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Conserved domains on  [gi|767988296|ref|XP_011544048|]
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von Willebrand factor A domain-containing protein 3A isoform X13 [Homo sapiens]

Protein Classification

vWA domain-containing protein( domain architecture ID 630)

vWA (von Willebrand factor type A) domain-containing protein may be involved in one of a wide variety of important cellular functions, including basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and immune defenses

CATH:  3.40.50.410
PubMed:  10830113|12579041|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 ...
 487-633 3.71e-19

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: 85.34  E-value: 3.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296 487 LLDTSGSM-GPYLQQVKtELVLLIWEQLRKCcDSFNLLSFAESFQSWQDTLVETTDAACHEAMQWVTHLQAQGSTSILQA 565
Cdd:cd01461    8 VIDTSGSMsGTKIEQTK-EALLTALKDLPPG-DYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGTNMNDA 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767988296 566 LLKAFSFHD-----LEGLYLLTDGKpDTSCSLVLNEVQKlREKRDVKVHT--ISLNCSDRaaveFLRKLASFTGG 633
Cdd:cd01461   86 LEAALELLNsspgsVPQIILLTDGE-VTNESQILKNVRE-ALSGRIRLFTfgIGSDVNTY----LLERLAREGRG 154
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 11-118 1.24e-15

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: 75.33  E-value: 1.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296  11 RVVVLLDISAtnSMY---IIHIQHSLRLLLEEqLSNKDCFNLIAFGSTIESWRPEMVPVSHNNLQSAWRWALNLRCRGSR 87
Cdd:cd01461    4 EVVFVIDTSG--SMSgtkIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767988296  88 NVLSALRKAVEvdFKDKDKHQSQGIYLFTGG 118
Cdd:cd01461   81 NMNDALEAALE--LLNSSPGSVPQIILLTDG 109
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 487-633 3.71e-19

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: 85.34  E-value: 3.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296 487 LLDTSGSM-GPYLQQVKtELVLLIWEQLRKCcDSFNLLSFAESFQSWQDTLVETTDAACHEAMQWVTHLQAQGSTSILQA 565
Cdd:cd01461    8 VIDTSGSMsGTKIEQTK-EALLTALKDLPPG-DYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGTNMNDA 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767988296 566 LLKAFSFHD-----LEGLYLLTDGKpDTSCSLVLNEVQKlREKRDVKVHT--ISLNCSDRaaveFLRKLASFTGG 633
Cdd:cd01461   86 LEAALELLNsspgsVPQIILLTDGE-VTNESQILKNVRE-ALSGRIRLFTfgIGSDVNTY----LLERLAREGRG 154
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 484-636 3.02e-16

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: 79.21  E-value: 3.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296 484 VCILLDTSGSMGPY--LQQVKTELVLLIWEQLRKccDSFNLLSFAESFqswqDTLVE-TTDAAchEAMQWVTHLQAQGST 560
Cdd:COG1240   95 VVLVVDASGSMAAEnrLEAAKGALLDFLDDYRPR--DRVGLVAFGGEA----EVLLPlTRDRE--ALKRALDELPPGGGT 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296 561 SILQALLKAFSFHDLEG------LYLLTDGKPDTSCSLVLNEVQKLREkRDVKVHTISLNcSDRAAVEFLRKLASFTGGR 634
Cdd:COG1240  167 PLGDALALALELLKRADparrkvIVLLTDGRDNAGRIDPLEAAELAAA-AGIRIYTIGVG-TEAVDEGLLREIAEATGGR 244


                 ..
gi 767988296 635 YH 636
Cdd:COG1240  245 YF 246
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 11-118 1.24e-15

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: 75.33  E-value: 1.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296  11 RVVVLLDISAtnSMY---IIHIQHSLRLLLEEqLSNKDCFNLIAFGSTIESWRPEMVPVSHNNLQSAWRWALNLRCRGSR 87
Cdd:cd01461    4 EVVFVIDTSG--SMSgtkIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767988296  88 NVLSALRKAVEvdFKDKDKHQSQGIYLFTGG 118
Cdd:cd01461   81 NMNDALEAALE--LLNSSPGSVPQIILLTDG 109
VWA_3 pfam13768
von Willebrand factor type A domain;
484-637 4.20e-13

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 67.42  E-value: 4.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296  484 VCILLDTSGSM-GPYLQQVKTELVLLiwEQLRKCcDSFNLLSFAESFQSWQDTLVETTDAACHEAMQWVTHLQAQ-GSTS 561
Cdd:pfam13768   3 VVIVVDVSSSMsGEPKLQKDALSVAL--RQLPTG-DKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPlGGSD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296  562 ILQALLKAFSFHDLEG----LYLLTDGKPDTSCSLVLNEVQklREKRDVKVHTISLNCSDRAAVefLRKLASFTGGRYHC 637
Cdd:pfam13768  80 LLGALKEAVRAPASPGyirhVLLLTDGSPMQGETRVSDLIS--RAPGKIRFFAYGLGASISAPM--LQLLAEASNGTYEF 155
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 484-651 2.95e-12

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: 65.55  E-value: 2.95e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296   484 VCILLDTSGSMGP-YLQQVKTELVLLIwEQLRKCCDS--FNLLSFAESFQSWQDTLVETTDAACHEAMQwVTHLQAQGST 560
Cdd:smart00327   2 VVFLLDGSGSMGGnRFELAKEFVLKLV-EQLDIGPDGdrVGLVTFSDDARVLFPLNDSRSKDALLEALA-SLSYKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296   561 SILQALLKAFS--FHDLEG--------LYLLTDGKPDTSCSLVLNEVQKLREKRdVKVHTISLncSDRAAVEFLRKLASF 630
Cdd:smart00327  80 NLGAALQYALEnlFSKSAGsrrgapkvVILITDGESNDGPKDLLKAAKELKRSG-VKVFVVGV--GNDVDEEELKKLASA 156

                          170       180
                   ....*....|....*....|.
gi 767988296   631 TGGRYHcpVGEDTLSKIHSLL 651
Cdd:smart00327 157 PGGVYV--FLPELLDLLIDLL 175
VWA_3 pfam13768
von Willebrand factor type A domain;
11-163 1.05e-10

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 60.49  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296   11 RVVVLLDISATNSMYIIHIQHSLRLLLEeQLSNKDCFNLIAFGSTIESWRPEMVPVSHNNLQSAWRW--ALNLRcRGSRN 88
Cdd:pfam13768   2 DVVIVVDVSSSMSGEPKLQKDALSVALR-QLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFikTLQPP-LGGSD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767988296   89 VLSALRKAVEVDFKDK-DKHqsqgIYLFTGGIPDQDMPTLSAYMAeacggcDLQLNVCLFYVG-EPKMDTTPPARYA 163
Cdd:pfam13768  80 LLGALKEAVRAPASPGyIRH----VLLLTDGSPMQGETRVSDLIS------RAPGKIRFFAYGlGASISAPMLQLLA 146
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
 484-633 9.14e-06

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: 9.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296  484 VCILLDTSGSMGP-----YLQQVKTELVLLIWEQlrkccDSFNLLSFAESFQSWQDTLVETTDAACHEAMQWVTHLQAQG 558
Cdd:TIGR00868 307 VCLVLDKSGSMTVedrlkRMNQAAKLFLLQTVEK-----GSWVGMVTFDSAAYIKNELIQITSSAERDALTANLPTAASG 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296  559 STSILQALLKAF-----SFHDLEG--LYLLTDGKpDTSCSLVLNEVQklreKRDVKVHTISLNcsdRAAVEFLRKLASFT 631
Cdd:TIGR00868 382 GTSICSGLKAAFqvikkSYQSTDGseIVLLTDGE-DNTISSCFEEVK----QSGAIIHTIALG---PSAAKELEELSDMT 453


                  ..
gi 767988296  632 GG 633
Cdd:TIGR00868 454 GG 455
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 487-633 3.71e-19

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: 85.34  E-value: 3.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296 487 LLDTSGSM-GPYLQQVKtELVLLIWEQLRKCcDSFNLLSFAESFQSWQDTLVETTDAACHEAMQWVTHLQAQGSTSILQA 565
Cdd:cd01461    8 VIDTSGSMsGTKIEQTK-EALLTALKDLPPG-DYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGTNMNDA 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767988296 566 LLKAFSFHD-----LEGLYLLTDGKpDTSCSLVLNEVQKlREKRDVKVHT--ISLNCSDRaaveFLRKLASFTGG 633
Cdd:cd01461   86 LEAALELLNsspgsVPQIILLTDGE-VTNESQILKNVRE-ALSGRIRLFTfgIGSDVNTY----LLERLAREGRG 154
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 484-633 1.07e-18

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 83.77  E-value: 1.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296 484 VCILLDTSGSMGPYLQQVKTELVLLIWEQLRKCC--DSFNLLSFAESFQSWQDTLVETTDAACHEAMQWVTHlQAQGSTS 561
Cdd:cd00198    3 IVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPpgDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK-GLGGGTN 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767988296 562 ILQALLKAFSFHDLEG-------LYLLTDGKPDTSCSLVLNEVQKLReKRDVKVHTISLncSDRAAVEFLRKLASFTGG 633
Cdd:cd00198   82 IGAALRLALELLKSAKrpnarrvIILLTDGEPNDGPELLAEAARELR-KLGITVYTIGI--GDDANEDELKEIADKTTG 157
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 484-636 3.02e-16

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: 79.21  E-value: 3.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296 484 VCILLDTSGSMGPY--LQQVKTELVLLIWEQLRKccDSFNLLSFAESFqswqDTLVE-TTDAAchEAMQWVTHLQAQGST 560
Cdd:COG1240   95 VVLVVDASGSMAAEnrLEAAKGALLDFLDDYRPR--DRVGLVAFGGEA----EVLLPlTRDRE--ALKRALDELPPGGGT 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296 561 SILQALLKAFSFHDLEG------LYLLTDGKPDTSCSLVLNEVQKLREkRDVKVHTISLNcSDRAAVEFLRKLASFTGGR 634
Cdd:COG1240  167 PLGDALALALELLKRADparrkvIVLLTDGRDNAGRIDPLEAAELAAA-AGIRIYTIGVG-TEAVDEGLLREIAEATGGR 244


                 ..
gi 767988296 635 YH 636
Cdd:COG1240  245 YF 246
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 11-118 1.24e-15

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: 75.33  E-value: 1.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296  11 RVVVLLDISAtnSMY---IIHIQHSLRLLLEEqLSNKDCFNLIAFGSTIESWRPEMVPVSHNNLQSAWRWALNLRCRGSR 87
Cdd:cd01461    4 EVVFVIDTSG--SMSgtkIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767988296  88 NVLSALRKAVEvdFKDKDKHQSQGIYLFTGG 118
Cdd:cd01461   81 NMNDALEAALE--LLNSSPGSVPQIILLTDG 109
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 484-636 5.36e-14

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 73.21  E-value: 5.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296 484 VCILLDTSGSM-GPYLQQVKTELVLLIwEQLRKcCDSFNLLSFAESFQswqdTLVETTDAA-CHEAMQWVTHLQAQGSTS 561
Cdd:COG2304   94 LVFVIDVSGSMsGDKLELAKEAAKLLV-DQLRP-GDRVSIVTFAGDAR----VLLPPTPATdRAKILAAIDRLQAGGGTA 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296 562 ILQALLKAFSF---HDLEG----LYLLTDGKPD---TSCSLVLNEVQKLREKrDVKVHTI----SLNcsdraaVEFLRKL 627
Cdd:COG2304  168 LGAGLELAYELarkHFIPGrvnrVILLTDGDANvgiTDPEELLKLAEEAREE-GITLTTLgvgsDYN------EDLLERL 240


                 ....*....
gi 767988296 628 ASFTGGRYH 636
Cdd:COG2304  241 ADAGGGNYY 249
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 12-152 1.69e-13

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: 68.75  E-value: 1.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296  12 VVVLLDISAtnSM---YIIHIQHSLRLLLE--EQLSNKDCFNLIAFGSTIESWRPEMVPVSHNNLQSAWRWaLNLRCRGS 86
Cdd:cd00198    3 IVFLLDVSG--SMggeKLDKAKEALKALVSslSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDA-LKKGLGGG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767988296  87 RNVLSALRKAVEVDFKDKDKHQSQGIYLFTGGIPDQDMPTLSAYMAEAcggCDLQLNVCLFYVGEP 152
Cdd:cd00198   80 TNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAAREL---RKLGITVYTIGIGDD 142
VWA_3 pfam13768
von Willebrand factor type A domain;
484-637 4.20e-13

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 67.42  E-value: 4.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296  484 VCILLDTSGSM-GPYLQQVKTELVLLiwEQLRKCcDSFNLLSFAESFQSWQDTLVETTDAACHEAMQWVTHLQAQ-GSTS 561
Cdd:pfam13768   3 VVIVVDVSSSMsGEPKLQKDALSVAL--RQLPTG-DKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPlGGSD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296  562 ILQALLKAFSFHDLEG----LYLLTDGKPDTSCSLVLNEVQklREKRDVKVHTISLNCSDRAAVefLRKLASFTGGRYHC 637
Cdd:pfam13768  80 LLGALKEAVRAPASPGyirhVLLLTDGSPMQGETRVSDLIS--RAPGKIRFFAYGLGASISAPM--LQLLAEASNGTYEF 155
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 479-628 6.03e-13

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 69.71  E-value: 6.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296 479 VLESKVCILLDTSGSM-GPYLQQVKTELVLLIWEQLRKccDSFNLLSFaeSFQSWQDTLVeTTDAACHEAMQWVTHLQAQ 557
Cdd:COG2425  116 LLEGPVVLCVDTSGSMaGSKEAAAKAAALALLRALRPN--RRFGVILF--DTEVVEDLPL-TADDGLEDAIEFLSGLFAG 190

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767988296 558 GSTSILQALLKAfsFHDLEG-------LYLLTDGKPDTSCSLVLNEVQklREKRDVKVHTISLncSDRAAVEFLRKLA 628
Cdd:COG2425  191 GGTDIAPALRAA--LELLEEpdyrnadIVLITDGEAGVSPEELLREVR--AKESGVRLFTVAI--GDAGNPGLLEALA 262
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 484-651 2.95e-12

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: 65.55  E-value: 2.95e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296   484 VCILLDTSGSMGP-YLQQVKTELVLLIwEQLRKCCDS--FNLLSFAESFQSWQDTLVETTDAACHEAMQwVTHLQAQGST 560
Cdd:smart00327   2 VVFLLDGSGSMGGnRFELAKEFVLKLV-EQLDIGPDGdrVGLVTFSDDARVLFPLNDSRSKDALLEALA-SLSYKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296   561 SILQALLKAFS--FHDLEG--------LYLLTDGKPDTSCSLVLNEVQKLREKRdVKVHTISLncSDRAAVEFLRKLASF 630
Cdd:smart00327  80 NLGAALQYALEnlFSKSAGsrrgapkvVILITDGESNDGPKDLLKAAKELKRSG-VKVFVVGV--GNDVDEEELKKLASA 156

                          170       180
                   ....*....|....*....|.
gi 767988296   631 TGGRYHcpVGEDTLSKIHSLL 651
Cdd:smart00327 157 PGGVYV--FLPELLDLLIDLL 175
VWA_3 pfam13768
von Willebrand factor type A domain;
11-163 1.05e-10

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 60.49  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296   11 RVVVLLDISATNSMYIIHIQHSLRLLLEeQLSNKDCFNLIAFGSTIESWRPEMVPVSHNNLQSAWRW--ALNLRcRGSRN 88
Cdd:pfam13768   2 DVVIVVDVSSSMSGEPKLQKDALSVALR-QLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFikTLQPP-LGGSD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767988296   89 VLSALRKAVEVDFKDK-DKHqsqgIYLFTGGIPDQDMPTLSAYMAeacggcDLQLNVCLFYVG-EPKMDTTPPARYA 163
Cdd:pfam13768  80 LLGALKEAVRAPASPGyIRH----VLLLTDGSPMQGETRVSDLIS------RAPGKIRFFAYGlGASISAPMLQLLA 146
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 485-611 2.30e-07

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: 51.12  E-value: 2.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296 485 CILLDTSGSM-GPYLQQVKTELVLLIwEQLRKcCDSFNLLSFAESfqswQDTLVETT----DAACHEAMQwvtHLQAQGS 559
Cdd:cd01465    4 VFVIDRSGSMdGPKLPLVKSALKLLV-DQLRP-DDRLAIVTYDGA----AETVLPATpvrdKAAILAAID---RLTAGGS 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767988296 560 TSI---LQALLKAFSFHDLEG----LYLLTDGKP---DTSCSLVLNEVQKLREKrDVKVHTI 611
Cdd:cd01465   75 TAGgagIQLGYQEAQKHFVPGgvnrILLATDGDFnvgETDPDELARLVAQKRES-GITLSTL 135
VWA pfam00092
von Willebrand factor type A domain;
484-629 3.77e-07

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 50.74  E-value: 3.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296  484 VCILLDTSGSMGPY-LQQVKTELVLLIwEQLRKCCDS--FNLLSFAESFQswqdTLVETTDAACH-EAMQWVTHL--QAQ 557
Cdd:pfam00092   2 IVFLLDGSGSIGGDnFEKVKEFLKKLV-ESLDIGPDGtrVGLVQYSSDVR----TEFPLNDYSSKeELLSAVDNLryLGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296  558 GSTSILQALLKA--FSFHDLEG--------LYLLTDGKPDtsCSLVLNEVQKLREkRDVKVHTISLNcsdRAAVEFLRKL 627
Cdd:pfam00092  77 GTTNTGKALKYAleNLFSSAAGarpgapkvVVLLTDGRSQ--DGDPEEVARELKS-AGVTVFAVGVG---NADDEELRKI 150


                  ..
gi 767988296  628 AS 629
Cdd:pfam00092 151 AS 152
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 483-614 2.69e-06

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: 47.73  E-value: 2.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296 483 KVCILLDTSGSMGPYLQQVKTELVLLIWEQLRKCCDSFNLLSFAESFQSWqdtLVETTDaACHEAMQWVTHLQAQGSTSI 562
Cdd:cd01462    2 PVILLVDQSGSMYGAPEEVAKAVALALLRIALAENRDTYLILFDSEFQTK---IVDKTD-DLEEPVEFLSGVQLGGGTDI 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767988296 563 LQALLKAFSF---HDLEG--LYLLTDGKPDTSCSLVLNEVqKLREKRDVKVHTISLN 614
Cdd:cd01462   78 NKALRYALELierRDPRKadIVLITDGYEGGVSDELLREV-ELKRSRVARFVALALG 133
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
 484-633 9.14e-06

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: 9.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296  484 VCILLDTSGSMGP-----YLQQVKTELVLLIWEQlrkccDSFNLLSFAESFQSWQDTLVETTDAACHEAMQWVTHLQAQG 558
Cdd:TIGR00868 307 VCLVLDKSGSMTVedrlkRMNQAAKLFLLQTVEK-----GSWVGMVTFDSAAYIKNELIQITSSAERDALTANLPTAASG 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296  559 STSILQALLKAF-----SFHDLEG--LYLLTDGKpDTSCSLVLNEVQklreKRDVKVHTISLNcsdRAAVEFLRKLASFT 631
Cdd:TIGR00868 382 GTSICSGLKAAFqvikkSYQSTDGseIVLLTDGE-DNTISSCFEEVK----QSGAIIHTIALG---PSAAKELEELSDMT 453


                  ..
gi 767988296  632 GG 633
Cdd:TIGR00868 454 GG 455
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
484-629 7.93e-05

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 44.15  E-value: 7.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296 484 VCILLDTSGSM-GPYLQQVKTELVLLIwEQLRKccDS-------FNLLSFAESFQswqdTLVETTDAachEAMQWvTHLQ 555
Cdd:COG4245    8 VYLLLDTSGSMsGEPIEALNEGLQALI-DELRQ--DPyaletveVSVITFDGEAK----VLLPLTDL---EDFQP-PDLS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296 556 AQGSTSILQAL---------LKAFSFHDLEG-----LYLLTDGKP-DTSCSLVLNEVQKLREKRDVKVHTISLncsDRAA 620
Cdd:COG4245   77 ASGGTPLGAALellldlierRVQKYTAEGKGdwrpvVFLITDGEPtDSDWEAALQRLKDGEAAKKANIFAIGV---GPDA 153

                        170
                 ....*....|
gi 767988296 621 -VEFLRKLAS 629
Cdd:COG4245  154 dTEVLKQLTD 163
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 484-629 7.25e-04

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: 41.17  E-value: 7.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296 484 VCILLDTSGSM-GPYLQQVKTELVLLIWEqLRkcCDSFNLLSfAE----SFQSWQDTLVETTDAacheAMQWVTHLQAQG 558
Cdd:cd01464    6 IYLLLDTSGSMaGEPIEALNQGLQMLQSE-LR--QDPYALES-VEisviTFDSAARVIVPLTPL----ESFQPPRLTASG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296 559 STSILQALLKAfsFHDLEG----------------LYLLTDGKP-DTSCSlvlnEVQKLREKRDVKVHTISLNCSDRAAV 621
Cdd:cd01464   78 GTSMGAALELA--LDCIDRrvqryradqkgdwrpwVFLLTDGEPtDDLTA----AIERIKEARDSKGRIVACAVGPKADL 151


                 ....*...
gi 767988296 622 EFLRKLAS 629
Cdd:cd01464  152 DTLKQITE 159
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 486-637 5.21e-03

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: 38.43  E-value: 5.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296 486 ILLDTSGSMGPY-LQQVKTELVLLIwEQLRKCCDS--FNLLSFAE---------SFQSWQDTLVEttdaacHEAMQWVTH 553
Cdd:cd01450    5 FLLDGSESVGPEnFEKVKDFIEKLV-EKLDIGPDKtrVGLVQYSDdvrvefslnDYKSKDDLLKA------VKNLKYLGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296 554 lqaqGSTSILQALLKAFSFHDLEG---------LYLLTDGKPDTScSLVLNEVQKLREKrDVKVHTISLNcsdRAAVEFL 624
Cdd:cd01450   78 ----GGTNTGKALQYALEQLFSESnarenvpkvIIVLTDGRSDDG-GDPKEAAAKLKDE-GIKVFVVGVG---PADEEEL 148

                        170
                 ....*....|...
gi 767988296 625 RKLASfTGGRYHC 637
Cdd:cd01450  149 REIAS-CPSERHV 160
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 12-121 7.99e-03

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: 38.14  E-value: 7.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988296  12 VVVLLDISATNSMYIIHI-QHSLRLLLEeQLSNKDCFNLIAFGSTIESWRP----EMVPVSHNNLQSAWRWALNLRCRGS 86
Cdd:cd01463   16 IVILLDVSGSMTGQRLHLaKQTVSSILD-TLSDNDFFNIITFSNEVNPVVPcfndTLVQATTSNKKVLKEALDMLEAKGI 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767988296  87 RNVLSALRKAVEVDFKDKDKHQS-------QGIYLFTGGIPD 121
Cdd:cd01463   95 ANYTKALEFAFSLLLKNLQSNHSgsrsqcnQAIMLITDGVPE 136
 
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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