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Conserved domains on  [gi|1720422301|ref|XP_030098369|]
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von Willebrand factor A domain-containing protein 3A isoform X1 [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 ...
 142-297 7.91e-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: 7.91e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  142 SRVGLLIDSSQVSSGSQtkEFQNDLTGLIDEQLSLKEKLYVLSFGVTINPLWPDPMEVSTSTLQELKLWVKTLQP-EGSS 220
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEP--KLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPpLGGS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  221 NLLQALKKVFAHKELN----SLVIILRSCPDQPSEFLSDFIQQSTLGrsvfIHVTTYKCDDHVPSAVLKNLTDALGGYYH 296
Cdd:pfam13768   79 DLLGALKEAVRAPASPgyirHVLLLTDGSPMQGETRVSDLISRAPGK----IRFFAYGLGASISAPMLQLLAEASNGTYE 154


                   .
gi 1720422301  297 C 297
Cdd:pfam13768  155 F 155
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 921-1074 1.50e-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: 1.50e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  921 LERNVCILLDTSGSM-GPHLQWIKtELVLLIWEQLRKHCaRFNLLSFAEDLQLWQDTLVESTEAACHKAMQWVAHLQAQG 999
Cdd:cd01461      1 LPKEVVFVIDTSGSMsGTKIEQTK-EALLTALKDLPPGD-YFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301 1000 STSVLAALTKAFSFQD-----VQGLYLLTDGKpDTSCSLILNTVQsFQKERGVKVHTISLTSADRTAteFLRELASLSGG 1074
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 ...
 483-623 1.79e-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: 1.79e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  483 RRVVILLDVSvtNSMY---IIHIQHSLRLLLEEqLSNKDYFNIIAFGSTIESWRPEMVAVSHDNLQRAWRWALGLQCQGS 559
Cdd:cd01461      3 KEVVFVIDTS--GSMSgtkIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGG 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720422301  560 RNVLGALRKAIEvdFKDKNKHESQGIYLFTGGIPDQDVHILSAyVAEAyggcdLQLNVCLFYVG 623
Cdd:cd01461     80 TNMNDALEAALE--LLNSSPGSVPQIILLTDGEVTNESQILKN-VREA-----LSGRIRLFTFG 135
 
Name Accession Description Interval E-value
VWA_3 pfam13768
von Willebrand factor type A domain;
142-297 7.91e-31

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 119.04  E-value: 7.91e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  142 SRVGLLIDSSQVSSGSQtkEFQNDLTGLIDEQLSLKEKLYVLSFGVTINPLWPDPMEVSTSTLQELKLWVKTLQP-EGSS 220
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEP--KLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPpLGGS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  221 NLLQALKKVFAHKELN----SLVIILRSCPDQPSEFLSDFIQQSTLGrsvfIHVTTYKCDDHVPSAVLKNLTDALGGYYH 296
Cdd:pfam13768   79 DLLGALKEAVRAPASPgyirHVLLLTDGSPMQGETRVSDLISRAPGK----IRFFAYGLGASISAPMLQLLAEASNGTYE 154


                   .
gi 1720422301  297 C 297
Cdd:pfam13768  155 F 155
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 921-1074 1.50e-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: 1.50e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  921 LERNVCILLDTSGSM-GPHLQWIKtELVLLIWEQLRKHCaRFNLLSFAEDLQLWQDTLVESTEAACHKAMQWVAHLQAQG 999
Cdd:cd01461      1 LPKEVVFVIDTSGSMsGTKIEQTK-EALLTALKDLPPGD-YFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301 1000 STSVLAALTKAFSFQD-----VQGLYLLTDGKpDTSCSLILNTVQsFQKERGVKVHTISLTSADRTAteFLRELASLSGG 1074
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- ...
 483-623 1.79e-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: 1.79e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  483 RRVVILLDVSvtNSMY---IIHIQHSLRLLLEEqLSNKDYFNIIAFGSTIESWRPEMVAVSHDNLQRAWRWALGLQCQGS 559
Cdd:cd01461      3 KEVVFVIDTS--GSMSgtkIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGG 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720422301  560 RNVLGALRKAIEvdFKDKNKHESQGIYLFTGGIPDQDVHILSAyVAEAyggcdLQLNVCLFYVG 623
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 ...
 907-1088 3.11e-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: 3.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  907 WLLSAGSRRLFGTILERNVCILLDTSGSMG--PHLQWIKTELVLLIwEQLRKHcARFNLLSFAEDLQLWQDtLVESTEAa 984
Cdd:COG1240     77 LALALAPLALARPQRGRDVVLVVDASGSMAaeNRLEAAKGALLDFL-DDYRPR-DRVGLVAFGGEAEVLLP-LTRDREA- 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  985 chkAMQWVAHLQAQGSTSVLAALTKAFS-FQDVQG-----LYLLTDGKPDTSCSLILNTVQSFqKERGVKVHTISlTSAD 1058
Cdd:COG1240    153 ---LKRALDELPPGGGTPLGDALALALElLKRADParrkvIVLLTDGRDNAGRIDPLEAAELA-AAAGIRIYTIG-VGTE 227

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1720422301 1059 RTATEFLRELASLSGGRYHcPVSD-KALSGI 1088
Cdd:COG1240    228 AVDEGLLREIAEATGGRYF-RADDlSELAAI 257
VWA_3 pfam13768
von Willebrand factor type A domain;
484-657 3.18e-14

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 71.27  E-value: 3.18e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  484 RVVILLDVSVTNSMYIIHIQHSLRLLLEeQLSNKDYFNIIAFGSTIESWRPEMVAVSHDNLQRAWRWALGLQ-CQGSRNV 562
Cdd:pfam13768    2 DVVIVVDVSSSMSGEPKLQKDALSVALR-QLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQpPLGGSDL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  563 LGALRKAIEVdfKDKNKHESQgIYLFTGGIPDQDVHILSAYVAeayggcDLQLNVCLFYVG-EPQMDTTPPacyasrtdt 641
Cdd:pfam13768   81 LGALKEAVRA--PASPGYIRH-VLLLTDGSPMQGETRVSDLIS------RAPGKIRFFAYGlGASISAPML--------- 142

                          170
                   ....*....|....*.
gi 1720422301  642 atayKEITQAARGRFH 657
Cdd:pfam13768  143 ----QLLAEASNGTYE 154
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 924-1077 1.72e-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: 1.72e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301   924 NVCILLDTSGSMGP-HLQWIKTELVLLIwEQLRKHC--ARFNLLSFAEDLQLWQDTLVESTEAACHKAMQwVAHLQAQGS 1000
Cdd:smart00327    1 DVVFLLDGSGSMGGnRFELAKEFVLKLV-EQLDIGPdgDRVGLVTFSDDARVLFPLNDSRSKDALLEALA-SLSYKLGGG 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  1001 TSVLAALTKAFS--FQDVQG--------LYLLTDGKPDTSCSLILNTVQsFQKERGVKVHTISLTSAdrTATEFLRELAS 1070
Cdd:smart00327   79 TNLGAALQYALEnlFSKSAGsrrgapkvVILITDGESNDGPKDLLKAAK-ELKRSGVKVFVVGVGND--VDEEELKKLAS 155


                    ....*..
gi 1720422301  1071 LSGGRYH 1077
Cdd:smart00327  156 APGGVYV 162
VWA_3 pfam13768
von Willebrand factor type A domain;
924-1078 3.54e-10

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 59.72  E-value: 3.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  924 NVCILLDTSGSMGPHLQWIKTELVLLIwEQLrKHCARFNLLSFAEDLQLWQDTLVESTEAACHKAMQWVAHLQAQ-GSTS 1002
Cdd:pfam13768    2 DVVIVVDVSSSMSGEPKLQKDALSVAL-RQL-PTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPlGGSD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301 1003 VLAALTKAF----SFQDVQGLYLLTDGKPDTSCSlilNTVQSFQKERGvKVHTISLTSADRTATEFLRELASLSGGRYHC 1078
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 ...
 920-1084 7.18e-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: 7.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  920 ILERNVCILLDTSGSMGPHLQWIK----TELVLLiweQLRKHCARFNLLSFAEDLQLwQDTLVESTEAACHKAMQWVAHL 995
Cdd:TIGR00868  302 IRQRIVCLVLDKSGSMTVEDRLKRmnqaAKLFLL---QTVEKGSWVGMVTFDSAAYI-KNELIQITSSAERDALTANLPT 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  996 QAQGSTSVLAALTKAF-----SFQDVQG--LYLLTDGKPDTSCSLILNTVQSfqkerGVKVHTISLtsaDRTATEFLREL 1068
Cdd:TIGR00868  378 AASGGTSICSGLKAAFqvikkSYQSTDGseIVLLTDGEDNTISSCFEEVKQS-----GAIIHTIAL---GPSAAKELEEL 449

                          170
                   ....*....|....*.
gi 1720422301 1069 ASLSGGrYHCPVSDKA 1084
Cdd:TIGR00868  450 SDMTGG-LRFYASDQA 464
 
Name Accession Description Interval E-value
VWA_3 pfam13768
von Willebrand factor type A domain;
142-297 7.91e-31

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 119.04  E-value: 7.91e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  142 SRVGLLIDSSQVSSGSQtkEFQNDLTGLIDEQLSLKEKLYVLSFGVTINPLWPDPMEVSTSTLQELKLWVKTLQP-EGSS 220
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEP--KLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPpLGGS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  221 NLLQALKKVFAHKELN----SLVIILRSCPDQPSEFLSDFIQQSTLGrsvfIHVTTYKCDDHVPSAVLKNLTDALGGYYH 296
Cdd:pfam13768   79 DLLGALKEAVRAPASPgyirHVLLLTDGSPMQGETRVSDLISRAPGK----IRFFAYGLGASISAPMLQLLAEASNGTYE 154


                   .
gi 1720422301  297 C 297
Cdd:pfam13768  155 F 155
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 921-1074 1.50e-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: 1.50e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  921 LERNVCILLDTSGSM-GPHLQWIKtELVLLIWEQLRKHCaRFNLLSFAEDLQLWQDTLVESTEAACHKAMQWVAHLQAQG 999
Cdd:cd01461      1 LPKEVVFVIDTSGSMsGTKIEQTK-EALLTALKDLPPGD-YFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301 1000 STSVLAALTKAFSFQD-----VQGLYLLTDGKpDTSCSLILNTVQsFQKERGVKVHTISLTSADRTAteFLRELASLSGG 1074
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- ...
 483-623 1.79e-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: 1.79e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  483 RRVVILLDVSvtNSMY---IIHIQHSLRLLLEEqLSNKDYFNIIAFGSTIESWRPEMVAVSHDNLQRAWRWALGLQCQGS 559
Cdd:cd01461      3 KEVVFVIDTS--GSMSgtkIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGG 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720422301  560 RNVLGALRKAIEvdFKDKNKHESQGIYLFTGGIPDQDVHILSAyVAEAyggcdLQLNVCLFYVG 623
Cdd:cd01461     80 TNMNDALEAALE--LLNSSPGSVPQIILLTDGEVTNESQILKN-VREA-----LSGRIRLFTFG 135
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 923-1074 5.88e-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: 5.88e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  923 RNVCILLDTSGSMGPHLQWIKTELVLLIWEQLRKHC--ARFNLLSFAEDLQLWQDTLVESTEAACHKAMQWVaHLQAQGS 1000
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPpgDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDAL-KKGLGGG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301 1001 TSVLAALTKAFSFQDVQG-------LYLLTDGKPDTSCSLILNTVQSFqKERGVKVHTISLtsADRTATEFLRELASLSG 1073
Cdd:cd00198     80 TNIGAALRLALELLKSAKrpnarrvIILLTDGEPNDGPELLAEAAREL-RKLGITVYTIGI--GDDANEDELKEIADKTT 156


                   .
gi 1720422301 1074 G 1074
Cdd:cd00198    157 G 157
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 907-1088 3.11e-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: 3.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  907 WLLSAGSRRLFGTILERNVCILLDTSGSMG--PHLQWIKTELVLLIwEQLRKHcARFNLLSFAEDLQLWQDtLVESTEAa 984
Cdd:COG1240     77 LALALAPLALARPQRGRDVVLVVDASGSMAaeNRLEAAKGALLDFL-DDYRPR-DRVGLVAFGGEAEVLLP-LTRDREA- 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  985 chkAMQWVAHLQAQGSTSVLAALTKAFS-FQDVQG-----LYLLTDGKPDTSCSLILNTVQSFqKERGVKVHTISlTSAD 1058
Cdd:COG1240    153 ---LKRALDELPPGGGTPLGDALALALElLKRADParrkvIVLLTDGRDNAGRIDPLEAAELA-AAAGIRIYTIG-VGTE 227

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1720422301 1059 RTATEFLRELASLSGGRYHcPVSD-KALSGI 1088
Cdd:COG1240    228 AVDEGLLREIAEATGGRYF-RADDlSELAAI 257
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 923-1077 1.88e-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: 1.88e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  923 RNVCILLDTSGSM-GPHLQWIKTELVLLIwEQLRKHcARFNLLSFAEDLQlwqdTLVESTEAA-CHKAMQWVAHLQAQGS 1000
Cdd:COG2304     92 LNLVFVIDVSGSMsGDKLELAKEAAKLLV-DQLRPG-DRVSIVTFAGDAR----VLLPPTPATdRAKILAAIDRLQAGGG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301 1001 TSVLAALTKAFS-FQDVQG------LYLLTDGKPD---TSCSLILNTVQSfQKERGVKVHTISL-TSADRtatEFLRELA 1069
Cdd:COG2304    166 TALGAGLELAYElARKHFIpgrvnrVILLTDGDANvgiTDPEELLKLAEE-AREEGITLTTLGVgSDYNE---DLLERLA 241


                   ....*...
gi 1720422301 1070 SLSGGRYH 1077
Cdd:COG2304    242 DAGGGNYY 249
VWA_3 pfam13768
von Willebrand factor type A domain;
484-657 3.18e-14

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 71.27  E-value: 3.18e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  484 RVVILLDVSVTNSMYIIHIQHSLRLLLEeQLSNKDYFNIIAFGSTIESWRPEMVAVSHDNLQRAWRWALGLQ-CQGSRNV 562
Cdd:pfam13768    2 DVVIVVDVSSSMSGEPKLQKDALSVALR-QLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQpPLGGSDL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  563 LGALRKAIEVdfKDKNKHESQgIYLFTGGIPDQDVHILSAYVAeayggcDLQLNVCLFYVG-EPQMDTTPPacyasrtdt 641
Cdd:pfam13768   81 LGALKEAVRA--PASPGYIRH-VLLLTDGSPMQGETRVSDLIS------RAPGKIRFFAYGlGASISAPML--------- 142

                          170
                   ....*....|....*.
gi 1720422301  642 atayKEITQAARGRFH 657
Cdd:pfam13768  143 ----QLLAEASNGTYE 154
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 483-627 3.60e-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: 3.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  483 RRVVILLDVSvtNSM---YIIHIQHSLRLLLE--EQLSNKDYFNIIAFGSTIESWRPEMVAVSHDNLQRAWRWaLGLQCQ 557
Cdd:cd00198      1 ADIVFLLDVS--GSMggeKLDKAKEALKALVSslSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDA-LKKGLG 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  558 GSRNVLGALRKAIEVDFKDKNKHESQGIYLFTGGIPDQDVHILSAYVAEAyggCDLQLNVCLFYVGEPQM 627
Cdd:cd00198     78 GGTNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAAREL---RKLGITVYTIGIGDDAN 144
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 907-1069 4.85e-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: 4.85e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  907 WLLSAGSRRLFGTILERNVCILLDTSGSM-GPHLQWIKTELVLLIwEQLRKHcARFNLLSFaeDLQLWQDTLVESTEAAc 985
Cdd:COG2425    103 LLLLAAPASAAVPLLEGPVVLCVDTSGSMaGSKEAAAKAAALALL-RALRPN-RRFGVILF--DTEVVEDLPLTADDGL- 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  986 HKAMQWVAHLQAQGSTSVLAALTKAFS-FQDVQG----LYLLTDGKPDTSCSLILNTVQsfQKERGVKVHTISLTSADrt 1060
Cdd:COG2425    178 EDAIEFLSGLFAGGGTDIAPALRAALElLEEPDYrnadIVLITDGEAGVSPEELLREVR--AKESGVRLFTVAIGDAG-- 253


                   ....*....
gi 1720422301 1061 ATEFLRELA 1069
Cdd:COG2425    254 NPGLLEALA 262
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 924-1077 1.72e-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: 1.72e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301   924 NVCILLDTSGSMGP-HLQWIKTELVLLIwEQLRKHC--ARFNLLSFAEDLQLWQDTLVESTEAACHKAMQwVAHLQAQGS 1000
Cdd:smart00327    1 DVVFLLDGSGSMGGnRFELAKEFVLKLV-EQLDIGPdgDRVGLVTFSDDARVLFPLNDSRSKDALLEALA-SLSYKLGGG 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  1001 TSVLAALTKAFS--FQDVQG--------LYLLTDGKPDTSCSLILNTVQsFQKERGVKVHTISLTSAdrTATEFLRELAS 1070
Cdd:smart00327   79 TNLGAALQYALEnlFSKSAGsrrgapkvVILITDGESNDGPKDLLKAAK-ELKRSGVKVFVVGVGND--VDEEELKKLAS 155


                    ....*..
gi 1720422301  1071 LSGGRYH 1077
Cdd:smart00327  156 APGGVYV 162
VWA_3 pfam13768
von Willebrand factor type A domain;
924-1078 3.54e-10

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 59.72  E-value: 3.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  924 NVCILLDTSGSMGPHLQWIKTELVLLIwEQLrKHCARFNLLSFAEDLQLWQDTLVESTEAACHKAMQWVAHLQAQ-GSTS 1002
Cdd:pfam13768    2 DVVIVVDVSSSMSGEPKLQKDALSVAL-RQL-PTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPlGGSD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301 1003 VLAALTKAF----SFQDVQGLYLLTDGKPDTSCSlilNTVQSFQKERGvKVHTISLTSADRTATEFLRELASLSGGRYHC 1078
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 ...
 924-1077 4.68e-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: 4.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  924 NVCILLDTSGSM-GPHLQWIKTELVLLIwEQLRKHcARFNLLSFAEDLQlwqdTLVEST----EAACHKAMQwvaHLQAQ 998
Cdd:cd01465      2 NLVFVIDRSGSMdGPKLPLVKSALKLLV-DQLRPD-DRLAIVTYDGAAE----TVLPATpvrdKAAILAAID---RLTAG 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  999 GSTSVLAAL-------TKAFSFQDVQGLYLLTDGKP---DTSCSLILNTVQSfQKERGVKVHTISLtsADRTATEFLREL 1068
Cdd:cd01465     73 GSTAGGAGIqlgyqeaQKHFVPGGVNRILLATDGDFnvgETDPDELARLVAQ-KRESGITLSTLGF--GDNYNEDLMEAI 149


                   ....*....
gi 1720422301 1069 ASLSGGRYH 1077
Cdd:cd01465    150 ADAGNGNTA 158
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
 920-1084 7.18e-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: 7.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  920 ILERNVCILLDTSGSMGPHLQWIK----TELVLLiweQLRKHCARFNLLSFAEDLQLwQDTLVESTEAACHKAMQWVAHL 995
Cdd:TIGR00868  302 IRQRIVCLVLDKSGSMTVEDRLKRmnqaAKLFLL---QTVEKGSWVGMVTFDSAAYI-KNELIQITSSAERDALTANLPT 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  996 QAQGSTSVLAALTKAF-----SFQDVQG--LYLLTDGKPDTSCSLILNTVQSfqkerGVKVHTISLtsaDRTATEFLREL 1068
Cdd:TIGR00868  378 AASGGTSICSGLKAAFqvikkSYQSTDGseIVLLTDGEDNTISSCFEEVKQS-----GAIIHTIAL---GPSAAKELEEL 449

                          170
                   ....*....|....*.
gi 1720422301 1069 ASLSGGrYHCPVSDKA 1084
Cdd:TIGR00868  450 SDMTGG-LRFYASDQA 464
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
913-1098 2.40e-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: 2.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  913 SRRLfgtilerNVCILLDTSGSM-GPHLQWIKTELVLLIwEQLRKHC-----ARFNLLSFAEDLQlwqdTLVESTEAAch 986
Cdd:COG4245      3 MRRL-------PVYLLLDTSGSMsGEPIEALNEGLQALI-DELRQDPyaletVEVSVITFDGEAK----VLLPLTDLE-- 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  987 kAMQWvAHLQAQGSTSVLAALTKAFS-FQDVQG-------------LYLLTDGKP-DTSCSLILNTVQSFQKERGVKVHT 1051
Cdd:COG4245     69 -DFQP-PDLSASGGTPLGAALELLLDlIERRVQkytaegkgdwrpvVFLITDGEPtDSDWEAALQRLKDGEAAKKANIFA 146

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1720422301 1052 ISL-TSADrtaTEFLRELASlsggryhcpvSDKALSGIQGLLTRGFIK 1098
Cdd:COG4245    147 IGVgPDAD---TEVLKQLTD----------PVRALDALDGLDFREFFK 181
VWA pfam00092
von Willebrand factor type A domain;
924-1076 4.93e-06

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 48.04  E-value: 4.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  924 NVCILLDTSGSMGPH-LQWIKTELVLLIwEQLR--KHCARFNLLSFAEDLQLWQDTLVESTEAachKAMQWVAHL--QAQ 998
Cdd:pfam00092    1 DIVFLLDGSGSIGGDnFEKVKEFLKKLV-ESLDigPDGTRVGLVQYSSDVRTEFPLNDYSSKE---ELLSAVDNLryLGG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  999 GSTSVLAALTKA--FSFQDVQG--------LYLLTDGKPDtsCSLILNTVQSFqKERGVKVHTISLTSADRTAtefLREL 1068
Cdd:pfam00092   77 GTTNTGKALKYAleNLFSSAAGarpgapkvVVLLTDGRSQ--DGDPEEVAREL-KSAGVTVFAVGVGNADDEE---LRKI 150


                   ....*...
gi 1720422301 1069 ASLSGGRY 1076
Cdd:pfam00092  151 ASEPGEGH 158
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 474-603 1.37e-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: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  474 RRIW---GTVCQRRVVILLDVSVTNSMYIIHI-QHSLRLLLEeQLSNKDYFNIIAFGSTIESWRP----EMVAVSHDNlQ 545
Cdd:cd01463      2 NRSWyiqAATSPKDIVILLDVSGSMTGQRLHLaKQTVSSILD-TLSDNDFFNIITFSNEVNPVVPcfndTLVQATTSN-K 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720422301  546 RAWRWALG-LQCQGSRNVLGALRKAIEV--DFKDKNKHES-----QGIYLFTGGIPDQDVHILSAY 603
Cdd:cd01463     80 KVLKEALDmLEAKGIANYTKALEFAFSLllKNLQSNHSGSrsqcnQAIMLITDGVPENYKEIFDKY 145
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 927-1078 1.73e-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: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  927 ILLDTSGSMGP-HLQWIKTELVLLIwEQLR--KHCARFNLLSFAEDLQLW----QDTLVESTEAAcHKAMQWVAHlqaqG 999
Cdd:cd01450      5 FLLDGSESVGPeNFEKVKDFIEKLV-EKLDigPDKTRVGLVQYSDDVRVEfslnDYKSKDDLLKA-VKNLKYLGG----G 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301 1000 STSVLAALTKAF--------SFQDVQG-LYLLTDGKPDTSCSLILNTVQsfQKERGVKVHTISLTSADRtatEFLRELAS 1070
Cdd:cd01450     79 GTNTGKALQYALeqlfsesnARENVPKvIIVLTDGRSDDGGDPKEAAAK--LKDEGIKVFVVGVGPADE---EELREIAS 153


                   ....*...
gi 1720422301 1071 lSGGRYHC 1078
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 ...
 925-1056 1.06e-03

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: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  925 VCILLDTSGSM-GPHLQWIKTELVLLIWeQLRKHCARFNLLSFAEDLQlwqdTLVESTEAACHKAMQWVAHLQAQGSTSV 1003
Cdd:cd01462      3 VILLVDQSGSMyGAPEEVAKAVALALLR-IALAENRDTYLILFDSEFQ----TKIVDKTDDLEEPVEFLSGVQLGGGTDI 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422301 1004 LAALTKAFSF---QDVQG--LYLLTDGKPDTSCSLILNTVqSFQKERGVKVHTISLTS 1056
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 ...
 923-1029 1.89e-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: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  923 RNVCILLDTSGSM-GPHLQWIKTElVLLIWEQLrKHCARFNLLSFAEDLQL----WQDTLVESTEAACHKAMQWVAHLQA 997
Cdd:cd01463     14 KDIVILLDVSGSMtGQRLHLAKQT-VSSILDTL-SDNDFFNIITFSNEVNPvvpcFNDTLVQATTSNKKVLKEALDMLEA 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1720422301  998 QGSTSVLAALTKAFSF--------QDVQG------LYLLTDGKPDT 1029
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 ...
 485-608 2.16e-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: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  485 VVILLDVSvtNSMYIIHIQ---HSLRLLLEeQLSNKDYFNIIAFgSTIESWRPEMVAVSHDNlQRAWRWAL-GLQCQGSR 560
Cdd:cd01466      3 LVAVLDVS--GSMAGDKLQlvkHALRFVIS-SLGDADRLSIVTF-STSAKRLSPLRRMTAKG-KRSAKRVVdGLQAGGGT 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1720422301  561 NVLGALRKAIEVDFKDKNKHESQGIYLFTGGIPDQDVHILSAYVAEAY 608
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 ...
 928-1077 4.47e-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: 38.91  E-value: 4.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422301  928 LLDTSGSM-GPHLQWIKTELVLLIwEQLRKhCARFNLLSFAEDLQLWQdTLVESTEAACHKAMQWVAHLQAQGSTSVLAA 1006
Cdd:cd01466      6 VLDVSGSMaGDKLQLVKHALRFVI-SSLGD-ADRLSIVTFSTSAKRLS-PLRRMTAKGKRSAKRVVDGLQAGGGTNVVGG 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422301 1007 LTKAFSFQD-------VQGLYLLTDGKPDtscsliLNTVQSFQKERGVKVHTISLTSADRTATefLRELASLSGGRYH 1077
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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