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Conserved domains on  [gi|1969806716|ref|NP_001378951|]
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inter-alpha-trypsin inhibitor heavy chain H3 isoform 5 precursor [Homo sapiens]

Protein Classification

inter-alpha-trypsin inhibitor heavy chain H( domain architecture ID 10652060)

inter-alpha-trypsin inhibitor heavy chain H may act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes

Gene Ontology:  GO:0030212|GO:0004867

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 ...
 681-868 5.50e-99

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: 306.82  E-value: 5.50e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 681 VTGLTVNGQITGDKRGSPDSKTRKTYFGKLGIANAQMDFQVEVTTEKITLWNRAVPSTFSWLDTVTVTQDGLSMMINR-K 759
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKnS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 760 NMVVSFGDGVTFVVVLHQVWKKHPVHRDFLGFYVVDSHRMSAQTHGLLGQFFQPFDFKVSDIRPGSDPTKPDATLVVKNH 839
Cdd:pfam06668  81 NVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKGH 160

                         170       180
                  ....*....|....*....|....*....
gi 1969806716 840 QLIVTRGSQKDYRKDASIGTKVVCWFVHN 868
Cdd:pfam06668 161 KLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
29-158 4.35e-66

Vault protein Inter-alpha-Trypsin domain;


:

Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 216.84  E-value: 4.35e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716   29 LLGKRSLPEGVANGIEVYSTKINSKVTSRFAHNVVTMRAVNRADTAKEVSFDVELPKTAFITNFTLTIDGVTYPGNVKEK 108
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1969806716  109 EVAKKQYEKAVSQGKTAGLVKASGRKLEKFTVSVNVAAGSKVTFELTYEE 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 5.63e-62

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: 207.07  E-value: 5.63e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 281 VPKNVAFVIDISGSMAGRKLEQTKEALLRILEDMQEEDYLNFILFSGDVSTWKEHLVQATPENLQEARTFVKSMEDKGMT 360
Cdd:cd01461     1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 361 NINDGLLRGISMLNKareehriPERSTSIVIMLTDGDanvgESRPEKIQENVRNAIGGKFPLYNLGFGNNLNYNFLENMA 440
Cdd:cd01461    81 NMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                         170       180
                  ....*....|....*....|..
gi 1969806716 441 LENHGFARRIYEDSDADLQLQG 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 ...
 681-868 5.50e-99

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: 306.82  E-value: 5.50e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 681 VTGLTVNGQITGDKRGSPDSKTRKTYFGKLGIANAQMDFQVEVTTEKITLWNRAVPSTFSWLDTVTVTQDGLSMMINR-K 759
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKnS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 760 NMVVSFGDGVTFVVVLHQVWKKHPVHRDFLGFYVVDSHRMSAQTHGLLGQFFQPFDFKVSDIRPGSDPTKPDATLVVKNH 839
Cdd:pfam06668  81 NVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKGH 160

                         170       180
                  ....*....|....*....|....*....
gi 1969806716 840 QLIVTRGSQKDYRKDASIGTKVVCWFVHN 868
Cdd:pfam06668 161 KLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
29-158 4.35e-66

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 216.84  E-value: 4.35e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716   29 LLGKRSLPEGVANGIEVYSTKINSKVTSRFAHNVVTMRAVNRADTAKEVSFDVELPKTAFITNFTLTIDGVTYPGNVKEK 108
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1969806716  109 EVAKKQYEKAVSQGKTAGLVKASGRKLEKFTVSVNVAAGSKVTFELTYEE 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 5.63e-62

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: 207.07  E-value: 5.63e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 281 VPKNVAFVIDISGSMAGRKLEQTKEALLRILEDMQEEDYLNFILFSGDVSTWKEHLVQATPENLQEARTFVKSMEDKGMT 360
Cdd:cd01461     1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 361 NINDGLLRGISMLNKareehriPERSTSIVIMLTDGDanvgESRPEKIQENVRNAIGGKFPLYNLGFGNNLNYNFLENMA 440
Cdd:cd01461    81 NMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                         170       180
                  ....*....|....*....|..
gi 1969806716 441 LENHGFARRIYEDSDADLQLQG 462
Cdd:cd01461   150 REGRGIARRIYETDDIESQLLR 171
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 274-473 1.40e-43

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 159.88  E-value: 1.40e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 274 APQGLPVVPKNVAFVIDISGSMAGRKLEQTKEALLRILEDMQEEDYLNFILFSGDVSTwkehLVQATP-ENLQEARTFVK 352
Cdd:COG2304    83 KAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARV----LLPPTPaTDRAKILAAID 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 353 SMEDKGMTNINDGLLRGISMLNKAREEHRIperstSIVIMLTDGDANVGESRPEKIQENVRNAIGGKFPLYNLGFGNNLN 432
Cdd:COG2304   159 RLQAGGGTALGAGLELAYELARKHFIPGRV-----NRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDYN 233

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1969806716 433 YNFLENMALENHGFARRIYEDSDADLQLQGFYEEVANPLLT 473
Cdd:COG2304   234 EDLLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRA 274
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 45-156 9.27e-41

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: 145.32  E-value: 9.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716  45 VYSTKINSKVTSRFAHNVVTMRAVNRADTAKEVSFDVELPKTAFITNFTLTIDGVTYPGNVKEKEVAKKQYEKAVSQGKT 124
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1969806716 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 5.41e-25

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: 102.53  E-value: 5.41e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716  284 NVAFVIDISGSMAGRKLEQTKEALLRILEDM---QEEDYLNFILFSGDVSTWKEhLVQATpeNLQEARTFVKSMEDK--G 358
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFP-LNDSR--SKDALLEALASLSYKlgG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716  359 MTNINDGLLRGISMLNKAREEHRIPERstSIVIMLTDGDANVGESRpekIQENVRNAIGGKFPLYNLGFGNNLNYNFLEN 438
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGSRRGAP--KVVILITDGESNDGPKD---LLKAAKELKRSGVKVFVVGVGNDVDEEELKK 152

                          170       180
                   ....*....|....*....|...
gi 1969806716  439 MALENHGfaRRIYEDSDADLQLQ 461
Cdd:smart00327 153 LASAPGG--VYVFLPELLDLLID 173
VWA pfam00092
von Willebrand factor type A domain;
284-466 7.24e-25

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 101.97  E-value: 7.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 284 NVAFVIDISGSMAGRKLEQTKEALLRILEDMQ---EEDYLNFILFSGDVstwKEHLVQATPENLQEARTFVKSME--DKG 358
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDV---RTEFPLNDYSSKEELLSAVDNLRylGGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 359 MTNINDGLLRGISMLNKAREEHRipERSTSIVIMLTDGDANVGEsrpekIQENVRNAIGGKFPLYNLGFGNNLNYNfLEN 438
Cdd:pfam00092  78 TTNTGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNADDEE-LRK 149

                         170       180
                  ....*....|....*....|....*...
gi 1969806716 439 MALENHgfARRIYEDSDADlQLQGFYEE 466
Cdd:pfam00092 150 IASEPG--EGHVFTVSDFE-ALEDLQDQ 174
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 281-427 4.08e-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: 40.37  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 281 VPKNVAFVIDISGSMAgRKLEQTKEALLRILED-MQEEDYLnFIL-----------FSGDVSTWKEHLVQATPENLQEAR 348
Cdd:TIGR03436  52 LPLTVGLVIDTSGSMR-NDLDRARAAAIRFLKTvLRPNDRV-FVVtfntrlrllqdFTSDPRLLEAALNRLKPPLRTDYN 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 349 TFVKSMEDKGMTNINDGL-LRGISMLnkAREEHRIPERSTSIVImlTDGDANvgESRPeKIQENVRNAIGGKFPLYNLGF 427
Cdd:TIGR03436 130 SSGAFVRDGGGTALYDAItLAALEQL--ANALAGIPGRKALIVI--SDGGDN--RSRD-TLERAIDAAQRADVAIYSIDA 202
 
Name Accession Description Interval E-value
ITI_HC_C pfam06668
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ...
 681-868 5.50e-99

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: 306.82  E-value: 5.50e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 681 VTGLTVNGQITGDKRGSPDSKTRKTYFGKLGIANAQMDFQVEVTTEKITLWNRAVPSTFSWLDTVTVTQDGLSMMINR-K 759
Cdd:pfam06668   1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIVVKPLGVKIEVTPEKITLKDGGDRLVLSWSDTASVKQDGLTVSVVKnS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 760 NMVVSFGDGVTFVVVLHQVWKKHPVHRDFLGFYVVDSHRMSAQTHGLLGQFFQPFDFKVSDIRPGSDPTKPDATLVVKNH 839
Cdd:pfam06668  81 NVTVTIGDGISFVVLLHRVWKKHPYQVDHLGFYILNSKGLSPSVHGLLGQFLHEPEVEVTDVRPGSDPEKPDATMKVKGH 160

                         170       180
                  ....*....|....*....|....*....
gi 1969806716 840 QLIVTRGSQKDYRKDASIGTKVVCWFVHN 868
Cdd:pfam06668 161 KLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
29-158 4.35e-66

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 216.84  E-value: 4.35e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716   29 LLGKRSLPEGVANGIEVYSTKINSKVTSRFAHNVVTMRAVNRADTAKEVSFDVELPKTAFITNFTLTIDGVTYPGNVKEK 108
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1969806716  109 EVAKKQYEKAVSQGKTAGLVKASGRKLEKFTVSVNVAAGSKVTFELTYEE 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 5.63e-62

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: 207.07  E-value: 5.63e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 281 VPKNVAFVIDISGSMAGRKLEQTKEALLRILEDMQEEDYLNFILFSGDVSTWKEHLVQATPENLQEARTFVKSMEDKGMT 360
Cdd:cd01461     1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 361 NINDGLLRGISMLNKareehriPERSTSIVIMLTDGDanvgESRPEKIQENVRNAIGGKFPLYNLGFGNNLNYNFLENMA 440
Cdd:cd01461    81 NMNDALEAALELLNS-------SPGSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                         170       180
                  ....*....|....*....|..
gi 1969806716 441 LENHGFARRIYEDSDADLQLQG 462
Cdd:cd01461   150 REGRGIARRIYETDDIESQLLR 171
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 274-473 1.40e-43

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 159.88  E-value: 1.40e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 274 APQGLPVVPKNVAFVIDISGSMAGRKLEQTKEALLRILEDMQEEDYLNFILFSGDVSTwkehLVQATP-ENLQEARTFVK 352
Cdd:COG2304    83 KAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARV----LLPPTPaTDRAKILAAID 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 353 SMEDKGMTNINDGLLRGISMLNKAREEHRIperstSIVIMLTDGDANVGESRPEKIQENVRNAIGGKFPLYNLGFGNNLN 432
Cdd:COG2304   159 RLQAGGGTALGAGLELAYELARKHFIPGRV-----NRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDYN 233

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1969806716 433 YNFLENMALENHGFARRIYEDSDADLQLQGFYEEVANPLLT 473
Cdd:COG2304   234 EDLLERLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRA 274
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 45-156 9.27e-41

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: 145.32  E-value: 9.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716  45 VYSTKINSKVTSRFAHNVVTMRAVNRADTAKEVSFDVELPKTAFITNFTLTIDGVTYPGNVKEKEVAKKQYEKAVSQGKT 124
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1969806716 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 ...
 284-459 9.60e-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: 113.14  E-value: 9.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 284 NVAFVIDISGSMAGRKLEQTKEALLRILEDMQEEDYLNFILFSGDVSTwkehLVQATP-ENLQEARTFVKSMEDKGMTNI 362
Cdd:cd01465     2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAET----VLPATPvRDKAAILAAIDRLTAGGSTAG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 363 NDGLLRGISMLnkarEEHRIPERsTSIVIMLTDGDANVGESRPEKIQENVRNAIGGKFPLYNLGFGNNLNYNFLENMAL- 441
Cdd:cd01465    78 GAGIQLGYQEA----QKHFVPGG-VNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAIADa 152

                         170
                  ....*....|....*...
gi 1969806716 442 ENHGFArriYEDSDADLQ 459
Cdd:cd01465   153 GNGNTA---YIDNLAEAR 167
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 284-461 5.41e-25

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: 102.53  E-value: 5.41e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716  284 NVAFVIDISGSMAGRKLEQTKEALLRILEDM---QEEDYLNFILFSGDVSTWKEhLVQATpeNLQEARTFVKSMEDK--G 358
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFP-LNDSR--SKDALLEALASLSYKlgG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716  359 MTNINDGLLRGISMLNKAREEHRIPERstSIVIMLTDGDANVGESRpekIQENVRNAIGGKFPLYNLGFGNNLNYNFLEN 438
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGSRRGAP--KVVILITDGESNDGPKD---LLKAAKELKRSGVKVFVVGVGNDVDEEELKK 152

                          170       180
                   ....*....|....*....|...
gi 1969806716  439 MALENHGfaRRIYEDSDADLQLQ 461
Cdd:smart00327 153 LASAPGG--VYVFLPELLDLLID 173
VWA pfam00092
von Willebrand factor type A domain;
284-466 7.24e-25

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 101.97  E-value: 7.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 284 NVAFVIDISGSMAGRKLEQTKEALLRILEDMQ---EEDYLNFILFSGDVstwKEHLVQATPENLQEARTFVKSME--DKG 358
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDV---RTEFPLNDYSSKEELLSAVDNLRylGGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 359 MTNINDGLLRGISMLNKAREEHRipERSTSIVIMLTDGDANVGEsrpekIQENVRNAIGGKFPLYNLGFGNNLNYNfLEN 438
Cdd:pfam00092  78 TTNTGKALKYALENLFSSAAGAR--PGAPKVVVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNADDEE-LRK 149

                         170       180
                  ....*....|....*....|....*...
gi 1969806716 439 MALENHgfARRIYEDSDADlQLQGFYEE 466
Cdd:pfam00092 150 IASEPG--EGHVFTVSDFE-ALEDLQDQ 174
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 274-468 9.64e-25

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: 104.64  E-value: 9.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 274 APQGLPVVPKNVAFVIDISGSMAGR-KLEQTKEALLRILEDMQEEDYLNFILFSGDVstwkeHLVQATPENLQEARTFVK 352
Cdd:COG1240    84 LALARPQRGRDVVLVVDASGSMAAEnRLEAAKGALLDFLDDYRPRDRVGLVAFGGEA-----EVLLPLTRDREALKRALD 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 353 SMEDKGMTNINDGLLRGISMLNKAREEHRiperstSIVIMLTDGDANVGESRPEKIQENVRNAiggKFPLYNLGFG-NNL 431
Cdd:COG1240   159 ELPPGGGTPLGDALALALELLKRADPARR------KVIVLLTDGRDNAGRIDPLEAAELAAAA---GIRIYTIGVGtEAV 229

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1969806716 432 NYNFLENMALENHGfarRIYEDSDADlQLQGFYEEVA 468
Cdd:COG1240   230 DEGLLREIAEATGG---RYFRADDLS-ELAAIYREID 262
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 274-440 9.45e-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: 95.90  E-value: 9.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 274 APQGLPVVPKNVAFVIDISGSMAGRKLEQTKEALLRILEDMQEEDYLNFILFSGDVstwKEHLVQATPENLQEARTFVKS 353
Cdd:COG2425   110 ASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEV---VEDLPLTADDGLEDAIEFLSG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 354 MEDKGMTNINDGLLRGISMLNKAREEHRiperstsIVIMLTDGDANVGesrPEKIQENVRNAIGGkFPLYNLGFGNNLNY 433
Cdd:COG2425   187 LFAGGGTDIAPALRAALELLEEPDYRNA-------DIVLITDGEAGVS---PEELLREVRAKESG-VRLFTVAIGDAGNP 255


                  ....*..
gi 1969806716 434 NFLENMA 440
Cdd:COG2425   256 GLLEALA 262
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 284-447 2.64e-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: 88.78  E-value: 2.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 284 NVAFVIDISGSMAGRKLEQTKEALLRILEDMQEE---DYLNFILFSGDVSTWKEHLVQATPENLQEARTFVKSMEDkGMT 360
Cdd:cd00198     2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASppgDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLG-GGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 361 NINDGLLRGISMLNKAREEHRipersTSIVIMLTDGDANVGESRPEKIQENVRNAiggKFPLYNLGFGNNLNYNFLENMA 440
Cdd:cd00198    81 NIGAALRLALELLKSAKRPNA-----RRVIILLTDGEPNDGPELLAEAARELRKL---GITVYTIGIGDDANEDELKEIA 152


                  ....*..
gi 1969806716 441 LENHGFA 447
Cdd:cd00198   153 DKTTGGA 159
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 281-446 4.39e-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: 71.66  E-value: 4.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 281 VPKNVAFVIDISGSMAGRKLEQTKEALLRILEDMQEEDYLNFILFSGDVST----WKEHLVQATPENLQEARTFVKSMED 356
Cdd:cd01463    12 SPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPvvpcFNDTLVQATTSNKKVLKEALDMLEA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 357 KGMTNINDGLLRGISMLNKAREEHRIPERST-SIVIML-TDGdanvGESRPEKI--QENVRNAIGGKFPLYNLGFG-NNL 431
Cdd:cd01463    92 KGIANYTKALEFAFSLLLKNLQSNHSGSRSQcNQAIMLiTDG----VPENYKEIfdKYNWDKNSEIPVRVFTYLIGrEVT 167

                         170
                  ....*....|....*
gi 1969806716 432 NYNFLENMALENHGF 446
Cdd:cd01463   168 DRREIQWMACENKGY 182
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 288-403 5.89e-14

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: 70.11  E-value: 5.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 288 VIDISGSMAGRKLEQTKEALLRILEDMQEEDYLNFILFSGDvSTWKEHLVQATPENLQEARTFVKSMEDKGMTNINDGLL 367
Cdd:cd01466     6 VLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTS-AKRLSPLRRMTAKGKRSAKRVVDGLQAGGGTNVVGGLK 84

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1969806716 368 RGISMLNKAREEHRIPErstsiVIMLTDGDANVGES 403
Cdd:cd01466    85 KALKVLGDRRQKNPVAS-----IMLLSDGQDNHGAV 115
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
274-440 3.19e-12

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 66.10  E-value: 3.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 274 APQGLPVVpknvaFVIDISGSMAGRKLEQTKEALLRILEDMQ------EEDYLNFILFSGDVSTwkehlvqATPenLQEA 347
Cdd:COG4245     2 PMRRLPVY-----LLLDTSGSMSGEPIEALNEGLQALIDELRqdpyalETVEVSVITFDGEAKV-------LLP--LTDL 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 348 RTF-VKSMEDKGMTNINDGLLRGISMLNK---AREEHRIPERSTSIVIMlTDG---DANVGESRpEKIQENVRNAIGGKF 420
Cdd:COG4245    68 EDFqPPDLSASGGTPLGAALELLLDLIERrvqKYTAEGKGDWRPVVFLI-TDGeptDSDWEAAL-QRLKDGEAAKKANIF 145

                         170       180
                  ....*....|....*....|
gi 1969806716 421 PlynLGFGNNLNYNFLENMA 440
Cdd:COG4245   146 A---IGVGPDADTEVLKQLT 162
VWA_3 pfam13768
von Willebrand factor type A domain;
283-448 1.98e-10

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 60.10  E-value: 1.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 283 KNVAFVIDISGSMAGRKLEQtKEALLRILEDMQEEDYLNFILFSGDVSTWKEHLVQATPENLQEARTFVKSMEdkgmtnI 362
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQ------P 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 363 NDGLLRGISMLNKAREEHRIPERSTSIVIMlTDGDANVGESRpekIQENVRNAIgGKFPLYNLGFGNNLNYNFLENMALE 442
Cdd:pfam13768  74 PLGGSDLLGALKEAVRAPASPGYIRHVLLL-TDGSPMQGETR---VSDLISRAP-GKIRFFAYGLGASISAPMLQLLAEA 148


                  ....*.
gi 1969806716 443 NHGFAR 448
Cdd:pfam13768 149 SNGTYE 154
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 285-401 9.42e-09

Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). In chlorophyll biosynthesis, insertion of Mg2+ into protoporphyrin IX is catalysed by magnesium chelatase in an ATP-dependent reaction. Magnesium chelatase is a three sub-unit (BchI, BchD and BchH) enzyme with a novel arrangement of domains: the C-terminal helical domain is located behind the nucleotide binding site. The BchD domain contains a AAA domain at its N-terminus and a VWA domain at its C-terminus. The VWA domain has been speculated to be involved in mediating protein-protein interactions.


Pssm-ID: 238728 [Multi-domain]  Cd Length: 178  Bit Score: 55.75  E-value: 9.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 285 VAFVIDISGSMAGR-KLEQTKEALLRILED-MQEEDYLNFILFSGDVStwkEHLVQATpENLQEARTFVKSMEDKGMTNI 362
Cdd:cd01451     3 VIFVVDASGSMAARhRMAAAKGAVLSLLRDaYQRRDKVALIAFRGTEA---EVLLPPT-RSVELAKRRLARLPTGGGTPL 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1969806716 363 NDGLLRGISMLNKAREEhripERSTSIVIMLTDGDANVG 401
Cdd:cd01451    79 AAGLLAAYELAAEQARD----PGQRPLIVVITDGRANVG 113
VWA_2 pfam13519
von Willebrand factor type A domain;
285-381 5.32e-08

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 51.52  E-value: 5.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 285 VAFVIDISGSMAGR-----KLEQTKEALLRILEDMQeEDYLNFILFSGDVstwkEHLVQATpENLQEARTFVKSMEDK-G 358
Cdd:pfam13519   1 LVFVLDTSGSMRNGdygptRLEAAKDAVLALLKSLP-GDRVGLVTFGDGP----EVLIPLT-KDRAKILRALRRLEPKgG 74

                          90       100
                  ....*....|....*....|...
gi 1969806716 359 MTNINDGLLRGISMLNKAREEHR 381
Cdd:pfam13519  75 GTNLAAALQLARAALKHRRKNQP 97
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 284-430 1.52e-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: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 284 NVAFVIDISGSMAGR------KLEQTKEALLRILEDMqEEDYLNFILFSGDVST----------WKEHLVQatpenlqea 347
Cdd:cd01467     4 DIMIALDVSGSMLAQdfvkpsRLEAAKEVLSDFIDRR-ENDRIGLVVFAGAAFTqapltldresLKELLED--------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 348 rtfVKSMEDKGMTNINDGLLRGISMLNKAREEHRiperstsIVIMLTDGDANVGESRPEKI-----QENVRnaiggkfpL 422
Cdd:cd01467    74 ---IKIGLAGQGTAIGDAIGLAIKRLKNSEAKER-------VIVLLTDGENNAGEIDPATAaelakNKGVR--------I 135


                  ....*...
gi 1969806716 423 YNLGFGNN 430
Cdd:cd01467   136 YTIGVGKS 143
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 284-440 4.43e-06

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: 4.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 284 NVAFVIDISGSMAGRKLEQTKEALLRILEDM---QEEDYLNFILFSGDVSTWKEHLVQATPENLQEArtfVKSMEDKGM- 359
Cdd:cd01450     2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLdigPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKA---VKNLKYLGGg 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 360 -TNINDGLLRGISMLNKareEHRIPERSTSIVIMLTDGDANVGESrPEKIQENVRNAiggKFPLYNLGFGnNLNYNFLEN 438
Cdd:cd01450    79 gTNTGKALQYALEQLFS---ESNARENVPKVIIVLTDGRSDDGGD-PKEAAAKLKDE---GIKVFVVGVG-PADEEELRE 150


                  ..
gi 1969806716 439 MA 440
Cdd:cd01450   151 IA 152
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 284-469 3.38e-04

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 42.37  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 284 NVAFVIDISGSMAG----RKLEQTKEALLRILEDMQEEDYLNFILFSGDVST-WKEHLVQAT-PENLQEARTFVKSM-ED 356
Cdd:cd01471     2 DLYLLVDGSGSIGYsnwvTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKElIRLSSPNSTnKDLALNAIRALLSLyYP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 357 KGMTNINDGLLRGISMLNKAREEHripERSTSIVIMLTDGDANvGESRPEKIQENVRNAiGGKFPLynLGFGNNLNYNFL 436
Cdd:cd01471    82 NGSTNTTSALLVVEKHLFDTRGNR---ENAPQLVIIMTDGIPD-SKFRTLKEARKLRER-GVIIAV--LGVGQGVNHEEN 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1969806716 437 ENMAlenhGFARRiyeDSDADLQLQGFYEEVAN 469
Cdd:cd01471   155 RSLV----GCDPD---DSPCPLYLQSSWSEVQN 180
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 285-429 3.14e-03

norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate reductases. Denitrification plays a major role in completing the nitrogen cycle by converting nitrate or nitrite to nitrogen gas. The pathway for microbial denitrification has been established as NO3- ------> NO2- ------> NO -------> N2O ---------> N2. This reaction generally occurs under oxygen limiting conditions. Genetic and biochemical studies have shown that the first srep of the biochemical pathway is catalyzed by periplasmic nitrate reductases. This family is widely present in proteobacteria and firmicutes. This version of the domain is also present in some archaeal members. The function of the vWA domain in this sub-group is not known. Members of this subgroup have a conserved MIDAS motif.


Pssm-ID: 238731 [Multi-domain]  Cd Length: 174  Bit Score: 39.62  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 285 VAFVIDISGSM-AGRKLEQTKEALLRILEDMQEEDYLNFIL-FSGDVST--WKEHLVQATPENLQEARTFVKSMEDKGMT 360
Cdd:cd01454     3 VTLLLDLSGSMrSDRRIDVAKKAAVLLAEALEACGVPHAILgFTTDAGGreRVRWIKIKDFDESLHERARKRLAALSPGG 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1969806716 361 NINDGL-LRGISMLNKAREEHRiperstSIVIMLTDGDAN------VGESRPEKIQENVRNAIGGKFPLYNLGFGN 429
Cdd:cd01454    83 NTRDGAaIRHAAERLLARPEKR------KILLVISDGEPNdldyyeGNVFATEDALRAVIEARKLGIEVFGITIDR 152
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 281-427 4.08e-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: 40.37  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 281 VPKNVAFVIDISGSMAgRKLEQTKEALLRILED-MQEEDYLnFIL-----------FSGDVSTWKEHLVQATPENLQEAR 348
Cdd:TIGR03436  52 LPLTVGLVIDTSGSMR-NDLDRARAAAIRFLKTvLRPNDRV-FVVtfntrlrllqdFTSDPRLLEAALNRLKPPLRTDYN 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 349 TFVKSMEDKGMTNINDGL-LRGISMLnkAREEHRIPERSTSIVImlTDGDANvgESRPeKIQENVRNAIGGKFPLYNLGF 427
Cdd:TIGR03436 130 SSGAFVRDGGGTALYDAItLAALEQL--ANALAGIPGRKALIVI--SDGGDN--RSRD-TLERAIDAAQRADVAIYSIDA 202
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
 285-411 5.49e-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: 40.64  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969806716 285 VAFVIDISGSMA--GRKLEQTKEALLRILEDMQEEDYLNFILFSgDVSTWKEHLVQATPENLQEARTFVKSMEDKGMTNI 362
Cdd:TIGR00868 307 VCLVLDKSGSMTveDRLKRMNQAAKLFLLQTVEKGSWVGMVTFD-SAAYIKNELIQITSSAERDALTANLPTAASGGTSI 385

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1969806716 363 NDGLLRGISMLNKAReehriPERSTSIVIMLTDGDANVGESRPEKIQEN 411
Cdd:TIGR00868 386 CSGLKAAFQVIKKSY-----QSTDGSEIVLLTDGEDNTISSCFEEVKQS 429
 
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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