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Conserved domains on  [gi|568924609|ref|XP_006502409|]
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chloride channel calcium activated 3A2 isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
hCaCC super family cl31034
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
15-579 0e+00

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]


The actual alignment was detected with superfamily member TIGR00868:

Pssm-ID: 129946 [Multi-domain]  Cd Length: 863  Bit Score: 1079.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609   15 MVPGLQVLLFLTLHLLQNTESSMVHLNSNGYEGVVIAINPSVPEDERLIPSIKEMVTQASTYLFEASQGRVYFRNISILV 94
Cdd:TIGR00868   1 MGPFRSVLFFLVLHLLEGAQSSMIQLNNNGYEGIVIAIDPSVPEDERLIQNIKDMVTKASTYLFEATEKRFYFKNVSILI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609   95 PMTWKSKSEYLMPKRESYDKADVIVADPHLQHGDDPYTLQYGQCGDRGQYIHFTPNFLLTDNLRIYGPRGRVFVHEWAHL 174
Cdd:TIGR00868  81 PMTWKSKPEYLMPKLESYKNADVIVAEPNLPHGDDPYTLQYGNCGEKGEYIHFTPDFLLGKKLLIYGPRGRVFVHEWAHL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  175 RWGVFDEYNVDRPFYISRKNTIEATRCSASITGKKVVHECQRGSCVTRACRRDSKTRLYEPKCTFIPDKIQTAGASIMFM 254
Cdd:TIGR00868 161 RWGVFDEYNNDQPFYLSRNKKIEATRCSAAITGTNVVPKCQGGSCVTRPCRRDSVTGLYEKKCTFIPDKQQTEKASIMFM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  255 QNLNSVVEFCTENNHNAEAPNLQNKMCNRRSTWDVIKASADFQNSPPMRGTeaPPPPTFSLLKSRRRVVCLVLDKSGSMD 334
Cdd:TIGR00868 241 QSIDSVVEFCTEKNHNKEAPNLQNKKCNLRSTWEVIQNSEDFKNTTPMTTQ--PPPPTFSLLKIRQRIVCLVLDKSGSMT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  335 KEDRLIRMNQAAELYLTQIVEKESMVGLVTFDSAAHIQNYLIKITSSSDYQKITANLPQQATGGTSICHGLQAGFQAITS 414
Cdd:TIGR00868 319 VEDRLKRMNQAAKLFLLQTVEKGSWVGMVTFDSAAYIKNELIQITSSAERDALTANLPTAASGGTSICSGLKAAFQVIKK 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  415 SDQSTSGSEIVLLTDGEDNGISSCFEAVSRSGAIIHTIALGPSAARELETLSDMTGGLRFYAN--KHVSSLIDAFSRISS 492
Cdd:TIGR00868 399 SYQSTDGSEIVLLTDGEDNTISSCFEEVKQSGAIIHTIALGPSAAKELEELSDMTGGLRFYASdqADNNGLIDAFGALSS 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  493 TSGSVSQQALQLESKAFNVRAGAWINSTVPVDSTVGNDTFFVITWTVQKPEIILQDPKGKKyiTSDFQDDELNiRSARLQ 572
Cdd:TIGR00868 479 GNGSASQQSIQLESKGLTLQNNAWMNGTVPVDSTVGKDTFFLITWEFLKPEIFLQDPSGKS--TSDFLVDKLN-KMAYLQ 555

                  ....*..
gi 568924609  573 IPGTAEV 579
Cdd:TIGR00868 556 IPGTAKV 562
 
Name Accession Description Interval E-value
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
15-579 0e+00

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: 1079.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609   15 MVPGLQVLLFLTLHLLQNTESSMVHLNSNGYEGVVIAINPSVPEDERLIPSIKEMVTQASTYLFEASQGRVYFRNISILV 94
Cdd:TIGR00868   1 MGPFRSVLFFLVLHLLEGAQSSMIQLNNNGYEGIVIAIDPSVPEDERLIQNIKDMVTKASTYLFEATEKRFYFKNVSILI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609   95 PMTWKSKSEYLMPKRESYDKADVIVADPHLQHGDDPYTLQYGQCGDRGQYIHFTPNFLLTDNLRIYGPRGRVFVHEWAHL 174
Cdd:TIGR00868  81 PMTWKSKPEYLMPKLESYKNADVIVAEPNLPHGDDPYTLQYGNCGEKGEYIHFTPDFLLGKKLLIYGPRGRVFVHEWAHL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  175 RWGVFDEYNVDRPFYISRKNTIEATRCSASITGKKVVHECQRGSCVTRACRRDSKTRLYEPKCTFIPDKIQTAGASIMFM 254
Cdd:TIGR00868 161 RWGVFDEYNNDQPFYLSRNKKIEATRCSAAITGTNVVPKCQGGSCVTRPCRRDSVTGLYEKKCTFIPDKQQTEKASIMFM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  255 QNLNSVVEFCTENNHNAEAPNLQNKMCNRRSTWDVIKASADFQNSPPMRGTeaPPPPTFSLLKSRRRVVCLVLDKSGSMD 334
Cdd:TIGR00868 241 QSIDSVVEFCTEKNHNKEAPNLQNKKCNLRSTWEVIQNSEDFKNTTPMTTQ--PPPPTFSLLKIRQRIVCLVLDKSGSMT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  335 KEDRLIRMNQAAELYLTQIVEKESMVGLVTFDSAAHIQNYLIKITSSSDYQKITANLPQQATGGTSICHGLQAGFQAITS 414
Cdd:TIGR00868 319 VEDRLKRMNQAAKLFLLQTVEKGSWVGMVTFDSAAYIKNELIQITSSAERDALTANLPTAASGGTSICSGLKAAFQVIKK 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  415 SDQSTSGSEIVLLTDGEDNGISSCFEAVSRSGAIIHTIALGPSAARELETLSDMTGGLRFYAN--KHVSSLIDAFSRISS 492
Cdd:TIGR00868 399 SYQSTDGSEIVLLTDGEDNTISSCFEEVKQSGAIIHTIALGPSAAKELEELSDMTGGLRFYASdqADNNGLIDAFGALSS 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  493 TSGSVSQQALQLESKAFNVRAGAWINSTVPVDSTVGNDTFFVITWTVQKPEIILQDPKGKKyiTSDFQDDELNiRSARLQ 572
Cdd:TIGR00868 479 GNGSASQQSIQLESKGLTLQNNAWMNGTVPVDSTVGKDTFFLITWEFLKPEIFLQDPSGKS--TSDFLVDKLN-KMAYLQ 555

                  ....*..
gi 568924609  573 IPGTAEV 579
Cdd:TIGR00868 556 IPGTAKV 562
CLCA pfam08434
Calcium-activated chloride channel N terminal; The CLCA family of calcium-activated chloride ...
38-302 0e+00

Calcium-activated chloride channel N terminal; The CLCA family of calcium-activated chloride channels has been identified in many epithelial and endothelial cell types as well as in smooth muscle cells and has four or five putative transmembrane regions. Additionally to their role as chloride channels some CLCA proteins function as adhesion molecules and may also have roles as tumour suppressors. This protein cleaves itself into an N-terminal portion and a C-terminal portion. The N-terminus contains an HEXXHXXXGXXDE motif which is essential for proteolytic cleavage.


Pssm-ID: 462476  Cd Length: 266  Bit Score: 548.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609   38 VHLNSNGYEGVVIAINPSVPEDERLIPSIKEMVTQASTYLFEASQGRVYFRNISILVPMTWKSKSEYLMPKRESYDKADV 117
Cdd:pfam08434   1 IKLNNNGYEGIVIAIDPGVPEDEKLIQQIKDMVTEASTYLFEATEKRFYFKNVSILIPETWKSKPEYKRPKHESYKNADV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  118 IVADPHLQHGDDPYTLQYGQCGDRGQYIHFTPNFLLTDNLRIYGPRGRVFVHEWAHLRWGVFDEYNVDRPFYISRKNTIE 197
Cdd:pfam08434  81 IVAPPTLPGGDDPYTLQYGGCGEKGEYIHFTPDFLLGKKLNEYGPRGRVFVHEWAHLRWGVFDEYNEDQPFYSSKSKKIE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  198 ATRCSASITGKKVVHECQRGSCVTRACRRDSKTRLYEPKCTFIPDKIQTAGASIMFMQNLNSVVEFCTENNHNAEAPNLQ 277
Cdd:pfam08434 161 ATRCSAGITGKNRVYKCQGGSCITRKCRIDSQTGLYEKGCQFIPDKVQTEKASIMFMQSIDSVVEFCNKKNHNQEAPNLQ 240
                         250       260
                  ....*....|....*....|....*
gi 568924609  278 NKMCNRRSTWDVIKASADFQNSPPM 302
Cdd:pfam08434 241 NKMCNYRSTWEVISNSEDFKNTTPM 265
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
321-475 9.16e-26

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: 103.80  E-value: 9.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 321 RVVCLVLDKSGSMdKEDRLIRMNQAAELYLTQIVEK--ESMVGLVTFDSAAHIQNYLIKITSSSDYQKITANLPQQATGG 398
Cdd:cd00198    1 ADIVFLLDVSGSM-GGEKLDKAKEALKALVSSLSASppGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 399 TSICHGLQAGFQAITSSDQSTSGSEIVLLTDGEDNGISSCFEAVSR----SGAIIHTIALGPSAAR-ELETLSDMTGGLR 473
Cdd:cd00198   80 TNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARelrkLGITVYTIGIGDDANEdELKEIADKTTGGA 159

                 ..
gi 568924609 474 FY 475
Cdd:cd00198  160 VF 161
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
300-490 4.13e-25

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: 105.02  E-value: 4.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 300 PPMRGTEAPPPPTFSLLKSRRRVVCLVLDKSGSMDKEDRLIRMNQAAELYLTQIVEKESmVGLVTFDSAAHIqnyLIKIT 379
Cdd:COG1240   72 VLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENRLEAAKGALLDFLDDYRPRDR-VGLVAFGGEAEV---LLPLT 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 380 ssSDYQKITANLPQ-QATGGTSICHGLQAGFQAITSSDQSTSGSeIVLLTDGEDN-GISSCFEAVS---RSGAIIHTIAL 454
Cdd:COG1240  148 --RDREALKRALDElPPGGGTPLGDALALALELLKRADPARRKV-IVLLTDGRDNaGRIDPLEAAElaaAAGIRIYTIGV 224
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568924609 455 GPSAARE--LETLSDMTGGLRFYANkHVSSLIDAFSRI 490
Cdd:COG1240  225 GTEAVDEglLREIAEATGGRYFRAD-DLSELAAIYREI 261
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
323-485 2.18e-23

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 97.14  E-value: 2.18e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609   323 VCLVLDKSGSMDkEDRLIRMNQAAELYLTQ--IVEKESMVGLVTFDSAAHIQNYLIKITSSSDYQKITANLPQQATGGTS 400
Cdd:smart00327   2 VVFLLDGSGSMG-GNRFELAKEFVLKLVEQldIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609   401 ICHGLQAGFQAITSSDQSTSGSE---IVLLTDGEDNG----ISSCFEAVSRSGAIIHTIALGPSAAR-ELETLSDMTGGL 472
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGApkvVILITDGESNDgpkdLLKAAKELKRSGVKVFVVGVGNDVDEeELKKLASAPGGV 160
                          170
                   ....*....|...
gi 568924609   473 RFYANKHVSSLID 485
Cdd:smart00327 161 YVFLPELLDLLID 173
 
Name Accession Description Interval E-value
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
15-579 0e+00

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: 1079.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609   15 MVPGLQVLLFLTLHLLQNTESSMVHLNSNGYEGVVIAINPSVPEDERLIPSIKEMVTQASTYLFEASQGRVYFRNISILV 94
Cdd:TIGR00868   1 MGPFRSVLFFLVLHLLEGAQSSMIQLNNNGYEGIVIAIDPSVPEDERLIQNIKDMVTKASTYLFEATEKRFYFKNVSILI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609   95 PMTWKSKSEYLMPKRESYDKADVIVADPHLQHGDDPYTLQYGQCGDRGQYIHFTPNFLLTDNLRIYGPRGRVFVHEWAHL 174
Cdd:TIGR00868  81 PMTWKSKPEYLMPKLESYKNADVIVAEPNLPHGDDPYTLQYGNCGEKGEYIHFTPDFLLGKKLLIYGPRGRVFVHEWAHL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  175 RWGVFDEYNVDRPFYISRKNTIEATRCSASITGKKVVHECQRGSCVTRACRRDSKTRLYEPKCTFIPDKIQTAGASIMFM 254
Cdd:TIGR00868 161 RWGVFDEYNNDQPFYLSRNKKIEATRCSAAITGTNVVPKCQGGSCVTRPCRRDSVTGLYEKKCTFIPDKQQTEKASIMFM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  255 QNLNSVVEFCTENNHNAEAPNLQNKMCNRRSTWDVIKASADFQNSPPMRGTeaPPPPTFSLLKSRRRVVCLVLDKSGSMD 334
Cdd:TIGR00868 241 QSIDSVVEFCTEKNHNKEAPNLQNKKCNLRSTWEVIQNSEDFKNTTPMTTQ--PPPPTFSLLKIRQRIVCLVLDKSGSMT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  335 KEDRLIRMNQAAELYLTQIVEKESMVGLVTFDSAAHIQNYLIKITSSSDYQKITANLPQQATGGTSICHGLQAGFQAITS 414
Cdd:TIGR00868 319 VEDRLKRMNQAAKLFLLQTVEKGSWVGMVTFDSAAYIKNELIQITSSAERDALTANLPTAASGGTSICSGLKAAFQVIKK 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  415 SDQSTSGSEIVLLTDGEDNGISSCFEAVSRSGAIIHTIALGPSAARELETLSDMTGGLRFYAN--KHVSSLIDAFSRISS 492
Cdd:TIGR00868 399 SYQSTDGSEIVLLTDGEDNTISSCFEEVKQSGAIIHTIALGPSAAKELEELSDMTGGLRFYASdqADNNGLIDAFGALSS 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  493 TSGSVSQQALQLESKAFNVRAGAWINSTVPVDSTVGNDTFFVITWTVQKPEIILQDPKGKKyiTSDFQDDELNiRSARLQ 572
Cdd:TIGR00868 479 GNGSASQQSIQLESKGLTLQNNAWMNGTVPVDSTVGKDTFFLITWEFLKPEIFLQDPSGKS--TSDFLVDKLN-KMAYLQ 555

                  ....*..
gi 568924609  573 IPGTAEV 579
Cdd:TIGR00868 556 IPGTAKV 562
CLCA pfam08434
Calcium-activated chloride channel N terminal; The CLCA family of calcium-activated chloride ...
38-302 0e+00

Calcium-activated chloride channel N terminal; The CLCA family of calcium-activated chloride channels has been identified in many epithelial and endothelial cell types as well as in smooth muscle cells and has four or five putative transmembrane regions. Additionally to their role as chloride channels some CLCA proteins function as adhesion molecules and may also have roles as tumour suppressors. This protein cleaves itself into an N-terminal portion and a C-terminal portion. The N-terminus contains an HEXXHXXXGXXDE motif which is essential for proteolytic cleavage.


Pssm-ID: 462476  Cd Length: 266  Bit Score: 548.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609   38 VHLNSNGYEGVVIAINPSVPEDERLIPSIKEMVTQASTYLFEASQGRVYFRNISILVPMTWKSKSEYLMPKRESYDKADV 117
Cdd:pfam08434   1 IKLNNNGYEGIVIAIDPGVPEDEKLIQQIKDMVTEASTYLFEATEKRFYFKNVSILIPETWKSKPEYKRPKHESYKNADV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  118 IVADPHLQHGDDPYTLQYGQCGDRGQYIHFTPNFLLTDNLRIYGPRGRVFVHEWAHLRWGVFDEYNVDRPFYISRKNTIE 197
Cdd:pfam08434  81 IVAPPTLPGGDDPYTLQYGGCGEKGEYIHFTPDFLLGKKLNEYGPRGRVFVHEWAHLRWGVFDEYNEDQPFYSSKSKKIE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  198 ATRCSASITGKKVVHECQRGSCVTRACRRDSKTRLYEPKCTFIPDKIQTAGASIMFMQNLNSVVEFCTENNHNAEAPNLQ 277
Cdd:pfam08434 161 ATRCSAGITGKNRVYKCQGGSCITRKCRIDSQTGLYEKGCQFIPDKVQTEKASIMFMQSIDSVVEFCNKKNHNQEAPNLQ 240
                         250       260
                  ....*....|....*....|....*
gi 568924609  278 NKMCNRRSTWDVIKASADFQNSPPM 302
Cdd:pfam08434 241 NKMCNYRSTWEVISNSEDFKNTTPM 265
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
321-475 9.16e-26

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: 103.80  E-value: 9.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 321 RVVCLVLDKSGSMdKEDRLIRMNQAAELYLTQIVEK--ESMVGLVTFDSAAHIQNYLIKITSSSDYQKITANLPQQATGG 398
Cdd:cd00198    1 ADIVFLLDVSGSM-GGEKLDKAKEALKALVSSLSASppGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 399 TSICHGLQAGFQAITSSDQSTSGSEIVLLTDGEDNGISSCFEAVSR----SGAIIHTIALGPSAAR-ELETLSDMTGGLR 473
Cdd:cd00198   80 TNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARelrkLGITVYTIGIGDDANEdELKEIADKTTGGA 159

                 ..
gi 568924609 474 FY 475
Cdd:cd00198  160 VF 161
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
300-490 4.13e-25

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: 105.02  E-value: 4.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 300 PPMRGTEAPPPPTFSLLKSRRRVVCLVLDKSGSMDKEDRLIRMNQAAELYLTQIVEKESmVGLVTFDSAAHIqnyLIKIT 379
Cdd:COG1240   72 VLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENRLEAAKGALLDFLDDYRPRDR-VGLVAFGGEAEV---LLPLT 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 380 ssSDYQKITANLPQ-QATGGTSICHGLQAGFQAITSSDQSTSGSeIVLLTDGEDN-GISSCFEAVS---RSGAIIHTIAL 454
Cdd:COG1240  148 --RDREALKRALDElPPGGGTPLGDALALALELLKRADPARRKV-IVLLTDGRDNaGRIDPLEAAElaaAAGIRIYTIGV 224
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568924609 455 GPSAARE--LETLSDMTGGLRFYANkHVSSLIDAFSRI 490
Cdd:COG1240  225 GTEAVDEglLREIAEATGGRYFRAD-DLSELAAIYREI 261
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
323-485 2.18e-23

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 97.14  E-value: 2.18e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609   323 VCLVLDKSGSMDkEDRLIRMNQAAELYLTQ--IVEKESMVGLVTFDSAAHIQNYLIKITSSSDYQKITANLPQQATGGTS 400
Cdd:smart00327   2 VVFLLDGSGSMG-GNRFELAKEFVLKLVEQldIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609   401 ICHGLQAGFQAITSSDQSTSGSE---IVLLTDGEDNG----ISSCFEAVSRSGAIIHTIALGPSAAR-ELETLSDMTGGL 472
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGApkvVILITDGESNDgpkdLLKAAKELKRSGVKVFVVGVGNDVDEeELKKLASAPGGV 160
                          170
                   ....*....|...
gi 568924609   473 RFYANKHVSSLID 485
Cdd:smart00327 161 YVFLPELLDLLID 173
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
310-514 8.18e-17

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 81.30  E-value: 8.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 310 PPTFSLLKSRRRVVCLVLDKSGSMDkEDRLIRMNQAAELYLTQIVEKESmVGLVTFDSAAHIqnyLIKITSSSDYQKITA 389
Cdd:COG2304   81 PPKAAAEERPPLNLVFVIDVSGSMS-GDKLELAKEAAKLLVDQLRPGDR-VSIVTFAGDARV---LLPPTPATDRAKILA 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 390 ---NLpqQATGGTSICHGLQAGFQAITSSDQSTSGSEIVLLTDGEDN-GISS------CFEAVSRSGAIIHTIALGPSAA 459
Cdd:COG2304  156 aidRL--QAGGGTALGAGLELAYELARKHFIPGRVNRVILLTDGDANvGITDpeellkLAEEAREEGITLTTLGVGSDYN 233
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568924609 460 RE-LETLSDMTGGlRFYankHVSSLIDA---FSRISSTSGSvsqQALQLESKAFNVRAG 514
Cdd:COG2304  234 EDlLERLADAGGG-NYY---YIDDPEEAekvFVREFSRIGY---ENRALATEDFPLPYG 285
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
324-475 1.74e-14

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: 71.54  E-value: 1.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 324 CLVLDKSGSMDkEDRLIRMNQAAELYLTQIVEKESmVGLVTFDSAAHIqnyLIKITSSSDYQKITANLPQ-QATGGTSIC 402
Cdd:cd01465    4 VFVIDRSGSMD-GPKLPLVKSALKLLVDQLRPDDR-LAIVTYDGAAET---VLPATPVRDKAAILAAIDRlTAGGSTAGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 403 HGLQAGFQAITSSDQSTSGSEIVLLTDGEDN-GISSC------FEAVSRSGAIIHTIALGpSAARE--LETLSDMTGGLR 473
Cdd:cd01465   79 AGIQLGYQEAQKHFVPGGVNRILLATDGDFNvGETDPdelarlVAQKRESGITLSTLGFG-DNYNEdlMEAIADAGNGNT 157

                 ..
gi 568924609 474 FY 475
Cdd:cd01465  158 AY 159
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
307-467 3.45e-14

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 72.79  E-value: 3.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 307 APPPPTFSLLKSRRRVVCLVLDKSGSMDKEdrliRMNQAAE--LYLTQIVEKESMVGLVTFDSAAHIQNYLIKITSSSDY 384
Cdd:COG2425  105 LLAAPASAAVPLLEGPVVLCVDTSGSMAGS----KEAAAKAaaLALLRALRPNRRFGVILFDTEVVEDLPLTADDGLEDA 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 385 QKITANLpqQATGGTSICHGLQAGFQAITSSDqsTSGSEIVLLTDGEDNGISScfEAVSR-----SGAIIHTIALGPSAA 459
Cdd:COG2425  181 IEFLSGL--FAGGGTDIAPALRAALELLEEPD--YRNADIVLITDGEAGVSPE--ELLREvrakeSGVRLFTVAIGDAGN 254

                 ....*....
gi 568924609 460 REL-ETLSD 467
Cdd:COG2425  255 PGLlEALAD 263
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
317-501 2.50e-13

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 68.80  E-value: 2.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 317 KSRRRVVCLVLDKSGSMDKEdRLIRMNQA-----AELYLTQIVEKESMVGLVTFDSAAHIqnyLIKITSSSDYQkitanL 391
Cdd:COG4245    2 PMRRLPVYLLLDTSGSMSGE-PIEALNEGlqaliDELRQDPYALETVEVSVITFDGEAKV---LLPLTDLEDFQ-----P 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 392 PQ-QATGGTSICHGLQAGFQAITSSDQSTSGSE-------IVLLTDGEDN------GISSCFEAVSRSGAIIHTIALGPS 457
Cdd:COG4245   73 PDlSASGGTPLGAALELLLDLIERRVQKYTAEGkgdwrpvVFLITDGEPTdsdweaALQRLKDGEAAKKANIFAIGVGPD 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568924609 458 AarELETLSDMTGGLRFYANKHVSSLIDAFSRISSTSGSVSQQA 501
Cdd:COG4245  153 A--DTEVLKQLTDPVRALDALDGLDFREFFKWLSASVSSVSRSV 194
VWA pfam00092
von Willebrand factor type A domain;
323-489 2.10e-11

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 62.68  E-value: 2.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  323 VCLVLDKSGSMDKEDrlirMNQAAElYLTQIVEK------ESMVGLVTFDSAAHIQNYLIKITSSSDYQKITANLPQQAT 396
Cdd:pfam00092   2 IVFLLDGSGSIGGDN----FEKVKE-FLKKLVESldigpdGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  397 GGTSICHGLQAgfqAITSSDQSTSGSE------IVLLTDGEDNGISSCFEAVS--RSGAIIHTIALGPSAARELETLSDM 468
Cdd:pfam00092  77 GTTNTGKALKY---ALENLFSSAAGARpgapkvVVLLTDGRSQDGDPEEVARElkSAGVTVFAVGVGNADDEELRKIASE 153
                         170       180
                  ....*....|....*....|.
gi 568924609  469 TGGLRFYANKHVSSLIDAFSR 489
Cdd:pfam00092 154 PGEGHVFTVSDFEALEDLQDQ 174
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
321-496 2.19e-09

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 58.86  E-value: 2.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  321 RVVCLVLDKSGSMdkEDRLIRMNQAAELYLTQIVEKESMVGLVTFDSAAH-IQNYlikiTSSSDYqkITANLPQQATGGT 399
Cdd:TIGR03436  54 LTVGLVIDTSGSM--RNDLDRARAAAIRFLKTVLRPNDRVFVVTFNTRLRlLQDF----TSDPRL--LEAALNRLKPPLR 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  400 SICHGLQAGFQAITS---SDQSTSGSE---------------IVLLTDGEDNG----ISSCFEAVSRSGAIIHTI----- 452
Cdd:TIGR03436 126 TDYNSSGAFVRDGGGtalYDAITLAALeqlanalagipgrkaLIVISDGGDNRsrdtLERAIDAAQRADVAIYSIdargl 205
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568924609  453 -ALGPSAAR--------ELETLSDMTGGLRFYANKHvsSLIDAFSRISSTSGS 496
Cdd:TIGR03436 206 rAPDLGAGAkaglggpeALERLAEETGGRAFYVNSN--DLDGAFAQIAEELRS 256
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
325-467 3.58e-09

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 56.15  E-value: 3.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 325 LVLDKSGSMDKEDRLIRMNqaaelYLTQIVEK------ESMVGLVTFDSAAHIQNYLIKITSSSDYQKITANLPQQATGG 398
Cdd:cd01450    5 FLLDGSESVGPENFEKVKD-----FIEKLVEKldigpdKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGG 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568924609 399 TSICHGLQAGFQAITSSDQSTSGSE--IVLLTDGEDNGISSCFEAVSR---SGAIIHTIALGPSAARELETLSD 467
Cdd:cd01450   80 TNTGKALQYALEQLFSESNARENVPkvIIVLTDGRSDDGGDPKEAAAKlkdEGIKVFVVGVGPADEEELREIAS 153
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
323-478 1.95e-08

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 54.26  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 323 VCLVLDKSGSMD-----KEDRLirmnQAAELYLTQIVEKES--MVGLVTFDSAAHIQNYLikitsSSDYQKITANLPQQA 395
Cdd:cd01467    5 IMIALDVSGSMLaqdfvKPSRL----EAAKEVLSDFIDRREndRIGLVVFAGAAFTQAPL-----TLDRESLKELLEDIK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 396 TG----GTSIchGLQAGFqAITSSDQSTSGSE-IVLLTDGEDN--GIS--SCFEAVSRSGAIIHTIALGPSAARE----- 461
Cdd:cd01467   76 IGlagqGTAI--GDAIGL-AIKRLKNSEAKERvIVLLTDGENNagEIDpaTAAELAKNKGVRIYTIGVGKSGSGPkpdgs 152
                        170       180
                 ....*....|....*....|....
gi 568924609 462 -------LETLSDMTGGLRFYANK 478
Cdd:cd01467  153 tildedsLVEIADKTGGRIFRALD 176
VWA_2 pfam13519
von Willebrand factor type A domain;
325-427 2.62e-08

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 51.91  E-value: 2.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609  325 LVLDKSGSMDKED----RLIRMNQAAELYLTQIveKESMVGLVTFDSAAHiqnylIKITSSSDYQKITANLP--QQATGG 398
Cdd:pfam13519   3 FVLDTSGSMRNGDygptRLEAAKDAVLALLKSL--PGDRVGLVTFGDGPE-----VLIPLTKDRAKILRALRrlEPKGGG 75
                          90       100
                  ....*....|....*....|....*....
gi 568924609  399 TSICHGLQAGFQAItSSDQSTSGSEIVLL 427
Cdd:pfam13519  76 TNLAAALQLARAAL-KHRRKNQPRRIVLI 103
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
325-475 1.73e-07

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: 50.85  E-value: 1.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 325 LVLDKSGSMDKeDRLIRMNQAAELYLTQIVEKESMvGLVTFDSAAHIQNYLIKITSSSdYQKITANLPQ-QATGGTSICH 403
Cdd:cd01466    5 AVLDVSGSMAG-DKLQLVKHALRFVISSLGDADRL-SIVTFSTSAKRLSPLRRMTAKG-KRSAKRVVDGlQAGGGTNVVG 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568924609 404 GLQAGFQAITSSDQSTSGSEIVLLTDGEDNGIsscfEAVSRSGAI---IHTIALGPS-AARELETLSDMTGGLRFY 475
Cdd:cd01466   82 GLKKALKVLGDRRQKNPVASIMLLSDGQDNHG----AVVLRADNApipIHTFGLGAShDPALLAFIAEITGGTFSY 153
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
319-472 6.69e-07

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: 49.52  E-value: 6.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 319 RRRVVcLVLDKSGSMDKedrlIRMNQAAELYLTqIVEKESMV---GLVTFDSAAH-IQNYLIKITSSS---DYQKITANl 391
Cdd:cd01461    2 PKEVV-FVIDTSGSMSG----TKIEQTKEALLT-ALKDLPPGdyfNIIGFSDTVEeFSPSSVSATAENvaaAIEYVNRL- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 392 pqQATGGTSICHGLQAGFQAITSSDQSTsgSEIVLLTDGEDNGISSCFEAV---SRSGAIIHTIALGPSAARE-LETLSD 467
Cdd:cd01461   75 --QALGGTNMNDALEAALELLNSSPGSV--PQIILLTDGEVTNESQILKNVreaLSGRIRLFTFGIGSDVNTYlLERLAR 150

                 ....*
gi 568924609 468 MTGGL 472
Cdd:cd01461  151 EGRGI 155
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
321-433 9.90e-07

Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). In chlorophyll biosynthesis, insertion of Mg2+ into protoporphyrin IX is catalysed by magnesium chelatase in an ATP-dependent reaction. Magnesium chelatase is a three sub-unit (BchI, BchD and BchH) enzyme with a novel arrangement of domains: the C-terminal helical domain is located behind the nucleotide binding site. The BchD domain contains a AAA domain at its N-terminus and a VWA domain at its C-terminus. The VWA domain has been speculated to be involved in mediating protein-protein interactions.


Pssm-ID: 238728 [Multi-domain]  Cd Length: 178  Bit Score: 49.20  E-value: 9.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 321 RVVCLVLDKSGSMDKEDRLIRMNQAAELYLTQIVEKESMVGLVTF-DSAAHIqnyLIKITSSSDY-QKITANLPQQatGG 398
Cdd:cd01451    1 NLVIFVVDASGSMAARHRMAAAKGAVLSLLRDAYQRRDKVALIAFrGTEAEV---LLPPTRSVELaKRRLARLPTG--GG 75
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568924609 399 TSICHGLQAGFQAITSSDQSTSG-SEIVLLTDGEDN 433
Cdd:cd01451   76 TPLAAGLLAAYELAAEQARDPGQrPLIVVITDGRAN 111
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
322-459 5.01e-06

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


Pssm-ID: 238739 [Multi-domain]  Cd Length: 152  Bit Score: 46.57  E-value: 5.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 322 VVCLvlDKSGSM--DKEDrlirMNQAAELYLTQIVEKESM-VGLVTFDSAahIQNYLIKITSSSDyQKITANLPQQATGG 398
Cdd:cd01462    4 ILLV--DQSGSMygAPEE----VAKAVALALLRIALAENRdTYLILFDSE--FQTKIVDKTDDLE-EPVEFLSGVQLGGG 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568924609 399 TSICHGLQAGFQAITSSDQStsGSEIVLLTDGEDNGISSCF----EAVSRSGAIIHTIALGPSAA 459
Cdd:cd01462   75 TDINKALRYALELIERRDPR--KADIVLITDGYEGGVSDELlrevELKRSRVARFVALALGDHGN 137
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
319-469 5.74e-06

VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 46.95  E-value: 5.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 319 RRRVVCLVLDKSGSMDKEDrlIR-MNQAAELYLTQIVEKE-----SMVGLVTFDSAAHIqnyLIKITSSSDYQ--KITAN 390
Cdd:cd01464    2 RRLPIYLLLDTSGSMAGEP--IEaLNQGLQMLQSELRQDPyalesVEISVITFDSAARV---IVPLTPLESFQppRLTAS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924609 391 lpqqatGGTSICHGLQAGFQAITSSDQSTSGSE-------IVLLTDGE-----DNGISSCFEAVSRSGAIIhTIALGPSA 458
Cdd:cd01464   77 ------GGTSMGAALELALDCIDRRVQRYRADQkgdwrpwVFLLTDGEptddlTAAIERIKEARDSKGRIV-ACAVGPKA 149
                        170
                 ....*....|.
gi 568924609 459 arELETLSDMT 469
Cdd:cd01464  150 --DLDTLKQIT 158
 
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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