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Conserved domains on  [gi|755522500|ref|XP_011240056|]
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von Willebrand factor A domain-containing protein 3A isoform X3 [Mus musculus]

Protein Classification

VWA domain-containing protein( domain architecture ID 630)

VWA (von Willebrand factor type A) domain-containing protein

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 ...
 74-229 7.40e-31

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 pfam13768:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 155  Bit Score: 119.04  E-value: 7.40e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500    74 SRVGLLIDSSQVSSGSQtkEFQNDLTGLIDEQLSLKEKLYVLSFGVTINPLWPDPMEVSTSTLQELKLWVKTLQP-EGSS 152
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEP--KLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPpLGGS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500   153 NLLQALKKVFAHKELN----SLVIILRSCPDQPSEFLSDFIQQSTLGrsvfIHVTTYKCDDHVPSAVLKNLTDALGGYYH 228
Cdd:pfam13768   79 DLLGALKEAVRAPASPgyirHVLLLTDGSPMQGETRVSDLISRAPGK----IRFFAYGLGASISAPMLQLLAEASNGTYE 154


                   .
gi 755522500   229 C 229
Cdd:pfam13768  155 F 155
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 853-1006 1.40e-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: 87.27  E-value: 1.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  853 LERNVCILLDTSGSM-GPHLQWIKtELVLLIWEQLRKHCaRFNLLSFAEDLQLWQDTLVESTEAACHKAMQWVAHLQAQG 931
Cdd:cd01461     1 LPKEVVFVIDTSGSMsGTKIEQTK-EALLTALKDLPPGD-YFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  932 STSVLAALTKAFSFQD-----VQGLYLLTDGKpDTSCSLILNTVQsFQKERGVKVHTISLTSADRTAteFLRELASLSGG 1006
Cdd:cd01461    79 GTNMNDALEAALELLNsspgsVPQIILLTDGE-VTNESQILKNVR-EALSGRIRLFTFGIGSDVNTY--LLERLAREGRG 154
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 415-555 1.67e-17

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: 81.11  E-value: 1.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  415 RRVVILLDVSvtNSMY---IIHIQHSLRLLLEEqLSNKDYFNIIAFGSTIESWRPEMVAVSHDNLQRAWRWALGLQCQGS 491
Cdd:cd01461     3 KEVVFVIDTS--GSMSgtkIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522500  492 RNVLGALRKAIEvdFKDKNKHESQGIYLFTGGIPDQDVHILSAyVAEAyggcdLQLNVCLFYVG 555
Cdd:cd01461    80 TNMNDALEAALE--LLNSSPGSVPQIILLTDGEVTNESQILKN-VREA-----LSGRIRLFTFG 135
 
Name Accession Description Interval E-value
VWA_3 pfam13768
von Willebrand factor type A domain;
74-229 7.40e-31

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 119.04  E-value: 7.40e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500    74 SRVGLLIDSSQVSSGSQtkEFQNDLTGLIDEQLSLKEKLYVLSFGVTINPLWPDPMEVSTSTLQELKLWVKTLQP-EGSS 152
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEP--KLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPpLGGS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500   153 NLLQALKKVFAHKELN----SLVIILRSCPDQPSEFLSDFIQQSTLGrsvfIHVTTYKCDDHVPSAVLKNLTDALGGYYH 228
Cdd:pfam13768   79 DLLGALKEAVRAPASPgyirHVLLLTDGSPMQGETRVSDLISRAPGK----IRFFAYGLGASISAPMLQLLAEASNGTYE 154


                   .
gi 755522500   229 C 229
Cdd:pfam13768  155 F 155
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 853-1006 1.40e-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: 87.27  E-value: 1.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  853 LERNVCILLDTSGSM-GPHLQWIKtELVLLIWEQLRKHCaRFNLLSFAEDLQLWQDTLVESTEAACHKAMQWVAHLQAQG 931
Cdd:cd01461     1 LPKEVVFVIDTSGSMsGTKIEQTK-EALLTALKDLPPGD-YFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  932 STSVLAALTKAFSFQD-----VQGLYLLTDGKpDTSCSLILNTVQsFQKERGVKVHTISLTSADRTAteFLRELASLSGG 1006
Cdd:cd01461    79 GTNMNDALEAALELLNsspgsVPQIILLTDGE-VTNESQILKNVR-EALSGRIRLFTFGIGSDVNTY--LLERLAREGRG 154
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 415-555 1.67e-17

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: 81.11  E-value: 1.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  415 RRVVILLDVSvtNSMY---IIHIQHSLRLLLEEqLSNKDYFNIIAFGSTIESWRPEMVAVSHDNLQRAWRWALGLQCQGS 491
Cdd:cd01461     3 KEVVFVIDTS--GSMSgtkIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522500  492 RNVLGALRKAIEvdFKDKNKHESQGIYLFTGGIPDQDVHILSAyVAEAyggcdLQLNVCLFYVG 555
Cdd:cd01461    80 TNMNDALEAALE--LLNSSPGSVPQIILLTDGEVTNESQILKN-VREA-----LSGRIRLFTFG 135
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 839-1020 2.89e-15

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: 76.90  E-value: 2.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  839 WLLSAGSRRLFGTILERNVCILLDTSGSMG--PHLQWIKTELVLLIwEQLRKHcARFNLLSFAEDLQLWQDtLVESTEAa 916
Cdd:COG1240    77 LALALAPLALARPQRGRDVVLVVDASGSMAaeNRLEAAKGALLDFL-DDYRPR-DRVGLVAFGGEAEVLLP-LTRDREA- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  917 chkAMQWVAHLQAQGSTSVLAALTKAFS-FQDVQG-----LYLLTDGKPDTSCSLILNTVQSFqKERGVKVHTISlTSAD 990
Cdd:COG1240   153 ---LKRALDELPPGGGTPLGDALALALElLKRADParrkvIVLLTDGRDNAGRIDPLEAAELA-AAAGIRIYTIG-VGTE 227

                         170       180       190
                  ....*....|....*....|....*....|.
gi 755522500  991 RTATEFLRELASLSGGRYHcPVSD-KALSGI 1020
Cdd:COG1240   228 AVDEGLLREIAEATGGRYF-RADDlSELAAI 257
VWA_3 pfam13768
von Willebrand factor type A domain;
416-589 2.97e-14

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 71.27  E-value: 2.97e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500   416 RVVILLDVSVTNSMYIIHIQHSLRLLLEeQLSNKDYFNIIAFGSTIESWRPEMVAVSHDNLQRAWRWALGLQ-CQGSRNV 494
Cdd:pfam13768    2 DVVIVVDVSSSMSGEPKLQKDALSVALR-QLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQpPLGGSDL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500   495 LGALRKAIEVdfKDKNKHESQgIYLFTGGIPDQDVHILSAYVAeayggcDLQLNVCLFYVG-EPQMDTTPPacyasrtdt 573
Cdd:pfam13768   81 LGALKEAVRA--PASPGYIRH-VLLLTDGSPMQGETRVSDLIS------RAPGKIRFFAYGlGASISAPML--------- 142

                          170
                   ....*....|....*.
gi 755522500   574 atayKEITQAARGRFH 589
Cdd:pfam13768  143 ----QLLAEASNGTYE 154
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 856-1009 1.61e-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: 67.09  E-value: 1.61e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500    856 NVCILLDTSGSMGP-HLQWIKTELVLLIwEQLRKHC--ARFNLLSFAEDLQLWQDTLVESTEAACHKAMQwVAHLQAQGS 932
Cdd:smart00327    1 DVVFLLDGSGSMGGnRFELAKEFVLKLV-EQLDIGPdgDRVGLVTFSDDARVLFPLNDSRSKDALLEALA-SLSYKLGGG 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500    933 TSVLAALTKAFS--FQDVQG--------LYLLTDGKPDTSCSLILNTVQsFQKERGVKVHTISLTSAdrTATEFLRELAS 1002
Cdd:smart00327   79 TNLGAALQYALEnlFSKSAGsrrgapkvVILITDGESNDGPKDLLKAAK-ELKRSGVKVFVVGVGND--VDEEELKKLAS 155


                    ....*..
gi 755522500   1003 LSGGRYH 1009
Cdd:smart00327  156 APGGVYV 162
VWA_3 pfam13768
von Willebrand factor type A domain;
856-1010 3.31e-10

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 59.72  E-value: 3.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500   856 NVCILLDTSGSMGPHLQWIKTELVLLIwEQLrKHCARFNLLSFAEDLQLWQDTLVESTEAACHKAMQWVAHLQAQ-GSTS 934
Cdd:pfam13768    2 DVVIVVDVSSSMSGEPKLQKDALSVAL-RQL-PTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPlGGSD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500   935 VLAALTKAF----SFQDVQGLYLLTDGKPDTSCSlilNTVQSFQKERGvKVHTISLTSADRTATEFLRELASLSGGRYHC 1010
Cdd:pfam13768   80 LLGALKEAVrapaSPGYIRHVLLLTDGSPMQGET---RVSDLISRAPG-KIRFFAYGLGASISAPMLQLLAEASNGTYEF 155
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
 852-1016 6.66e-07

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: 53.73  E-value: 6.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500   852 ILERNVCILLDTSGSMGPHLQWIK----TELVLLiweQLRKHCARFNLLSFAEDLQLwQDTLVESTEAACHKAMQWVAHL 927
Cdd:TIGR00868  302 IRQRIVCLVLDKSGSMTVEDRLKRmnqaAKLFLL---QTVEKGSWVGMVTFDSAAYI-KNELIQITSSAERDALTANLPT 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500   928 QAQGSTSVLAALTKAF-----SFQDVQG--LYLLTDGKPDTSCSLILNTVQSfqkerGVKVHTISLtsaDRTATEFLREL 1000
Cdd:TIGR00868  378 AASGGTSICSGLKAAFqvikkSYQSTDGseIVLLTDGEDNTISSCFEEVKQS-----GAIIHTIAL---GPSAAKELEEL 449

                          170
                   ....*....|....*.
gi 755522500  1001 ASLSGGrYHCPVSDKA 1016
Cdd:TIGR00868  450 SDMTGG-LRFYASDQA 464
 
Name Accession Description Interval E-value
VWA_3 pfam13768
von Willebrand factor type A domain;
74-229 7.40e-31

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 119.04  E-value: 7.40e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500    74 SRVGLLIDSSQVSSGSQtkEFQNDLTGLIDEQLSLKEKLYVLSFGVTINPLWPDPMEVSTSTLQELKLWVKTLQP-EGSS 152
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEP--KLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPpLGGS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500   153 NLLQALKKVFAHKELN----SLVIILRSCPDQPSEFLSDFIQQSTLGrsvfIHVTTYKCDDHVPSAVLKNLTDALGGYYH 228
Cdd:pfam13768   79 DLLGALKEAVRAPASPgyirHVLLLTDGSPMQGETRVSDLISRAPGK----IRFFAYGLGASISAPMLQLLAEASNGTYE 154


                   .
gi 755522500   229 C 229
Cdd:pfam13768  155 F 155
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 853-1006 1.40e-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: 87.27  E-value: 1.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  853 LERNVCILLDTSGSM-GPHLQWIKtELVLLIWEQLRKHCaRFNLLSFAEDLQLWQDTLVESTEAACHKAMQWVAHLQAQG 931
Cdd:cd01461     1 LPKEVVFVIDTSGSMsGTKIEQTK-EALLTALKDLPPGD-YFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  932 STSVLAALTKAFSFQD-----VQGLYLLTDGKpDTSCSLILNTVQsFQKERGVKVHTISLTSADRTAteFLRELASLSGG 1006
Cdd:cd01461    79 GTNMNDALEAALELLNsspgsVPQIILLTDGE-VTNESQILKNVR-EALSGRIRLFTFGIGSDVNTY--LLERLAREGRG 154
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 415-555 1.67e-17

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: 81.11  E-value: 1.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  415 RRVVILLDVSvtNSMY---IIHIQHSLRLLLEEqLSNKDYFNIIAFGSTIESWRPEMVAVSHDNLQRAWRWALGLQCQGS 491
Cdd:cd01461     3 KEVVFVIDTS--GSMSgtkIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522500  492 RNVLGALRKAIEvdFKDKNKHESQGIYLFTGGIPDQDVHILSAyVAEAyggcdLQLNVCLFYVG 555
Cdd:cd01461    80 TNMNDALEAALE--LLNSSPGSVPQIILLTDGEVTNESQILKN-VREA-----LSGRIRLFTFG 135
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 855-1006 5.50e-17

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: 79.53  E-value: 5.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  855 RNVCILLDTSGSMGPHLQWIKTELVLLIWEQLRKHC--ARFNLLSFAEDLQLWQDTLVESTEAACHKAMQWVaHLQAQGS 932
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPpgDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDAL-KKGLGGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  933 TSVLAALTKAFSFQDVQG-------LYLLTDGKPDTSCSLILNTVQSFqKERGVKVHTISLtsADRTATEFLRELASLSG 1005
Cdd:cd00198    80 TNIGAALRLALELLKSAKrpnarrvIILLTDGEPNDGPELLAEAAREL-RKLGITVYTIGI--GDDANEDELKEIADKTT 156


                  .
gi 755522500 1006 G 1006
Cdd:cd00198   157 G 157
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 839-1020 2.89e-15

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: 76.90  E-value: 2.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  839 WLLSAGSRRLFGTILERNVCILLDTSGSMG--PHLQWIKTELVLLIwEQLRKHcARFNLLSFAEDLQLWQDtLVESTEAa 916
Cdd:COG1240    77 LALALAPLALARPQRGRDVVLVVDASGSMAaeNRLEAAKGALLDFL-DDYRPR-DRVGLVAFGGEAEVLLP-LTRDREA- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  917 chkAMQWVAHLQAQGSTSVLAALTKAFS-FQDVQG-----LYLLTDGKPDTSCSLILNTVQSFqKERGVKVHTISlTSAD 990
Cdd:COG1240   153 ---LKRALDELPPGGGTPLGDALALALElLKRADParrkvIVLLTDGRDNAGRIDPLEAAELA-AAAGIRIYTIG-VGTE 227

                         170       180       190
                  ....*....|....*....|....*....|.
gi 755522500  991 RTATEFLRELASLSGGRYHcPVSD-KALSGI 1020
Cdd:COG1240   228 AVDEGLLREIAEATGGRYF-RADDlSELAAI 257
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 855-1009 1.74e-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: 75.14  E-value: 1.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  855 RNVCILLDTSGSM-GPHLQWIKTELVLLIwEQLRKHcARFNLLSFAEDLQlwqdTLVESTEAA-CHKAMQWVAHLQAQGS 932
Cdd:COG2304    92 LNLVFVIDVSGSMsGDKLELAKEAAKLLV-DQLRPG-DRVSIVTFAGDAR----VLLPPTPATdRAKILAAIDRLQAGGG 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  933 TSVLAALTKAFS-FQDVQG------LYLLTDGKPD---TSCSLILNTVQSfQKERGVKVHTISL-TSADRtatEFLRELA 1001
Cdd:COG2304   166 TALGAGLELAYElARKHFIpgrvnrVILLTDGDANvgiTDPEELLKLAEE-AREEGITLTTLGVgSDYNE---DLLERLA 241


                  ....*...
gi 755522500 1002 SLSGGRYH 1009
Cdd:COG2304   242 DAGGGNYY 249
VWA_3 pfam13768
von Willebrand factor type A domain;
416-589 2.97e-14

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 71.27  E-value: 2.97e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500   416 RVVILLDVSVTNSMYIIHIQHSLRLLLEeQLSNKDYFNIIAFGSTIESWRPEMVAVSHDNLQRAWRWALGLQ-CQGSRNV 494
Cdd:pfam13768    2 DVVIVVDVSSSMSGEPKLQKDALSVALR-QLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQpPLGGSDL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500   495 LGALRKAIEVdfKDKNKHESQgIYLFTGGIPDQDVHILSAYVAeayggcDLQLNVCLFYVG-EPQMDTTPPacyasrtdt 573
Cdd:pfam13768   81 LGALKEAVRA--PASPGYIRH-VLLLTDGSPMQGETRVSDLIS------RAPGKIRFFAYGlGASISAPML--------- 142

                          170
                   ....*....|....*.
gi 755522500   574 atayKEITQAARGRFH 589
Cdd:pfam13768  143 ----QLLAEASNGTYE 154
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 415-559 3.37e-14

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: 71.44  E-value: 3.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  415 RRVVILLDVSvtNSM---YIIHIQHSLRLLLE--EQLSNKDYFNIIAFGSTIESWRPEMVAVSHDNLQRAWRWaLGLQCQ 489
Cdd:cd00198     1 ADIVFLLDVS--GSMggeKLDKAKEALKALVSslSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDA-LKKGLG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  490 GSRNVLGALRKAIEVDFKDKNKHESQGIYLFTGGIPDQDVHILSAYVAEAyggCDLQLNVCLFYVGEPQM 559
Cdd:cd00198    78 GGTNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAAREL---RKLGITVYTIGIGDDAN 144
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 839-1001 4.51e-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: 70.48  E-value: 4.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  839 WLLSAGSRRLFGTILERNVCILLDTSGSM-GPHLQWIKTELVLLIwEQLRKHcARFNLLSFaeDLQLWQDTLVESTEAAc 917
Cdd:COG2425   103 LLLLAAPASAAVPLLEGPVVLCVDTSGSMaGSKEAAAKAAALALL-RALRPN-RRFGVILF--DTEVVEDLPLTADDGL- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  918 HKAMQWVAHLQAQGSTSVLAALTKAFS-FQDVQG----LYLLTDGKPDTSCSLILNTVQsfQKERGVKVHTISLTSADrt 992
Cdd:COG2425   178 EDAIEFLSGLFAGGGTDIAPALRAALElLEEPDYrnadIVLITDGEAGVSPEELLREVR--AKESGVRLFTVAIGDAG-- 253


                  ....*....
gi 755522500  993 ATEFLRELA 1001
Cdd:COG2425   254 NPGLLEALA 262
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 856-1009 1.61e-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: 67.09  E-value: 1.61e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500    856 NVCILLDTSGSMGP-HLQWIKTELVLLIwEQLRKHC--ARFNLLSFAEDLQLWQDTLVESTEAACHKAMQwVAHLQAQGS 932
Cdd:smart00327    1 DVVFLLDGSGSMGGnRFELAKEFVLKLV-EQLDIGPdgDRVGLVTFSDDARVLFPLNDSRSKDALLEALA-SLSYKLGGG 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500    933 TSVLAALTKAFS--FQDVQG--------LYLLTDGKPDTSCSLILNTVQsFQKERGVKVHTISLTSAdrTATEFLRELAS 1002
Cdd:smart00327   79 TNLGAALQYALEnlFSKSAGsrrgapkvVILITDGESNDGPKDLLKAAK-ELKRSGVKVFVVGVGND--VDEEELKKLAS 155


                    ....*..
gi 755522500   1003 LSGGRYH 1009
Cdd:smart00327  156 APGGVYV 162
VWA_3 pfam13768
von Willebrand factor type A domain;
856-1010 3.31e-10

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 59.72  E-value: 3.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500   856 NVCILLDTSGSMGPHLQWIKTELVLLIwEQLrKHCARFNLLSFAEDLQLWQDTLVESTEAACHKAMQWVAHLQAQ-GSTS 934
Cdd:pfam13768    2 DVVIVVDVSSSMSGEPKLQKDALSVAL-RQL-PTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPlGGSD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500   935 VLAALTKAF----SFQDVQGLYLLTDGKPDTSCSlilNTVQSFQKERGvKVHTISLTSADRTATEFLRELASLSGGRYHC 1010
Cdd:pfam13768   80 LLGALKEAVrapaSPGYIRHVLLLTDGSPMQGET---RVSDLISRAPG-KIRFFAYGLGASISAPMLQLLAEASNGTYEF 155
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 856-1009 4.38e-09

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: 56.90  E-value: 4.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  856 NVCILLDTSGSM-GPHLQWIKTELVLLIwEQLRKHcARFNLLSFAEDLQlwqdTLVEST----EAACHKAMQwvaHLQAQ 930
Cdd:cd01465     2 NLVFVIDRSGSMdGPKLPLVKSALKLLV-DQLRPD-DRLAIVTYDGAAE----TVLPATpvrdKAAILAAID---RLTAG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  931 GSTSVLAAL-------TKAFSFQDVQGLYLLTDGKP---DTSCSLILNTVQSfQKERGVKVHTISLtsADRTATEFLREL 1000
Cdd:cd01465    73 GSTAGGAGIqlgyqeaQKHFVPGGVNRILLATDGDFnvgETDPDELARLVAQ-KRESGITLSTLGF--GDNYNEDLMEAI 149


                  ....*....
gi 755522500 1001 ASLSGGRYH 1009
Cdd:cd01465   150 ADAGNGNTA 158
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
 852-1016 6.66e-07

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: 53.73  E-value: 6.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500   852 ILERNVCILLDTSGSMGPHLQWIK----TELVLLiweQLRKHCARFNLLSFAEDLQLwQDTLVESTEAACHKAMQWVAHL 927
Cdd:TIGR00868  302 IRQRIVCLVLDKSGSMTVEDRLKRmnqaAKLFLL---QTVEKGSWVGMVTFDSAAYI-KNELIQITSSAERDALTANLPT 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500   928 QAQGSTSVLAALTKAF-----SFQDVQG--LYLLTDGKPDTSCSLILNTVQSfqkerGVKVHTISLtsaDRTATEFLREL 1000
Cdd:TIGR00868  378 AASGGTSICSGLKAAFqvikkSYQSTDGseIVLLTDGEDNTISSCFEEVKQS-----GAIIHTIAL---GPSAAKELEEL 449

                          170
                   ....*....|....*.
gi 755522500  1001 ASLSGGrYHCPVSDKA 1016
Cdd:TIGR00868  450 SDMTGG-LRFYASDQA 464
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
845-1030 2.25e-06

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 49.54  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  845 SRRLfgtilerNVCILLDTSGSM-GPHLQWIKTELVLLIwEQLRKHC-----ARFNLLSFAEDLQlwqdTLVESTEAAch 918
Cdd:COG4245     3 MRRL-------PVYLLLDTSGSMsGEPIEALNEGLQALI-DELRQDPyaletVEVSVITFDGEAK----VLLPLTDLE-- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  919 kAMQWvAHLQAQGSTSVLAALTKAFS-FQDVQG-------------LYLLTDGKP-DTSCSLILNTVQSFQKERGVKVHT 983
Cdd:COG4245    69 -DFQP-PDLSASGGTPLGAALELLLDlIERRVQkytaegkgdwrpvVFLITDGEPtDSDWEAALQRLKDGEAAKKANIFA 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 755522500  984 ISL-TSADrtaTEFLRELASlsggryhcpvSDKALSGIQGLLTRGFIK 1030
Cdd:COG4245   147 IGVgPDAD---TEVLKQLTD----------PVRALDALDGLDFREFFK 181
VWA pfam00092
von Willebrand factor type A domain;
856-1008 4.61e-06

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 48.04  E-value: 4.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500   856 NVCILLDTSGSMGPH-LQWIKTELVLLIwEQLR--KHCARFNLLSFAEDLQLWQDTLVESTEAachKAMQWVAHL--QAQ 930
Cdd:pfam00092    1 DIVFLLDGSGSIGGDnFEKVKEFLKKLV-ESLDigPDGTRVGLVQYSSDVRTEFPLNDYSSKE---ELLSAVDNLryLGG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500   931 GSTSVLAALTKA--FSFQDVQG--------LYLLTDGKPDtsCSLILNTVQSFqKERGVKVHTISLTSADRTAtefLREL 1000
Cdd:pfam00092   77 GTTNTGKALKYAleNLFSSAAGarpgapkvVVLLTDGRSQ--DGDPEEVAREL-KSAGVTVFAVGVGNADDEE---LRKI 150


                   ....*...
gi 755522500  1001 ASLSGGRY 1008
Cdd:pfam00092  151 ASEPGEGH 158
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 406-535 1.28e-05

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: 47.00  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  406 RRIW---GTVCQRRVVILLDVSVTNSMYIIHI-QHSLRLLLEeQLSNKDYFNIIAFGSTIESWRP----EMVAVSHDNlQ 477
Cdd:cd01463     2 NRSWyiqAATSPKDIVILLDVSGSMTGQRLHLaKQTVSSILD-TLSDNDFFNIITFSNEVNPVVPcfndTLVQATTSN-K 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755522500  478 RAWRWALG-LQCQGSRNVLGALRKAIEV--DFKDKNKHES-----QGIYLFTGGIPDQDVHILSAY 535
Cdd:cd01463    80 KVLKEALDmLEAKGIANYTKALEFAFSLllKNLQSNHSGSrsqcnQAIMLITDGVPENYKEIFDKY 145
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 859-1010 1.62e-04

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: 43.43  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  859 ILLDTSGSMGP-HLQWIKTELVLLIwEQLR--KHCARFNLLSFAEDLQLW----QDTLVESTEAAcHKAMQWVAHlqaqG 931
Cdd:cd01450     5 FLLDGSESVGPeNFEKVKDFIEKLV-EKLDigPDKTRVGLVQYSDDVRVEfslnDYKSKDDLLKA-VKNLKYLGG----G 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  932 STSVLAALTKAF--------SFQDVQG-LYLLTDGKPDTSCSLILNTVQsfQKERGVKVHTISLTSADRtatEFLRELAS 1002
Cdd:cd01450    79 GTNTGKALQYALeqlfsesnARENVPKvIIVLTDGRSDDGGDPKEAAAK--LKDEGIKVFVVGVGPADE---EELREIAS 153


                  ....*...
gi 755522500 1003 lSGGRYHC 1010
Cdd:cd01450   154 -CPSERHV 160
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 857-988 9.96e-04

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: 40.79  E-value: 9.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  857 VCILLDTSGSM-GPHLQWIKTELVLLIWeQLRKHCARFNLLSFAEDLQlwqdTLVESTEAACHKAMQWVAHLQAQGSTSV 935
Cdd:cd01462     3 VILLVDQSGSMyGAPEEVAKAVALALLR-IALAENRDTYLILFDSEFQ----TKIVDKTDDLEEPVEFLSGVQLGGGTDI 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 755522500  936 LAALTKAFSF---QDVQG--LYLLTDGKPDTSCSLILNTVqSFQKERGVKVHTISLTS 988
Cdd:cd01462    78 NKALRYALELierRDPRKadIVLITDGYEGGVSDELLREV-ELKRSRVARFVALALGD 134
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 855-961 1.77e-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: 40.84  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  855 RNVCILLDTSGSM-GPHLQWIKTElVLLIWEQLrKHCARFNLLSFAEDLQL----WQDTLVESTEAACHKAMQWVAHLQA 929
Cdd:cd01463    14 KDIVILLDVSGSMtGQRLHLAKQT-VSSILDTL-SDNDFFNIITFSNEVNPvvpcFNDTLVQATTSNKKVLKEALDMLEA 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 755522500  930 QGSTSVLAALTKAFSF--------QDVQG------LYLLTDGKPDT 961
Cdd:cd01463    92 KGIANYTKALEFAFSLllknlqsnHSGSRsqcnqaIMLITDGVPEN 137
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 417-540 2.02e-03

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: 40.07  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  417 VVILLDVSvtNSMYIIHIQ---HSLRLLLEeQLSNKDYFNIIAFgSTIESWRPEMVAVSHDNlQRAWRWAL-GLQCQGSR 492
Cdd:cd01466     3 LVAVLDVS--GSMAGDKLQlvkHALRFVIS-SLGDADRLSIVTF-STSAKRLSPLRRMTAKG-KRSAKRVVdGLQAGGGT 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 755522500  493 NVLGALRKAIEVDFKDKNKHESQGIYLFTGGIPDQDVHILSAYVAEAY 540
Cdd:cd01466    78 NVVGGLKKALKVLGDRRQKNPVASIMLLSDGQDNHGAVVLRADNAPIP 125
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 860-1009 4.19e-03

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: 38.91  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522500  860 LLDTSGSM-GPHLQWIKTELVLLIwEQLRKhCARFNLLSFAEDLQLWQdTLVESTEAACHKAMQWVAHLQAQGSTSVLAA 938
Cdd:cd01466     6 VLDVSGSMaGDKLQLVKHALRFVI-SSLGD-ADRLSIVTFSTSAKRLS-PLRRMTAKGKRSAKRVVDGLQAGGGTNVVGG 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755522500  939 LTKAFSFQD-------VQGLYLLTDGKPDtscsliLNTVQSFQKERGVKVHTISLTSADRTATefLRELASLSGGRYH 1009
Cdd:cd01466    83 LKKALKVLGdrrqknpVASIMLLSDGQDN------HGAVVLRADNAPIPIHTFGLGASHDPAL--LAFIAEITGGTFS 152
 
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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