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Conserved domains on  [gi|67677852|gb|AAH96879|]
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Zgc:112265 [Danio rerio]

Protein Classification

VIT and vWA domain-containing protein( domain architecture ID 8721)

VIT (vault protein inter-alpha-trypsin) and vWA (von Willebrand factor type A) domain-containing protein similar to Mus musculus von Willebrand factor A domain-containing protein 5B2 isoform 2

CATH:  3.40.50.410
PubMed:  12579041|10830113|12388743
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 267-443 7.24e-58

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


The actual alignment was detected with superfamily member cd01461:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 171  Bit Score: 195.90  E-value: 7.24e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 267 IPKNVVFIIDRSGSMHGRRIRQTRSALLTILKDLDEDDHFGLITFDAEIDFWKRELLQATKANRENAESFVKRIQDRGAT 346
Cdd:cd01461   1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 347 NINDAVLAGVDMINRNPrkGTASILILLTDGDptagETNIEKIMANVKEAIGSKFPLYCLGFGYDVNFDFLTKMSLENNA 426
Cdd:cd01461  81 NMNDALEAALELLNSSP--GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLAREGRG 154

                       170
                ....*....|....*..
gi 67677852 427 VARRIYEDSDADIQLQG 443
Cdd:cd01461 155 IARRIYETDDIESQLLR 171
VIT_2 super family cl02699
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 20-144 1.75e-46

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.


The actual alignment was detected with superfamily member smart00609:

Pssm-ID: 470654 [Multi-domain]  Cd Length: 130  Bit Score: 162.53  E-value: 1.75e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852     20 SAPVEKKQNVDIYSFYINSTVSSRYATTIITSRVANKLSEPQEIQFEVKIPKNAFISKFRMIIEGKTYDGVVKKKEEAQQ 99
Cdd:smart00609   6 GLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEVAQK 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 67677852    100 QYNKAVSRGESAGLIKSVGRTLEDFKTSVTVAANSKVTFELTYEE 144
Cdd:smart00609  86 QYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 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- ...
 267-443 7.24e-58

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: 195.90  E-value: 7.24e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 267 IPKNVVFIIDRSGSMHGRRIRQTRSALLTILKDLDEDDHFGLITFDAEIDFWKRELLQATKANRENAESFVKRIQDRGAT 346
Cdd:cd01461   1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 347 NINDAVLAGVDMINRNPrkGTASILILLTDGDptagETNIEKIMANVKEAIGSKFPLYCLGFGYDVNFDFLTKMSLENNA 426
Cdd:cd01461  81 NMNDALEAALELLNSSP--GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLAREGRG 154

                       170
                ....*....|....*..
gi 67677852 427 VARRIYEDSDADIQLQG 443
Cdd:cd01461 155 IARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
20-144 1.75e-46

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 162.53  E-value: 1.75e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852     20 SAPVEKKQNVDIYSFYINSTVSSRYATTIITSRVANKLSEPQEIQFEVKIPKNAFISKFRMIIEGKTYDGVVKKKEEAQQ 99
Cdd:smart00609   6 GLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEVAQK 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 67677852    100 QYNKAVSRGESAGLIKSVGRTLEDFKTSVTVAANSKVTFELTYEE 144
Cdd:smart00609  86 QYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 260-456 1.10e-44

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 162.96  E-value: 1.10e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 260 APSDVPRIPKNVVFIIDRSGSMHGRRIRQTRSALLTILKDLDEDDHFGLITFDAEIdfwkRELLQATKA-NRENAESFVK 338
Cdd:COG2304  83 KAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDA----RVLLPPTPAtDRAKILAAID 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 339 RIQDRGATNINDAVLAGVDMINRNPRKGTASILILLTDGDPTAGETNIEKIMANVKEAIGSKFPLYCLGFGYDVNFDFLT 418
Cdd:COG2304 159 RLQAGGGTALGAGLELAYELARKHFIPGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDYNEDLLE 238

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 67677852 419 KMSLENNAVARRIYEDSDADIQLQGFYDEVAVPLLTDI 456
Cdd:COG2304 239 RLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALA 276
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 31-142 4.49e-36

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: 131.84  E-value: 4.49e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852    31 IYSFYINSTVSSRYATTIITSRVANKLSEPQEIQFEVKIPKNAFISKFRMIIEGKTYDGVVKKKEEAQQQYNKAVSRGES 110
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 67677852   111 AGLIKSVGRTLedFKTSV-TVAANSKVTFELTY 142
Cdd:pfam08487  81 AGLLEQDTPDV--FTTSVgNIPPGEKVTVELTY 111
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 270-437 4.89e-23

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: 97.14  E-value: 4.89e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852    270 NVVFIIDRSGSMHGRRIRQTRSALLTILKDLDE---DDHFGLITFDAEIdfwKRELLQATKANRENAESFVKRIQDR--G 344
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIgpdGDRVGLVTFSDDA---RVLFPLNDSRSKDALLEALASLSYKlgG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852    345 ATNINDAVLAGVDMIN---RNPRKGTASILILLTDGDPTAGETNIEKImanVKEAIGSKFPLYCLGFGYDVNFDFLTKMS 421
Cdd:smart00327  78 GTNLGAALQYALENLFsksAGSRRGAPKVVILITDGESNDGPKDLLKA---AKELKRSGVKVFVVGVGNDVDEEELKKLA 154

                          170
                   ....*....|....*.
gi 67677852    422 LENNAVARRIYEDSDA 437
Cdd:smart00327 155 SAPGGVYVFLPELLDL 170
VWA pfam00092
von Willebrand factor type A domain;
270-447 1.07e-21

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 93.11  E-value: 1.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852   270 NVVFIIDRSGSMHGRRIRQTRSALLTILKDLDED---DHFGLITFDAEidfWKRELLQATKANRENAESFVKRI--QDRG 344
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGpdgTRVGLVQYSSD---VRTEFPLNDYSSKEELLSAVDNLryLGGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852   345 ATNINDAVLAGVDMIN---RNPRKGTASILILLTDGDPTAGEtniekIMANVKEAIGSKFPLYCLGFGyDVNFDFLTKMS 421
Cdd:pfam00092  78 TTNTGKALKYALENLFssaAGARPGAPKVVVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVG-NADDEELRKIA 151

                         170       180
                  ....*....|....*....|....*.
gi 67677852   422 LENNavARRIYEDSDADiQLQGFYDE 447
Cdd:pfam00092 152 SEPG--EGHVFTVSDFE-ALEDLQDQ 174
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 268-396 7.35e-06

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: 48.84  E-value: 7.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852   268 PKNVVFIIDRSGSMHGRRIRQtRSALLTILKD-LDEDDHFGLITFDAEI----DFW--KRELLQATK----ANRENAESF 336
Cdd:TIGR03436  53 PLTVGLVIDTSGSMRNDLDRA-RAAAIRFLKTvLRPNDRVFVVTFNTRLrllqDFTsdPRLLEAALNrlkpPLRTDYNSS 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67677852   337 VKRIQDRGATNINDAVLAGV--DMINRNPRKGTASILILLTDGDPTAGETNIEKIMANVKEA 396
Cdd:TIGR03436 132 GAFVRDGGGTALYDAITLAAleQLANALAGIPGRKALIVISDGGDNRSRDTLERAIDAAQRA 193
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 267-443 7.24e-58

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: 195.90  E-value: 7.24e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 267 IPKNVVFIIDRSGSMHGRRIRQTRSALLTILKDLDEDDHFGLITFDAEIDFWKRELLQATKANRENAESFVKRIQDRGAT 346
Cdd:cd01461   1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 347 NINDAVLAGVDMINRNPrkGTASILILLTDGDptagETNIEKIMANVKEAIGSKFPLYCLGFGYDVNFDFLTKMSLENNA 426
Cdd:cd01461  81 NMNDALEAALELLNSSP--GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLERLAREGRG 154

                       170
                ....*....|....*..
gi 67677852 427 VARRIYEDSDADIQLQG 443
Cdd:cd01461 155 IARRIYETDDIESQLLR 171
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
20-144 1.75e-46

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 162.53  E-value: 1.75e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852     20 SAPVEKKQNVDIYSFYINSTVSSRYATTIITSRVANKLSEPQEIQFEVKIPKNAFISKFRMIIEGKTYDGVVKKKEEAQQ 99
Cdd:smart00609   6 GLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEVAQK 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 67677852    100 QYNKAVSRGESAGLIKSVGRTLEDFKTSVTVAANSKVTFELTYEE 144
Cdd:smart00609  86 QYEKAVSQGKTAGLVRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 260-456 1.10e-44

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 162.96  E-value: 1.10e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 260 APSDVPRIPKNVVFIIDRSGSMHGRRIRQTRSALLTILKDLDEDDHFGLITFDAEIdfwkRELLQATKA-NRENAESFVK 338
Cdd:COG2304  83 KAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDA----RVLLPPTPAtDRAKILAAID 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 339 RIQDRGATNINDAVLAGVDMINRNPRKGTASILILLTDGDPTAGETNIEKIMANVKEAIGSKFPLYCLGFGYDVNFDFLT 418
Cdd:COG2304 159 RLQAGGGTALGAGLELAYELARKHFIPGRVNRVILLTDGDANVGITDPEELLKLAEEAREEGITLTTLGVGSDYNEDLLE 238

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 67677852 419 KMSLENNAVARRIYEDSDADIQLQGFYDEVAVPLLTDI 456
Cdd:COG2304 239 RLADAGGGNYYYIDDPEEAEKVFVREFSRIGYENRALA 276
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 31-142 4.49e-36

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: 131.84  E-value: 4.49e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852    31 IYSFYINSTVSSRYATTIITSRVANKLSEPQEIQFEVKIPKNAFISKFRMIIEGKTYDGVVKKKEEAQQQYNKAVSRGES 110
Cdd:pfam08487   1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 67677852   111 AGLIKSVGRTLedFKTSV-TVAANSKVTFELTY 142
Cdd:pfam08487  81 AGLLEQDTPDV--FTTSVgNIPPGEKVTVELTY 111
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 265-449 3.70e-27

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: 111.57  E-value: 3.70e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 265 PRIPKNVVFIIDRSGSMHGR-RIRQTRSALLTILKDLDEDDHFGLITFDAEIdfwkrELLQATKANRENAESFVKRIQDR 343
Cdd:COG1240  89 PQRGRDVVLVVDASGSMAAEnRLEAAKGALLDFLDDYRPRDRVGLVAFGGEA-----EVLLPLTRDREALKRALDELPPG 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 344 GATNINDAVLAGVDMInRNPRKGTASILILLTDGDPTAGETNIEKImanVKEAIGSKFPLYCLGFGYD-VNFDFLTKMSL 422
Cdd:COG1240 164 GGTPLGDALALALELL-KRADPARRKVIVLLTDGRDNAGRIDPLEA---AELAAAAGIRIYTIGVGTEaVDEGLLREIAE 239

                       170       180
                ....*....|....*....|....*..
gi 67677852 423 ENNAVARRIyedSDADiQLQGFYDEVA 449
Cdd:COG1240 240 ATGGRYFRA---DDLS-ELAAIYREID 262
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 270-440 6.92e-27

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: 107.74  E-value: 6.92e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 270 NVVFIIDRSGSMHGRRIRQTRSALLTILKDLDEDDHFGLITFDAEIdfwkRELLQATKAN-RENAESFVKRIQDRGATNI 348
Cdd:cd01465   2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAA----ETVLPATPVRdKAAILAAIDRLTAGGSTAG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 349 NDAVLAGVDMINRNPRKGTASILILLTDGDPTAGETNIEKIMANVKEAIGSKFPLYCLGFGYDVNFDFLTKMSLENNAVA 428
Cdd:cd01465  78 GAGIQLGYQEAQKHFVPGGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAIADAGNGNT 157

                       170
                ....*....|..
gi 67677852 429 RriYEDSDADIQ 440
Cdd:cd01465 158 A--YIDNLAEAR 167
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 264-421 4.13e-26

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 108.61  E-value: 4.13e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 264 VPRIPKNVVFIIDRSGSMHGRRIRQTRSALLTILKDLDEDDHFGLITFDAEIdfwKRELLQATKANRENAESFVKRIQDR 343
Cdd:COG2425 114 VPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEV---VEDLPLTADDGLEDAIEFLSGLFAG 190

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67677852 344 GATNINDAVLAGVDMINRNPRKGTasILILLTDGDPTAGETNIEKIMANVKeaigSKFPLYCLGFGYDVNFDFLTKMS 421
Cdd:COG2425 191 GGTDIAPALRAALELLEEPDYRNA--DIVLITDGEAGVSPEELLREVRAKE----SGVRLFTVAIGDAGNPGLLEALA 262
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 270-428 1.90e-24

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 100.72  E-value: 1.90e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 270 NVVFIIDRSGSMHGRRIRQTRSALLTILKDLD---EDDHFGLITFDAEIdfwKRELLQATKANRENAESFVKRIQDR--G 344
Cdd:cd00198   2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSaspPGDRVGLVTFGSNA---RVVLPLTTDTDKADLLEAIDALKKGlgG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 345 ATNINDAVLAGVDMINRNPRKGTASILILLTDGDPTAGETNIEKImanVKEAIGSKFPLYCLGFGYDVNFDFLTKMSLEN 424
Cdd:cd00198  79 GTNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEA---ARELRKLGITVYTIGIGDDANEDELKEIADKT 155


                ....
gi 67677852 425 NAVA 428
Cdd:cd00198 156 TGGA 159
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 270-437 4.89e-23

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: 97.14  E-value: 4.89e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852    270 NVVFIIDRSGSMHGRRIRQTRSALLTILKDLDE---DDHFGLITFDAEIdfwKRELLQATKANRENAESFVKRIQDR--G 344
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIgpdGDRVGLVTFSDDA---RVLFPLNDSRSKDALLEALASLSYKlgG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852    345 ATNINDAVLAGVDMIN---RNPRKGTASILILLTDGDPTAGETNIEKImanVKEAIGSKFPLYCLGFGYDVNFDFLTKMS 421
Cdd:smart00327  78 GTNLGAALQYALENLFsksAGSRRGAPKVVILITDGESNDGPKDLLKA---AKELKRSGVKVFVVGVGNDVDEEELKKLA 154

                          170
                   ....*....|....*.
gi 67677852    422 LENNAVARRIYEDSDA 437
Cdd:smart00327 155 SAPGGVYVFLPELLDL 170
VWA pfam00092
von Willebrand factor type A domain;
270-447 1.07e-21

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 93.11  E-value: 1.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852   270 NVVFIIDRSGSMHGRRIRQTRSALLTILKDLDED---DHFGLITFDAEidfWKRELLQATKANRENAESFVKRI--QDRG 344
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGpdgTRVGLVQYSSD---VRTEFPLNDYSSKEELLSAVDNLryLGGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852   345 ATNINDAVLAGVDMIN---RNPRKGTASILILLTDGDPTAGEtniekIMANVKEAIGSKFPLYCLGFGyDVNFDFLTKMS 421
Cdd:pfam00092  78 TTNTGKALKYALENLFssaAGARPGAPKVVVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVG-NADDEELRKIA 151

                         170       180
                  ....*....|....*....|....*.
gi 67677852   422 LENNavARRIYEDSDADiQLQGFYDE 447
Cdd:pfam00092 152 SEPG--EGHVFTVSDFE-ALEDLQDQ 174
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
265-421 1.14e-18

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 84.98  E-value: 1.14e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 265 PRIPknVVFIIDRSGSMHGRRIRQTRSALLTILKDLDEDD------HFGLITFDAEIdfwkRELLQATKanrenAESF-V 337
Cdd:COG4245   4 RRLP--VYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPyaletvEVSVITFDGEA----KVLLPLTD-----LEDFqP 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 338 KRIQDRGATNINDAVLAGVDMINRNPRKGTAS-------ILILLTDGDPTAGETN--IEKIMANVKEAIGSKFPlycLGF 408
Cdd:COG4245  73 PDLSASGGTPLGAALELLLDLIERRVQKYTAEgkgdwrpVVFLITDGEPTDSDWEaaLQRLKDGEAAKKANIFA---IGV 149

                       170
                ....*....|...
gi 67677852 409 GYDVNFDFLTKMS 421
Cdd:COG4245 150 GPDADTEVLKQLT 162
VWA_2 pfam13519
von Willebrand factor type A domain;
271-373 9.57e-13

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 65.01  E-value: 9.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852   271 VVFIIDRSGSMHGRRIRQTR-----SALLTILKDLDEdDHFGLITFDAEIdfwkrELLQATKANRENAESFVKRIQDR-G 344
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRleaakDAVLALLKSLPG-DRVGLVTFGDGP-----EVLIPLTKDRAKILRALRRLEPKgG 74

                          90       100
                  ....*....|....*....|....*....
gi 67677852   345 ATNINDAVLAGVDMINRNPRKGTASILIL 373
Cdd:pfam13519  75 GTNLAAALQLARAALKHRRKNQPRRIVLI 103
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 271-411 5.02e-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: 64.72  E-value: 5.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 271 VVFIIDRSGSMHGRRIRQTRSALLTILKDLDEDDHFGLITFDAEIdfwKR--ELLQATKANRENAESFVKRIQDRGATNI 348
Cdd:cd01466   3 LVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSA---KRlsPLRRMTAKGKRSAKRVVDGLQAGGGTNV 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67677852 349 NDAVLAGVDMINRNPRKGTASILILLTDGDPTAgetniekiMANVKEAIGSKFPLYCLGFGYD 411
Cdd:cd01466  80 VGGLKKALKVLGDRRQKNPVASIMLLSDGQDNH--------GAVVLRADNAPIPIHTFGLGAS 134
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 265-421 1.81e-11

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: 63.51  E-value: 1.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 265 PRIPknVVFIIDRSGSMHGRRIRQTRSALLTILKDLDEDD------HFGLITFDAEIdfwkRELLQATkanreNAESF-V 337
Cdd:cd01464   2 RRLP--IYLLLDTSGSMAGEPIEALNQGLQMLQSELRQDPyalesvEISVITFDSAA----RVIVPLT-----PLESFqP 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 338 KRIQDRGATNINDAVLAGVDMINRNPRKGTAS-------ILILLTDGDPTAGET-NIEKImanvKEAIGSKFPLYCLGFG 409
Cdd:cd01464  71 PRLTASGGTSMGAALELALDCIDRRVQRYRADqkgdwrpWVFLLTDGEPTDDLTaAIERI----KEARDSKGRIVACAVG 146

                       170
                ....*....|..
gi 67677852 410 YDVNFDFLTKMS 421
Cdd:cd01464 147 PKADLDTLKQIT 158
VWA_3 pfam13768
von Willebrand factor type A domain;
269-417 3.92e-11

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 62.03  E-value: 3.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852   269 KNVVFIIDRSGSMHGRRIRQtRSALLTILKDLDEDDHFGLITFDAEIDFWKRELLQATKANRENAESFVKRIQ-DRGATN 347
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQpPLGGSD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 67677852   348 indaVLAGVDMINRNPRKGT-ASILILLTDGDPTAGETNIEKIMANVKEaigsKFPLYCLGFGYDVNFDFL 417
Cdd:pfam13768  80 ----LLGALKEAVRAPASPGyIRHVLLLTDGSPMQGETRVSDLISRAPG----KIRFFAYGLGASISAPML 142
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 268-388 5.16e-09

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: 57.02  E-value: 5.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 268 PKNVVFIIDRSGSMHGRRIRQTRSALLTILKDLDEDDHFGLITFDAE----IDFWKRELLQATKANRENAESFVKRIQDR 343
Cdd:cd01463  13 PKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEvnpvVPCFNDTLVQATTSNKKVLKEALDMLEAK 92

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 67677852 344 GATNINDA------VLAGVDMINRNPRKGTAS-ILILLTDGDPTAGETNIEK 388
Cdd:cd01463  93 GIANYTKAlefafsLLLKNLQSNHSGSRSQCNqAIMLITDGVPENYKEIFDK 144
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 270-421 5.75e-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: 56.15  E-value: 5.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 270 NVVFIIDRSGSMHGRRIRQTRSALLTILKDLD---EDDHFGLITF--DAEIDFwkrELLQATkaNRENAESFVKRIQDRG 344
Cdd:cd01450   2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDigpDKTRVGLVQYsdDVRVEF---SLNDYK--SKDDLLKAVKNLKYLG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 345 --ATNINDAVLAGVDMIN--RNPRKGTASILILLTDGDPTAGeTNIEKIMANVKEaigSKFPLYCLGFGyDVNFDFLTKM 420
Cdd:cd01450  77 ggGTNTGKALQYALEQLFseSNARENVPKVIIVLTDGRSDDG-GDPKEAAAKLKD---EGIKVFVVGVG-PADEEELREI 151


                .
gi 67677852 421 S 421
Cdd:cd01450 152 A 152
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 269-387 2.39e-08

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: 53.89  E-value: 2.39e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 269 KNVVFIIDRSGSMHGRRIRQTRSALLTILKD-LDEDDHFGLITFDAEidfWKRELLQATkANRENAESFVKRIQDRGATN 347
Cdd:cd01462   1 GPVILLVDQSGSMYGAPEEVAKAVALALLRIaLAENRDTYLILFDSE---FQTKIVDKT-DDLEEPVEFLSGVQLGGGTD 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 67677852 348 INDAVLAGVDMI-NRNPRKGTasiLILLTDGdpTAGETNIE 387
Cdd:cd01462  77 INKALRYALELIeRRDPRKAD---IVLITDG--YEGGVSDE 112
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 271-382 1.28e-06

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: 49.58  E-value: 1.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 271 VVFIIDRSGSMHGR-RIRQTRSALLTILKDLDED-DHFGLITF---DAEIdfwkreLLQATKaNRENAESFVKRIQDRGA 345
Cdd:cd01451   3 VIFVVDASGSMAARhRMAAAKGAVLSLLRDAYQRrDKVALIAFrgtEAEV------LLPPTR-SVELAKRRLARLPTGGG 75

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 67677852 346 TNINDAVLAGVDMINRNPR-KGTASILILLTDGDPTAG 382
Cdd:cd01451  76 TPLAAGLLAAYELAAEQARdPGQRPLIVVITDGRANVG 113
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 268-396 7.35e-06

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: 48.84  E-value: 7.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852   268 PKNVVFIIDRSGSMHGRRIRQtRSALLTILKD-LDEDDHFGLITFDAEI----DFW--KRELLQATK----ANRENAESF 336
Cdd:TIGR03436  53 PLTVGLVIDTSGSMRNDLDRA-RAAAIRFLKTvLRPNDRVFVVTFNTRLrllqDFTsdPRLLEAALNrlkpPLRTDYNSS 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67677852   337 VKRIQDRGATNINDAVLAGV--DMINRNPRKGTASILILLTDGDPTAGETNIEKIMANVKEA 396
Cdd:TIGR03436 132 GAFVRDGGGTALYDAITLAAleQLANALAGIPGRKALIVISDGGDNRSRDTLERAIDAAQRA 193
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
 271-392 1.28e-05

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: 49.11  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852   271 VVFIIDRSGSM--HGRRIRQTRSALLTILKDLDEDDHFGLITFD--AEIdfwKRELLQATKANRENAESFVKRIQDRGAT 346
Cdd:TIGR00868 307 VCLVLDKSGSMtvEDRLKRMNQAAKLFLLQTVEKGSWVGMVTFDsaAYI---KNELIQITSSAERDALTANLPTAASGGT 383

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 67677852   347 NINDAVLAGVDMINRNPRKGTASILILLTDGDPTAGETNIEKIMAN 392
Cdd:TIGR00868 384 SICSGLKAAFQVIKKSYQSTDGSEIVLLTDGEDNTISSCFEEVKQS 429
YeaD2 COG1721
Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];
270-376 1.67e-03

Uncharacterized conserved protein, DUF58 family, contains vWF domain [Function unknown];


Pssm-ID: 441327 [Multi-domain]  Cd Length: 287  Bit Score: 41.35  E-value: 1.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 270 NVVFIIDRSGSMHGRRIRQTRS--------ALLTILkdLDEDDHFGLITFDAEIDFWkrellQATKANRENAESFVK--- 338
Cdd:COG1721 149 TVVLLLDTSASMRFGSGGPSKLdlaveaaaSLAYLA--LRQGDRVGLLTFGDRVRRY-----LPPRRGRRHLLRLLEala 221

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 67677852 339 RIQDRGATNINDAvlagVDMINRNPRKGtaSILILLTD 376
Cdd:COG1721 222 RLEPAGETDLAAA----LRRLARRLPRR--SLVVLISD 253
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 271-398 1.75e-03

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


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 40.42  E-value: 1.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 271 VVFIIDRSGSMHGRRIRQTRSALLTILKDLDEDD---HFGLITFDAEIdfwKRELLQATKANRENAESFVKRIQDRG--- 344
Cdd:cd01469   3 IVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPtktQFGLVQYSESF---RTEFTLNEYRTKEEPLSLVKHISQLLglt 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 67677852 345 --ATNINDAVLAGVDmINRNPRKGTASILILLTDGDPTAGETNIEKI----MANV-KEAIG 398
Cdd:cd01469  80 ntATAIQYVVTELFS-ESNGARKDATKVLVVITDGESHDDPLLKDVIpqaeREGIiRYAIG 139
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 270-412 2.40e-03

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: 40.01  E-value: 2.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 270 NVVFIIDRSGSMHGRRIRQ-TR-SALLTILKDL---DEDDHFGLITFDaeidfwKRELLQAT-KANRENAESFVKRIQ-- 341
Cdd:cd01467   4 DIMIALDVSGSMLAQDFVKpSRlEAAKEVLSDFidrRENDRIGLVVFA------GAAFTQAPlTLDRESLKELLEDIKig 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67677852 342 -DRGATNINDAVLAGVDMINrnPRKGTASILILLTDGDPTAGEtnIEKI-MANVKEAIGSKfpLYCLGFGYDV 412
Cdd:cd01467  78 lAGQGTAIGDAIGLAIKRLK--NSEAKERVIVLLTDGENNAGE--IDPAtAAELAKNKGVR--IYTIGVGKSG 144
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 269-377 2.40e-03

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: 39.69  E-value: 2.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67677852 269 KNVVFIIDRSGSMHGrRIRQTRSALLTILKDLD---EDDHFGLITFDAEidfwKRELLQATKANRENAESFVKRIQD--- 342
Cdd:cd01476   1 LDLLFVLDSSGSVRG-KFEKYKKYIERIVEGLEigpTATRVALITYSGR----GRQRVRFNLPKHNDGEELLEKVDNlrf 75

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 67677852 343 -RGATNINDAVLAGVDMINRNP--RKGTASILILLTDG 377
Cdd:cd01476  76 iGGTTATGAAIEVALQQLDPSEgrREGIPKVVVVLTDG 113
 
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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