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Conserved domains on  [gi|575771903|ref|NP_001276562|]
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inter alpha-trypsin inhibitor, heavy chain 4 isoform 4 precursor [Mus musculus]

Protein Classification

VIT and vWA_interalpha_trypsin_inhibitor domain-containing protein( domain architecture ID 10652053)

VIT and vWA_interalpha_trypsin_inhibitor domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 271-452 7.25e-72

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: 234.03  E-value: 7.25e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 271 MSKNVIFVIDKSGSMSGKKIQQTREALVKILKDLSPQDQFNLIEFSGEANQWKQSLVQATEENLNKAVNYASRIRAHGGT 350
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 351 NINNAVLLAVELLDRSNqaellpsKSVSLIILLTDGDptvgETNPTIIQNNVREAINGQYSLFCLGFGFDVNYPFLEKMA 430
Cdd:cd01461   81 NMNDALEAALELLNSSP-------GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 575771903 431 LDNGGLARRIYEDSDSALQLQD 452
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
19-148 2.76e-66

Vault protein Inter-alpha-Trypsin domain;


:

Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 217.23  E-value: 2.76e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903    19 LLAVLPTTTAEKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRADAVQEATFQVELPRKAFITNFSMIIDGVTYPGVVKEK 98
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 575771903    99 AEAQKQYSAAVGRGESAGIVKTTGRQTEKFEVSVNVAPGSKITFELIYQE 148
Cdd:smart00609  81 EVAQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 271-452 7.25e-72

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: 234.03  E-value: 7.25e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 271 MSKNVIFVIDKSGSMSGKKIQQTREALVKILKDLSPQDQFNLIEFSGEANQWKQSLVQATEENLNKAVNYASRIRAHGGT 350
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 351 NINNAVLLAVELLDRSNqaellpsKSVSLIILLTDGDptvgETNPTIIQNNVREAINGQYSLFCLGFGFDVNYPFLEKMA 430
Cdd:cd01461   81 NMNDALEAALELLNSSP-------GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 575771903 431 LDNGGLARRIYEDSDSALQLQD 452
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
19-148 2.76e-66

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 217.23  E-value: 2.76e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903    19 LLAVLPTTTAEKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRADAVQEATFQVELPRKAFITNFSMIIDGVTYPGVVKEK 98
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 575771903    99 AEAQKQYSAAVGRGESAGIVKTTGRQTEKFEVSVNVAPGSKITFELIYQE 148
Cdd:smart00609  81 EVAQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 264-479 6.16e-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: 152.18  E-value: 6.16e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 264 APENLPTMSKNVIFVIDKSGSMSGKKIQQTREALVKILKDLSPQDQFNLIEFSGEANQwkqsLVQATE-ENLNKAVNYAS 342
Cdd:COG2304   83 KAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARV----LLPPTPaTDRAKILAAID 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 343 RIRAHGGTNINNAVLLAVELLDRSNQAEllpskSVSLIILLTDGDPTVGETNPTIIQNNVREAINGQYSLFCLGFGFDVN 422
Cdd:COG2304  159 RLQAGGGTALGAGLELAYELARKHFIPG-----RVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDYN 233

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 575771903 423 YPFLEKMALDNGGLARRIyedsDSALQLQdfyhEVANPLLSSVAFEYPSDAVEEVTR 479
Cdd:COG2304  234 EDLLERLADAGGGNYYYI----DDPEEAE----KVFVREFSRIGYENRALATEDFPL 282
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 35-146 7.03e-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: 145.70  E-value: 7.03e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903   35 IYSLTVDSRVSSRFAHTVVTSRVVNRADAVQEATFQVELPRKAFITNFSMIIDGVTYPGVVKEKAEAQKQYSAAVGRGES 114
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 575771903  115 AGIVKTTGRqtEKFEVSV-NVAPGSKITFELIY 146
Cdd:pfam08487  81 AGLLEQDTP--DVFTTSVgNIPPGEKVTVELTY 111
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 274-452 1.01e-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: 104.84  E-value: 1.01e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903   274 NVIFVIDKSGSMSGKKIQQTREALVKILKDLS---PQDQFNLIEFSGEANQWKQSLVQATEENLNKAVNyASRIRAHGGT 350
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALA-SLSYKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903   351 NINNAVLLAVELLDRSNQAELLPSKSVslIILLTDGDPTVGETNptiIQNNVREAINGQYSLFCLGFGFDVNYPFLEKMA 430
Cdd:smart00327  80 NLGAALQYALENLFSKSAGSRRGAPKV--VILITDGESNDGPKD---LLKAAKELKRSGVKVFVVGVGNDVDEEELKKLA 154

                          170       180
                   ....*....|....*....|..
gi 575771903   431 LDNGGlaRRIYEDSDSALQLQD 452
Cdd:smart00327 155 SAPGG--VYVFLPELLDLLIDL 174
VWA pfam00092
von Willebrand factor type A domain;
274-456 6.03e-25

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 102.35  E-value: 6.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903  274 NVIFVIDKSGSMSGKKIQQTREALVKILKDLS---PQDQFNLIEFSGEANQWKQSLVQATEENLNKAVNYAsRIRAHGGT 350
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNL-RYLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903  351 NINNAVLLAVELLDRSNQAEllPSKSVSLIILLTDGDPTVGEtnptiIQNNVREAINGQYSLFCLGFGFDVNYPfLEKMA 430
Cdd:pfam00092  80 NTGKALKYALENLFSSAAGA--RPGAPKVVVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNADDEE-LRKIA 151

                         170       180
                  ....*....|....*....|....*.
gi 575771903  431 LDNGglARRIYEDSDSAlQLQDFYHE 456
Cdd:pfam00092 152 SEPG--EGHVFTVSDFE-ALEDLQDQ 174
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 266-473 9.54e-05

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: 45.38  E-value: 9.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903  266 ENLPTmskNVIFVIDKSGSMSgKKIQQTREALVKILKD-LSPQDQFNLIEFSGEA----------NQWKQSLVQATEENL 334
Cdd:TIGR03436  50 TDLPL---TVGLVIDTSGSMR-NDLDRARAAAIRFLKTvLRPNDRVFVVTFNTRLrllqdftsdpRLLEAALNRLKPPLR 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903  335 NKAVNYASRIRAHGGTNINNAVLLAV-ELLDRSNQAelLPSKSVslIILLTDG-----DPTVGETNPTIIQNNVR----- 403
Cdd:TIGR03436 126 TDYNSSGAFVRDGGGTALYDAITLAAlEQLANALAG--IPGRKA--LIVISDGgdnrsRDTLERAIDAAQRADVAiysid 201

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575771903  404 ---EAINGQYSLFCLGFGFDvnyPFLEKMALDNGGLArrIYEDSDSalqLQDFYHEVANPLLSS--VAFeYPSDA 473
Cdd:TIGR03436 202 argLRAPDLGAGAKAGLGGP---EALERLAEETGGRA--FYVNSND---LDGAFAQIAEELRSQylIGY-YPPNP 267
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 271-452 7.25e-72

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: 234.03  E-value: 7.25e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 271 MSKNVIFVIDKSGSMSGKKIQQTREALVKILKDLSPQDQFNLIEFSGEANQWKQSLVQATEENLNKAVNYASRIRAHGGT 350
Cdd:cd01461    1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 351 NINNAVLLAVELLDRSNqaellpsKSVSLIILLTDGDptvgETNPTIIQNNVREAINGQYSLFCLGFGFDVNYPFLEKMA 430
Cdd:cd01461   81 NMNDALEAALELLNSSP-------GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLA 149

                        170       180
                 ....*....|....*....|..
gi 575771903 431 LDNGGLARRIYEDSDSALQLQD 452
Cdd:cd01461  150 REGRGIARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
19-148 2.76e-66

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 217.23  E-value: 2.76e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903    19 LLAVLPTTTAEKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRADAVQEATFQVELPRKAFITNFSMIIDGVTYPGVVKEK 98
Cdd:smart00609   1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 575771903    99 AEAQKQYSAAVGRGESAGIVKTTGRQTEKFEVSVNVAPGSKITFELIYQE 148
Cdd:smart00609  81 EVAQKQYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 264-479 6.16e-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: 152.18  E-value: 6.16e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 264 APENLPTMSKNVIFVIDKSGSMSGKKIQQTREALVKILKDLSPQDQFNLIEFSGEANQwkqsLVQATE-ENLNKAVNYAS 342
Cdd:COG2304   83 KAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARV----LLPPTPaTDRAKILAAID 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 343 RIRAHGGTNINNAVLLAVELLDRSNQAEllpskSVSLIILLTDGDPTVGETNPTIIQNNVREAINGQYSLFCLGFGFDVN 422
Cdd:COG2304  159 RLQAGGGTALGAGLELAYELARKHFIPG-----RVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDYN 233

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 575771903 423 YPFLEKMALDNGGLARRIyedsDSALQLQdfyhEVANPLLSSVAFEYPSDAVEEVTR 479
Cdd:COG2304  234 EDLLERLADAGGGNYYYI----DDPEEAE----KVFVREFSRIGYENRALATEDFPL 282
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 35-146 7.03e-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: 145.70  E-value: 7.03e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903   35 IYSLTVDSRVSSRFAHTVVTSRVVNRADAVQEATFQVELPRKAFITNFSMIIDGVTYPGVVKEKAEAQKQYSAAVGRGES 114
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 575771903  115 AGIVKTTGRqtEKFEVSV-NVAPGSKITFELIY 146
Cdd:pfam08487  81 AGLLEQDTP--DVFTTSVgNIPPGEKVTVELTY 111
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 171-430 4.49e-27

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 111.31  E-value: 4.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 171 HLQMDIYIFEPQGISILETESTFMTPELANALTTSQNKTKAHIRFKPTLSQQQKSQSEQDTVLNGDFIVRYDVNRSDSGG 250
Cdd:COG2425   16 LAPAPATALLLAGLLRAALALGLALALRAALLALLLLLLRAALALLTLLAGLVLLALDALLLAALLAALLDALLLAVLLL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 251 SIQIEEGYFVH-HFAPENLPTMSKNVIFVIDKSGSMSGKKIQQTREALVKILKDLSPQDQFNLIEFSGEAnqwKQSLVQA 329
Cdd:COG2425   96 ALLLLAALLLLaAPASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEV---VEDLPLT 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 330 TEENLNKAVNYASRIRAHGGTNINNAVLLAVELLDRSNQAEllpsksvSLIILLTDGDPTVGETNptiIQNNVREAINGq 409
Cdd:COG2425  173 ADDGLEDAIEFLSGLFAGGGTDIAPALRAALELLEEPDYRN-------ADIVLITDGEAGVSPEE---LLREVRAKESG- 241

                        250       260
                 ....*....|....*....|.
gi 575771903 410 YSLFCLGFGFDVNYPFLEKMA 430
Cdd:COG2425  242 VRLFTVAIGDAGNPGLLEALA 262
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 274-435 7.84e-26

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: 104.66  E-value: 7.84e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 274 NVIFVIDKSGSMSGKKIQQTREALVKILKDLSPQDQFNLIEFSGEAnqwkQSLVQAT----EENLNKAVnyaSRIRAHGG 349
Cdd:cd01465    2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAA----ETVLPATpvrdKAAILAAI---DRLTAGGS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 350 TNINNAVLLAVELLDRSnqaelLPSKSVSLIILLTDGDPTVGETNPTIIQNNVREAINGQYSLFCLGFGFDVNYPFLEKM 429
Cdd:cd01465   75 TAGGAGIQLGYQEAQKH-----FVPGGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAI 149


                 ....*.
gi 575771903 430 ALDNGG 435
Cdd:cd01465  150 ADAGNG 155
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 274-452 1.01e-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: 104.84  E-value: 1.01e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903   274 NVIFVIDKSGSMSGKKIQQTREALVKILKDLS---PQDQFNLIEFSGEANQWKQSLVQATEENLNKAVNyASRIRAHGGT 350
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALA-SLSYKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903   351 NINNAVLLAVELLDRSNQAELLPSKSVslIILLTDGDPTVGETNptiIQNNVREAINGQYSLFCLGFGFDVNYPFLEKMA 430
Cdd:smart00327  80 NLGAALQYALENLFSKSAGSRRGAPKV--VILITDGESNDGPKD---LLKAAKELKRSGVKVFVVGVGNDVDEEELKKLA 154

                          170       180
                   ....*....|....*....|..
gi 575771903   431 LDNGGlaRRIYEDSDSALQLQD 452
Cdd:smart00327 155 SAPGG--VYVFLPELLDLLIDL 174
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 269-458 3.80e-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: 105.79  E-value: 3.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 269 PTMSKNVIFVIDKSGSMSGK-KIQQTREALVKILKDLSPQDQFNLIEFSGEANqwkqsLVQATEENLNKAVNYASRIRAH 347
Cdd:COG1240   89 PQRGRDVVLVVDASGSMAAEnRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAE-----VLLPLTRDREALKRALDELPPG 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 348 GGTNINNAVLLAVELLDRSNqaellPSKSVsLIILLTDGDPTVGETNPTIIqnnVREAINGQYSLFCLGFGFD-VNYPFL 426
Cdd:COG1240  164 GGTPLGDALALALELLKRAD-----PARRK-VIVLLTDGRDNAGRIDPLEA---AELAAAAGIRIYTIGVGTEaVDEGLL 234

                        170       180       190
                 ....*....|....*....|....*....|..
gi 575771903 427 EKMALDNGGLARRIyedsDSALQLQDFYHEVA 458
Cdd:COG1240  235 REIAEATGGRYFRA----DDLSELAAIYREID 262
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 274-435 3.87e-25

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 102.64  E-value: 3.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 274 NVIFVIDKSGSMSGKKIQQTREALVKILKDLS---PQDQFNLIEFSGEANQWKQSLVQATEENLNKAVNyASRIRAHGGT 350
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSaspPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAID-ALKKGLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 351 NINNAVLLAVELLDRSNQaellpSKSVSLIILLTDGDPTVGETNPtiiQNNVREAINGQYSLFCLGFGFDVNYPFLEKMA 430
Cdd:cd00198   81 NIGAALRLALELLKSAKR-----PNARRVIILLTDGEPNDGPELL---AEAARELRKLGITVYTIGIGDDANEDELKEIA 152


                 ....*
gi 575771903 431 LDNGG 435
Cdd:cd00198  153 DKTTG 157
VWA pfam00092
von Willebrand factor type A domain;
274-456 6.03e-25

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 102.35  E-value: 6.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903  274 NVIFVIDKSGSMSGKKIQQTREALVKILKDLS---PQDQFNLIEFSGEANQWKQSLVQATEENLNKAVNYAsRIRAHGGT 350
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNL-RYLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903  351 NINNAVLLAVELLDRSNQAEllPSKSVSLIILLTDGDPTVGEtnptiIQNNVREAINGQYSLFCLGFGFDVNYPfLEKMA 430
Cdd:pfam00092  80 NTGKALKYALENLFSSAAGA--RPGAPKVVVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVGNADDEE-LRKIA 151

                         170       180
                  ....*....|....*....|....*.
gi 575771903  431 LDNGglARRIYEDSDSAlQLQDFYHE 456
Cdd:pfam00092 152 SEPG--EGHVFTVSDFE-ALEDLQDQ 174
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
274-464 1.49e-16

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 78.81  E-value: 1.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 274 NVIFVIDKSGSMSGKKIQQTREALVKILKDLSPQDQ------FNLIEFSGEAnQWKQSLVQAteENLnkavnYASRIRAH 347
Cdd:COG4245    7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYaletveVSVITFDGEA-KVLLPLTDL--EDF-----QPPDLSAS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 348 GGTNINNAVLLAVELLDRSNQAelLPSKSVS----LIILLTDGDPTVGETNPTI--IQNNVReaiNGQYSLFCLGFGFDV 421
Cdd:COG4245   79 GGTPLGAALELLLDLIERRVQK--YTAEGKGdwrpVVFLITDGEPTDSDWEAALqrLKDGEA---AKKANIFAIGVGPDA 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 575771903 422 NYPFLEKMALDNGGLarriyeDSDSALQLQDFYHEVANPLLSS 464
Cdd:COG4245  154 DTEVLKQLTDPVRAL------DALDGLDFREFFKWLSASVSSV 190
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 275-436 1.47e-12

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: 66.26  E-value: 1.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 275 VIFVIDKSGSMSGKKIQQTREALVKILKDLSPQDQFNLIEFSGEANQwKQSLVQATEENLNKAVNYASRIRAHGGTNINN 354
Cdd:cd01466    3 LVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKR-LSPLRRMTAKGKRSAKRVVDGLQAGGGTNVVG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 355 AVLLAVELLDRSNQAELLPSksvslIILLTDGDPTVGETnptiiqnnVREAINGQYSLFCLGFGFDVNYPFLEKMALDNG 434
Cdd:cd01466   82 GLKKALKVLGDRRQKNPVAS-----IMLLSDGQDNHGAV--------VLRADNAPIPIHTFGLGASHDPALLAFIAEITG 148


                 ..
gi 575771903 435 GL 436
Cdd:cd01466  149 GT 150
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 270-435 1.36e-11

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: 64.34  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 270 TMSKNVIFVIDKSGSMSGKK---IQQTREAlvkILKDLSPQDQFNLIEFSGEANQ----WKQSLVQATEEN---LNKAVN 339
Cdd:cd01463   11 TSPKDIVILLDVSGSMTGQRlhlAKQTVSS---ILDTLSDNDFFNIITFSNEVNPvvpcFNDTLVQATTSNkkvLKEALD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 340 yasRIRAHGGTNINNAVLLAVELLDRSNQAELLPSKSV--SLIILLTDGDPtvgETNPTIIQN-NVREAINGQYSLFCLG 416
Cdd:cd01463   88 ---MLEAKGIANYTKALEFAFSLLLKNLQSNHSGSRSQcnQAIMLITDGVP---ENYKEIFDKyNWDKNSEIPVRVFTYL 161

                        170       180
                 ....*....|....*....|
gi 575771903 417 FGFDV-NYPFLEKMALDNGG 435
Cdd:cd01463  162 IGREVtDRREIQWMACENKG 181
VWA_3 pfam13768
von Willebrand factor type A domain;
273-438 4.25e-11

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 62.03  E-value: 4.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903  273 KNVIFVIDKSGSMSGKKIQQtREALVKILKDLSPQDQFNLIEFSGEANQWKQSLVQATEENLNKAVNYASRIRAH-GGTN 351
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPlGGSD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903  352 INNAVLLAVELLDrsnqaellPSKSVSLIILLTDGDPTVGEtnpTIIQNNVREAInGQYSLFCLGFGFDVNYPFLEKMAL 431
Cdd:pfam13768  80 LLGALKEAVRAPA--------SPGYIRHVLLLTDGSPMQGE---TRVSDLISRAP-GKIRFFAYGLGASISAPMLQLLAE 147


                  ....*..
gi 575771903  432 DNGGLAR 438
Cdd:pfam13768 148 ASNGTYE 154
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 274-430 1.22e-09

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 58.07  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 274 NVIFVIDKSGSMSGKKIQQTREALVKILKDLSP---QDQFNLIEFSGEANQWKQSLVQATEENLNKAVNyASRIRAHGGT 350
Cdd:cd01450    2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIgpdKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVK-NLKYLGGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 351 NINNAVLLAVELLDRSNQAEllpSKSVSLIILLTDGDPTVGetnpTIIQNNVREAINGQYSLFCLGFGfDVNYPFLEKMA 430
Cdd:cd01450   81 NTGKALQYALEQLFSESNAR---ENVPKVIIVLTDGRSDDG----GDPKEAAAKLKDEGIKVFVVGVG-PADEEELREIA 152
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 273-386 3.73e-09

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


Pssm-ID: 238739 [Multi-domain]  Cd Length: 152  Bit Score: 56.20  E-value: 3.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 273 KNVIFVIDKSGSMSGKKIQQTREALVKILKDLSPQDQ-FNLIEFSGEanqWKQSLVQATEeNLNKAVNYASRIRAHGGTN 351
Cdd:cd01462    1 GPVILLVDQSGSMYGAPEEVAKAVALALLRIALAENRdTYLILFDSE---FQTKIVDKTD-DLEEPVEFLSGVQLGGGTD 76

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 575771903 352 INNAVLLAVELLDRSNqaellPSKSVslIILLTDG 386
Cdd:cd01462   77 INKALRYALELIERRD-----PRKAD--IVLITDG 104
VWA_2 pfam13519
von Willebrand factor type A domain;
275-365 9.12e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 53.84  E-value: 9.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903  275 VIFVIDKSGSMSGKKIQQTREALVK-----ILKDLsPQDQFNLIEFSGEANqwkqsLVQATEENLNKAVNYASRIRA-HG 348
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRLEAAKdavlaLLKSL-PGDRVGLVTFGDGPE-----VLIPLTKDRAKILRALRRLEPkGG 74

                          90
                  ....*....|....*..
gi 575771903  349 GTNINNAVLLAVELLDR 365
Cdd:pfam13519  75 GTNLAAALQLARAALKH 91
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 275-389 1.02e-07

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: 52.73  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 275 VIFVIDKSGSMSGKKIQQTREALVKILKDLSpQDQFNL-------IEFSGEANQwKQSLVQAteENLnkavnYASRIRAH 347
Cdd:cd01464    6 IYLLLDTSGSMAGEPIEALNQGLQMLQSELR-QDPYALesveisvITFDSAARV-IVPLTPL--ESF-----QPPRLTAS 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 575771903 348 GGTNINNAVLLAVELLDRSNQaellpsKSVS--------LIILLTDGDPT 389
Cdd:cd01464   77 GGTSMGAALELALDCIDRRVQ------RYRAdqkgdwrpWVFLLTDGEPT 120
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 274-425 3.52e-07

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: 51.18  E-value: 3.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 274 NVIFVIDKSGSMSGKKIQQ-TR-EALVKILKDL---SPQDQFNLIEFSGEAnqWKQSLVQATEENLNKAVNYASRIRAHG 348
Cdd:cd01467    4 DIMIALDVSGSMLAQDFVKpSRlEAAKEVLSDFidrRENDRIGLVVFAGAA--FTQAPLTLDRESLKELLEDIKIGLAGQ 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575771903 349 GTNINNAVLLAVELLDRSNQAEllpsksvSLIILLTDGDPTVGETNPtIIQNNVREAINGQysLFCLGFGFDVNYPF 425
Cdd:cd01467   82 GTAIGDAIGLAIKRLKNSEAKE-------RVIVLLTDGENNAGEIDP-ATAAELAKNKGVR--IYTIGVGKSGSGPK 148
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 273-386 3.31e-05

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 45.08  E-value: 3.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 273 KNVIFVIDKSGSMSGkKIQQTREALVKILKDLSPQ---DQFNLIEFSGEANQ---WKQSLVQaTEENLNKAVNyasRIRA 346
Cdd:cd01476    1 LDLLFVLDSSGSVRG-KFEKYKKYIERIVEGLEIGptaTRVALITYSGRGRQrvrFNLPKHN-DGEELLEKVD---NLRF 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 575771903 347 HGG-TNINNAVLLAVELLDRSNQAEllpSKSVSLIILLTDG 386
Cdd:cd01476   76 IGGtTATGAAIEVALQQLDPSEGRR---EGIPKVVVVLTDG 113
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 275-391 7.72e-05

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: 44.19  E-value: 7.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 275 VIFVIDKSGSMSG-KKIQQTREALVKILKD-LSPQDQFNLIEFSGEAnqwKQSLVQATeENLNKAVNYASRIRAHGGTNI 352
Cdd:cd01451    3 VIFVVDASGSMAArHRMAAAKGAVLSLLRDaYQRRDKVALIAFRGTE---AEVLLPPT-RSVELAKRRLARLPTGGGTPL 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 575771903 353 NNAVLLAVELLDRSNQAEllpsKSVSLIILLTDGDPTVG 391
Cdd:cd01451   79 AAGLLAAYELAAEQARDP----GQRPLIVVITDGRANVG 113
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 266-473 9.54e-05

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: 45.38  E-value: 9.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903  266 ENLPTmskNVIFVIDKSGSMSgKKIQQTREALVKILKD-LSPQDQFNLIEFSGEA----------NQWKQSLVQATEENL 334
Cdd:TIGR03436  50 TDLPL---TVGLVIDTSGSMR-NDLDRARAAAIRFLKTvLRPNDRVFVVTFNTRLrllqdftsdpRLLEAALNRLKPPLR 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903  335 NKAVNYASRIRAHGGTNINNAVLLAV-ELLDRSNQAelLPSKSVslIILLTDG-----DPTVGETNPTIIQNNVR----- 403
Cdd:TIGR03436 126 TDYNSSGAFVRDGGGTALYDAITLAAlEQLANALAG--IPGRKA--LIVISDGgdnrsRDTLERAIDAAQRADVAiysid 201

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575771903  404 ---EAINGQYSLFCLGFGFDvnyPFLEKMALDNGGLArrIYEDSDSalqLQDFYHEVANPLLSS--VAFeYPSDA 473
Cdd:TIGR03436 202 argLRAPDLGAGAKAGLGGP---EALERLAEETGGRA--FYVNSND---LDGAFAQIAEELRSQylIGY-YPPNP 267
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 277-386 6.22e-04

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


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 41.73  E-value: 6.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903 277 FVIDKSGSMSGK--KIQQTREALVKilKDLSPQDQFNLIEFSGEANqwKQSLVQATEENLNKAVNYASRIRAHGGTNINN 354
Cdd:cd01474    9 FVLDKSGSVAANwiEIYDFVEQLVD--RFNSPGLRFSFITFSTRAT--KILPLTDDSSAIIKGLEVLKKVTPSGQTYIHE 84

                         90       100       110
                 ....*....|....*....|....*....|..
gi 575771903 355 AVLLAVELLDRSNQAELlpsKSVSLIILLTDG 386
Cdd:cd01474   85 GLENANEQIFNRNGGGR---ETVSVIIALTDG 113
vWA-TerF-like pfam10138
vWA found in TerF C terminus; vWA domain fused to TerD domain typified by the TerF protein. ...
 275-433 2.54e-03

vWA found in TerF C terminus; vWA domain fused to TerD domain typified by the TerF protein. Some times found as solos.


Pssm-ID: 401947 [Multi-domain]  Cd Length: 200  Bit Score: 39.96  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903  275 VIFVIDKSGSMSGKKIQQTREALVKILKDLSPQ--DQFNL--IEFSGEANQWKQSLVQATEENLNKAVNYASRIRAHGGT 350
Cdd:pfam10138   4 VGLVLDASGSMSGLYRRGTVQRVVERMLPVAAQldDDGELdvWLFGTRAARLPDVTLADLPGWVERLHLGRDRYRKLGGQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771903  351 NINNAVLLAVelldrSNQAELLPSKSVSLIILLTDGDPTVGETNPTIIQNNVREAINGQYslfcLGFGfDVNYPFLEKma 430
Cdd:pfam10138  84 NNEPPVMEAV-----IDYYRKNPADLPTLVLFITDGGVTDNAAIERLLREASREPIFWQF----VGIG-RSGYGFLEK-- 151


                  ...
gi 575771903  431 LDN 433
Cdd:pfam10138 152 LDT 154
 
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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