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Conserved domains on  [gi|1720422311|ref|XP_030098373|]
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von Willebrand factor A domain-containing protein 3A isoform X4 [Mus musculus]

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 ...
 580-733 1.01e-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: 1.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 580 LERNVCILLDTSGSM-GPHLQWIKtELVLLIWEQLRKHCaRFNLLSFAEDLQLWQDTLVESTEAACHKAMQWVAHLQAQG 658
Cdd:cd01461     1 LPKEVVFVIDTSGSMsGTKIEQTK-EALLTALKDLPPGD-YFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 659 STSVLAALTKAFSFQD-----VQGLYLLTDGKpDTSCSLILNTVQsFQKERGVKVHTISLTSADRTAteFLRELASLSGG 733
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 ...
 142-282 1.20e-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: 1.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 142 RRVVILLDVSvtNSMY---IIHIQHSLRLLLEEqLSNKDYFNIIAFGSTIESWRPEMVAVSHDNLQRAWRWALGLQCQGS 218
Cdd:cd01461     3 KEVVFVIDTS--GSMSgtkIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720422311 219 RNVLGALRKAIEvdFKDKNKHESQGIYLFTGGIPDQDVHILSAyVAEAyggcdLQLNVCLFYVG 282
Cdd:cd01461    80 TNMNDALEAALE--LLNSSPGSVPQIILLTDGEVTNESQILKN-VREA-----LSGRIRLFTFG 135
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 580-733 1.01e-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: 1.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 580 LERNVCILLDTSGSM-GPHLQWIKtELVLLIWEQLRKHCaRFNLLSFAEDLQLWQDTLVESTEAACHKAMQWVAHLQAQG 658
Cdd:cd01461     1 LPKEVVFVIDTSGSMsGTKIEQTK-EALLTALKDLPPGD-YFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 659 STSVLAALTKAFSFQD-----VQGLYLLTDGKpDTSCSLILNTVQsFQKERGVKVHTISLTSADRTAteFLRELASLSGG 733
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- ...
 142-282 1.20e-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: 1.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 142 RRVVILLDVSvtNSMY---IIHIQHSLRLLLEEqLSNKDYFNIIAFGSTIESWRPEMVAVSHDNLQRAWRWALGLQCQGS 218
Cdd:cd01461     3 KEVVFVIDTS--GSMSgtkIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720422311 219 RNVLGALRKAIEvdFKDKNKHESQGIYLFTGGIPDQDVHILSAyVAEAyggcdLQLNVCLFYVG 282
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 ...
 566-747 2.02e-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: 2.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 566 WLLSAGSRRLFGTILERNVCILLDTSGSMG--PHLQWIKTELVLLIwEQLRKHcARFNLLSFAEDLQLWQDtLVESTEAa 643
Cdd:COG1240    77 LALALAPLALARPQRGRDVVLVVDASGSMAaeNRLEAAKGALLDFL-DDYRPR-DRVGLVAFGGEAEVLLP-LTRDREA- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 644 chkAMQWVAHLQAQGSTSVLAALTKAFS-FQDVQG-----LYLLTDGKPDTSCSLILNTVQSFqKERGVKVHTISlTSAD 717
Cdd:COG1240   153 ---LKRALDELPPGGGTPLGDALALALElLKRADParrkvIVLLTDGRDNAGRIDPLEAAELA-AAAGIRIYTIG-VGTE 227

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1720422311 718 RTATEFLRELASLSGGRYHcPVSD-KALSGI 747
Cdd:COG1240   228 AVDEGLLREIAEATGGRYF-RADDlSELAAI 257
VWA_3 pfam13768
von Willebrand factor type A domain;
143-316 2.15e-14

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 71.27  E-value: 2.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 143 RVVILLDVSVTNSMYIIHIQHSLRLLLEeQLSNKDYFNIIAFGSTIESWRPEMVAVSHDNLQRAWRWALGLQ-CQGSRNV 221
Cdd:pfam13768   2 DVVIVVDVSSSMSGEPKLQKDALSVALR-QLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQpPLGGSDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 222 LGALRKAIEVdfKDKNKHESQgIYLFTGGIPDQDVHILSAYVAeayggcDLQLNVCLFYVG-EPQMDTTPPacyasrtdt 300
Cdd:pfam13768  81 LGALKEAVRA--PASPGYIRH-VLLLTDGSPMQGETRVSDLIS------RAPGKIRFFAYGlGASISAPML--------- 142

                         170
                  ....*....|....*.
gi 1720422311 301 atayKEITQAARGRFH 316
Cdd:pfam13768 143 ----QLLAEASNGTYE 154
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 583-736 1.15e-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: 1.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311  583 NVCILLDTSGSMGP-HLQWIKTELVLLIwEQLRKHC--ARFNLLSFAEDLQLWQDTLVESTEAACHKAMQwVAHLQAQGS 659
Cdd:smart00327   1 DVVFLLDGSGSMGGnRFELAKEFVLKLV-EQLDIGPdgDRVGLVTFSDDARVLFPLNDSRSKDALLEALA-SLSYKLGGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311  660 TSVLAALTKAFS--FQDVQG--------LYLLTDGKPDTSCSLILNTVQsFQKERGVKVHTISLTSAdrTATEFLRELAS 729
Cdd:smart00327  79 TNLGAALQYALEnlFSKSAGsrrgapkvVILITDGESNDGPKDLLKAAK-ELKRSGVKVFVVGVGND--VDEEELKKLAS 155


                   ....*..
gi 1720422311  730 LSGGRYH 736
Cdd:smart00327 156 APGGVYV 162
VWA_3 pfam13768
von Willebrand factor type A domain;
583-737 2.40e-10

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 59.72  E-value: 2.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 583 NVCILLDTSGSMGPHLQWIKTELVLLIwEQLrKHCARFNLLSFAEDLQLWQDTLVESTEAACHKAMQWVAHLQAQ-GSTS 661
Cdd:pfam13768   2 DVVIVVDVSSSMSGEPKLQKDALSVAL-RQL-PTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPlGGSD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 662 VLAALTKAF----SFQDVQGLYLLTDGKPDTSCSlilNTVQSFQKERGvKVHTISLTSADRTATEFLRELASLSGGRYHC 737
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 ...
 579-743 4.57e-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: 4.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 579 ILERNVCILLDTSGSMGPHLQWIK----TELVLLiweQLRKHCARFNLLSFAEDLQLwQDTLVESTEAACHKAMQWVAHL 654
Cdd:TIGR00868 302 IRQRIVCLVLDKSGSMTVEDRLKRmnqaAKLFLL---QTVEKGSWVGMVTFDSAAYI-KNELIQITSSAERDALTANLPT 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 655 QAQGSTSVLAALTKAF-----SFQDVQG--LYLLTDGKPDTSCSLILNTVQSfqkerGVKVHTISLtsaDRTATEFLREL 727
Cdd:TIGR00868 378 AASGGTSICSGLKAAFqvikkSYQSTDGseIVLLTDGEDNTISSCFEEVKQS-----GAIIHTIAL---GPSAAKELEEL 449

                         170
                  ....*....|....*.
gi 1720422311 728 ASLSGGrYHCPVSDKA 743
Cdd:TIGR00868 450 SDMTGG-LRFYASDQA 464
 
Name Accession Description Interval E-value
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 580-733 1.01e-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: 1.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 580 LERNVCILLDTSGSM-GPHLQWIKtELVLLIWEQLRKHCaRFNLLSFAEDLQLWQDTLVESTEAACHKAMQWVAHLQAQG 658
Cdd:cd01461     1 LPKEVVFVIDTSGSMsGTKIEQTK-EALLTALKDLPPGD-YFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 659 STSVLAALTKAFSFQD-----VQGLYLLTDGKpDTSCSLILNTVQsFQKERGVKVHTISLTSADRTAteFLRELASLSGG 733
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- ...
 142-282 1.20e-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: 1.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 142 RRVVILLDVSvtNSMY---IIHIQHSLRLLLEEqLSNKDYFNIIAFGSTIESWRPEMVAVSHDNLQRAWRWALGLQCQGS 218
Cdd:cd01461     3 KEVVFVIDTS--GSMSgtkIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720422311 219 RNVLGALRKAIEvdFKDKNKHESQGIYLFTGGIPDQDVHILSAyVAEAyggcdLQLNVCLFYVG 282
Cdd:cd01461    80 TNMNDALEAALE--LLNSSPGSVPQIILLTDGEVTNESQILKN-VREA-----LSGRIRLFTFG 135
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 582-733 3.97e-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: 3.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 582 RNVCILLDTSGSMGPHLQWIKTELVLLIWEQLRKHC--ARFNLLSFAEDLQLWQDTLVESTEAACHKAMQWVaHLQAQGS 659
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPpgDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDAL-KKGLGGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 660 TSVLAALTKAFSFQDVQG-------LYLLTDGKPDTSCSLILNTVQSFqKERGVKVHTISLtsADRTATEFLRELASLSG 732
Cdd:cd00198    80 TNIGAALRLALELLKSAKrpnarrvIILLTDGEPNDGPELLAEAAREL-RKLGITVYTIGI--GDDANEDELKEIADKTT 156


                  .
gi 1720422311 733 G 733
Cdd:cd00198   157 G 157
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 566-747 2.02e-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: 2.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 566 WLLSAGSRRLFGTILERNVCILLDTSGSMG--PHLQWIKTELVLLIwEQLRKHcARFNLLSFAEDLQLWQDtLVESTEAa 643
Cdd:COG1240    77 LALALAPLALARPQRGRDVVLVVDASGSMAaeNRLEAAKGALLDFL-DDYRPR-DRVGLVAFGGEAEVLLP-LTRDREA- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 644 chkAMQWVAHLQAQGSTSVLAALTKAFS-FQDVQG-----LYLLTDGKPDTSCSLILNTVQSFqKERGVKVHTISlTSAD 717
Cdd:COG1240   153 ---LKRALDELPPGGGTPLGDALALALElLKRADParrkvIVLLTDGRDNAGRIDPLEAAELA-AAAGIRIYTIG-VGTE 227

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1720422311 718 RTATEFLRELASLSGGRYHcPVSD-KALSGI 747
Cdd:COG1240   228 AVDEGLLREIAEATGGRYF-RADDlSELAAI 257
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 582-736 1.21e-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: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 582 RNVCILLDTSGSM-GPHLQWIKTELVLLIwEQLRKHcARFNLLSFAEDLQlwqdTLVESTEAA-CHKAMQWVAHLQAQGS 659
Cdd:COG2304    92 LNLVFVIDVSGSMsGDKLELAKEAAKLLV-DQLRPG-DRVSIVTFAGDAR----VLLPPTPATdRAKILAAIDRLQAGGG 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 660 TSVLAALTKAFS-FQDVQG------LYLLTDGKPD---TSCSLILNTVQSfQKERGVKVHTISL-TSADRtatEFLRELA 728
Cdd:COG2304   166 TALGAGLELAYElARKHFIpgrvnrVILLTDGDANvgiTDPEELLKLAEE-AREEGITLTTLGVgSDYNE---DLLERLA 241


                  ....*...
gi 1720422311 729 SLSGGRYH 736
Cdd:COG2304   242 DAGGGNYY 249
VWA_3 pfam13768
von Willebrand factor type A domain;
143-316 2.15e-14

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 71.27  E-value: 2.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 143 RVVILLDVSVTNSMYIIHIQHSLRLLLEeQLSNKDYFNIIAFGSTIESWRPEMVAVSHDNLQRAWRWALGLQ-CQGSRNV 221
Cdd:pfam13768   2 DVVIVVDVSSSMSGEPKLQKDALSVALR-QLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQpPLGGSDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 222 LGALRKAIEVdfKDKNKHESQgIYLFTGGIPDQDVHILSAYVAeayggcDLQLNVCLFYVG-EPQMDTTPPacyasrtdt 300
Cdd:pfam13768  81 LGALKEAVRA--PASPGYIRH-VLLLTDGSPMQGETRVSDLIS------RAPGKIRFFAYGlGASISAPML--------- 142

                         170
                  ....*....|....*.
gi 1720422311 301 atayKEITQAARGRFH 316
Cdd:pfam13768 143 ----QLLAEASNGTYE 154
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 142-286 2.43e-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: 2.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 142 RRVVILLDVSvtNSM---YIIHIQHSLRLLLE--EQLSNKDYFNIIAFGSTIESWRPEMVAVSHDNLQRAWRWaLGLQCQ 216
Cdd:cd00198     1 ADIVFLLDVS--GSMggeKLDKAKEALKALVSslSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDA-LKKGLG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 217 GSRNVLGALRKAIEVDFKDKNKHESQGIYLFTGGIPDQDVHILSAYVAEAyggCDLQLNVCLFYVGEPQM 286
Cdd:cd00198    78 GGTNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAAREL---RKLGITVYTIGIGDDAN 144
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 566-728 3.15e-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: 3.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 566 WLLSAGSRRLFGTILERNVCILLDTSGSM-GPHLQWIKTELVLLIwEQLRKHcARFNLLSFaeDLQLWQDTLVESTEAAc 644
Cdd:COG2425   103 LLLLAAPASAAVPLLEGPVVLCVDTSGSMaGSKEAAAKAAALALL-RALRPN-RRFGVILF--DTEVVEDLPLTADDGL- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 645 HKAMQWVAHLQAQGSTSVLAALTKAFS-FQDVQG----LYLLTDGKPDTSCSLILNTVQsfQKERGVKVHTISLTSADrt 719
Cdd:COG2425   178 EDAIEFLSGLFAGGGTDIAPALRAALElLEEPDYrnadIVLITDGEAGVSPEELLREVR--AKESGVRLFTVAIGDAG-- 253


                  ....*....
gi 1720422311 720 ATEFLRELA 728
Cdd:COG2425   254 NPGLLEALA 262
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 583-736 1.15e-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: 1.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311  583 NVCILLDTSGSMGP-HLQWIKTELVLLIwEQLRKHC--ARFNLLSFAEDLQLWQDTLVESTEAACHKAMQwVAHLQAQGS 659
Cdd:smart00327   1 DVVFLLDGSGSMGGnRFELAKEFVLKLV-EQLDIGPdgDRVGLVTFSDDARVLFPLNDSRSKDALLEALA-SLSYKLGGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311  660 TSVLAALTKAFS--FQDVQG--------LYLLTDGKPDTSCSLILNTVQsFQKERGVKVHTISLTSAdrTATEFLRELAS 729
Cdd:smart00327  79 TNLGAALQYALEnlFSKSAGsrrgapkvVILITDGESNDGPKDLLKAAK-ELKRSGVKVFVVGVGND--VDEEELKKLAS 155


                   ....*..
gi 1720422311  730 LSGGRYH 736
Cdd:smart00327 156 APGGVYV 162
VWA_3 pfam13768
von Willebrand factor type A domain;
583-737 2.40e-10

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 59.72  E-value: 2.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 583 NVCILLDTSGSMGPHLQWIKTELVLLIwEQLrKHCARFNLLSFAEDLQLWQDTLVESTEAACHKAMQWVAHLQAQ-GSTS 661
Cdd:pfam13768   2 DVVIVVDVSSSMSGEPKLQKDALSVAL-RQL-PTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPlGGSD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 662 VLAALTKAF----SFQDVQGLYLLTDGKPDTSCSlilNTVQSFQKERGvKVHTISLTSADRTATEFLRELASLSGGRYHC 737
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 ...
 583-736 3.16e-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: 3.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 583 NVCILLDTSGSM-GPHLQWIKTELVLLIwEQLRKHcARFNLLSFAEDLQlwqdTLVEST----EAACHKAMQwvaHLQAQ 657
Cdd:cd01465     2 NLVFVIDRSGSMdGPKLPLVKSALKLLV-DQLRPD-DRLAIVTYDGAAE----TVLPATpvrdKAAILAAID---RLTAG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 658 GSTSVLAAL-------TKAFSFQDVQGLYLLTDGKP---DTSCSLILNTVQSfQKERGVKVHTISLtsADRTATEFLREL 727
Cdd:cd01465    73 GSTAGGAGIqlgyqeaQKHFVPGGVNRILLATDGDFnvgETDPDELARLVAQ-KRESGITLSTLGF--GDNYNEDLMEAI 149


                  ....*....
gi 1720422311 728 ASLSGGRYH 736
Cdd:cd01465   150 ADAGNGNTA 158
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
 579-743 4.57e-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: 4.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 579 ILERNVCILLDTSGSMGPHLQWIK----TELVLLiweQLRKHCARFNLLSFAEDLQLwQDTLVESTEAACHKAMQWVAHL 654
Cdd:TIGR00868 302 IRQRIVCLVLDKSGSMTVEDRLKRmnqaAKLFLL---QTVEKGSWVGMVTFDSAAYI-KNELIQITSSAERDALTANLPT 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 655 QAQGSTSVLAALTKAF-----SFQDVQG--LYLLTDGKPDTSCSLILNTVQSfqkerGVKVHTISLtsaDRTATEFLREL 727
Cdd:TIGR00868 378 AASGGTSICSGLKAAFqvikkSYQSTDGseIVLLTDGEDNTISSCFEEVKQS-----GAIIHTIAL---GPSAAKELEEL 449

                         170
                  ....*....|....*.
gi 1720422311 728 ASLSGGrYHCPVSDKA 743
Cdd:TIGR00868 450 SDMTGG-LRFYASDQA 464
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
572-757 1.61e-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: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 572 SRRLfgtilerNVCILLDTSGSM-GPHLQWIKTELVLLIwEQLRKHC-----ARFNLLSFAEDLQlwqdTLVESTEAAch 645
Cdd:COG4245     3 MRRL-------PVYLLLDTSGSMsGEPIEALNEGLQALI-DELRQDPyaletVEVSVITFDGEAK----VLLPLTDLE-- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 646 kAMQWvAHLQAQGSTSVLAALTKAFS-FQDVQG-------------LYLLTDGKP-DTSCSLILNTVQSFQKERGVKVHT 710
Cdd:COG4245    69 -DFQP-PDLSASGGTPLGAALELLLDlIERRVQkytaegkgdwrpvVFLITDGEPtDSDWEAALQRLKDGEAAKKANIFA 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1720422311 711 ISL-TSADrtaTEFLRELASlsggryhcpvSDKALSGIQGLLTRGFIK 757
Cdd:COG4245   147 IGVgPDAD---TEVLKQLTD----------PVRALDALDGLDFREFFK 181
VWA pfam00092
von Willebrand factor type A domain;
583-735 3.33e-06

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 48.04  E-value: 3.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 583 NVCILLDTSGSMGPH-LQWIKTELVLLIwEQLR--KHCARFNLLSFAEDLQLWQDTLVESTEAachKAMQWVAHL--QAQ 657
Cdd:pfam00092   1 DIVFLLDGSGSIGGDnFEKVKEFLKKLV-ESLDigPDGTRVGLVQYSSDVRTEFPLNDYSSKE---ELLSAVDNLryLGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 658 GSTSVLAALTKA--FSFQDVQG--------LYLLTDGKPDtsCSLILNTVQSFqKERGVKVHTISLTSADRTAtefLREL 727
Cdd:pfam00092  77 GTTNTGKALKYAleNLFSSAAGarpgapkvVVLLTDGRSQ--DGDPEEVAREL-KSAGVTVFAVGVGNADDEE---LRKI 150


                  ....*...
gi 1720422311 728 ASLSGGRY 735
Cdd:pfam00092 151 ASEPGEGH 158
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 133-262 9.22e-06

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: 9.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 133 RRIW---GTVCQRRVVILLDVSVTNSMYIIHI-QHSLRLLLEeQLSNKDYFNIIAFGSTIESWRP----EMVAVSHDNlQ 204
Cdd:cd01463     2 NRSWyiqAATSPKDIVILLDVSGSMTGQRLHLaKQTVSSILD-TLSDNDFFNIITFSNEVNPVVPcfndTLVQATTSN-K 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720422311 205 RAWRWALG-LQCQGSRNVLGALRKAIEV--DFKDKNKHES-----QGIYLFTGGIPDQDVHILSAY 262
Cdd:cd01463    80 KVLKEALDmLEAKGIANYTKALEFAFSLllKNLQSNHSGSrsqcnQAIMLITDGVPENYKEIFDKY 145
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 586-737 1.17e-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: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 586 ILLDTSGSMGP-HLQWIKTELVLLIwEQLR--KHCARFNLLSFAEDLQLW----QDTLVESTEAAcHKAMQWVAHlqaqG 658
Cdd:cd01450     5 FLLDGSESVGPeNFEKVKDFIEKLV-EKLDigPDKTRVGLVQYSDDVRVEfslnDYKSKDDLLKA-VKNLKYLGG----G 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 659 STSVLAALTKAF--------SFQDVQG-LYLLTDGKPDTSCSLILNTVQsfQKERGVKVHTISLTSADRtatEFLRELAS 729
Cdd:cd01450    79 GTNTGKALQYALeqlfsesnARENVPKvIIVLTDGRSDDGGDPKEAAAK--LKDEGIKVFVVGVGPADE---EELREIAS 153


                  ....*...
gi 1720422311 730 lSGGRYHC 737
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 ...
 584-715 7.24e-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: 7.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 584 VCILLDTSGSM-GPHLQWIKTELVLLIWeQLRKHCARFNLLSFAEDLQlwqdTLVESTEAACHKAMQWVAHLQAQGSTSV 662
Cdd:cd01462     3 VILLVDQSGSMyGAPEEVAKAVALALLR-IALAENRDTYLILFDSEFQ----TKIVDKTDDLEEPVEFLSGVQLGGGTDI 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422311 663 LAALTKAFSF---QDVQG--LYLLTDGKPDTSCSLILNTVqSFQKERGVKVHTISLTS 715
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 ...
 582-688 1.27e-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: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 582 RNVCILLDTSGSM-GPHLQWIKTElVLLIWEQLrKHCARFNLLSFAEDLQL----WQDTLVESTEAACHKAMQWVAHLQA 656
Cdd:cd01463    14 KDIVILLDVSGSMtGQRLHLAKQT-VSSILDTL-SDNDFFNIITFSNEVNPvvpcFNDTLVQATTSNKKVLKEALDMLEA 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720422311 657 QGSTSVLAALTKAFSF--------QDVQG------LYLLTDGKPDT 688
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 ...
 144-267 1.47e-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: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 144 VVILLDVSvtNSMYIIHIQ---HSLRLLLEeQLSNKDYFNIIAFgSTIESWRPEMVAVSHDNlQRAWRWAL-GLQCQGSR 219
Cdd:cd01466     3 LVAVLDVS--GSMAGDKLQlvkHALRFVIS-SLGDADRLSIVTF-STSAKRLSPLRRMTAKG-KRSAKRVVdGLQAGGGT 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1720422311 220 NVLGALRKAIEVDFKDKNKHESQGIYLFTGGIPDQDVHILSAYVAEAY 267
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 ...
 587-736 3.04e-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: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422311 587 LLDTSGSM-GPHLQWIKTELVLLIwEQLRKhCARFNLLSFAEDLQLWQdTLVESTEAACHKAMQWVAHLQAQGSTSVLAA 665
Cdd:cd01466     6 VLDVSGSMaGDKLQLVKHALRFVI-SSLGD-ADRLSIVTFSTSAKRLS-PLRRMTAKGKRSAKRVVDGLQAGGGTNVVGG 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422311 666 LTKAFSFQD-------VQGLYLLTDGKPDtscsliLNTVQSFQKERGVKVHTISLTSADRTATefLRELASLSGGRYH 736
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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