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Conserved domains on  [gi|159110717|ref|NP_032433|]
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inter-alpha-trypsin inhibitor heavy chain H3 isoform 1 preproprotein [Mus musculus]

Protein Classification

VIT and ITI_HC_C domain-containing protein( domain architecture ID 10652063)

protein containing domains VIT, vWFA, and ITI_HC_C

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 682-870 3.14e-100

Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal region of inter-alpha-trypsin inhibitor heavy chains. Inter-alpha-trypsin inhibitors are glycoproteins with a high inhibitory activity against trypsin, built up from different combinations of four polypeptides: bikunin and the three heavy chains that belong to this family (HC1, HC2, HC3). The heavy chains do not have any protease inhibitory properties but have the capacity to interact in vitro and in vivo with hyaluronic acid, which promotes the stability of the extra-cellular matrix. All family members contain the pfam00092 domain.


:

Pssm-ID: 461981  Cd Length: 189  Bit Score: 309.90  E-value: 3.14e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717  682 VTGITVTGQIIGDKRSNASSRTGKTYFGKLGITNAWMDFRVEVTTEKIILGTGAELSTFSWLDTITVTQTGLSVTINRKK 761
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717  762 NMVVSFGDGISFVIILHQVWKKHPVHQDFLGFYVVDSHRMSAQTHGLLGQFFQPFDFKVFGIRPGSDPTKPDATMVVKNH 841
Cdd:pfam06668  81 NVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKGH 160

                         170       180
                  ....*....|....*....|....*....
gi 159110717  842 RLTVTRGSQKDYRKDASVGTKVICWFVHN 870
Cdd:pfam06668 161 KLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
29-158 2.29e-67

Vault protein Inter-alpha-Trypsin domain;


:

Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 220.31  E-value: 2.29e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717    29 LLGKRSLPEGVVDGIEVYSTKISCKVTSRFAHNVVTTRAVNRADTAKEVSFDVELPKTAFITNFTLTIDGVTYPGNVKEK 108
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 159110717   109 EVAQKQYEKAVSQGKTAGLVKASGRKLEKFTVSVNVAAGSKVTFELTYEE 158
Cdd:smart00609  81 EVAQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 281-462 6.20e-59

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 cd01461:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 171  Bit Score: 198.59  E-value: 6.20e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 281 VPKNIVFVIDVSGSMSGRKIQQTREALLKILDDVKEDDYLNFILFSTDVTTWKDHLVQATPANLKEAKTFVKNIHDQSMT 360
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 361 NINDGLLKGIEMLNKaredhtvPERSTSIIIMLTDGDantgESRPEKIQENVRNAIGGKFPLYNLGFGNNLNYNFLETLA 440
Cdd:cd01461   81 NMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 159110717 441 LENHGLARRIYEDSDANLQLQG 462
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
 
Name Accession Description Interval E-value
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 682-870 3.14e-100

Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal region of inter-alpha-trypsin inhibitor heavy chains. Inter-alpha-trypsin inhibitors are glycoproteins with a high inhibitory activity against trypsin, built up from different combinations of four polypeptides: bikunin and the three heavy chains that belong to this family (HC1, HC2, HC3). The heavy chains do not have any protease inhibitory properties but have the capacity to interact in vitro and in vivo with hyaluronic acid, which promotes the stability of the extra-cellular matrix. All family members contain the pfam00092 domain.


Pssm-ID: 461981  Cd Length: 189  Bit Score: 309.90  E-value: 3.14e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717  682 VTGITVTGQIIGDKRSNASSRTGKTYFGKLGITNAWMDFRVEVTTEKIILGTGAELSTFSWLDTITVTQTGLSVTINRKK 761
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717  762 NMVVSFGDGISFVIILHQVWKKHPVHQDFLGFYVVDSHRMSAQTHGLLGQFFQPFDFKVFGIRPGSDPTKPDATMVVKNH 841
Cdd:pfam06668  81 NVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKGH 160

                         170       180
                  ....*....|....*....|....*....
gi 159110717  842 RLTVTRGSQKDYRKDASVGTKVICWFVHN 870
Cdd:pfam06668 161 KLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
29-158 2.29e-67

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 220.31  E-value: 2.29e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717    29 LLGKRSLPEGVVDGIEVYSTKISCKVTSRFAHNVVTTRAVNRADTAKEVSFDVELPKTAFITNFTLTIDGVTYPGNVKEK 108
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 159110717   109 EVAQKQYEKAVSQGKTAGLVKASGRKLEKFTVSVNVAAGSKVTFELTYEE 158
Cdd:smart00609  81 EVAQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 281-462 6.20e-59

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


Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 198.59  E-value: 6.20e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 281 VPKNIVFVIDVSGSMSGRKIQQTREALLKILDDVKEDDYLNFILFSTDVTTWKDHLVQATPANLKEAKTFVKNIHDQSMT 360
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 361 NINDGLLKGIEMLNKaredhtvPERSTSIIIMLTDGDantgESRPEKIQENVRNAIGGKFPLYNLGFGNNLNYNFLETLA 440
Cdd:cd01461   81 NMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 159110717 441 LENHGLARRIYEDSDANLQLQG 462
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 274-480 4.15e-41

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 152.95  E-value: 4.15e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 274 APQGLPVVPKNIVFVIDVSGSMSGRKIQQTREALLKILDDVKEDDYLNFILFSTDVTTwkdhLVQATPA-NLKEAKTFVK 352
Cdd:COG2304   83 KAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARV----LLPPTPAtDRAKILAAID 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 353 NIHDQSMTNINDGLLKGIEMLNKAREDHTVperstSIIIMLTDGDANTGESRPEKIQENVRNAIGGKFPLYNLGFGNNLN 432
Cdd:COG2304  159 RLQAGGGTALGAGLELAYELARKHFIPGRV-----NRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDYN 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 159110717 433 YNFLETLALENHGLARRIYEDSDANLQLQGFYEEVANPLLTNVEVEYP 480
Cdd:COG2304  234 EDLLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFP 281
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 45-156 2.35e-39

Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilization and tumour metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.


Pssm-ID: 462492 [Multi-domain]  Cd Length: 111  Bit Score: 141.08  E-value: 2.35e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717   45 VYSTKISCKVTSRFAHNVVTTRAVNRADTAKEVSFDVELPKTAFITNFTLTIDGVTYPGNVKEKEVAQKQYEKAVSQGKT 124
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 159110717  125 AGLVKASGRklEKFTVSV-NVAAGSKVTFELTY 156
Cdd:pfam08487  81 AGLLEQDTP--DVFTTSVgNIPPGEKVTVELTY 111
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 284-461 6.62e-26

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: 105.23  E-value: 6.62e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717   284 NIVFVIDVSGSMSGRKIQQTREALLKI---LDDVKEDDYLNFILFSTDVTTWKDhLVQATpaNLKEAKTFVKNIHDQSM- 359
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLveqLDIGPDGDRVGLVTFSDDARVLFP-LNDSR--SKDALLEALASLSYKLGg 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717   360 -TNINDGLLKGIEMLNKAREDHTvpERSTSIIIMLTDGDANTGESRpekIQENVRNAIGGKFPLYNLGFGNNLNYNFLET 438
Cdd:smart00327  78 gTNLGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDGPKD---LLKAAKELKRSGVKVFVVGVGNDVDEEELKK 152

                          170       180
                   ....*....|....*....|...
gi 159110717   439 LALENHGLARRIYEDSDANLQLQ 461
Cdd:smart00327 153 LASAPGGVYVFLPELLDLLIDLL 175
VWA pfam00092
von Willebrand factor type A domain;
284-466 1.35e-23

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 98.50  E-value: 1.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717  284 NIVFVIDVSGSMSGRKIQQTREALLKILDDV---KEDDYLNFILFSTDVTTWKDhLVQATpaNLKEAKTFVKNI--HDQS 358
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEFP-LNDYS--SKEELLSAVDNLryLGGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717  359 MTNINDGLLKGIEMLNKAREDHtvPERSTSIIIMLTDGDANTGEsrpekIQENVRNAIGGKFPLYNLGFGNNLNYNfLET 438
Cdd:pfam00092  78 TTNTGKALKYALENLFSSAAGA--RPGAPKVVVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNADDEE-LRK 149

                         170       180
                  ....*....|....*....|....*...
gi 159110717  439 LALENHglARRIYEDSDANlQLQGFYEE 466
Cdd:pfam00092 150 IASEPG--EGHVFTVSDFE-ALEDLQDQ 174
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
 285-411 1.85e-03

calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out AC found a row in 1A13.INFO that was not parsed out EC found a row in 1A13.INFO that was not parsed out GA found a row in 1A13.INFO that was not parsed out SO found a row in 1A13.INFO that was not parsed out RH found a row in 1A13.INFO that was not parsed out EN found a row in 1A13.INFO that was not parsed out GS found a row in 1A13.INFO that was not parsed out AL found a row in 1A13.INFO that was not parsed out The Epithelial Chloride Channel (E-ClC) Family (TC 1.A.13) found a row in 1A13.INFO that was not parsed out found a row in 1A13.INFO that was not parsed out Mammals have multiple isoforms of epithelial chloride channel proteins. The first member of this family to be characterized was a respiratory epithelium, Ca found a row in 1A13.INFO that was not parsed out 2+-regulated, chloride channel protein isolated from bovine tracheal apical membranes. It was biochemically characterized as a 140 kDa complex. The purified found a row in 1A13.INFO that was not parsed out complex when reconstituted in a planar lipid bilayer behaved as an anion-selective channel. It was regulated by Ca 2+ via a calmodulin kinase II-dependent found a row in 1A13.INFO that was not parsed out mechanism. When the cRNA was injected into Xenopus oocytes, an outward rectifying, DIDS-sensitive, anion conductance was measured. A related gene, found a row in 1A13.INFO that was not parsed out Lu-ECAM, was cloned from the bovine aortic endothelial cell line, BAEC. It is expressed in the lung and spleen but not in the trachea. Homologues are found in found a row in 1A13.INFO that was not parsed out several mammals, and at least three paralogues(hCaCC-1-3) are present in humans, each with different tissue distributions. found a row in 1A13.INFO that was not parsed out [Transport and binding proteins, Anions]


Pssm-ID: 129946 [Multi-domain]  Cd Length: 863  Bit Score: 42.18  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717  285 IVFVIDVSGSMS--GRKIQQTREALLKILDDVKEDDYLNFILFSTdVTTWKDHLVQATPANlkEAKTFVKNIHDQSM--T 360
Cdd:TIGR00868 307 VCLVLDKSGSMTveDRLKRMNQAAKLFLLQTVEKGSWVGMVTFDS-AAYIKNELIQITSSA--ERDALTANLPTAASggT 383

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 159110717  361 NINDGLLKGIEMLNKARedhtvPERSTSIIIMLTDGDANTGESRPEKIQEN 411
Cdd:TIGR00868 384 SICSGLKAAFQVIKKSY-----QSTDGSEIVLLTDGEDNTISSCFEEVKQS 429
 
Name Accession Description Interval E-value
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 682-870 3.14e-100

Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal region of inter-alpha-trypsin inhibitor heavy chains. Inter-alpha-trypsin inhibitors are glycoproteins with a high inhibitory activity against trypsin, built up from different combinations of four polypeptides: bikunin and the three heavy chains that belong to this family (HC1, HC2, HC3). The heavy chains do not have any protease inhibitory properties but have the capacity to interact in vitro and in vivo with hyaluronic acid, which promotes the stability of the extra-cellular matrix. All family members contain the pfam00092 domain.


Pssm-ID: 461981  Cd Length: 189  Bit Score: 309.90  E-value: 3.14e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717  682 VTGITVTGQIIGDKRSNASSRTGKTYFGKLGITNAWMDFRVEVTTEKIILGTGAELSTFSWLDTITVTQTGLSVTINRKK 761
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717  762 NMVVSFGDGISFVIILHQVWKKHPVHQDFLGFYVVDSHRMSAQTHGLLGQFFQPFDFKVFGIRPGSDPTKPDATMVVKNH 841
Cdd:pfam06668  81 NVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKGH 160

                         170       180
                  ....*....|....*....|....*....
gi 159110717  842 RLTVTRGSQKDYRKDASVGTKVICWFVHN 870
Cdd:pfam06668 161 KLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
29-158 2.29e-67

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 220.31  E-value: 2.29e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717    29 LLGKRSLPEGVVDGIEVYSTKISCKVTSRFAHNVVTTRAVNRADTAKEVSFDVELPKTAFITNFTLTIDGVTYPGNVKEK 108
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 159110717   109 EVAQKQYEKAVSQGKTAGLVKASGRKLEKFTVSVNVAAGSKVTFELTYEE 158
Cdd:smart00609  81 EVAQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 281-462 6.20e-59

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


Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 198.59  E-value: 6.20e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 281 VPKNIVFVIDVSGSMSGRKIQQTREALLKILDDVKEDDYLNFILFSTDVTTWKDHLVQATPANLKEAKTFVKNIHDQSMT 360
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 361 NINDGLLKGIEMLNKaredhtvPERSTSIIIMLTDGDantgESRPEKIQENVRNAIGGKFPLYNLGFGNNLNYNFLETLA 440
Cdd:cd01461   81 NMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 159110717 441 LENHGLARRIYEDSDANLQLQG 462
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 274-480 4.15e-41

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 152.95  E-value: 4.15e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 274 APQGLPVVPKNIVFVIDVSGSMSGRKIQQTREALLKILDDVKEDDYLNFILFSTDVTTwkdhLVQATPA-NLKEAKTFVK 352
Cdd:COG2304   83 KAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARV----LLPPTPAtDRAKILAAID 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 353 NIHDQSMTNINDGLLKGIEMLNKAREDHTVperstSIIIMLTDGDANTGESRPEKIQENVRNAIGGKFPLYNLGFGNNLN 432
Cdd:COG2304  159 RLQAGGGTALGAGLELAYELARKHFIPGRV-----NRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDYN 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 159110717 433 YNFLETLALENHGLARRIYEDSDANLQLQGFYEEVANPLLTNVEVEYP 480
Cdd:COG2304  234 EDLLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALATEDFP 281
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 45-156 2.35e-39

Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilization and tumour metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.


Pssm-ID: 462492 [Multi-domain]  Cd Length: 111  Bit Score: 141.08  E-value: 2.35e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717   45 VYSTKISCKVTSRFAHNVVTTRAVNRADTAKEVSFDVELPKTAFITNFTLTIDGVTYPGNVKEKEVAQKQYEKAVSQGKT 124
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 159110717  125 AGLVKASGRklEKFTVSV-NVAAGSKVTFELTY 156
Cdd:pfam08487  81 AGLLEQDTP--DVFTTSVgNIPPGEKVTVELTY 111
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 284-445 7.42e-29

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: 113.52  E-value: 7.42e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 284 NIVFVIDVSGSMSGRKIQQTREALLKILDDVKEDDYLNFILFSTDVTTwkdhLVQATPANLKEA-KTFVKNIHDQSMTNI 362
Cdd:cd01465    2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAET----VLPATPVRDKAAiLAAIDRLTAGGSTAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 363 NDGLLKGIEMLNKAREDhtvpeRSTSIIIMLTDGDANTGESRPEKIQENVRNAIGGKFPLYNLGFGNNLNYNFLETLALE 442
Cdd:cd01465   78 GAGIQLGYQEAQKHFVP-----GGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAIADA 152


                 ...
gi 159110717 443 NHG 445
Cdd:cd01465  153 GNG 155
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 284-461 6.62e-26

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: 105.23  E-value: 6.62e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717   284 NIVFVIDVSGSMSGRKIQQTREALLKI---LDDVKEDDYLNFILFSTDVTTWKDhLVQATpaNLKEAKTFVKNIHDQSM- 359
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLveqLDIGPDGDRVGLVTFSDDARVLFP-LNDSR--SKDALLEALASLSYKLGg 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717   360 -TNINDGLLKGIEMLNKAREDHTvpERSTSIIIMLTDGDANTGESRpekIQENVRNAIGGKFPLYNLGFGNNLNYNFLET 438
Cdd:smart00327  78 gTNLGAALQYALENLFSKSAGSR--RGAPKVVILITDGESNDGPKD---LLKAAKELKRSGVKVFVVGVGNDVDEEELKK 152

                          170       180
                   ....*....|....*....|...
gi 159110717   439 LALENHGLARRIYEDSDANLQLQ 461
Cdd:smart00327 153 LASAPGGVYVFLPELLDLLIDLL 175
VWA pfam00092
von Willebrand factor type A domain;
284-466 1.35e-23

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 98.50  E-value: 1.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717  284 NIVFVIDVSGSMSGRKIQQTREALLKILDDV---KEDDYLNFILFSTDVTTWKDhLVQATpaNLKEAKTFVKNI--HDQS 358
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdigPDGTRVGLVQYSSDVRTEFP-LNDYS--SKEELLSAVDNLryLGGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717  359 MTNINDGLLKGIEMLNKAREDHtvPERSTSIIIMLTDGDANTGEsrpekIQENVRNAIGGKFPLYNLGFGNNLNYNfLET 438
Cdd:pfam00092  78 TTNTGKALKYALENLFSSAAGA--RPGAPKVVVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNADDEE-LRK 149

                         170       180
                  ....*....|....*....|....*...
gi 159110717  439 LALENHglARRIYEDSDANlQLQGFYEE 466
Cdd:pfam00092 150 IASEPG--EGHVFTVSDFE-ALEDLQDQ 174
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 284-440 1.51e-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: 98.02  E-value: 1.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 284 NIVFVIDVSGSMSGRKIQQTREALLKILDDVK---EDDYLNFILFSTDVTTWKDHLVQATPANLKEAKTFVKNIHDQSmT 360
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSaspPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGG-T 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 361 NINDGLLKGIEMLNKAREDHtvperSTSIIIMLTDGDANTGESRPEKIQENVRNAiggKFPLYNLGFGNNLNYNFLETLA 440
Cdd:cd00198   81 NIGAALRLALELLKSAKRPN-----ARRVIILLTDGEPNDGPELLAEAARELRKL---GITVYTIGIGDDANEDELKEIA 152
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 274-468 2.24e-22

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: 97.70  E-value: 2.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 274 APQGLPVVPKNIVFVIDVSGSMSGR-KIQQTREALLKILDDVKEDDYLNFILFSTDVTtwkdhLVQATPANLKEAKTFVK 352
Cdd:COG1240   84 LALARPQRGRDVVLVVDASGSMAAEnRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAE-----VLLPLTRDREALKRALD 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 353 NIHDQSMTNINDGLLKGIEMLNKAREDhtvperSTSIIIMLTDGDANTGESRPEKIQENVRNAiggKFPLYNLGFG-NNL 431
Cdd:COG1240  159 ELPPGGGTPLGDALALALELLKRADPA------RRKVIVLLTDGRDNAGRIDPLEAAELAAAA---GIRIYTIGVGtEAV 229

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 159110717 432 NYNFLETLALENHGLARRIyedSDANlQLQGFYEEVA 468
Cdd:COG1240  230 DEGLLREIAEATGGRYFRA---DDLS-ELAAIYREID 262
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 274-440 4.70e-22

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 96.67  E-value: 4.70e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 274 APQGLPVVPKNIVFVIDVSGSMSGRKIQQTREALLKILDDVKEDDYLNFILFSTDVTTwkDHLVQATPaNLKEAKTFVKN 353
Cdd:COG2425  110 ASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVE--DLPLTADD-GLEDAIEFLSG 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 354 IHDQSMTNINDGLLKGIEMLNKaredhtvPERSTSIIIMLTDGDANTGesrPEKIQENVRNAIGGkFPLYNLGFGNNLNY 433
Cdd:COG2425  187 LFAGGGTDIAPALRAALELLEE-------PDYRNADIVLITDGEAGVS---PEELLREVRAKESG-VRLFTVAIGDAGNP 255


                 ....*..
gi 159110717 434 NFLETLA 440
Cdd:COG2425  256 GLLEALA 262
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 285-440 7.72e-15

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


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 72.81  E-value: 7.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 285 IVFVIDVSGSMSGRKIQQTREALLKILDDVKEDDYLNFILFSTDVTTWKDhLVQATPANLKEAKTFVKNIHDQSMTNIND 364
Cdd:cd01466    3 LVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSP-LRRMTAKGKRSAKRVVDGLQAGGGTNVVG 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 159110717 365 GLLKGIEMLNKAREDHtvpeRSTSIIIMlTDGDANTGESrpekiqenVRNAIGGKFPLYNLGFGNNLNYNFLETLA 440
Cdd:cd01466   82 GLKKALKVLGDRRQKN----PVASIMLL-SDGQDNHGAV--------VLRADNAPIPIHTFGLGASHDPALLAFIA 144
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 281-445 2.55e-14

VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The alpha 2 and delta subunits result from proteolytic processing of a single gene product and carries at its N-terminus the VWA and cache domains, The alpha 2 delta gene family has orthologues in D. melanogaster and C. elegans but none have been detected in aither A. thaliana or yeast. The exact biochemical function of the VWA domain is not known but the alpha 2 delta complex has been shown to regulate various functional properties of the channel complex.


Pssm-ID: 238740 [Multi-domain]  Cd Length: 190  Bit Score: 72.43  E-value: 2.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 281 VPKNIVFVIDVSGSMSGRKIQQTREALLKILDDVKEDDYLNFILFSTDVTT----WKDHLVQATPANLKEAKTFVKNIHD 356
Cdd:cd01463   12 SPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPvvpcFNDTLVQATTSNKKVLKEALDMLEA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 357 QSMTNINDGLLKGIEMLNKAREDHTVPERST--SIIIMLTDGdantGESRPEKI--QENVRNAIGGKFPLYNLGFG-NNL 431
Cdd:cd01463   92 KGIANYTKALEFAFSLLLKNLQSNHSGSRSQcnQAIMLITDG----VPENYKEIfdKYNWDKNSEIPVRVFTYLIGrEVT 167

                        170
                 ....*....|....
gi 159110717 432 NYNFLETLALENHG 445
Cdd:cd01463  168 DRREIQWMACENKG 181
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
284-440 4.91e-13

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 68.80  E-value: 4.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 284 NIVFVIDVSGSMSGRKIQQTREALLKILDDVKEDDYLN------FILFSTDVTTwkdhlvqATPanLKEAKTF-VKNIHD 356
Cdd:COG4245    7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYALetvevsVITFDGEAKV-------LLP--LTDLEDFqPPDLSA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 357 QSMTNINDGLLKGIEMLNKAREDHTvPERSTS---IIIMLTDG---DANTGESRpEKIQENVRNAIGGKFPlynLGFGNN 430
Cdd:COG4245   78 SGGTPLGAALELLLDLIERRVQKYT-AEGKGDwrpVVFLITDGeptDSDWEAAL-QRLKDGEAAKKANIFA---IGVGPD 152

                        170
                 ....*....|
gi 159110717 431 LNYNFLETLA 440
Cdd:COG4245  153 ADTEVLKQLT 162
VWA_3 pfam13768
von Willebrand factor type A domain;
283-448 2.23e-09

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 57.02  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717  283 KNIVFVIDVSGSMSGRKIQQtREALLKILDDVKEDDYLNFILFSTDVTTWKDHLVQATPANLKEAKTFVKNI-HDQSMTN 361
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLqPPLGGSD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717  362 INDGLLKGIEMLNKaredhtvPERSTSIIIMlTDGDANTGESRpekIQENVRNAIgGKFPLYNLGFGNNLNYNFLETLAL 441
Cdd:pfam13768  80 LLGALKEAVRAPAS-------PGYIRHVLLL-TDGSPMQGETR---VSDLISRAP-GKIRFFAYGLGASISAPMLQLLAE 147


                  ....*..
gi 159110717  442 ENHGLAR 448
Cdd:pfam13768 148 ASNGTYE 154
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 284-414 1.24e-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: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 54.99  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 284 NIVFVIDVSGSMSGRKIQQTREALLKI---LDDVKEDDYLNFILFSTDVTTWKDHLVQATPANLKEAktfVKNIHDQSM- 359
Cdd:cd01450    2 DIVFLLDGSESVGPENFEKVKDFIEKLvekLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKA---VKNLKYLGGg 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 159110717 360 -TNINDGLLKGIEMLNKAREDHtvpERSTSIIIMLTDGDANTGESrPEKIQENVRN 414
Cdd:cd01450   79 gTNTGKALQYALEQLFSESNAR---ENVPKVIIVLTDGRSDDGGD-PKEAAAKLKD 130
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 284-447 1.83e-06

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 49.25  E-value: 1.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 284 NIVFVIDVSGSMSGRKIQQ------TREALLKILDDvKEDDYLNFILFStdvttwkDHLVQATP--ANLKEAKTFVKNIH 355
Cdd:cd01467    4 DIMIALDVSGSMLAQDFVKpsrleaAKEVLSDFIDR-RENDRIGLVVFA-------GAAFTQAPltLDRESLKELLEDIK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 356 ---DQSMTNINDGLLKGIEMLNKAredhtvpERSTSIIIMLTDGDANTGESRPEKI-----QENVRnaiggkfpLYNLGF 427
Cdd:cd01467   76 iglAGQGTAIGDAIGLAIKRLKNS-------EAKERVIVLLTDGENNAGEIDPATAaelakNKGVR--------IYTIGV 140

                        170       180       190
                 ....*....|....*....|....*....|.
gi 159110717 428 GNN-----------LNYNFLETLALENHGLA 447
Cdd:cd01467  141 GKSgsgpkpdgstiLDEDSLVEIADKTGGRI 171
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 285-396 1.01e-05

VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 46.95  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 285 IVFVIDVSGSMSGRKIQQTREALLKILDDVKEDDY-LNFILFStdVTTWKDHLVQATPanLKEAKTF-VKNIHDQSMTNI 362
Cdd:cd01464    6 IYLLLDTSGSMAGEPIEALNQGLQMLQSELRQDPYaLESVEIS--VITFDSAARVIVP--LTPLESFqPPRLTASGGTSM 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 159110717 363 NDGLLKGIEMLNKAREDHTVPERS--TSIIIMLTDG 396
Cdd:cd01464   82 GAALELALDCIDRRVQRYRADQKGdwRPWVFLLTDG 117
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 284-469 1.43e-05

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: 46.61  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 284 NIVFVIDVSGSMSG----RKIQQTREALLKILDDVKEDDYLNFILFSTDVTT-WKdhlVQATPANLKEAKTFVknIHD-Q 357
Cdd:cd01471    2 DLYLLVDGSGSIGYsnwvTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKElIR---LSSPNSTNKDLALNA--IRAlL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 358 SM------TNINDGLLKGIEMLNKARedhtvPERSTSI--IIMLTDGDANTgESRPEKIQENVRNAiGGKFPLynLGFGN 429
Cdd:cd01471   77 SLyypngsTNTTSALLVVEKHLFDTR-----GNRENAPqlVIIMTDGIPDS-KFRTLKEARKLRER-GVIIAV--LGVGQ 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 159110717 430 NLNYNFLETLAlenhGLARRiyeDSDANLQLQGFYEEVAN 469
Cdd:cd01471  148 GVNHEENRSLV----GCDPD---DSPCPLYLQSSWSEVQN 180
VWA_2 pfam13519
von Willebrand factor type A domain;
285-393 6.96e-05

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 42.66  E-value: 6.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717  285 IVFVIDVSGSMSGRKIQQTR-----EALLKILDDVKEdDYLNFILFSTDV---TTWKDhlvqatpaNLKEAKTFVKNIHD 356
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRleaakDAVLALLKSLPG-DRVGLVTFGDGPevlIPLTK--------DRAKILRALRRLEP 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 159110717  357 QSM-TNINDGLLKGIEMLNKAREDHtvpersTSIIIML 393
Cdd:pfam13519  72 KGGgTNLAAALQLARAALKHRRKNQ------PRRIVLI 103
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 284-440 9.82e-04

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


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 41.12  E-value: 9.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 284 NIVFVIDVSGSMSGRKIQQTREALLKILDdvKEDDY---LNF--ILFSTDVTTW------KDHLVQATPANLKEAKtfVK 352
Cdd:cd01470    2 NIYIALDASDSIGEEDFDEAKNAIKTLIE--KISSYevsPRYeiISYASDPKEIvsirdfNSNDADDVIKRLEDFN--YD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717 353 NIHDQSMTNINDGLLKGIEMLnkAREDHTVPERSTSI---IIMLTDGDANTGESrPEKIQENVRNAIG----GKFP---- 421
Cdd:cd01470   78 DHGDKTGTNTAAALKKVYERM--ALEKVRNKEAFNETrhvIILFTDGKSNMGGS-PLPTVDKIKNLVYknnkSDNPredy 154

                        170       180
                 ....*....|....*....|.
gi 159110717 422 --LYNLGFGNNLNYNFLETLA 440
Cdd:cd01470  155 ldVYVFGVGDDVNKEELNDLA 175
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
 285-411 1.85e-03

calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out AC found a row in 1A13.INFO that was not parsed out EC found a row in 1A13.INFO that was not parsed out GA found a row in 1A13.INFO that was not parsed out SO found a row in 1A13.INFO that was not parsed out RH found a row in 1A13.INFO that was not parsed out EN found a row in 1A13.INFO that was not parsed out GS found a row in 1A13.INFO that was not parsed out AL found a row in 1A13.INFO that was not parsed out The Epithelial Chloride Channel (E-ClC) Family (TC 1.A.13) found a row in 1A13.INFO that was not parsed out found a row in 1A13.INFO that was not parsed out Mammals have multiple isoforms of epithelial chloride channel proteins. The first member of this family to be characterized was a respiratory epithelium, Ca found a row in 1A13.INFO that was not parsed out 2+-regulated, chloride channel protein isolated from bovine tracheal apical membranes. It was biochemically characterized as a 140 kDa complex. The purified found a row in 1A13.INFO that was not parsed out complex when reconstituted in a planar lipid bilayer behaved as an anion-selective channel. It was regulated by Ca 2+ via a calmodulin kinase II-dependent found a row in 1A13.INFO that was not parsed out mechanism. When the cRNA was injected into Xenopus oocytes, an outward rectifying, DIDS-sensitive, anion conductance was measured. A related gene, found a row in 1A13.INFO that was not parsed out Lu-ECAM, was cloned from the bovine aortic endothelial cell line, BAEC. It is expressed in the lung and spleen but not in the trachea. Homologues are found in found a row in 1A13.INFO that was not parsed out several mammals, and at least three paralogues(hCaCC-1-3) are present in humans, each with different tissue distributions. found a row in 1A13.INFO that was not parsed out [Transport and binding proteins, Anions]


Pssm-ID: 129946 [Multi-domain]  Cd Length: 863  Bit Score: 42.18  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717  285 IVFVIDVSGSMS--GRKIQQTREALLKILDDVKEDDYLNFILFSTdVTTWKDHLVQATPANlkEAKTFVKNIHDQSM--T 360
Cdd:TIGR00868 307 VCLVLDKSGSMTveDRLKRMNQAAKLFLLQTVEKGSWVGMVTFDS-AAYIKNELIQITSSA--ERDALTANLPTAASggT 383

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 159110717  361 NINDGLLKGIEMLNKARedhtvPERSTSIIIMLTDGDANTGESRPEKIQEN 411
Cdd:TIGR00868 384 SICSGLKAAFQVIKKSY-----QSTDGSEIVLLTDGEDNTISSCFEEVKQS 429
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 281-427 4.35e-03

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 39.98  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717  281 VPKNIVFVIDVSGSMSgRKIQQTREALLKILDDVKED-DYLNFILFSTDV------TTWKDHLVQAtpanLKEAKTFVKN 353
Cdd:TIGR03436  52 LPLTVGLVIDTSGSMR-NDLDRARAAAIRFLKTVLRPnDRVFVVTFNTRLrllqdfTSDPRLLEAA----LNRLKPPLRT 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159110717  354 IHDQSMTNINDGL---------LKGIEMLnkAREDHTVPERstSIIIMLTDGDANtgESRPeKIQENVRNAIGGKFPLYN 424
Cdd:TIGR03436 127 DYNSSGAFVRDGGgtalydaitLAALEQL--ANALAGIPGR--KALIVISDGGDN--RSRD-TLERAIDAAQRADVAIYS 199


                  ...
gi 159110717  425 LGF 427
Cdd:TIGR03436 200 IDA 202
 
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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