLGYALDYAQRYIFVKsagSRIEDGVLQFLVLLVAGRSSDRVDG--PASNLKQSGVVPFIFQAKNADPAELEQIVLSP 383
Cdd:cd01450    81 NTGKALQYALEQLFSE---SNARENVPKVIIVLTDGRSDDGGDPkeAAAKLKDEGIKVFVVGVGPADEEELREIASCP 155
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
1032-1205 1.01e-32

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 126.03  E-value: 1.01e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   1032 DIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRHAN 1111
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   1112 TKVGLEHLRVNHFVPEAGSRLDqrVPQIAFVITGGKS---VEDAQDVSLALTQRGVKVFAVGVRN-IDSEEVGKIASNSA 1187
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRG--APKVVILITDGESndgPKDLLKAAKELKRSGVKVFVVGVGNdVDEEELKKLASAPG 158
                           170
                    ....*....|....*...
gi 240255535   1188 TAFrVGNVQELSELSEQV 1205
Cdd:smart00327  159 GVY-VFLPELLDLLIDLL 175
VWA pfam00092
von Willebrand factor type A domain;
2012-2199 6.38e-32

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 123.92  E-value: 6.38e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  2012 DMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDpkasqhFARVAVVQHApsesvDNasmppVKVEFSLTDYGSKEKL 2091
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPD------GTRVGLVQYS-----SD-----VRTEFPLNDYSSKEEL 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  2092 VDFLSRGMTQLQGTRALGSAIEYTIENVFESAPNPRDL--KIVVLMLTGEVPEQQLEEaqrVILQAKCKGYFFVVLGIGr 2169
Cdd:pfam00092   65 LSAVDNLRYLGGGTTNTGKALKYALENLFSSAAGARPGapKVVVLLTDGRSQDGDPEE---VARELKSAGVTVFAVGVG- 140
                          170       180       190
                   ....*....|....*....|....*....|
gi 240255535  2170 KVNIKEVYTFASEPNDVFFKLVDKSTELNE 2199
Cdd:pfam00092  141 NADDEELRKIASEPGEGHVFTVSDFEALED 170
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
827-1006 8.79e-32

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 125.19  E-value: 8.79e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  827 AADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLR-LRGGS 905
Cdd:cd01475     2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEyLETGT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  906 plNTGKALEFVARNLFVKSAGSR-IEDGVPQHLVLVLGGKSQDDVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDP- 983
Cdd:cd01475    82 --MTGLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEPl 159
                         170       180
                  ....*....|....*....|....
gi 240255535  984 -RLVFTVREFRELPNIEERIMNSF 1006
Cdd:cd01475   160 aDHVFYVEDFSTIEELTKKFQGKI 183
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
38-189 2.09e-31

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 124.03  E-value: 2.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   38 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLdGSALY 117
Cdd:cd01475     4 DLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL-ETGTM 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240255535  118 TGSALDFVRNNLFTSSAGYR-AAEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIA 189
Cdd:cd01475    83 TGLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIA 155
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1503-1765 2.45e-31

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 130.03  E-value: 2.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1503 GLDGLDGeDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVGIRGDPGNPGqdsqERGPKGETGDLGPMGVPGRDGVPG 1582
Cdd:NF038329  109 GLQQLKG-DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERG----EKGPAGPQGEAGPQGPAGKDGEAG 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1583 gpgetgknggfgrrgppgAKGNKGGPGQPGFEGEqgtrgaqgpagpagppgligeqgisgprgsggaagapgergrTGPL 1662
Cdd:NF038329  184 ------------------AKGPAGEKGPQGPRGE------------------------------------------TGPA 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1663 GRKGEPGEPGPKGGIGNRGPRGETGDDGRdgvgseGRRGKKGERGfpgypgpkgnpgepglngttgPKGIRGRRGNSGPP 1742
Cdd:NF038329  204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGD------GQQGPDGDPG---------------------PTGEDGPQGPDGPA 256
                         250       260
                  ....*....|....*....|...
gi 240255535 1743 GIVGQKGDPGYPGPAGPKGNRGD 1765
Cdd:NF038329  257 GKDGPRGDRGEAGPDGPDGKDGE 279
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
230-385 1.42e-30

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 119.87  E-value: 1.42e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    230 DILFLFDGSANLVGQ-FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKALN 308
Cdd:smart00327    1 DVVFLLDGSGSMGGNrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    309 LGYALDYAQRYIFVKSAGSRieDGVLQFLVLLVAGRSSD---RVDGPASNLKQSGVVPFIFQAKNA-DPAELEQIVLSPA 384
Cdd:smart00327   81 LGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDgpkDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLASAPG 158

                    .
gi 240255535    385 F 385
Cdd:smart00327  159 G 159
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1513-1764 1.65e-30

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: 127.33  E-value: 1.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1513 DKGLPGSSGEkgnpGRRGDKGPRGEKGERGDVGIRGDPGnpgqdsqERGPKGETGDLGPMGVPGRDGVPGGPGETGKngg 1592
Cdd:NF038329  107 DEGLQQLKGD----GEKGEPGPAGPAGPAGEQGPRGDRG-------ETGPAGPAGPPGPQGERGEKGPAGPQGEAGP--- 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1593 fgrrgppgakgnkggpgqpgfegeqgtrgaqgpagpAGPPGLIGEQGisgprgsggaagAPGERGRTGPLGRKGEPGEPG 1672
Cdd:NF038329  173 ------------------------------------QGPAGKDGEAG------------AKGPAGEKGPQGPRGETGPAG 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1673 PKGGIGNRGPRGETGDD------GRDGVGSEGRRGKKGERGFPGYPGPKGNPGE------PGLNGTTGPKGIRGRRGNSG 1740
Cdd:NF038329  205 EQGPAGPAGPDGEAGPAgedgpaGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKdgprgdRGEAGPDGPDGKDGERGPVG 284
                         250       260
                  ....*....|....*....|....
gi 240255535 1741 PPGIVGQKGDPGYPGPAGPKGNRG 1764
Cdd:NF038329  285 PAGKDGQNGKDGLPGKDGKDGQNG 308
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
230-384 8.70e-30

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 117.39  E-value: 8.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  230 DILFLFDGSANlVGQ--FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKAl 307
Cdd:cd01482     2 DIVFLVDGSWS-IGRsnFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNT- 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240255535  308 NLGYALDYAQRYIFVKSAGSRieDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPA 384
Cdd:cd01482    80 RTGKALTHVREKNFTPDAGAR--PGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIASKPS 154
Kunitz_collagen_alpha6_VI cd22630
Kunitz-type domain from the alpha6 chain of human type VI collagen, and similar proteins; This ...
2503-2555 1.89e-29

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


Pssm-ID: 438673  Cd Length: 55  Bit Score: 112.31  E-value: 1.89e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2503 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22630     1 DACSLDQDEGECQNYVLKWYYDQEQKECSQFWYGGCGGNKNRFETQEECEALC 53
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
422-571 9.00e-28

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 113.63  E-value: 9.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  422 DVVFLLDGSEGVR-SGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTpN 500
Cdd:cd01475     4 DLVFLIDSSRSVRpENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGT-M 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240255535  501 TGAALEFVLRNILVSSAGSR-ITEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTI 571
Cdd:cd01475    83 TGLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREI 154
Kunitz_papilin_lacunin-like cd22639
Drosophila melanogaster Kunitz domain 1, Manduca sexta lacunin Kunitz domain 1, and simialr ...
2505-2555 3.94e-27

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


Pssm-ID: 438681  Cd Length: 52  Bit Score: 105.73  E-value: 3.94e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240255535 2505 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22639     1 CSLPKDRGPCRNYTVKWYFDMAYGGCSRFWYGGCGGNGNRFDTEEECKAVC 51
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
626-797 2.05e-26

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 109.78  E-value: 2.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  626 DVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKgGRQIN 704
Cdd:cd01475     4 DLVFLIDSSRSVRPEnFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL-ETGTM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  705 VGNALEYVSRNIFKRPLGSR-IEEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTIA-RNADQEELVKISLSP--EY 780
Cdd:cd01475    83 TGLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGvGRADEEELREIASEPlaDH 162
                         170
                  ....*....|....*..
gi 240255535  781 VFSVSTFRELPSLEQKL 797
Cdd:cd01475   163 VFYVEDFSTIEELTKKF 179
Kunitz_BPTI pfam00014
Kunitz/Bovine pancreatic trypsin inhibitor domain; Indicative of a protease inhibitor, usually ...
2504-2555 3.91e-26

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


Pssm-ID: 425421  Cd Length: 53  Bit Score: 102.72  E-value: 3.91e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 240255535  2504 ICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:pfam00014    1 ICSLPPDSGPCKASIPRWYYNPTTGTCEPFTYGGCGGNANNFESLEECESTC 52
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
1029-1184 4.30e-26

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 108.63  E-value: 4.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1029 KKADIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKgGR 1108
Cdd:cd01475     1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL-ET 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240255535 1109 HANTKVGLEHLRVNHFVPEAGSR-LDQRVPQIAFVITGGKSVEDAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIAS 1184
Cdd:cd01475    80 GTMTGLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIAS 156
Kunitz_papilin cd22635
Kunitz domain of papilin, and similar proteins; This model includes the Kunitz domain found in ...
2505-2555 1.37e-25

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


Pssm-ID: 438678  Cd Length: 52  Bit Score: 101.18  E-value: 1.37e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 240255535 2505 CKLPKDEGT-CRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22635     1 CLLDKDAGTvCGDYVQRWYYDPATGACNRFWYGGCGGNANRFATEAECLRTC 52
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
829-998 1.76e-25

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 105.52  E-value: 1.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  829 DIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPlN 908
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLT-N 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  909 TGKALEFVARNLFVKSAGSRieDGVPQHLVLVLGGKSQDDvSRFAQVIRSS---GIV--SLGVGD---RNIDRTELQTIT 980
Cdd:cd01469    81 TATAIQYVVTELFSESNGAR--KDATKVLVVITDGESHDD-PLLKDVIPQAereGIIryAIGVGGhfqRENSREELKTIA 157
                         170       180
                  ....*....|....*....|
gi 240255535  981 NDP--RLVFTVREFRELPNI 998
Cdd:cd01469   158 SKPpeEHFFNVTDFAALKDI 177
Kunitz-type cd00109
Kunitz/Bovine pancreatic trypsin inhibitor (BPTI) domain; This family contains the Kunitz ...
2505-2555 2.75e-25

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


Pssm-ID: 438633  Cd Length: 51  Bit Score: 100.32  E-value: 2.75e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240255535 2505 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd00109     1 CLLPPDPGPCRAYFPRWYYNSETGQCEEFIYGGCGGNANNFETKEECEATC 51
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
828-988 2.84e-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: 104.40  E-value: 2.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  828 ADIVFLIDSSEGVRpDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDV--FPEFYLKTYRSQAPVLDAIRRLRLRGGS 905
Cdd:cd01476     1 LDLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGrqRVRFNLPKHNDGEELLEKVDNLRFIGGT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  906 PlNTGKALEFvARNLFVKSAGSRieDGVPQHLVLVLGGKSQDDVSRFAQVIRS---SGIVSLGVGDR-NIDRTELQTITN 981
Cdd:cd01476    80 T-ATGAAIEV-ALQQLDPSEGRR--EGIPKVVVVLTDGRSHDDPEKQARILRAvpnIETFAVGTGDPgTVDTEELHSITG 155

                  ....*..
gi 240255535  982 DPRLVFT 988
Cdd:cd01476   156 NEDHIFT 162
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
625-784 2.93e-25

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 104.18  E-value: 2.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  625 RDVVFLIDGSQSAGPE-FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQI 703
Cdd:cd00198     1 ADIVFLLDVSGSMGGEkLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  704 NVGNALEYVSRNIFKRPLGSRieegvPQFLVLISSGKSDD---EVDDPAVELKQFGVAPFTIA--RNADQEELVKISLSP 778
Cdd:cd00198    81 NIGAALRLALELLKSAKRPNA-----RRVIILLTDGEPNDgpeLLAEAARELRKLGITVYTIGigDDANEDELKEIADKT 155

                  ....*.
gi 240255535  779 EYVFSV 784
Cdd:cd00198   156 TGGAVF 161
Kunitz_collagen_alpha1_XXVIII cd22628
Kunitz-type domain from the alpha1 chain of type XXVIII collagen, and similar proteins; This ...
2505-2555 6.76e-25

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


Pssm-ID: 438671  Cd Length: 51  Bit Score: 99.28  E-value: 6.76e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240255535 2505 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22628     1 CLEPLDPGPCREYVVKWYYDKQANSCAQFWYGGCEGNRNRFETEEECRKTC 51
KU smart00131
BPTI/Kunitz family of serine protease inhibitors; Serine protease inhibitors. One member of ...
2503-2555 8.09e-25

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


Pssm-ID: 197529  Cd Length: 53  Bit Score: 98.88  E-value: 8.09e-25
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 240255535   2503 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:smart00131    1 DVCLLPPDTGPCGGSIPRYYYDPETGTCEPFTYGGCGGNANNFESLEECERTC 53
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
38-188 6.07e-24

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 100.89  E-value: 6.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   38 DIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSAlY 117
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLT-N 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240255535  118 TGSALDFVRNNLFTSSAGYRaaEGIPKLLVLITGGKSLD--EISQPAQELKRSSIMAFAIGNKGADQAE--LEEI 188
Cdd:cd01469    81 TATAIQYVVTELFSESNGAR--KDATKVLVVITDGESHDdpLLKDVIPQAEREGIIRYAIGVGGHFQREnsREEL 153
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
421-551 3.78e-23

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 98.24  E-value: 3.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  421 KDVVFLLDGSEGVRSGFPLLKEFVQRVVESLDVGQDRVRVAVVQYS--DRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPT 498
Cdd:cd01476     1 LDLLFVLDSSGSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535  499 pNTGAALEFVLrNILVSSAGSRitEGVPQLLIVLTADRSGDDVRNPSVVVKRG 551
Cdd:cd01476    81 -ATGAAIEVAL-QQLDPSEGRR--EGIPKVVVVLTDGRSHDDPEKQARILRAV 129
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
626-793 5.02e-23

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 98.58  E-value: 5.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  626 DVVFLIDGSQSAGP-EFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQiN 704
Cdd:cd01469     2 DIVFVLDGSGSIYPdDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLT-N 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  705 VGNALEYVSRNIFKRPLGSRieEGVPQFLVLISSGKSDDEVDDPAV--ELKQFGVAPFTIA------RNADQEELVKISL 776
Cdd:cd01469    81 TATAIQYVVTELFSESNGAR--KDATKVLVVITDGESHDDPLLKDVipQAEREGIIRYAIGvgghfqRENSREELKTIAS 158
                         170
                  ....*....|....*....
gi 240255535  777 SP--EYVFSVSTFRELPSL 793
Cdd:cd01469   159 KPpeEHFFNVTDFAALKDI 177
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
828-983 8.78e-23

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: 97.25  E-value: 8.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  828 ADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPL 907
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  908 NTGKALEFVARNLFvksagSRIEDGVPQHLVLVLGGKSQDD---VSRFAQVIRSSGI--VSLGVGDRNiDRTELQTITND 982
Cdd:cd00198    81 NIGAALRLALELLK-----SAKRPNARRVIILLTDGEPNDGpelLAEAARELRKLGItvYTIGIGDDA-NEDELKEIADK 154

                  .
gi 240255535  983 P 983
Cdd:cd00198   155 T 155
VWA pfam00092
von Willebrand factor type A domain;
1795-1973 1.36e-22

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 96.96  E-value: 1.36e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1795 ELAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIaesnCPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQVaLT 1874
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDI----GPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRY-LG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1875 SKQQSLETAMSFVARNTFKRVRNG-FLMRKVAVFFSNTPTrASPQLREAVLKLSDAGITPLFL-TRQEDRQLINALQiNN 1952
Cdd:pfam00092   76 GGTTNTGKALKYALENLFSSAAGArPGAPKVVVLLTDGRS-QDGDPEEVARELKSAGVTVFAVgVGNADDEELRKIA-SE 153
                          170       180
                   ....*....|....*....|.
gi 240255535  1953 TAVGHALVLPAGRDLTDFLEN 1973
Cdd:pfam00092  154 PGEGHVFTVSDFEALEDLQDQ 174
Kunitz_TFPI2_1-like cd22616
Kunitz domain 1 (KD1) of tissue factor pathway inhibitor 2 (TFPI2) and similar proteins; This ...
2502-2555 1.86e-22

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


Pssm-ID: 438659  Cd Length: 57  Bit Score: 92.30  E-value: 1.86e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240255535 2502 TDICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22616     2 AEICLLPPDEGPCRALIPRYYYDRYTQTCREFSYGGCEGNANNFESLEDCEKTC 55
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
1796-1936 2.93e-22

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 95.82  E-value: 2.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1796 LAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIAesncPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQvALTS 1875
Cdd:cd01450     3 IVFLLDGSESVGPENFEKVKDFIEKLVEKLDIG----PDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLK-YLGG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240255535 1876 KQQSLETAMSFVARNTFKRVRNGFLMRKVAVFFSNTPTRASPQLREAVLKLSDAGITPLFL 1936
Cdd:cd01450    78 GGTNTGKALQYALEQLFSESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVV 138
Kunitz_collagen_alpha6_VI-like cd22631
Kunitz-type domain from the alpha6 chain of fish type VI collagen, and similar proteins; This ...
2505-2555 2.93e-22

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


Pssm-ID: 438674 [Multi-domain]  Cd Length: 51  Bit Score: 91.52  E-value: 2.93e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240255535 2505 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22631     1 CLLGQDAGSCQNYTMMWFFDSKQGRCSRFWYGGCGGNANRFETQEECENLC 51
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
1032-1201 3.62e-22

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 95.89  E-value: 3.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1032 DIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRhAN 1111
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGL-TN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1112 TKVGLEHLRVNHFVPEAGSRLDqrVPQIAFVITGGKSVEDA--QDVSLALTQRGVKVFAVGV-----RNIDSEEVGKIAS 1184
Cdd:cd01469    81 TATAIQYVVTELFSESNGARKD--ATKVLVVITDGESHDDPllKDVIPQAEREGIIRYAIGVgghfqRENSREELKTIAS 158
                         170
                  ....*....|....*....
gi 240255535 1185 NSATA--FRVGNVQELSEL 1201
Cdd:cd01469   159 KPPEEhfFNVTDFAALKDI 177
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
422-576 1.15e-21

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 94.34  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  422 DVVFLLDGSEGVR-SGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTpN 500
Cdd:cd01469     2 DIVFVLDGSGSIYpDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLT-N 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  501 TGAALEFVLRNILVSSAGSRitEGVPQLLIVLTADRSGDDVRNPSVV--VKRGGAVPIGIGIGNA-----DITEMQTISF 573
Cdd:cd01469    81 TATAIQYVVTELFSESNGAR--KDATKVLVVITDGESHDDPLLKDVIpqAEREGIIRYAIGVGGHfqrenSREELKTIAS 158

                  ...
gi 240255535  574 IPD 576
Cdd:cd01469   159 KPP 161
Kunitz_papilin_mig6-like cd22637
Drosophila melanogaster Kunitz domains 5, 6, 7, and Caenorhabditis elegans Kunitz domain 5 of ...
2505-2555 2.09e-21

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


Pssm-ID: 438679  Cd Length: 51  Bit Score: 89.34  E-value: 2.09e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240255535 2505 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22637     1 CDQPKDTGPCDNWVLKWYYDSKKGSCRQFYYGGCGGNDNRFDTEEECEARC 51
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
37-189 5.03e-21

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: 92.24  E-value: 5.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   37 RDIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSAL 116
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240255535  117 YTGSALDFVRNNLFTssagyRAAEGIPKLLVLITGGKSLD---EISQPAQELKRSSIMAFAIG-NKGADQAELEEIA 189
Cdd:cd00198    81 NIGAALRLALELLKS-----AKRPNARRVIILLTDGEPNDgpeLLAEAARELRKLGITVYTIGiGDDANEDELKEIA 152
Kunitz_HAI1_2-like cd22624
Kunitz domain 2 of hepatocyte growth factor activator inhibitor-1 (HAI1); This model includes ...
2505-2555 5.65e-21

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


Pssm-ID: 438667  Cd Length: 61  Bit Score: 88.34  E-value: 5.65e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240255535 2505 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22624     2 CTEPPVTGPCRASFTRWYYDPLSRKCHRFTYGGCDGNENNFETEDECMETC 52
Kunitz_collagen_alpha1_VII cd22627
Kunitz-type domain from the alpha1 chain of type VII collagen, and similar proteins; This ...
2503-2555 6.53e-21

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


Pssm-ID: 438670  Cd Length: 53  Bit Score: 88.07  E-value: 6.53e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2503 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22627     1 DPCLLPMDEGSCSDYTLLWYYHQKAGECRPFVYGGCGGNANRFSSKEDCELRC 53
Kunitz_amblin-like cd22638
Caenorhabditis elegans Kunitz domain 11 of papilin (also called abnormal cell migration ...
2505-2555 8.48e-21

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


Pssm-ID: 438680  Cd Length: 51  Bit Score: 87.44  E-value: 8.48e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240255535 2505 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22638     1 CTLKPETGPCRAYIEKWYYDPSTQSCKTFIYGGCGGNGNRFDSEEDCQETC 51
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
1796-1971 2.08e-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: 90.98  E-value: 2.08e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   1796 LAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIaesnCPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQVALtS 1875
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDI----GPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKL-G 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   1876 KQQSLETAMSFVARNTFKRVRNGFLM-RKVAVFFSN-TPTRASPQLREAVLKLSDAGITP--LFLTRQEDRQLINALQIN 1951
Cdd:smart00327   77 GGTNLGAALQYALENLFSKSAGSRRGaPKVVILITDgESNDGPKDLLKAAKELKRSGVKVfvVGVGNDVDEEELKKLASA 156
                           170       180
                    ....*....|....*....|
gi 240255535   1952 NTAVGHALVLPAgRDLTDFL 1971
Cdd:smart00327  157 PGGVYVFLPELL-DLLIDLL 175
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
422-572 2.60e-20

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 89.93  E-value: 2.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  422 DVVFLLDGSEGVRSG-FPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPN 500
Cdd:cd00198     2 DIVFLLDVSGSMGGEkLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGTN 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240255535  501 TGAALEFVLRNILvssagSRITEGVPQLLIVLT---ADRSGDDVRNPSVVVKRGGAVPIGIGIGN-ADITEMQTIS 572
Cdd:cd00198    82 IGAALRLALELLK-----SAKRPNARRVIILLTdgePNDGPELLAEAARELRKLGITVYTIGIGDdANEDELKEIA 152
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
2011-2188 4.20e-20

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 89.27  E-value: 4.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 2011 IDMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDPkasqhfARVAVVQHAPSesvdnasmppVKVEFSLTDYGSKEK 2090
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDK------TRVGLVQYSDD----------VRVEFSLNDYKSKDD 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 2091 LVDFLsRGMTQLQGTR-ALGSAIEYTIENVF-ESAPNPRDLKIVVLMLTGEvpEQQLEEAQRVILQAKCKGYFFVVLGIG 2168
Cdd:cd01450    65 LLKAV-KNLKYLGGGGtNTGKALQYALEQLFsESNARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVG 141
                         170       180
                  ....*....|....*....|
gi 240255535 2169 rKVNIKEVYTFASEPNDVFF 2188
Cdd:cd01450   142 -PADEEELREIASCPSERHV 160
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
38-198 8.74e-20

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 88.61  E-value: 8.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   38 DIVFLVDGSSALGlANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYA--DTVRPEFYFNTHPTKREVITAVRKMKPLDGSA 115
Cdd:cd01476     2 DLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSgrGRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  116 lYTGSALDFVrNNLFTSSAGYRaaEGIPKLLVLITGGKSLDEISQPAQELKR---SSIMAFAIGNKGA-DQAELEEIAFD 191
Cdd:cd01476    81 -ATGAAIEVA-LQQLDPSEGRR--EGIPKVVVVLTDGRSHDDPEKQARILRAvpnIETFAVGTGDPGTvDTEELHSITGN 156

                  ....*..
gi 240255535  192 SSLVFIP 198
Cdd:cd01476   157 EDHIFTD 163
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
2012-2201 1.05e-19

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 88.67  E-value: 1.05e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   2012 DMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDpkasqhFARVAVVQHApsesvDNasmppVKVEFSLTDYGSKEKL 2091
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPD------GDRVGLVTFS-----DD-----ARVLFPLNDSRSKDAL 64
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   2092 VDFLSRGMTQLQGTRALGSAIEYTIENVFESAPNPR-DLKIVVLMLTGEVPEQQLEEAQRVILQAKCKGYFFVVLGIGRK 2170
Cdd:smart00327   65 LEALASLSYKLGGGTNLGAALQYALENLFSKSAGSRrGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGND 144
                           170       180       190
                    ....*....|....*....|....*....|.
gi 240255535   2171 VNIKEVYTFASEPNDVFFKLVDKSTELNEEP 2201
Cdd:smart00327  145 VDEEELKKLASAPGGVYVFLPELLDLLIDLL 175
Kunitz_actitoxin-like cd22633
Kunitz-type actitoxins such as Anemonia viridis U-actitoxin-Avd3l, and similar proteins; This ...
2504-2555 1.97e-18

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


Pssm-ID: 438676  Cd Length: 55  Bit Score: 81.04  E-value: 1.97e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 240255535 2504 ICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22633     4 ICLLPKDVGGCRARFPRYYYNSSTRRCEKFRYGGCGGNANNFHTLEECEKVC 55
Kunitz_boophilin_2-like cd22600
second Kunitz domain of Rhipicephalus microplus boophilin and similar proteins; This group ...
2505-2557 3.89e-18

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


Pssm-ID: 438643  Cd Length: 54  Bit Score: 80.16  E-value: 3.89e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2505 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVCAP 2557
Cdd:cd22600     2 CKPAAESGLCAAYLERWFFNVTTGACETFVYGGCGGNANNYKSQEECELACLR 54
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
626-782 3.91e-18

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 83.99  E-value: 3.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  626 DVVFLIDGSQSAGPEFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPK--VEFLLNAHSSKDEVQNAVQRLRPKGGrQI 703
Cdd:cd01476     2 DLLFVLDSSGSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGG-TT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  704 NVGNALEYVSrNIFKRPLGSRieEGVPQFLVLISSGKSDDEVDDPAVELK-QFGVAPFTIAR----NADQEELVKISLSP 778
Cdd:cd01476    81 ATGAAIEVAL-QQLDPSEGRR--EGIPKVVVVLTDGRSHDDPEKQARILRaVPNIETFAVGTgdpgTVDTEELHSITGNE 157

                  ....
gi 240255535  779 EYVF 782
Cdd:cd01476   158 DHIF 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
1031-1189 5.25e-18

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: 83.38  E-value: 5.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1031 ADIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRHA 1110
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1111 NTKVGLEHLRVNHFvpeagSRLDQRVPQIAFVITGGKS---VEDAQDVSLALTQRGVKVFAVGVRN-IDSEEVGKIASNS 1186
Cdd:cd00198    81 NIGAALRLALELLK-----SAKRPNARRVIILLTDGEPndgPELLAEAARELRKLGITVYTIGIGDdANEDELKEIADKT 155

                  ...
gi 240255535 1187 ATA 1189
Cdd:cd00198   156 TGG 158
Kunitz_eppin cd22611
Kunitz domain of epididymal protease inhibitor eppin and similar proteins; This subfamily ...
2503-2555 1.18e-17

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


Pssm-ID: 438654  Cd Length: 57  Bit Score: 78.99  E-value: 1.18e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2503 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22611     1 DVCSLPKESGPCMAYFPRWWYDKETNTCSKFIYGGCQGNNNNFQSEAICQNIC 53
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
230-383 2.08e-17

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 83.59  E-value: 2.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  230 DILFLFDGSANLVGQ-FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMK-IKTGKAl 307
Cdd:cd01475     4 DLVFLIDSSRSVRPEnFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEyLETGTM- 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240255535  308 nLGYALDYAQRYIFVKSAGSR-IEDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSP 383
Cdd:cd01475    83 -TGLAIQYAMNNAFSEAEGARpGSERVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGRADEEELREIASEP 158
Kunitz_boophilin_1-like cd22599
first Kunitz domain of Rhipicephalus microplus boophilin and similar proteins; This group ...
2504-2556 3.80e-17

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


Pssm-ID: 438642  Cd Length: 61  Bit Score: 77.51  E-value: 3.80e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2504 ICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVCA 2556
Cdd:cd22599     5 ICRLPADEGICRALIPRFYFNTETGQCTEFIYGGCGGNENNFETIEECEKACG 57
Kunitz_SCI-I-like cd22634
chymotrypsin inhibitor SCI-I_III-like; This model includes the Kunitz-type chymotrypsin ...
2504-2555 4.29e-17

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


Pssm-ID: 438677  Cd Length: 57  Bit Score: 77.17  E-value: 4.29e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 240255535 2504 ICKLP-----KDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22634     1 ICGQPhslggGDGISCFAYIPSWSYNPDKNECEEFIYGGCGGNDNRFSTKAECEQKC 57
Kunitz_huwentoxin cd22598
Kunitz-type toxin huwentoxin-XI; This model contains Kunitz-type serine protease inhibitor ...
2503-2556 6.45e-17

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


Pssm-ID: 438641  Cd Length: 53  Bit Score: 76.57  E-value: 6.45e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240255535 2503 DICKLPKDEGTCRDFILKWYYDPNTksCARFWYGGCGGNENKFGSQKECEKVCA 2556
Cdd:cd22598     1 DTCRLPSDRGRCKASFERWYFNGRT--CAKFIYGGCGGNDNKFPTQEACMKRCA 52
Kunitz_TFPI1_2-like cd22614
Kunitz protease inhibitor (KPI) domain 2 (KPI-2 or K2) of tissue factor pathway inhibitor ...
2503-2555 8.70e-17

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


Pssm-ID: 438657  Cd Length: 56  Bit Score: 76.20  E-value: 8.70e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2503 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22614     3 DFCFLEEDPGICRGLITRYFYNNQSKQCERFKYGGCLGNQNNFESLEECQNTC 55
Kunitz_TFPI1_TFPI2_3-like cd22615
Kunitz protease inhibitor (KPI) domain 3 (KPI-3 or K3) of tissue factor pathway inhibitor ...
2504-2555 1.02e-16

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


Pssm-ID: 438658  Cd Length: 54  Bit Score: 76.18  E-value: 1.02e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 240255535 2504 ICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22615     3 FCLSPKDEGLCSASVTRYYYNSATKTCEPFNYTGCGGNNNNFTSKKDCLRVC 54
Kunitz_textilinin-like cd22594
venom Kunitz-type proteins such as textilinin, BF9 and PILP; This group includes toxins ...
2505-2556 1.21e-16

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


Pssm-ID: 438637  Cd Length: 56  Bit Score: 75.82  E-value: 1.21e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 240255535 2505 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVCA 2556
Cdd:cd22594     5 CELPADPGPCNAYKPAFYYNPASHKCLEFIYGGCGGNANNFKTIDECHRTCA 56
Kunitz_bikunin_2-like cd22597
second Kunitz domain of bikunin and similar proteins; This subfamily includes the C-terminal ...
2503-2555 2.18e-16

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


Pssm-ID: 438640  Cd Length: 55  Bit Score: 75.11  E-value: 2.18e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2503 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22597     2 AACRLPIVPGPCKGFVDLWAFDAVQGKCVPFSYGGCQGNGNKFYSEKECEEYC 54
Kunitz_WFIKKN_2-like cd22606
second Kunitz domain of WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing proteins; ...
2504-2555 5.16e-16

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


Pssm-ID: 438649  Cd Length: 53  Bit Score: 73.93  E-value: 5.16e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 240255535 2504 ICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22606     1 ICSLPAVQGPCKAWEPRWAYNSLLKQCQSFVYGGCEGNENNFESKEACEDAC 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1710-1764 7.29e-16

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 73.68  E-value: 7.29e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 240255535  1710 GYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAGPKGNRG 1764
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Kunitz_SmCI_3-like cd22603
third Kunitz domain of Carboxypeptidase Inhibitor SmCI and similar domains; This group ...
2503-2555 1.24e-15

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


Pssm-ID: 438646  Cd Length: 53  Bit Score: 72.85  E-value: 1.24e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2503 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22603     1 EDCLLPSETGPCKGSFPRYYYDKETGKCKEFIYGGCQGNANNFETKEECERAC 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1707-1763 2.62e-15

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 72.14  E-value: 2.62e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 240255535  1707 GFPGYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAGPKGNR 1763
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Kunitz_PPTI-like cd22608
Pseudocerastes persicus trypsin inhibitor (PPTI), Kunitz-type serine protease inhibitor ...
2503-2555 3.35e-15

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


Pssm-ID: 438651  Cd Length: 54  Bit Score: 71.56  E-value: 3.35e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2503 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22608     2 KFCYLPADPGPCKAYIPRFYYNSASNKCQQFIYGGCKGNANNFETKDECRYTC 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1704-1759 3.37e-15

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 71.76  E-value: 3.37e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 240255535  1704 GERGFPGYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAGP 1759
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Kunitz_conkunitzin cd22593
conkunitzin-S1 and -S2, and similar proteins; This model includes Kunitz-type conkunitzin-S1 ...
2505-2555 4.61e-15

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


Pssm-ID: 438636  Cd Length: 51  Bit Score: 71.10  E-value: 4.61e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240255535 2505 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22593     1 CSLPLDEGSGNSSLTRWYYDPKKGQCKPFTYKGKGGNENNFLTKEDCEETC 51
Kunitz_ELP-like cd22632
early lactation protein (ELP), colostrum trypsin inhibitor (CTI), and similar proteins; This ...
2503-2555 7.93e-15

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


Pssm-ID: 438675  Cd Length: 55  Bit Score: 70.54  E-value: 7.93e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2503 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22632     2 SLCQLPPARGPCRSNILRYFYNSTSRECEPFIYGGCNGNANNFETVEMCLRTC 54
Kunitz_HAI1_1-like cd22623
Kunitz domain 1 of hepatocyte growth factor activator inhibitor-1 (HAI-1); This model includes ...
2505-2558 9.77e-15

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


Pssm-ID: 438666  Cd Length: 59  Bit Score: 70.65  E-value: 9.77e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240255535 2505 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVCAPV 2558
Cdd:cd22623     6 CLAPKKVGPCRGSFPRWHYNAASGKCEEFVFGGCKGNKNNYLSEEECLSACRGV 59
Kunitz_TFPI1_1-like cd22613
Kunitz protease inhibitor (KPI) domain 1 (KPI-1 or K1) of tissue factor pathway inhibitor ...
2504-2555 2.18e-14

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


Pssm-ID: 438656  Cd Length: 55  Bit Score: 69.31  E-value: 2.18e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 240255535 2504 ICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22613     3 FCAFKADDGPCKAIMKRFFFNIFTRQCEEFIYGGCEGNENRFETLEECKKTC 54
Kunitz_BmTI-like cd22604
Kunitz-type serine protease inhibitor 6 (BmTI-6), A (BmTI-A), and similar proteins; This group ...
2500-2555 3.99e-14

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


Pssm-ID: 438647 [Multi-domain]  Cd Length: 56  Bit Score: 68.63  E-value: 3.99e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 240255535 2500 TETDICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22604     1 DFEKQCSPTADSGPCFAYFPMWWYNVKTGQCEEFIYGGCQGNDNRYETEEECEKTC 56
Kunitz_ABPP-like cd22607
Kunitz domain found in the amyloid-beta precursor protein (ABPP) subfamily; This subfamily ...
2504-2555 5.19e-14

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


Pssm-ID: 438650  Cd Length: 52  Bit Score: 68.22  E-value: 5.19e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 240255535 2504 ICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22607     1 VCSEQAETGPCRAMMPRWYFDVTEGKCAPFIYGGCGGNRNNFESEEYCMAVC 52
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
229-380 5.33e-14

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 71.83  E-value: 5.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  229 RDILFLFDGSANLVGQ-FPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKAL 307
Cdd:cd00198     1 ADIVFLLDVSGSMGGEkLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240255535  308 NLGYALDYAQRYIFvksagSRIEDGVLQFLVLLVAGRSSDRVDGP---ASNLKQSGVVPFIFQAKN-ADPAELEQIV 380
Cdd:cd00198    81 NIGAALRLALELLK-----SAKRPNARRVIILLTDGEPNDGPELLaeaARELRKLGITVYTIGIGDdANEDELKEIA 152
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
2011-2196 6.47e-14

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 73.57  E-value: 6.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 2011 IDMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDPkasqhfARVAVVQHAPSesvdnasmppVKVEFSLTDYGSKEK 2090
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDA------TRVGLVQYSST----------VKQEFPLGRFKSKAD 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 2091 LVDFLSRGMTQLQGTRAlGSAIEYTIENVFESA----PNPRDLKIVVLMLTGEVPEQQLEEAQRvilQAKCKGYFFVVLG 2166
Cdd:cd01475    67 LKRAVRRMEYLETGTMT-GLAIQYAMNNAFSEAegarPGSERVPRVGIVVTDGRPQDDVSEVAA---KARALGIEMFAVG 142
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 240255535 2167 IGRkVNIKEVYTFASEPND--VF----FKLVDKSTE 2196
Cdd:cd01475   143 VGR-ADEEELREIASEPLAdhVFyvedFSTIEELTK 177
Kunitz_HAI2_1-like cd22621
Kunitz-type domain 1 (KD1) of hepatocyte growth factor activator inhibitor type 2 (HAI-2), and ...
2503-2555 7.18e-14

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


Pssm-ID: 438664  Cd Length: 53  Bit Score: 67.88  E-value: 7.18e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2503 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22621     1 DFCHLPKVVGRCRASFPRWWYNATSQSCQEFIFGGCKGNLNNFLSEQECLQKC 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1698-1754 9.13e-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: 9.13e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 240255535  1698 GRRGKKGERGFPGYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYP 1754
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Kunitz_ixolaris_2 cd22626
Kunitz-type domain 2 (K2) of Ixolaris, and similar proteins; This model includes the second ...
2505-2555 9.41e-14

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


Pssm-ID: 438669  Cd Length: 51  Bit Score: 67.49  E-value: 9.41e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240255535 2505 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22626     1 CSLELDYGVGKAYIPRWYFNTSNARCEMFIFGGIGGNKNNFETLEECKKTC 51
Kunitz_KTT cd22620
scorpion venom Kunitz-type toxin (KTT) such as LmKTT-1a, BmKTT-1, and BmKTT-2; This model ...
2505-2557 1.58e-13

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


Pssm-ID: 438663  Cd Length: 58  Bit Score: 67.21  E-value: 1.58e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2505 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVCAP 2557
Cdd:cd22620     3 CQLPSDTGRGKASFTRYYYNEESGKCETFIYGGVGGNSNNFLTKEDCCKECAQ 55
Kunitz_SmCI_1-like cd22601
first Kunitz domain of Carboxypeptidase Inhibitor SmCI and similar domains; This group ...
2503-2556 2.58e-13

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


Pssm-ID: 438644  Cd Length: 55  Bit Score: 66.37  E-value: 2.58e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240255535 2503 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVCA 2556
Cdd:cd22601     2 DVCDLPADRGPCTAYIPRWFYNKTTKKCEKFVYGGCQGNKNRFETKDDCLANCG 55
Kunitz_HAI2_2-like cd22622
Kunitz-type domain 2 (KD2) of hepatocyte growth factor activator inhibitor type 2 (HAI-2), and ...
2505-2555 3.11e-13

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


Pssm-ID: 438665  Cd Length: 53  Bit Score: 66.23  E-value: 3.11e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240255535 2505 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22622     3 CAAPRVTGPCRAAFPRWYYDPESQSCKEFIYGGCRGNKNNYLSEEECMDRC 53
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1468-1758 4.63e-13

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 74.30  E-value: 4.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1468 PPGVNGTQGFQGCpgqrgvKGSRGFPGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVGIR 1547
Cdd:COG5164    11 PSDPGGVTTPAGS------QGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1548 GDPGN--PGQDSQERGPKGETGDLGPMGVPGRDGVPGGPGETGKNGGFGRRGPPGAKGNKGGPGQPGFEGEQGTRgaqgp 1625
Cdd:COG5164    85 QNQGGtrPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPP----- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1626 agpagppgliGEQGISGPRGSGGAAGAPGERGRTGPlGRKGEPGEPGPKGGIGNRGPRGETGDDGrdgvgsegrrgkkge 1705
Cdd:COG5164   160 ----------GDGGSTTPPGPGGSTTPPDDGGSTTP-PNKGETGTDIPTGGTPRQGPDGPVKKDD--------------- 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535 1706 rgfpgyPGPKGNPgEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAG 1758
Cdd:COG5164   214 ------KNGKGNP-PDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTA 259
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
422-558 4.79e-13

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 69.72  E-value: 4.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  422 DVVFLLDGSEGV-RSGFPLLKEFVQRVVESL------DVGQDRVRVAVVQYSDRTRPEF-YLNSYMNKQDVVNAVRQLTL 493
Cdd:cd01480     4 DITFVLDSSESVgLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLEY 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240255535  494 LGGPTpNTGAALEFVLRNILVSSAGsriteGVPQLLIVLTADRS-GDDVRNPSVVVKRGGAVPIGI 558
Cdd:cd01480    84 IGGGT-FTDCALKYATEQLLEGSHQ-----KENKFLLVITDGHSdGSPDGGIEKAVNEADHLGIKI 143
Kunitz_TFPI2_2-like cd22617
Kunitz domain 2 (KD2) of tissue factor pathway inhibitor 2 (TFPI2) and similar proteins; This ...
2503-2555 6.34e-13

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


Pssm-ID: 438660  Cd Length: 54  Bit Score: 65.10  E-value: 6.34e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2503 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22617     2 KVCREVPDEGPCRALITRYFYNMTSMRCEEFTYGGCYGNGNNFRDKSSCISAC 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1695-1757 7.31e-13

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 65.21  E-value: 7.31e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240255535  1695 GSEGRRGKKGERGFPGYPGPKGNPGEPglngttGPKGIRGRRGNSGPPGIVGQKGDPGYPGPA 1757
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPP------GPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Kunitz_dendrotoxin cd22595
dendrotoxins I, K, B and similar proteins; This group includes toxins isolated from snake ...
2505-2555 7.36e-13

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


Pssm-ID: 438638  Cd Length: 56  Bit Score: 65.15  E-value: 7.36e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240255535 2505 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22595     4 CKLPVRPGPCKAFISAFYYNWKAKKCHPFTYSGCGGNANRFKTIEECRRTC 54
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
2011-2202 7.45e-13

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 68.92  E-value: 7.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 2011 IDMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMspDPKASQhfarVAVVQHAPSesvdnasmppVKVEFSLTDYGSKEK 2090
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDI--GPTKTQ----FGLVQYSES----------FRTEFTLNEYRTKEE 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 2091 lVDFLSRGMTQLQGTRALGSAIEYTIENVF--ESAPNPRDLKIVVLMLTGEVPEQQLEEAqrVILQAKCKGYFFVVLGIG 2168
Cdd:cd01469    65 -PLSLVKHISQLLGLTNTATAIQYVVTELFseSNGARKDATKVLVVITDGESHDDPLLKD--VIPQAEREGIIRYAIGVG 141
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 240255535 2169 ----RKVNIKEVYTFASEPNDVFFKLVDkstelNEEPL 2202
Cdd:cd01469   142 ghfqRENSREELKTIASKPPEEHFFNVT-----DFAAL 174
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1506-1565 1.87e-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: 64.05  E-value: 1.87e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1506 GLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVGIRGDPGNPGQDsqerGPKGE 1565
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP----GAPGP 56
Kunitz_SmCI_2-like cd22602
second Kunitz domain of Carboxypeptidase Inhibitor SmCI and similar domains; This group ...
2505-2555 2.15e-12

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


Pssm-ID: 438645  Cd Length: 51  Bit Score: 63.71  E-value: 2.15e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240255535 2505 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22602     1 CSLPSKVGPCRVSARRWFHNPETEKCEVFIYGGCHGNANRFATETECQEVC 51
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
422-561 2.57e-12

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 67.80  E-value: 2.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  422 DVVFLLD--GSEGVRSGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSY--MNKQ---DVVNAVRQLTLL 494
Cdd:cd01471     2 DLYLLVDgsGSIGYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPnsTNKDlalNAIRALLSLYYP 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240255535  495 GGPTpNTGAALEFVlRNILVSSAGSRitEGVPQLLIVLTADRSGDDVRNPSVVVK---RGGAVP-IGIGIG 561
Cdd:cd01471    82 NGST-NTTSALLVV-EKHLFDTRGNR--ENAPQLVIIMTDGIPDSKFRTLKEARKlreRGVIIAvLGVGQG 148
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
1701-1769 4.28e-12

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 71.09  E-value: 4.28e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240255535 1701 GKKGERGFPGYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAGPKGNRGDSIDQ 1769
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
829-967 4.92e-12

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 67.03  E-value: 4.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  829 DIVFLIDSSEGV-RPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAP--VLDAIRRLR---LR 902
Cdd:cd01471     2 DLYLLVDGSGSIgYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKdlALNAIRALLslyYP 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  903 GGSPlNTGKALEFVARNLFvKSAGSRieDGVPQhLVLVLGGKSQDDVSR---FAQVIRSSG--IVSLGVG 967
Cdd:cd01471    82 NGST-NTTSALLVVEKHLF-DTRGNR--ENAPQ-LVIIMTDGIPDSKFRtlkEARKLRERGviIAVLGVG 146
VWA_2 pfam13519
von Willebrand factor type A domain;
627-736 5.72e-12

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 64.24  E-value: 5.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   627 VVFLIDGSQSAGP------EFQYVRTLIERLVDYLDvgfdTTRVAVIQFSDDPKVEFLLNahSSKDEVQNAVQRLRPKGG 700
Cdd:pfam13519    1 LVFVLDTSGSMRNgdygptRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 240255535   701 rQINVGNALEYVSRNIFKRPlgsrieEGVPQFLVLI 736
Cdd:pfam13519   75 -GTNLAAALQLARAALKHRR------KNQPRRIVLI 103
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1500-1555 6.58e-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: 6.58e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 240255535  1500 GEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVGIRGDPGNPGQ 1555
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
38-182 7.49e-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: 66.25  E-value: 7.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   38 DIVFLVDGSSALGLANFNAIRDFIAKVIQRL------EIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVIT-AVRKMKP 110
Cdd:cd01480     4 DITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTSLKeAVDNLEY 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240255535  111 LDGsALYTGSALDFVRNNLFTSSAGyraaeGIPKLLVLITGGKSLDE----ISQPAQELKRSSI--MAFAIGNKGADQ 182
Cdd:cd01480    84 IGG-GTFTDCALKYATEQLLEGSHQ-----KENKFLLVITDGHSDGSpdggIEKAVNEADHLGIkiFFVAVGSQNEEP 155
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
626-795 7.64e-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: 66.25  E-value: 7.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  626 DVVFLIDGSQSAGPE-FQYVRTLIERLVD------YLDVGFDTTRVAVIQFSDDPKVEF-LLNAHSSKDEVQNAVQRLRP 697
Cdd:cd01480     4 DITFVLDSSESVGLQnFDITKNFVKRVAErflkdyYRKDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  698 KGGrQINVGNALEYVSRNIFKRPLGsrieeGVPQFLVLISSGKSDDEVD----DPAVELKQFGVAPFTIARNADQEE-LV 772
Cdd:cd01480    84 IGG-GTFTDCALKYATEQLLEGSHQ-----KENKFLLVITDGHSDGSPDggieKAVNEADHLGIKIFFVAVGSQNEEpLS 157
                         170       180
                  ....*....|....*....|....*.
gi 240255535  773 KIS---LSPEYVFSVSTFRELPSLEQ 795
Cdd:cd01480   158 RIAcdgKSALYRENFAELLWSFFIDD 183
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
230-371 9.50e-12

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 65.84  E-value: 9.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  230 DILFLFDGSANLV-GQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVK---RMKIKTGK 305
Cdd:cd01469     2 DIVFVLDGSGSIYpDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKhisQLLGLTNT 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240255535  306 ALnlgyALDYAQRYIFVKSAGSRieDGVLQFLVLLVAGRSSDRVDGPAsNLKQS---GVVPFI------FQAKNA 371
Cdd:cd01469    82 AT----AIQYVVTELFSESNGAR--KDATKVLVVITDGESHDDPLLKD-VIPQAereGIIRYAigvgghFQRENS 149
Kunitz_bikunin_1-like cd22596
first Kunitz domain of bikunin and similar proteins; This subfamily includes the N-terminal ...
2503-2555 1.28e-11

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


Pssm-ID: 438639  Cd Length: 54  Bit Score: 61.50  E-value: 1.28e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2503 DICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22596     1 DSCKLPPDAGPCFGMIQRYFYNSSSMACQTFNYGGCLGNQNNFVTEKECLQTC 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1482-1537 2.71e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 60.59  E-value: 2.71e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 240255535  1482 GQRGVKGSRGFPGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGE 1537
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1491-1545 3.93e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 60.20  E-value: 3.93e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 240255535  1491 GFPGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVG 1545
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1485-1541 7.21e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 59.43  E-value: 7.21e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 240255535  1485 GVKGSRGFPGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGER 1541
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
827-999 7.89e-11

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 63.56  E-value: 7.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  827 AADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRL------NIGPSKVRVGVVQFSNDVFPEF-YLKTYRSQAPVLDAIRRL 899
Cdd:cd01480     2 PVDITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  900 R-LRGGSplNTGKALEFVARNLFVKSAGsriedGVPQHLVLVLGGKSQ----DDVSRFAQVIRSSGI--VSLGVGDRNID 972
Cdd:cd01480    82 EyIGGGT--FTDCALKYATEQLLEGSHQ-----KENKFLLVITDGHSDgspdGGIEKAVNEADHLGIkiFFVAVGSQNEE 154
                         170       180       190
                  ....*....|....*....|....*....|...
gi 240255535  973 RteLQTITNDP------RLVFTVREFRELPNIE 999
Cdd:cd01480   155 P--LSRIACDGksalyrENFAELLWSFFIDDET 185
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
230-379 8.17e-11

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 62.80  E-value: 8.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  230 DILFLFDGSANLVGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVK--VESRFDEHQSKPEILNLVKRMKIKTGKAl 307
Cdd:cd01476     2 DLLFVLDSSGSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGTT- 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240255535  308 NLGYALDYAQRYiFVKSAGSRieDGVLQFLVLLVAGRSSDRVDGPASNLkQSGVVPFIFQAKNADP-----AELEQI 379
Cdd:cd01476    81 ATGAAIEVALQQ-LDPSEGRR--EGIPKVVVVLTDGRSHDDPEKQARIL-RAVPNIETFAVGTGDPgtvdtEELHSI 153
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1479-1535 9.48e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 59.04  E-value: 9.48e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 240255535  1479 GCPGQRGVKGSRGFPGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPR 1535
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
609-775 9.97e-11

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 64.96  E-value: 9.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  609 LQPVLQPLPSPGVGGKRDVVFLID--GSQSAGPEFQYVRTLIERLVDYLDvgfDTTRVAVIQFSDDPKVefLLNAHSSKD 686
Cdd:COG1240    77 LALALAPLALARPQRGRDVVLVVDasGSMAAENRLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEV--LLPLTRDRE 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  687 EVQNAVQRLRPKGGRQInvGNALeYVSRNIFKrplgsRIEEGVPQFLVLISSGKSDDEVDDP---AVELKQFGVAPFTIA 763
Cdd:COG1240   152 ALKRALDELPPGGGTPL--GDAL-ALALELLK-----RADPARRKVIVLLTDGRDNAGRIDPleaAELAAAAGIRIYTIG 223
                         170
                  ....*....|....*
gi 240255535  764 ---RNADQEELVKIS 775
Cdd:COG1240   224 vgtEAVDEGLLREIA 238
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
1796-1936 1.09e-10

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


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 62.63  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1796 LAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIAesncPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQvaLTS 1875
Cdd:cd01472     3 IVFLVDGSESIGLSNFNLVKDFVKRVVERLDIG----PDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLR--YIG 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240255535 1876 KQQSLETAMSFVARNTFK---RVRNGFlmRKVAVFFsnTPTRASPQLREAVLKLSDAGITPLFL 1936
Cdd:cd01472    77 GGTNTGKALKYVRENLFTeasGSREGV--PKVLVVI--TDGKSQDDVEEPAVELKQAGIEVFAV 136
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
2011-2188 1.15e-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: 62.20  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 2011 IDMAFILDSAETTTLFQFNEMKKYIAYLVRQLDmspdpkASQHFARVAVVQHApsesvDNAsmppvKVEFSLTDYGSKEK 2090
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLS------ASPPGDRVGLVTFG-----SNA-----RVVLPLTTDTDKAD 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 2091 LVDFLSRGMTQLQGTRALGSAIEYTIENVFESAPNPRdlKIVVLMLTGEVPEQQLEEAQRVILQAKCKGYFFVVLGIGRK 2170
Cdd:cd00198    65 LLEAIDALKKGLGGGTNIGAALRLALELLKSAKRPNA--RRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDD 142
                         170
                  ....*....|....*...
gi 240255535 2171 VNIKEVYTFASEPNDVFF 2188
Cdd:cd00198   143 ANEDELKEIADKTTGGAV 160
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
38-176 1.26e-10

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 62.79  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   38 DIVFLVDGSSALGLAN-FNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTK-----REVITAVRKMkPL 111
Cdd:cd01471     2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTnkdlaLNAIRALLSL-YY 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  112 DGSALYTGSALDFVRNNLFTsSAGYRaaEGIPKLLVLITGGKSlDEISQP---AQELK-RSSIMA-FAIG 176
Cdd:cd01471    81 PNGSTNTTSALLVVEKHLFD-TRGNR--ENAPQLVIIMTDGIP-DSKFRTlkeARKLReRGVIIAvLGVG 146
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1524-1589 1.37e-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: 1.37e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240255535  1524 GNPGRRGDKGPRGEKGERGDVGIRGDPGNPGqdsqERGPkgetgdlgpmgvPGRDGVPGGPGETGK 1589
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPG----EPGP------------PGPPGPPGPPGPPGA 50
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
1526-1765 2.79e-10

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 65.44  E-value: 2.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1526 PGRRGDKGPRGEKGERGDVGIRGDPGNPGQDsqerGPKGETGDLGPmgvPGRDGVPGGPGETGKNGgfgrrgppgAKGNK 1605
Cdd:COG5164     6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGST----RPAGNTGGTRP---AQNQGSTTPAGNTGGTR---------PAGNQ 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1606 GGPGQPGFEGEQGTrgaqgpagpagppglIGEQGisgprgsggAAGAPGERGRTGPLGRKGEPGEPGPKGGIgnrGPRGE 1685
Cdd:COG5164    70 GATGPAQNQGGTTP---------------AQNQG---------GTRPAGNTGGTTPAGDGGATGPPDDGGAT---GPPDD 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1686 TGDDGRDGVGSEGRRGKKGER-GFPGYPGPKGNPGEPGLNGTTGPKGIRGRRG--NSGPPGIVGQKGDPGYPGPAGPKGN 1762
Cdd:COG5164   123 GGSTTPPSGGSTTPPGDGGSTpPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTppDDGGSTTPPNKGETGTDIPTGGTPR 202

                  ...
gi 240255535 1763 RGD 1765
Cdd:COG5164   203 QGP 205
Kunitz_SHPI cd22618
Stichodactyla helianthus Kunitz inhibitor protein ShPI-1, Heteractis crispa protease inhibitor ...
2504-2555 3.58e-10

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


Pssm-ID: 438661  Cd Length: 53  Bit Score: 57.55  E-value: 3.58e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 240255535 2504 ICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22618     1 ICSEPKVVGPCKAYFPRFYFDSETGKCTPFIYGGCGGNGNNFETLHACRAIC 52
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
1031-1190 4.25e-10

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 60.88  E-value: 4.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1031 ADIVFLLDGSINFRrDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTD--EFFLKDFSTKRQIIDAINKVVYKGGR 1108
Cdd:cd01476     1 LDLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1109 HAnTKVGLEhLRVNHFVPEAGSRldQRVPQIAFVITGGKSVEDAQDVSLAL-TQRGVKVFAVGVRNI---DSEEVGKIAS 1184
Cdd:cd01476    80 TA-TGAAIE-VALQQLDPSEGRR--EGIPKVVVVLTDGRSHDDPEKQARILrAVPNIETFAVGTGDPgtvDTEELHSITG 155

                  ....*.
gi 240255535 1185 NSATAF 1190
Cdd:cd01476   156 NEDHIF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
2012-2188 5.72e-10

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 60.49  E-value: 5.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 2012 DMAFILDSAETTTlFQFNEMKKYIAYLVRQLDMSPDPKasqhfaRVAVVQHapsesvdnASMPPVKVEFSLTDYGSKEKL 2091
Cdd:cd01476     2 DLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTAT------RVALITY--------SGRGRQRVRFNLPKHNDGEEL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 2092 VDFLsRGMTQLQGTRALGSAIEYTIENVFESAP-NPRDLKIVVLMLTG---EVPEQQLEEAQRVilqakcKGYFFVVLGI 2167
Cdd:cd01476    67 LEKV-DNLRFIGGTTATGAAIEVALQQLDPSEGrREGIPKVVVVLTDGrshDDPEKQARILRAV------PNIETFAVGT 139
                         170       180
                  ....*....|....*....|...
gi 240255535 2168 G--RKVNIKEVYTFASEPNDVFF 2188
Cdd:cd01476   140 GdpGTVDTEELHSITGNEDHIFT 162
VWA_2 pfam13519
von Willebrand factor type A domain;
423-532 6.06e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 58.46  E-value: 6.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   423 VVFLLDGSEGVRSG------FPLLKEFVQRVVESLDvgqdRVRVAVVQYSDRTRPEFYLNSymNKQDVVNAVRQLTLLGG 496
Cdd:pfam13519    1 LVFVLDTSGSMRNGdygptrLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 240255535   497 PTpNTGAALEFVLRNIlvssagSRITEGVPQLLIVL 532
Cdd:pfam13519   75 GT-NLAAALQLARAAL------KHRRKNQPRRIVLI 103
Kunitz_TKDP-like cd22609
trophoblast Kunitz domain protein (TKDP) and similar proteins; This model contains the ...
2505-2555 7.02e-10

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


Pssm-ID: 438652  Cd Length: 52  Bit Score: 56.69  E-value: 7.02e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240255535 2505 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22609     2 CLEPKVVGVCKASMTRYFYNAQTGHCEQFVYGGCGGNRNNFLTLEDCMKTC 52
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
2011-2149 9.75e-10

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


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 59.55  E-value: 9.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 2011 IDMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDPkasqhfARVAVVQHApsesvDNasmppVKVEFSLTDYGSKEk 2090
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDG------VRVGVVQYS-----DD-----PRTEFYLNTYRSKD- 63
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240255535 2091 lvDFLS--RGMTQLQGTRALGSAIEYTIENVFESAPNPRD--LKIVVLMLTG----EVPEQQLEEAQ 2149
Cdd:cd01472    64 --DVLEavKNLRYIGGGTNTGKALKYVRENLFTEASGSREgvPKVLVVITDGksqdDVEEPAVELKQ 128
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
2012-2187 1.42e-09

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 59.26  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 2012 DMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDPkasqhfARVAVVQHApsesvDNasmppVKVEFSLTDYGSKEKL 2091
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDK------IRVAVVQFS-----DT-----PRPEFYLNTHSTKADV 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 2092 VDFLSRgmTQLQGTRAL--GSAIEYTIENVFESAPNPRD----LKIVVLMLTGEvPEQQLEEAQRVILQAKckgyfFVVL 2165
Cdd:cd01481    66 LGAVRR--LRLRGGSQLntGSALDYVVKNLFTKSAGSRIeegvPQFLVLITGGK-SQDDVERPAVALKRAG-----IVPF 137
                         170       180
                  ....*....|....*....|...
gi 240255535 2166 GIGRK-VNIKEVYTFASEPNDVF 2187
Cdd:cd01481   138 AIGARnADLAELQQIAFDPSFVF 160
Kunitz_BPTI cd22592
bovine pancreatic trypsin inhibitor; This model contains bovine pancreatic trypsin inhibitor ...
2505-2555 1.79e-09

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


Pssm-ID: 438635  Cd Length: 52  Bit Score: 55.34  E-value: 1.79e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240255535 2505 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22592     2 CLEPPYTGPCKARIIRYFYNAKSGLCETFVYGGCRAKRNNFLSAEDCMRTC 52
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
1231-1387 2.09e-09

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 59.01  E-value: 2.09e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   1231 DVILGFDGSRDqnvfVAQKGFESKVDAILNRISQMHRvscsggRSPTVRVSVVAnTPSGPVEAFDFDEYQ--PEMLEKFR 1308
Cdd:smart00327    1 DVVFLLDGSGS----MGGNRFELAKEFVLKLVEQLDI------GPDGDRVGLVT-FSDDARVLFPLNDSRskDALLEALA 69
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   1309 NMRsqhpYVLTEDT---------LKVYLNKFRQSSPDSVKVVIHFTDGADGDLA-DLHRASENLRQEGVRaLILVGLERV 1378
Cdd:smart00327   70 SLS----YKLGGGTnlgaalqyaLENLFSKSAGSRRGAPKVVILITDGESNDGPkDLLKAAKELKRSGVK-VFVVGVGND 144

                    ....*....
gi 240255535   1379 VNLERLMHL 1387
Cdd:smart00327  145 VDEEELKKL 153
VWA_2 pfam13519
von Willebrand factor type A domain;
830-921 3.14e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 56.53  E-value: 3.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   830 IVFLIDSSEGVRPDG-----FAHIRDFVSRIVRRLNIgpskVRVGVVQFSNDVFPEFYLKtyRSQAPVLDAIRRLRLRGG 904
Cdd:pfam13519    1 LVFVLDTSGSMRNGDygptrLEAAKDAVLALLKSLPG----DRVGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGG 74
                           90
                   ....*....|....*..
gi 240255535   905 SPlNTGKALEFVARNLF 921
Cdd:pfam13519   75 GT-NLAAALQLARAALK 90
Kunitz_B2B cd22619
Kunitz-type serine protease inhibitor subunit of beta 2-bungarotoxin, and similar proteins; ...
2505-2555 4.17e-09

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


Pssm-ID: 438662  Cd Length: 58  Bit Score: 54.49  E-value: 4.17e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240255535 2505 CKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22619     7 CDKPPDTKRCKRVVRAFYYNPSAKTCLQFVYGGCNGNGNHFKSKALCRCHC 57
Kunitz_WFIKKN_1-like cd22605
first Kunitz domain of WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing proteins; ...
2506-2555 8.12e-09

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


Pssm-ID: 438648  Cd Length: 52  Bit Score: 53.52  E-value: 8.12e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 240255535 2506 KLPkDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22605     4 KEP-DREDCGEEQVRWYFDAKRGNCFTFTYGGCDGNRNHFETYEECRLAC 52
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
1798-1934 1.86e-08

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 56.18  E-value: 1.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1798 FALDTSEGVNQDTFGRMRDVVLSIVNDLTIAesncPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQVaLTSKQ 1877
Cdd:cd01481     5 FLIDGSDNVGSGNFPAIRDFIERIVQSLDVG----PDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRL-RGGSQ 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240255535 1878 QSLETAMSFVARNTFK-----RVRNGFLMRKVAVffsnTPTRASPQLREAVLKLSDAGITPL 1934
Cdd:cd01481    80 LNTGSALDYVVKNLFTksagsRIEEGVPQFLVLI----TGGKSQDDVERPAVALKRAGIVPF 137
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
812-1002 2.14e-08

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 57.64  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  812 LLASTRYPPPAVESDAADIVFLIDSSeG--VRPDGFAHIRDFVSRIVRRLnigPSKVRVGVVQFSNDVFPEFYLKTYRSQ 889
Cdd:COG1240    77 LALALAPLALARPQRGRDVVLVVDAS-GsmAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTRDREA 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  890 apVLDAIRRLRLRGGSPLntGKALEfVARNLFvksagSRIEDGVPQHLVLVLGGK---SQDDVSRFAQVIRSSGI--VSL 964
Cdd:COG1240   153 --LKRALDELPPGGGTPL--GDALA-LALELL-----KRADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIriYTI 222
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 240255535  965 GVGDRNIDRTELQTI---TNDPrlVFTVREFRELPNIEERI 1002
Cdd:COG1240   223 GVGTEAVDEGLLREIaeaTGGR--YFRADDLSELAAIYREI 261
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
1032-1171 4.25e-08

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 55.47  E-value: 4.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1032 DIVFLLDGSINFRR-DSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKD-FSTKRQ----IIDAINKVVYK 1105
Cdd:cd01471     2 DLYLLVDGSGSIGYsNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSpNSTNKDlalnAIRALLSLYYP 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240255535 1106 GGRhANTKVGLehLRVN-HFVPEAGSRldQRVPQIAFVITGGKSVEDAQDVSLA--LTQRGVKVFAVGV 1171
Cdd:cd01471    82 NGS-TNTTSAL--LVVEkHLFDTRGNR--ENAPQLVIIMTDGIPDSKFRTLKEArkLRERGVIIAVLGV 145
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
1796-1953 5.58e-08

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 54.49  E-value: 5.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1796 LAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIAesncPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQvALTS 1875
Cdd:cd00198     3 IVFLLDVSGSMGGEKLDKAKEALKALVSSLSAS----PPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALK-KGLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1876 KQQSLETAMSFVARNTFKRVRNGflMRKVAVFFSN-TPTRASPQLREAVLKLSDAGIT--PLFLTRQEDRQLINALQINN 1952
Cdd:cd00198    78 GGTNIGAALRLALELLKSAKRPN--ARRVIILLTDgEPNDGPELLAEAARELRKLGITvyTIGIGDDANEDELKEIADKT 155

                  .
gi 240255535 1953 T 1953
Cdd:cd00198   156 T 156
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
1010-1201 6.79e-08

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 56.49  E-value: 6.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1010 AATPAPPGVDTPPPSRPEKKKADIVFLLD--GSINfRRDSFQEVLRFVSEIVDTvYEDGDsiQVGLVQYNSDPtdeFFLK 1087
Cdd:COG1240    72 VLLLLLALALAPLALARPQRGRDVVLVVDasGSMA-AENRLEAAKGALLDFLDD-YRPRD--RVGLVAFGGEA---EVLL 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1088 DFST-KRQIIDAINKVVYKGGrhanT------KVGLEHLRvnhfvpeagsRLDQRVPQIAFVITGGK---SVEDAQDVSL 1157
Cdd:COG1240   145 PLTRdREALKRALDELPPGGG----TplgdalALALELLK----------RADPARRKVIVLLTDGRdnaGRIDPLEAAE 210
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 240255535 1158 ALTQRGVKVFAVGV--RNIDSEEVGKIASNS-ATAFRVGNVQELSEL 1201
Cdd:COG1240   211 LAAAAGIRIYTIGVgtEAVDEGLLREIAEATgGRYFRADDLSELAAI 257
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1660-1722 1.61e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.18  E-value: 1.61e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240255535  1660 GPLGRKGEPGEPGPKGGIGNRGPRGEtgddgrdgvgsegrrgkkgergfPGYPGPKGNPGEPG 1722
Cdd:pfam01391   16 GPPGPPGPPGPPGPPGEPGPPGPPGP-----------------------PGPPGPPGAPGAPG 55
Kunitz_ixolaris_1 cd22625
Kunitz-type domain 1 (K1) of Ixolaris, and similar proteins; This model includes the first ...
2505-2555 2.23e-07

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


Pssm-ID: 438668  Cd Length: 53  Bit Score: 49.57  E-value: 2.23e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2505 CKLPKDEG-TCRDFILKWY-YDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22625     1 CTLPIQEItTCESQPTKRYgYNKKTQQCEEFLGTECGGGGNSFEEAKECWSSC 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1431-1501 2.50e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.41  E-value: 2.50e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240255535  1431 GQRGDRGPIGSIGPKGIPGEDGyrgypgdeggpgergPPGVNGTQGFQGCPGQRGVKGSRGFPGEKGEVGE 1501
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPG---------------PPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1452-1526 2.87e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.41  E-value: 2.87e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240255535  1452 GYRGYPGDeggpgergppgvngtqgfQGCPGQRGVKGSRGFPGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNP 1526
Cdd:pfam01391    1 GPPGPPGP------------------PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
623-809 4.56e-07

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


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 52.51  E-value: 4.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  623 GKRDVVFLIDGSQSAG---PE-FQYVRTLIERLVDyldvgfDTTRVAVIQFSDDPKVEFLLNAHSSKdEVQNA--VQRLR 696
Cdd:cd01474     3 GHFDLYFVLDKSGSVAanwIEiYDFVEQLVDRFNS------PGLRFSFITFSTRATKILPLTDDSSA-IIKGLevLKKVT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  697 PKGgrQINVGNALEYVSRNIFKRPLGSRIEEGVpqfLVLISSGKSDDEV----DDPAVELKQFGVAPFTIA-RNADQEEL 771
Cdd:cd01474    76 PSG--QTYIHEGLENANEQIFNRNGGGRETVSV---IIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGvTDFLKSQL 150
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 240255535  772 VKISLSPEYVFSV-STFRELpsleQKLLTPITTLTSEQI 809
Cdd:cd01474   151 INIADSKEYVFPVtSGFQAL----SGIIESVVKKACIEI 185
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
626-743 5.15e-07

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 52.39  E-value: 5.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  626 DVVFLIDGSQSAGPE--FQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSS--KDEVQNAVQRLR----P 697
Cdd:cd01471     2 DLYLLVDGSGSIGYSnwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNStnKDLALNAIRALLslyyP 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 240255535  698 KGgrQINVGNALEYVSRNIFKRPlGSRieEGVPQFLVLISSGKSDD 743
Cdd:cd01471    82 NG--STNTTSALLVVEKHLFDTR-GNR--ENAPQLVIIMTDGIPDS 122
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
230-351 8.65e-07

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 51.62  E-value: 8.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  230 DILFLFDGSANlVG--QFPVVRDFLYKIIDELN----VKPE--GTRIAVAQYSDDVKVESRFDEH-QSKPEILNLVKRMK 300
Cdd:cd01480     4 DITFVLDSSES-VGlqNFDITKNFVKRVAERFLkdyyRKDPagSWRVGVVQYSDQQEVEAGFLRDiRNYTSLKEAVDNLE 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240255535  301 IkTGKALNLGYALDYAQRYIFVKSAGsriedGVLQFLVLLVAGRSSDRVDG 351
Cdd:cd01480    83 Y-IGGGTFTDCALKYATEQLLEGSHQ-----KENKFLLVITDGHSDGSPDG 127
VWA_2 pfam13519
von Willebrand factor type A domain;
1796-1908 1.24e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 49.21  E-value: 1.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1796 LAFALDTSEGVNQDTFGRMR-DVVLSIVNDLtiAESNcpRGARVAVVTYNNEVTTEIRFADSKRKsvLLDKIKNLQValT 1874
Cdd:pfam13519    1 LVFVLDTSGSMRNGDYGPTRlEAAKDAVLAL--LKSL--PGDRVGLVTFGDGPEVLIPLTKDRAK--ILRALRRLEP--K 72
                           90       100       110
                   ....*....|....*....|....*....|....
gi 240255535  1875 SKQQSLETAMSFvARNTFKRVRNGflMRKVAVFF 1908
Cdd:pfam13519   73 GGGTNLAAALQL-ARAALKHRRKN--QPRRIVLI 103
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
827-1012 1.39e-06

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


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 50.97  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  827 AADIVFLIDSSEGVRpDGFAHIRDFVSRIVRRLNigPSKVRVGVVQFSNDVFPEFYLKTYRSQ-APVLDAIRRLRLRGGS 905
Cdd:cd01474     4 HFDLYFVLDKSGSVA-ANWIEIYDFVEQLVDRFN--SPGLRFSFITFSTRATKILPLTDDSSAiIKGLEVLKKVTPSGQT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  906 PLntGKALEFVARNLFVKSAGSRIEDGVpqhLVLVLGGKSQDDV----SRFAQVIRSSGIVSLGVGDRNIDRTELQTITN 981
Cdd:cd01474    81 YI--HEGLENANEQIFNRNGGGRETVSV---IIALTDGQLLLNGhkypEHEAKLSRKLGAIVYCVGVTDFLKSQLINIAD 155
                         170       180       190
                  ....*....|....*....|....*....|..
gi 240255535  982 DPRLVFTVRE-FRELpnieERIMNSFGPSAAT 1012
Cdd:cd01474   156 SKEYVFPVTSgFQAL----SGIIESVVKKACI 183
PHA03169 PHA03169
hypothetical protein; Provisional
1475-1612 1.58e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 53.05  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1475 QGFQGCPGQRGVKGSRGFPGEKGEVGEIGLD---------GLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVG 1545
Cdd:PHA03169   89 QGGPSGSGSESVGSPTPSPSGSAEELASGLSpentsgsspESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQ 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1546 IRG----DPGNPG----QDSQERGPKGETGDLGPMGV-----PGRDGVPGGPGETGKNGGFGRRGPPGAKGNKG-GPGQP 1611
Cdd:PHA03169  169 PSHedspEEPEPPtsepEPDSPGPPQSETPTSSPPPQsppdePGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEReGPPFP 248

                  .
gi 240255535 1612 G 1612
Cdd:PHA03169  249 G 249
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
37-189 2.32e-06

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 51.48  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   37 RDIVFLVDGS-SALGLANFN----AIRDFIAKVIQRLEIGqdLIqvAVAQYADTVRPefyfnthPT--KREVITAVRKMK 109
Cdd:COG1240    93 RDVVLVVDASgSMAAENRLEaakgALLDFLDDYRPRDRVG--LV--AFGGEAEVLLP-------LTrdREALKRALDELP 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  110 PLDGSALYTG--SALDFVRnnlftssagyRAAEGIPKLLVLITGGK---SLDEISQPAQELKRSSIMAFAI--GNKGADQ 182
Cdd:COG1240   162 PGGGTPLGDAlaLALELLK----------RADPARRKVIVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIgvGTEAVDE 231

                  ....*..
gi 240255535  183 AELEEIA 189
Cdd:COG1240   232 GLLREIA 238
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
2012-2192 3.94e-06

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 49.21  E-value: 3.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 2012 DMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDPkasqhfARVAVVQHapseSVDnasmppVKVEFSLTDYGSKEKL 2091
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDG------VQVGLVQY----SDD------PRTEFDLNAYTSKEDV 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 2092 VDFLSRgMTQLQGTRALGSAIEYTIENVF-ESAPNPRDLKIVVLMLTGEVPEQQLEEAQRVilqAKCKGYFFVVLGIgRK 2170
Cdd:cd01482    66 LAAIKN-LPYKGGNTRTGKALTHVREKNFtPDAGARPGVPKVVILITDGKSQDDVELPARV---LRNLGVNVFAVGV-KD 140
                         170       180
                  ....*....|....*....|..
gi 240255535 2171 VNIKEVYTFASEPNDVFFKLVD 2192
Cdd:cd01482   141 ADESELKMIASKPSETHVFNVA 162
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
1031-1201 6.02e-06

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 49.31  E-value: 6.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1031 ADIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDG------DSIQVGLVQYNSDPTDEF-FLKDFSTKRQIIDAINKVV 1103
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYyrkdpaGSWRVGVVQYSDQQEVEAgFLRDIRNYTSLKEAVDNLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1104 Y-KGGRHANT--KVGLEHLRVnhfvpeaGSRLDQRvpQIAFVITGG-----------KSVEDAQDVslaltqrGVKVFAV 1169
Cdd:cd01480    83 YiGGGTFTDCalKYATEQLLE-------GSHQKEN--KFLLVITDGhsdgspdggieKAVNEADHL-------GIKIFFV 146
                         170       180       190
                  ....*....|....*....|....*....|..
gi 240255535 1170 GVRNIDSEEVGKIASNSATAFRVGNVQELSEL 1201
Cdd:cd01480   147 AVGSQNEEPLSRIACDGKSALYRENFAELLWS 178
VWA_2 pfam13519
von Willebrand factor type A domain;
39-138 8.49e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 46.52  E-value: 8.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535    39 IVFLVDGS-----SALGLANFNAIRDFIAKVIQRLEIGQdliqVAVAQYADTVRPEFYFNTHPTKreVITAVRKMKPLDG 113
Cdd:pfam13519    1 LVFVLDTSgsmrnGDYGPTRLEAAKDAVLALLKSLPGDR----VGLVTFGDGPEVLIPLTKDRAK--ILRALRRLEPKGG 74
                           90       100
                   ....*....|....*....|....*
gi 240255535   114 SAlYTGSALDFVRNNLFTSSAGYRA 138
Cdd:pfam13519   75 GT-NLAAALQLARAALKHRRKNQPR 98
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
625-775 1.01e-05

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 50.10  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  625 RDVVFLIDGSQS-AGPEFQYVRTLIERLVDYLDvgfDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGrqI 703
Cdd:COG2304    92 LNLVFVIDVSGSmSGDKLELAKEAAKLLVDQLR---PGDRVSIVTFAGDARVLLPPTPATDRAKILAAIDRLQAGGG--T 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  704 NVGNALEYVsrniFKRPLGSRIEEGVPQfLVLISSGKSDDEVDDPAV------ELKQFGVAPFTIA--RNADQEELVKIS 775
Cdd:COG2304   167 ALGAGLELA----YELARKHFIPGRVNR-VILLTDGDANVGITDPEEllklaeEAREEGITLTTLGvgSDYNEDLLERLA 241
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
1477-1759 1.30e-05

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


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 50.38  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1477 FQGCPGQrGVKGSRGFPGEKGEvgeigldgldGEDGDKGLPGSSGekGNPGRRGDKGPRGEKGERGdvgirgdPGNPGQD 1556
Cdd:cd21118   121 WQGSGGH-GAYGSQGGPGVQGH----------GIPGGTGGPWASG--GNYGTNSLGGSVGQGGNGG-------PLNYGTN 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1557 SQ----------ERGPKGETGDLGPmgvPGRDGVPGGpgetgknggfgrrgppgakGNKGGPGQPGFEGEQGTRGAQGPA 1626
Cdd:cd21118   181 SQgavaqpgygtVRGNNQNSGCTNP---PPSGSHESF-------------------SNSGGSSSSGSSGSQGSHGSNGQG 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1627 GPAGPpgliGEQGISGPRGSGGAAGAPGERGRTGPLGRKGEPGEPGPKGGIGNRGPRGETGDDGrdgvGSEGRRGKKger 1706
Cdd:cd21118   239 SSGSS----GGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSSGGSG----GSGGGNKPE--- 307
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240255535 1707 gfPGYPGPK-GNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAGP 1759
Cdd:cd21118   308 --CNNPGNDvRMAGGGGSQGSKESSGSHGSNGGNGQAEAVGGLNTLNSDASTLP 359
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
1230-1384 1.34e-05

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 47.67  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1230 LDVILGFDGSRDqnvfVAQKGFESKVDAILNRISQMHrvscSGGRSptVRVSVVANTPSGPVEaFDFDEYQ--PEMLEKF 1307
Cdd:cd01450     1 LDIVFLLDGSES----VGPENFEKVKDFIEKLVEKLD----IGPDK--TRVGLVQYSDDVRVE-FSLNDYKskDDLLKAV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1308 RNMRSQ-HPYVLTEDTLKV---YLNKFRQSSPDSVKVVIHFTDGADGDLADLHRASENLRQEGVrALILVGLERVV--NL 1381
Cdd:cd01450    70 KNLKYLgGGGTNTGKALQYaleQLFSESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGI-KVFVVGVGPADeeEL 148

                  ...
gi 240255535 1382 ERL 1384
Cdd:cd01450   149 REI 151
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1734-1766 1.24e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 1.24e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 240255535  1734 GRRGNSGPPGIVGQKGDPGYPGPAGPKGNRGDS 1766
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEP 33
Kunitz_MitTx cd22610
Micrurus tener tener Kunitz-type neurotoxin MitTx-alpha; Micrurus tener tener Kunitz-type ...
2514-2555 1.86e-04

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


Pssm-ID: 438653  Cd Length: 59  Bit Score: 41.54  E-value: 1.86e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 240255535 2514 CRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVC 2555
Cdd:cd22610    16 CGAFVDSYYFNRSRITCVHFFYGQCDVNQNHFTTMSECNRVC 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1579-1683 1.92e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 1.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1579 GVPGGPGETGknggfgrrgppgAKGNKGGPGQPGFEGEQGTRgaqgpagpagppgliGEqgisgprgsggaagapgergr 1658
Cdd:pfam01391    1 GPPGPPGPPG------------PPGPPGPPGPPGPPGPPGPP---------------GE--------------------- 32
                           90       100
                   ....*....|....*....|....*
gi 240255535  1659 TGPLGRKGEPGEPGPKGGIGNRGPR 1683
Cdd:pfam01391   33 PGPPGPPGPPGPPGPPGAPGAPGPP 57
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
1793-1932 2.15e-04

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


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 45.07  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1793 PTELAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIAesncPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQVA 1872
Cdd:cd01475     2 PTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVG----PDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240255535 1873 LTSKQQSLetAMSFVARNTFK-----RVRNGFLMRKVAVFfsnTPTRASPQLREAVLKLSDAGIT 1932
Cdd:cd01475    78 ETGTMTGL--AIQYAMNNAFSeaegaRPGSERVPRVGIVV---TDGRPQDDVSEVAAKARALGIE 137
VWA pfam00092
von Willebrand factor type A domain;
1231-1384 2.35e-04

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 44.19  E-value: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1231 DVILGFDGSRDqnvfVAQKGFESKVDAILNRISQMhrvscsgGRSP-TVRVSVV--ANTPsgpVEAFDFDEYQ--PEMLE 1305
Cdd:pfam00092    1 DIVFLLDGSGS----IGGDNFEKVKEFLKKLVESL-------DIGPdGTRVGLVqySSDV---RTEFPLNDYSskEELLS 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1306 KFRNMRSQ-HPYVLTEDTLK-VYLNKFRQSS---PDSVKVVIHFTDGADGDLaDLHRASENLRQEGVRaLILVGLERVVN 1380
Cdd:pfam00092   67 AVDNLRYLgGGTTNTGKALKyALENLFSSAAgarPGAPKVVVLLTDGRSQDG-DPEEVARELKSAGVT-VFAVGVGNADD 144

                   ....*.
gi 240255535  1381 --LERL 1384
Cdd:pfam00092  145 eeLRKI 150
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
1031-1206 3.48e-04

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


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 44.04  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1031 ADIVFLLD--GSINfrrDSFQEVLRFVSEIVDTVYEDGdsIQVGLVQYNSDPTDEFFLKDFSTK-RQIIDAINKVVYKGG 1107
Cdd:cd01474     5 FDLYFVLDksGSVA---ANWIEIYDFVEQLVDRFNSPG--LRFSFITFSTRATKILPLTDDSSAiIKGLEVLKKVTPSGQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1108 RHANTkvGLEHLRVNHFVPEAGSRldqRVPQIAFVITGGKSVED----AQDVSLALTQRGVKVFAVGVRNIDSEEVGKIA 1183
Cdd:cd01474    80 TYIHE--GLENANEQIFNRNGGGR---ETVSVIIALTDGQLLLNghkyPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIA 154
                         170       180
                  ....*....|....*....|....
gi 240255535 1184 SNSATAFRV-GNVQELSELSEQVL 1206
Cdd:cd01474   155 DSKEYVFPVtSGFQALSGIIESVV 178
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
413-572 4.13e-04

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 44.54  E-value: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  413 APAPVSGEKDVVFLLD--GSEGVRSGFPLLKEFVQRVVESLdvgQDRVRVAVVQYSDRTRPEFYLNSymNKQDVVNAVRQ 490
Cdd:COG1240    85 ALARPQRGRDVVLVVDasGSMAAENRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLTR--DREALKRALDE 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  491 LTLLGGpTPnTGAALEfvlrniLVSSAGSRITEGVPQLLIVLT---ADRSGDDVRNPSVVVKRGGA--VPIGIGIGNADI 565
Cdd:COG1240   160 LPPGGG-TP-LGDALA------LALELLKRADPARRKVIVLLTdgrDNAGRIDPLEAAELAAAAGIriYTIGVGTEAVDE 231

                  ....*..
gi 240255535  566 TEMQTIS 572
Cdd:COG1240   232 GLLREIA 238
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
2011-2212 4.35e-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: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 2011 IDMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDPKASQHFARVAVVQHAPSESVDNASMPpvkvefSLTDYGSKEK 2090
Cdd:cd01480     3 VDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRKDPAGSWRVGVVQYSDQQEVEAGFLR------DIRNYTSLKE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 2091 LVDflsrGMTQLQGTRALGSAIEYTIENVFESAPNPRdLKIVVLMLTGEV-------PEQQLEEAQRVILqakckGYFFV 2163
Cdd:cd01480    77 AVD----NLEYIGGGTFTDCALKYATEQLLEGSHQKE-NKFLLVITDGHSdgspdggIEKAVNEADHLGI-----KIFFV 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 240255535 2164 VlgIGRKVNikevytfasEPNDVFfkLVDKSTELNEEPlmrFGRLLPSF 2212
Cdd:cd01480   147 A--VGSQNE---------EPLSRI--ACDGKSALYREN---FAELLWSF 179
PHA03169 PHA03169
hypothetical protein; Provisional
1481-1715 4.57e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 45.35  E-value: 4.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1481 PGQRGVKGSRGF------PGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVGiRGDPGNPG 1554
Cdd:PHA03169   33 AGRRRGTAARAAkpappaPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSP-TPSPSGSA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1555 QDSQERGPKGETGDLGPMGvPGRDGVPGGPGETGKNGGFGRRGPPGAKGNKGGPGQPGFEGEQGTRGaqgpagpagppgl 1634
Cdd:PHA03169  112 EELASGLSPENTSGSSPES-PASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEE------------- 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1635 iGEQGISGPRGSGGAagapgergrtGPLGRKGEPGEPGPKGGIGNRGPRGETGD-----DGRDGVGSEGRRGKKGERGfP 1709
Cdd:PHA03169  178 -PEPPTSEPEPDSPG----------PPQSETPTSSPPPQSPPDEPGEPQSPTPQqapspNTQQAVEHEDEPTEPEREG-P 245

                  ....*.
gi 240255535 1710 GYPGPK 1715
Cdd:PHA03169  246 PFPGHR 251
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1573-1685 4.85e-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: 4.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1573 GVPGRDGVPGGPgetgknggfgrrgppgakGNKGGPGQPGFEGEQGTRgaqgpagpagppgligeqgisgprgsggaaga 1652
Cdd:pfam01391    1 GPPGPPGPPGPP------------------GPPGPPGPPGPPGPPGPP-------------------------------- 30
                           90       100       110
                   ....*....|....*....|....*....|...
gi 240255535  1653 pgergrtGPLGRKGEPGEPGPKGGIGNRGPRGE 1685
Cdd:pfam01391   31 -------GEPGPPGPPGPPGPPGPPGAPGAPGP 56
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
1794-1931 5.97e-04

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 43.04  E-value: 5.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1794 TELAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIAesncPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQV-- 1871
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIG----PDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYkg 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240255535 1872 --ALTSKqqsletAMSFVARNTFK---RVRNGFlmRKVAVFFsnTPTRASPQLREAVLKLSDAGI 1931
Cdd:cd01482    77 gnTRTGK------ALTHVREKNFTpdaGARPGV--PKVVILI--TDGKSQDDVELPARVLRNLGV 131
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
1793-1870 6.43e-04

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 43.14  E-value: 6.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1793 PTELAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIAESNCPR--GARVAVVTYNNEVTTEIRFADSKR-KSVLLDKIKNL 1869
Cdd:cd01480     2 PVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRKDPagSWRVGVVQYSDQQEVEAGFLRDIRnYTSLKEAVDNL 81

                  .
gi 240255535 1870 Q 1870
Cdd:cd01480    82 E 82
VWA_2 pfam13519
von Willebrand factor type A domain;
1033-1120 7.47e-04

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 41.12  E-value: 7.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  1033 IVFLLDGS-----INFRRDSFQEVLRFVSEIVDTVYEDgdsiQVGLVQYNSDPTDEFFLKDfsTKRQIIDAINKVVYKGG 1107
Cdd:pfam13519    1 LVFVLDTSgsmrnGDYGPTRLEAAKDAVLALLKSLPGD----RVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74
                           90
                   ....*....|...
gi 240255535  1108 rHANTKVGLEHLR 1120
Cdd:pfam13519   75 -GTNLAAALQLAR 86
VWA_2 pfam13519
von Willebrand factor type A domain;
231-321 9.16e-04

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 40.74  E-value: 9.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535   231 ILFLFDGSANLVGQ------FPVVRDFLYKIIDELNvkpeGTRIAVAQYSDDVKVESRFDEHQSKpeILNLVKRMKIKTG 304
Cdd:pfam13519    1 LVFVLDTSGSMRNGdygptrLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLTKDRAK--ILRALRRLEPKGG 74
                           90
                   ....*....|....*..
gi 240255535   305 KAlNLGYALDYAQRYIF 321
Cdd:pfam13519   75 GT-NLAAALQLARAALK 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
2386-2454 1.34e-03

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.17  E-value: 1.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240255535 2386 REVQVFEITENSAKLHWERAEPPGP----YFYDLTVTSAHDQSLVLKQNLTVTDRVIGGLLAGQTYHVAVVCY 2454
Cdd:cd00063     5 TNLRVTDVTSTSVTLSWTPPEDDGGpitgYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
828-968 1.82e-03

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


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 41.49  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  828 ADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIgpsKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPL 907
Cdd:cd01465     1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRP---DDRLAIVTYDGAAETVLPATPVRDKAAILAAIDRLTAGGSTAG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240255535  908 NTG--KALEFVARNlFVKSAGSRI---EDGVPQHlvlvlGGKSQDDVSRFAQVIRSSGI--VSLGVGD 968
Cdd:cd01465    78 GAGiqLGYQEAQKH-FVPGGVNRIllaTDGDFNV-----GETDPDELARLVAQKRESGItlSTLGFGD 139
PHA03169 PHA03169
hypothetical protein; Provisional
1521-1748 2.10e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.04  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1521 GEKGNPGRRGDKGPRGEK---------GERGDVGIRGDPGNPGQDSQE-----RGPKGETGDLGPMGvPGRDGVPGGPGE 1586
Cdd:PHA03169   28 GTREQAGRRRGTAARAAKpappapttsGPQVRAVAEQGHRQTESDTETaeesrHGEKEERGQGGPSG-SGSESVGSPTPS 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1587 TGKNGGFGRRGPPGAKGNKGGPGQPGFEGEQGTrgaqgpagpagppgligeqgisgprgsggaagapgERGRTGPlgrkG 1666
Cdd:PHA03169  107 PSGSAEELASGLSPENTSGSSPESPASHSPPPS-----------------------------------PPSHPGP----H 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1667 EPGEPGPKGGIGNRGPRGETGDDGRDGV-------------GSEGRRGKKGERGFPGYPGPK--GNPGEPGLNGTTGPKG 1731
Cdd:PHA03169  148 EPAPPESHNPSPNQQPSSFLQPSHEDSPeepepptsepepdSPGPPQSETPTSSPPPQSPPDepGEPQSPTPQQAPSPNT 227
                         250       260       270
                  ....*....|....*....|....*....|....
gi 240255535 1732 IRG----------RRGNSGPPG-------IVGQK 1748
Cdd:PHA03169  228 QQAvehedeptepEREGPPFPGhrshsytVVGWK 261
Kunitz_ornithodorin_C-like cd22612
C-terminal Kunitz domain of inhibitor ornithodorin and similar proteins; The Kunitz inhibitor ...
2512-2555 2.21e-03

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


Pssm-ID: 438655  Cd Length: 49  Bit Score: 38.03  E-value: 2.21e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 240255535 2512 GTCRDFILKWYYDPNTKSCARFWYGgCGGNENKFGSQKECEKVC 2555
Cdd:cd22612     7 TSCAEGAEITYYDSDSRTCKVLAAG-CPSGENAFESEIECQVAC 49
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
1509-1766 3.27e-03

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


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 42.68  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1509 GEDGDKGLPGSSGEKGN---PGRRGDKGPRGEKGERGDVGIRG--DPG-NPGQDSQERGPKGETGDLGPMGVPGRDGVpG 1582
Cdd:cd21118    70 GEEGGSTLGSRGDVFEHrlgEAARSLGNAGNEIGRQAEDIIRHgvDAVhNSWQGSGGHGAYGSQGGPGVQGHGIPGGT-G 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1583 GPGETGKNGGFGRRGPPGAKGNKGGP-----------GQPGFEGEQGTRGaqgpagpagppgligEQGIsgprgsggaag 1651
Cdd:cd21118   149 GPWASGGNYGTNSLGGSVGQGGNGGPlnygtnsqgavAQPGYGTVRGNNQ---------------NSGC----------- 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1652 apgergrTGPLGRKGEPGEpGPKGGIGNRGPRGETGDDGRDGVGSEGRRGKKGERGFPGypGPKGNPGEPGlnGTTGpkg 1731
Cdd:cd21118   203 -------TNPPPSGSHESF-SNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNG--SSSSNSGNSG--GSNG--- 267
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 240255535 1732 irGRRGNSGPPGIVGQKGDPGYPGPAGPKGNRGDS 1766
Cdd:cd21118   268 --GSSGNSGSGSGGSSSGGSNGWGGSSSSGGSGGS 300
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
626-790 3.48e-03

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 41.06  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  626 DVVFLIDGSQS-AGPEFQYV----RTLIERLVDYLDVGfDTTRVAVIQFSDDPKVEFLLnahSSKDEVQnaVQRLRPKGG 700
Cdd:COG4245     7 PVYLLLDTSGSmSGEPIEALneglQALIDELRQDPYAL-ETVEVSVITFDGEAKVLLPL---TDLEDFQ--PPDLSASGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535  701 rqINVGNALEYVsRNIFKRPLGSRIEEGVPQF---LVLISSGK-SDDEVDDPAVELKQFGVAP----FTIA--RNADQEE 770
Cdd:COG4245    81 --TPLGAALELL-LDLIERRVQKYTAEGKGDWrpvVFLITDGEpTDSDWEAALQRLKDGEAAKkaniFAIGvgPDADTEV 157
                         170       180
                  ....*....|....*....|...
gi 240255535  771 LVKISlSPEYVFSVS---TFREL 790
Cdd:COG4245   158 LKQLT-DPVRALDALdglDFREF 179
PRK12678 PRK12678
transcription termination factor Rho; Provisional
1482-1568 4.93e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.20  E-value: 4.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1482 GQRGVKGSRGFPGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVGIRGDPGNPGQDSQERG 1561
Cdd:PRK12678  134 GEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGD 213

                  ....*..
gi 240255535 1562 PKGETGD 1568
Cdd:PRK12678  214 RREERGR 220
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
1794-1892 5.33e-03

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 40.42  E-value: 5.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255535 1794 TELAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIAESNCprgaRVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNL-QVA 1872
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKT----QFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHIsQLL 76
                          90       100
                  ....*....|....*....|
gi 240255535 1873 LTSKQQsleTAMSFVARNTF 1892
Cdd:cd01469    77 GLTNTA---TAIQYVVTELF 93
PTZ00146 PTZ00146
fibrillarin; Provisional
1663-1721 7.73e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 40.87  E-value: 7.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 240255535 1663 GRKGEPGEPGPKGGIGNRGPRGETGddGRDGVGSEGRRGKKGERGFPGYPGPKGNPGEP 1721
Cdd:PTZ00146    5 GFGGGRGGGRGGGGGGGRGGGGRGG--GRGGGRGRGRGGGGGGRGGGGGGGPGKVIVVP 61
 
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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