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Conserved domains on  [gi|85701714|ref|NP_001028371|]
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calcium-activated chloride channel regulator 4 precursor [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 ...
 20-864 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: 1353.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714    20 GSDTSLIKLNGNGYEDIIIAIDPAVPEDTTIIEHIKGMVTKASTYLFEATEKRFFFKNVSILIPESWKNSSQYRRPKQES 99
Cdd:TIGR00868  18 GAQSSMIQLNNNGYEGIVIAIDPSVPEDERLIQNIKDMVTKASTYLFEATEKRFYFKNVSILIPMTWKSKPEYLMPKLES 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   100 YKHADIKVAPPAFEGRDEPYTRQFTQCEEKAEYIHFTPDFVLGRKQVEYGDSGKLLVHEWAHLRWGVFDEYNEDQPFYSA 179
Cdd:TIGR00868  98 YKNADVIVAEPNLPHGDDPYTLQYGNCGEKGEYIHFTPDFLLGKKLLIYGPRGRVFVHEWAHLRWGVFDEYNNDQPFYLS 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   180 SSKKIEATRCSTGITGMNRVHTCQGGSCITRRCRTNSTTKLYEKDCQFFPDKVQSEKASIMFMQSIDSVTEFCKKENHNR 259
Cdd:TIGR00868 178 RNKKIEATRCSAAITGTNVVPKCQGGSCVTRPCRRDSVTGLYEKKCTFIPDKQQTEKASIMFMQSIDSVVEFCTEKNHNK 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   260 EAPTLHNEKCQWRSTWEVISSSEDFNSSTPMETPPAPPFFSLLRISERIVCLVLDVSGSMSSSDRLNRMNQAAKYFLSQI 339
Cdd:TIGR00868 258 EAPNLQNKKCNLRSTWEVIQNSEDFKNTTPMTTQPPPPTFSLLKIRQRIVCLVLDKSGSMTVEDRLKRMNQAAKLFLLQT 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   340 IENRSWVGMVHFSSQATIVHELIQMNSDIERNKLLQTLPTSAIGGTSICSGIKTAFQVFKNGEYQTDGTEILLLSDGEDS 419
Cdd:TIGR00868 338 VEKGSWVGMVTFDSAAYIKNELIQITSSAERDALTANLPTAASGGTSICSGLKAAFQVIKKSYQSTDGSEIVLLTDGEDN 417

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   420 TAKDCIDEVKDSGSIVHFIALGPSADLAVTNMSILTGGNHKLATDEAQNNGLIDAFGALASENTDITQKSLQLESKGAIL 499
Cdd:TIGR00868 418 TISSCFEEVKQSGAIIHTIALGPSAAKELEELSDMTGGLRFYASDQADNNGLIDAFGALSSGNGSASQQSIQLESKGLTL 497

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   500 NNSLWLNDTVVIDSTVGRDTFFLVTWSKQAPAIYLRDPKGTQTTNFTMDFVSKMAYLSIPGTAEVGVWTYNLEAKENSEI 579
Cdd:TIGR00868 498 QNNAWMNGTVPVDSTVGKDTFFLITWEFLKPEIFLQDPSGKSTSDFLVDKLNKMAYLQIPGTAKVGTWTYSLQASANPQT 577

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   580 LTITVTSRAANSSVPPISVNAKVNTDTNTFPSPMIVYAEVLQGYTPIIGARVTATIESNSGKTEELVLLDNGAGADAFKD 659
Cdd:TIGR00868 578 LTLTVTSRARSPTLPPVTVTAKMNKDTAKFPSPMIVYAKISQGFLPVLGANVTALIESENGHTVTLELLDNGAGADTVKN 657

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   660 DGVYSRFFTAYSVNGRYSLKVRADGGTNSARRSLRHPSSRAAYIPGWVVDGEIQGNPPRPEM-TEATQPVLENFSRTASG 738
Cdd:TIGR00868 658 DGIYSRYFTAYDGNGRYSLKVRALGGVNTARLSLRPPWNKALYIPGWIENGEIKLNPPRPDInKDDLQATQEDFSRTASG 737

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   739 GAFVMSNVPIGPLPDQYPPNRITDLQATLDGEEISLTWTAPGDDYDVGRVQQYIIRTSENIIDLRDNFNNSLRVDTTKLT 818
Cdd:TIGR00868 738 GSFVVSGVPPGPHPDVFPPSKITDLEAGFQGDNIILTWTAPGDVLDHGRADRYIIRISTSILDLRDDFNDATQVNTTDLI 817

                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....*.
gi 85701714   819 PKEANSKETFAFKPENISEENATYIFIAIESVDKNNLSSGPSNIAQ 864
Cdd:TIGR00868 818 PKEANSKEVFVFKPEGIPIENGTDLFIAVQAIDKANLTSEVSNIAQ 863
 
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 ...
 20-864 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: 1353.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714    20 GSDTSLIKLNGNGYEDIIIAIDPAVPEDTTIIEHIKGMVTKASTYLFEATEKRFFFKNVSILIPESWKNSSQYRRPKQES 99
Cdd:TIGR00868  18 GAQSSMIQLNNNGYEGIVIAIDPSVPEDERLIQNIKDMVTKASTYLFEATEKRFYFKNVSILIPMTWKSKPEYLMPKLES 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   100 YKHADIKVAPPAFEGRDEPYTRQFTQCEEKAEYIHFTPDFVLGRKQVEYGDSGKLLVHEWAHLRWGVFDEYNEDQPFYSA 179
Cdd:TIGR00868  98 YKNADVIVAEPNLPHGDDPYTLQYGNCGEKGEYIHFTPDFLLGKKLLIYGPRGRVFVHEWAHLRWGVFDEYNNDQPFYLS 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   180 SSKKIEATRCSTGITGMNRVHTCQGGSCITRRCRTNSTTKLYEKDCQFFPDKVQSEKASIMFMQSIDSVTEFCKKENHNR 259
Cdd:TIGR00868 178 RNKKIEATRCSAAITGTNVVPKCQGGSCVTRPCRRDSVTGLYEKKCTFIPDKQQTEKASIMFMQSIDSVVEFCTEKNHNK 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   260 EAPTLHNEKCQWRSTWEVISSSEDFNSSTPMETPPAPPFFSLLRISERIVCLVLDVSGSMSSSDRLNRMNQAAKYFLSQI 339
Cdd:TIGR00868 258 EAPNLQNKKCNLRSTWEVIQNSEDFKNTTPMTTQPPPPTFSLLKIRQRIVCLVLDKSGSMTVEDRLKRMNQAAKLFLLQT 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   340 IENRSWVGMVHFSSQATIVHELIQMNSDIERNKLLQTLPTSAIGGTSICSGIKTAFQVFKNGEYQTDGTEILLLSDGEDS 419
Cdd:TIGR00868 338 VEKGSWVGMVTFDSAAYIKNELIQITSSAERDALTANLPTAASGGTSICSGLKAAFQVIKKSYQSTDGSEIVLLTDGEDN 417

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   420 TAKDCIDEVKDSGSIVHFIALGPSADLAVTNMSILTGGNHKLATDEAQNNGLIDAFGALASENTDITQKSLQLESKGAIL 499
Cdd:TIGR00868 418 TISSCFEEVKQSGAIIHTIALGPSAAKELEELSDMTGGLRFYASDQADNNGLIDAFGALSSGNGSASQQSIQLESKGLTL 497

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   500 NNSLWLNDTVVIDSTVGRDTFFLVTWSKQAPAIYLRDPKGTQTTNFTMDFVSKMAYLSIPGTAEVGVWTYNLEAKENSEI 579
Cdd:TIGR00868 498 QNNAWMNGTVPVDSTVGKDTFFLITWEFLKPEIFLQDPSGKSTSDFLVDKLNKMAYLQIPGTAKVGTWTYSLQASANPQT 577

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   580 LTITVTSRAANSSVPPISVNAKVNTDTNTFPSPMIVYAEVLQGYTPIIGARVTATIESNSGKTEELVLLDNGAGADAFKD 659
Cdd:TIGR00868 578 LTLTVTSRARSPTLPPVTVTAKMNKDTAKFPSPMIVYAKISQGFLPVLGANVTALIESENGHTVTLELLDNGAGADTVKN 657

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   660 DGVYSRFFTAYSVNGRYSLKVRADGGTNSARRSLRHPSSRAAYIPGWVVDGEIQGNPPRPEM-TEATQPVLENFSRTASG 738
Cdd:TIGR00868 658 DGIYSRYFTAYDGNGRYSLKVRALGGVNTARLSLRPPWNKALYIPGWIENGEIKLNPPRPDInKDDLQATQEDFSRTASG 737

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   739 GAFVMSNVPIGPLPDQYPPNRITDLQATLDGEEISLTWTAPGDDYDVGRVQQYIIRTSENIIDLRDNFNNSLRVDTTKLT 818
Cdd:TIGR00868 738 GSFVVSGVPPGPHPDVFPPSKITDLEAGFQGDNIILTWTAPGDVLDHGRADRYIIRISTSILDLRDDFNDATQVNTTDLI 817

                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....*.
gi 85701714   819 PKEANSKETFAFKPENISEENATYIFIAIESVDKNNLSSGPSNIAQ 864
Cdd:TIGR00868 818 PKEANSKEVFVFKPEGIPIENGTDLFIAVQAIDKANLTSEVSNIAQ 863
CLCA pfam08434
Calcium-activated chloride channel N terminal; The CLCA family of calcium-activated chloride ...
 26-290 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: 567.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714    26 IKLNGNGYEDIIIAIDPAVPEDTTIIEHIKGMVTKASTYLFEATEKRFFFKNVSILIPESWKNSSQYRRPKQESYKHADI 105
Cdd:pfam08434   1 IKLNNNGYEGIVIAIDPGVPEDEKLIQQIKDMVTEASTYLFEATEKRFYFKNVSILIPETWKSKPEYKRPKHESYKNADV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   106 KVAPPAFEGRDEPYTRQFTQCEEKAEYIHFTPDFVLGRKQVEYGDSGKLLVHEWAHLRWGVFDEYNEDQPFYSASSKKIE 185
Cdd:pfam08434  81 IVAPPTLPGGDDPYTLQYGGCGEKGEYIHFTPDFLLGKKLNEYGPRGRVFVHEWAHLRWGVFDEYNEDQPFYSSKSKKIE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   186 ATRCSTGITGMNRVHTCQGGSCITRRCRTNSTTKLYEKDCQFFPDKVQSEKASIMFMQSIDSVTEFCKKENHNREAPTLH 265
Cdd:pfam08434 161 ATRCSAGITGKNRVYKCQGGSCITRKCRIDSQTGLYEKGCQFIPDKVQTEKASIMFMQSIDSVVEFCNKKNHNQEAPNLQ 240

                         250       260
                  ....*....|....*....|....*
gi 85701714   266 NEKCQWRSTWEVISSSEDFNSSTPM 290
Cdd:pfam08434 241 NKMCNYRSTWEVISNSEDFKNTTPM 265
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 307-459 2.06e-24

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: 100.33  E-value: 2.06e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 307 RIVCLVLDVSGSMSSsDRLNRMNQAAKYFLSQIIE--NRSWVGMVHFSSQATIVHELIQMNSDIERNKLLQTLPTSAIGG 384
Cdd:cd00198   1 ADIVFLLDVSGSMGG-EKLDKAKEALKALVSSLSAspPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 385 TSICSGIKTAFQVFKNGEYQTDGTEILLLSDGEDS----TAKDCIDEVKDSGSIVHFIALGPSADLAV-TNMSILTGGNH 459
Cdd:cd00198  80 TNIGAALRLALELLKSAKRPNARRVIILLTDGEPNdgpeLLAEAARELRKLGITVYTIGIGDDANEDElKEIADKTTGGA 159
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 289-479 2.79e-19

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: 88.84  E-value: 2.79e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 289 PMETPPAPPFFSLLRISERIVCLVLDVSGSMSSSDRLNRMNQAAKYFLSQiIENRSWVGMVHFSSQATIVHELiqmNSDI 368
Cdd:COG1240  75 LLLALALAPLALARPQRGRDVVLVVDASGSMAAENRLEAAKGALLDFLDD-YRPRDRVGLVAFGGEAEVLLPL---TRDR 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 369 ER-NKLLQTLPTSaiGGTSICSGIKTAFQVFKNGEYQTDGTeILLLSDGEDS----TAKDCIDEVKDSGSIVHFIALG-P 442
Cdd:COG1240 151 EAlKRALDELPPG--GGTPLGDALALALELLKRADPARRKV-IVLLTDGRDNagriDPLEAAELAAAAGIRIYTIGVGtE 227

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 85701714 443 SADLAV-TNMSILTGGNHKLATDeaqNNGLIDAFGALA 479
Cdd:COG1240 228 AVDEGLlREIAEATGGRYFRADD---LSELAAIYREID 262
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 309-448 5.05e-18

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: 82.50  E-value: 5.05e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714    309 VCLVLDVSGSMSSSdRLNRMNQAAKYFLSQ--IIENRSWVGMVHFSSQATIVHELIQMNSDIERNKLLQTLPTSAIGGTS 386
Cdd:smart00327   2 VVFLLDGSGSMGGN-RFELAKEFVLKLVEQldIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 85701714    387 ICSGIKTAFQVFKNGEYQTDGTE---ILLLSDGEDST----AKDCIDEVKDSGSIVHFIALGPSADLAV 448
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGApkvVILITDGESNDgpkdLLKAAKELKRSGVKVFVVGVGNDVDEEE 149
 
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 ...
 20-864 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: 1353.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714    20 GSDTSLIKLNGNGYEDIIIAIDPAVPEDTTIIEHIKGMVTKASTYLFEATEKRFFFKNVSILIPESWKNSSQYRRPKQES 99
Cdd:TIGR00868  18 GAQSSMIQLNNNGYEGIVIAIDPSVPEDERLIQNIKDMVTKASTYLFEATEKRFYFKNVSILIPMTWKSKPEYLMPKLES 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   100 YKHADIKVAPPAFEGRDEPYTRQFTQCEEKAEYIHFTPDFVLGRKQVEYGDSGKLLVHEWAHLRWGVFDEYNEDQPFYSA 179
Cdd:TIGR00868  98 YKNADVIVAEPNLPHGDDPYTLQYGNCGEKGEYIHFTPDFLLGKKLLIYGPRGRVFVHEWAHLRWGVFDEYNNDQPFYLS 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   180 SSKKIEATRCSTGITGMNRVHTCQGGSCITRRCRTNSTTKLYEKDCQFFPDKVQSEKASIMFMQSIDSVTEFCKKENHNR 259
Cdd:TIGR00868 178 RNKKIEATRCSAAITGTNVVPKCQGGSCVTRPCRRDSVTGLYEKKCTFIPDKQQTEKASIMFMQSIDSVVEFCTEKNHNK 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   260 EAPTLHNEKCQWRSTWEVISSSEDFNSSTPMETPPAPPFFSLLRISERIVCLVLDVSGSMSSSDRLNRMNQAAKYFLSQI 339
Cdd:TIGR00868 258 EAPNLQNKKCNLRSTWEVIQNSEDFKNTTPMTTQPPPPTFSLLKIRQRIVCLVLDKSGSMTVEDRLKRMNQAAKLFLLQT 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   340 IENRSWVGMVHFSSQATIVHELIQMNSDIERNKLLQTLPTSAIGGTSICSGIKTAFQVFKNGEYQTDGTEILLLSDGEDS 419
Cdd:TIGR00868 338 VEKGSWVGMVTFDSAAYIKNELIQITSSAERDALTANLPTAASGGTSICSGLKAAFQVIKKSYQSTDGSEIVLLTDGEDN 417

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   420 TAKDCIDEVKDSGSIVHFIALGPSADLAVTNMSILTGGNHKLATDEAQNNGLIDAFGALASENTDITQKSLQLESKGAIL 499
Cdd:TIGR00868 418 TISSCFEEVKQSGAIIHTIALGPSAAKELEELSDMTGGLRFYASDQADNNGLIDAFGALSSGNGSASQQSIQLESKGLTL 497

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   500 NNSLWLNDTVVIDSTVGRDTFFLVTWSKQAPAIYLRDPKGTQTTNFTMDFVSKMAYLSIPGTAEVGVWTYNLEAKENSEI 579
Cdd:TIGR00868 498 QNNAWMNGTVPVDSTVGKDTFFLITWEFLKPEIFLQDPSGKSTSDFLVDKLNKMAYLQIPGTAKVGTWTYSLQASANPQT 577

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   580 LTITVTSRAANSSVPPISVNAKVNTDTNTFPSPMIVYAEVLQGYTPIIGARVTATIESNSGKTEELVLLDNGAGADAFKD 659
Cdd:TIGR00868 578 LTLTVTSRARSPTLPPVTVTAKMNKDTAKFPSPMIVYAKISQGFLPVLGANVTALIESENGHTVTLELLDNGAGADTVKN 657

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   660 DGVYSRFFTAYSVNGRYSLKVRADGGTNSARRSLRHPSSRAAYIPGWVVDGEIQGNPPRPEM-TEATQPVLENFSRTASG 738
Cdd:TIGR00868 658 DGIYSRYFTAYDGNGRYSLKVRALGGVNTARLSLRPPWNKALYIPGWIENGEIKLNPPRPDInKDDLQATQEDFSRTASG 737

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   739 GAFVMSNVPIGPLPDQYPPNRITDLQATLDGEEISLTWTAPGDDYDVGRVQQYIIRTSENIIDLRDNFNNSLRVDTTKLT 818
Cdd:TIGR00868 738 GSFVVSGVPPGPHPDVFPPSKITDLEAGFQGDNIILTWTAPGDVLDHGRADRYIIRISTSILDLRDDFNDATQVNTTDLI 817

                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....*.
gi 85701714   819 PKEANSKETFAFKPENISEENATYIFIAIESVDKNNLSSGPSNIAQ 864
Cdd:TIGR00868 818 PKEANSKEVFVFKPEGIPIENGTDLFIAVQAIDKANLTSEVSNIAQ 863
CLCA pfam08434
Calcium-activated chloride channel N terminal; The CLCA family of calcium-activated chloride ...
 26-290 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: 567.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714    26 IKLNGNGYEDIIIAIDPAVPEDTTIIEHIKGMVTKASTYLFEATEKRFFFKNVSILIPESWKNSSQYRRPKQESYKHADI 105
Cdd:pfam08434   1 IKLNNNGYEGIVIAIDPGVPEDEKLIQQIKDMVTEASTYLFEATEKRFYFKNVSILIPETWKSKPEYKRPKHESYKNADV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   106 KVAPPAFEGRDEPYTRQFTQCEEKAEYIHFTPDFVLGRKQVEYGDSGKLLVHEWAHLRWGVFDEYNEDQPFYSASSKKIE 185
Cdd:pfam08434  81 IVAPPTLPGGDDPYTLQYGGCGEKGEYIHFTPDFLLGKKLNEYGPRGRVFVHEWAHLRWGVFDEYNEDQPFYSSKSKKIE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   186 ATRCSTGITGMNRVHTCQGGSCITRRCRTNSTTKLYEKDCQFFPDKVQSEKASIMFMQSIDSVTEFCKKENHNREAPTLH 265
Cdd:pfam08434 161 ATRCSAGITGKNRVYKCQGGSCITRKCRIDSQTGLYEKGCQFIPDKVQTEKASIMFMQSIDSVVEFCNKKNHNQEAPNLQ 240

                         250       260
                  ....*....|....*....|....*
gi 85701714   266 NEKCQWRSTWEVISSSEDFNSSTPM 290
Cdd:pfam08434 241 NKMCNYRSTWEVISNSEDFKNTTPM 265
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 307-459 2.06e-24

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: 100.33  E-value: 2.06e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 307 RIVCLVLDVSGSMSSsDRLNRMNQAAKYFLSQIIE--NRSWVGMVHFSSQATIVHELIQMNSDIERNKLLQTLPTSAIGG 384
Cdd:cd00198   1 ADIVFLLDVSGSMGG-EKLDKAKEALKALVSSLSAspPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 385 TSICSGIKTAFQVFKNGEYQTDGTEILLLSDGEDS----TAKDCIDEVKDSGSIVHFIALGPSADLAV-TNMSILTGGNH 459
Cdd:cd00198  80 TNIGAALRLALELLKSAKRPNARRVIILLTDGEPNdgpeLLAEAARELRKLGITVYTIGIGDDANEDElKEIADKTTGGA 159
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 289-479 2.79e-19

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: 88.84  E-value: 2.79e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 289 PMETPPAPPFFSLLRISERIVCLVLDVSGSMSSSDRLNRMNQAAKYFLSQiIENRSWVGMVHFSSQATIVHELiqmNSDI 368
Cdd:COG1240  75 LLLALALAPLALARPQRGRDVVLVVDASGSMAAENRLEAAKGALLDFLDD-YRPRDRVGLVAFGGEAEVLLPL---TRDR 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 369 ER-NKLLQTLPTSaiGGTSICSGIKTAFQVFKNGEYQTDGTeILLLSDGEDS----TAKDCIDEVKDSGSIVHFIALG-P 442
Cdd:COG1240 151 EAlKRALDELPPG--GGTPLGDALALALELLKRADPARRKV-IVLLTDGRDNagriDPLEAAELAAAAGIRIYTIGVGtE 227

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 85701714 443 SADLAV-TNMSILTGGNHKLATDeaqNNGLIDAFGALA 479
Cdd:COG1240 228 AVDEGLlREIAEATGGRYFRADD---LSELAAIYREID 262
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 309-448 5.05e-18

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: 82.50  E-value: 5.05e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714    309 VCLVLDVSGSMSSSdRLNRMNQAAKYFLSQ--IIENRSWVGMVHFSSQATIVHELIQMNSDIERNKLLQTLPTSAIGGTS 386
Cdd:smart00327   2 VVFLLDGSGSMGGN-RFELAKEFVLKLVEQldIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 85701714    387 ICSGIKTAFQVFKNGEYQTDGTE---ILLLSDGEDST----AKDCIDEVKDSGSIVHFIALGPSADLAV 448
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRRGApkvVILITDGESNDgpkdLLKAAKELKRSGVKVFVVGVGNDVDEEE 149
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 293-445 1.42e-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: 74.72  E-value: 1.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 293 PPAPPFFSLLRISERIVCLVLDVSGSMSSSdrlnRMNQA---AKYFLSQIIENRSwVGMVHFSSQATIVHELiqmNSDIE 369
Cdd:COG2425 105 LLAAPASAAVPLLEGPVVLCVDTSGSMAGS----KEAAAkaaALALLRALRPNRR-FGVILFDTEVVEDLPL---TADDG 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 370 RNKLLQTLPTS-AIGGTSICSGIKTAFQVFKNGEYQTdgTEILLLSDGED-STAKDCIDEV--KDSGSIVHFIALGPSAD 445
Cdd:COG2425 177 LEDAIEFLSGLfAGGGTDIAPALRAALELLEEPDYRN--ADIVLITDGEAgVSPEELLREVraKESGVRLFTVAIGDAGN 254
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 309-459 1.19e-11

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 66.66  E-value: 1.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 309 VCLVLDVSGSMsSSDRLNRMNQAAKYFLSQIIENrSWVGMVHFSSQATIVHELIQMNsdiERNKLLQTLPT-SAIGGTSI 387
Cdd:COG2304  94 LVFVIDVSGSM-SGDKLELAKEAAKLLVDQLRPG-DRVSIVTFAGDARVLLPPTPAT---DRAKILAAIDRlQAGGGTAL 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 388 CSGIKTAFQVFKngEYQTDGTE--ILLLSDGED----STAKDCIDEVK---DSGSIVHFIALGPSADLAV-TNMSILTGG 457
Cdd:COG2304 169 GAGLELAYELAR--KHFIPGRVnrVILLTDGDAnvgiTDPEELLKLAEearEEGITLTTLGVGSDYNEDLlERLADAGGG 246


                ..
gi 85701714 458 NH 459
Cdd:COG2304 247 NY 248
VWA_2 pfam13519
von Willebrand factor type A domain;
311-401 1.68e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 58.84  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   311 LVLDVSGSMSSSDRLNRMNQAAKYFLSQIIE--NRSWVGMVHFSSQATIvheLIQMNSDIE--RNKLLQTLPTSaiGGTS 386
Cdd:pfam13519   3 FVLDTSGSMRNGDYGPTRLEAAKDAVLALLKslPGDRVGLVTFGDGPEV---LIPLTKDRAkiLRALRRLEPKG--GGTN 77

                          90
                  ....*....|....*
gi 85701714   387 ICSGIKTAFQVFKNG 401
Cdd:pfam13519  78 LAAALQLARAALKHR 92
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
309-448 2.62e-10

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 60.71  E-value: 2.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 309 VCLVLDVSGSMsSSDRLNRMNQAAKYFLSQIIEN-----RSWVGMVHFSSQATIVHELIQMnSDIERNKLlqtlptSAIG 383
Cdd:COG4245   8 VYLLLDTSGSM-SGEPIEALNEGLQALIDELRQDpyaleTVEVSVITFDGEAKVLLPLTDL-EDFQPPDL------SASG 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 85701714 384 GTSICSGIKTA-------FQVFKNGEYQTDGTEILLLSDGE--DSTAKDCIDEVKDS-----GSIVhFIALGPSADLAV 448
Cdd:COG4245  80 GTPLGAALELLldlierrVQKYTAEGKGDWRPVVFLITDGEptDSDWEAALQRLKDGeaakkANIF-AIGVGPDADTEV 157
VWA pfam00092
von Willebrand factor type A domain;
309-441 3.66e-10

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 59.98  E-value: 3.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   309 VCLVLDVSGSMSSSDrLNRMNQAAKYFLSQI-IENRSW-VGMVHFSSQATIVHELIQMNSDIERNKLLQTLPTSAIGGTS 386
Cdd:pfam00092   2 IVFLLDGSGSIGGDN-FEKVKEFLKKLVESLdIGPDGTrVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714   387 ICSGIKTAFQ-VFKNGEYQTDGTE--ILLLSDGE--DSTAKDCIDEVKDSGSIVHFIALG 441
Cdd:pfam00092  81 TGKALKYALEnLFSSAAGARPGAPkvVVLLTDGRsqDGDPEEVARELKSAGVTVFAVGVG 140
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 309-462 1.52e-09

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: 58.11  E-value: 1.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 309 VCLVLDVSGSMSSSD--RLNRMnQAAKYFLSQIIENRS--WVGMVHFSSQATIVHELIQmnsdiERNKLLQTLPTSAIG- 383
Cdd:cd01467   5 IMIALDVSGSMLAQDfvKPSRL-EAAKEVLSDFIDRREndRIGLVVFAGAAFTQAPLTL-----DRESLKELLEDIKIGl 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 384 ---GTSICSGIKTAFQVFKNGEyqTDGTEILLLSDGEDSTAK----DCIDEVKDSGSIVHFIALGPSAD--LAVTNMSIL 454
Cdd:cd01467  79 agqGTAIGDAIGLAIKRLKNSE--AKERVIVLLTDGENNAGEidpaTAAELAKNKGVRIYTIGVGKSGSgpKPDGSTILD 156


                ....*...
gi 85701714 455 TGGNHKLA 462
Cdd:cd01467 157 EDSLVEIA 164
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 309-451 2.57e-09

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: 57.35  E-value: 2.57e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 309 VCLVLDVSGSMsSSDRLNRMNQAAKYFLSQIIEN-----RSWVGMVHFSSQATIVHELIqmnsDIERNKlLQTLPTSaiG 383
Cdd:cd01464   6 IYLLLDTSGSM-AGEPIEALNQGLQMLQSELRQDpyaleSVEISVITFDSAARVIVPLT----PLESFQ-PPRLTAS--G 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 85701714 384 GTSICSGI-KTAFQVFKN-GEYQTDGTE-----ILLLSDGEDS----TAKDCIDEVKDSGSIVHFIALGPSADLAVTNM 451
Cdd:cd01464  78 GTSMGAALeLALDCIDRRvQRYRADQKGdwrpwVFLLTDGEPTddltAAIERIKEARDSKGRIVACAVGPKADLDTLKQ 156
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 311-442 2.52e-08

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: 54.22  E-value: 2.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 311 LVLDVSGSMSSSDRlnrmnQAAKYFLSQIIEN-----RSW-VGMVHFSSQATIVHELIQMNSDIERNKLLQTLPTSAIGG 384
Cdd:cd01450   5 FLLDGSESVGPENF-----EKVKDFIEKLVEKldigpDKTrVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGG 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 85701714 385 TSICSGIKTAFQVFKNGEYQTDGTE--ILLLSDGE---DSTAKDCIDEVKDSGSIVHFIALGP 442
Cdd:cd01450  80 TNTGKALQYALEQLFSESNARENVPkvIIVLTDGRsddGGDPKEAAAKLKDEGIKVFVVGVGP 142
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 308-450 4.66e-08

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: 53.16  E-value: 4.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 308 IVClVLDVSGSMSSsDRLNRMNQAAKYFLSQIIEnRSWVGMVHFSSQATIVHELIQMNSDIERnKLLQTLP-TSAIGGTS 386
Cdd:cd01466   3 LVA-VLDVSGSMAG-DKLQLVKHALRFVISSLGD-ADRLSIVTFSTSAKRLSPLRRMTAKGKR-SAKRVVDgLQAGGGTN 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 85701714 387 ICSGIKTAFQVFKNGEYQTDGTEILLLSDGEDSTAKDCIdEVKDSGSIVHFIALGPSADLAVTN 450
Cdd:cd01466  79 VVGGLKKALKVLGDRRQKNPVASIMLLSDGQDNHGAVVL-RADNAPIPIHTFGLGASHDPALLA 141
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 307-423 5.62e-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: 50.74  E-value: 5.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 307 RIVCLVLDVSGSMSSSDRLNRMNQAAKYFLSQIIENRSWVGMVHF-SSQATIvheLIQMNSDIER-NKLLQTLPTSaiGG 384
Cdd:cd01451   1 NLVIFVVDASGSMAARHRMAAAKGAVLSLLRDAYQRRDKVALIAFrGTEAEV---LLPPTRSVELaKRRLARLPTG--GG 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 85701714 385 TSICSGIKTAFQVFKNGEYQTDGTEIL-LLSDGEDSTAKD 423
Cdd:cd01451  76 TPLAAGLLAAYELAAEQARDPGQRPLIvVITDGRANVGPD 115
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 310-431 3.57e-06

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: 48.04  E-value: 3.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 310 CLVLDVSGSMsSSDRLNRMNQAAKYFLSQIIENRSwVGMVHFSSQATIVHELIQMNSDIERNKLLQTLptSAIGGTSICS 389
Cdd:cd01465   4 VFVIDRSGSM-DGPKLPLVKSALKLLVDQLRPDDR-LAIVTYDGAAETVLPATPVRDKAAILAAIDRL--TAGGSTAGGA 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 85701714 390 GIKTAFQVFKNGEYQTDGTEILLLSDGEDSTAKDCIDEVKDS 431
Cdd:cd01465  80 GIQLGYQEAQKHFVPGGVNRILLATDGDFNVGETDPDELARL 121
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 308-444 6.71e-05

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: 43.88  E-value: 6.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 308 IVCLvlDVSGSMSSSDRLNRMNQAAKYFLSQIIENRSWVGMVHFSSQATIVHELIQMnsdieRNKLLQTL-PTSAIGGTS 386
Cdd:cd01462   4 ILLV--DQSGSMYGAPEEVAKAVALALLRIALAENRDTYLILFDSEFQTKIVDKTDD-----LEEPVEFLsGVQLGGGTD 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 85701714 387 ICSGIKTAFQVFKNGEYQtdGTEILLLSDGEDSTAKD---CIDEVKDSG-SIVHFIALGPSA 444
Cdd:cd01462  77 INKALRYALELIERRDPR--KADIVLITDGYEGGVSDellREVELKRSRvARFVALALGDHG 136
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 309-441 8.27e-05

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 44.30  E-value: 8.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 309 VCLVLDVSGSMSSSDRLNRMNQAAKYFLSQ--IIENRSWVGMVHFSsqaTIVHELIQMNSDIERNK--------LLQTLP 378
Cdd:cd01471   3 LYLLVDGSGSIGYSNWVTHVVPFLHTFVQNlnISPDEINLYLVTFS---TNAKELIRLSSPNSTNKdlalnairALLSLY 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 85701714 379 TSAiGGTSICSGIKTAFQVFKNG-EYQTDGTE-ILLLSDGEDSTAKDCIDEV---KDSGSIVHFIALG 441
Cdd:cd01471  80 YPN-GSTNTTSALLVVEKHLFDTrGNRENAPQlVIIMTDGIPDSKFRTLKEArklRERGVIIAVLGVG 146
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 291-468 1.21e-04

VWA ywmD 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. Not much is known about the function of the members of this subgroup. All members of this subgroup however have a conserved MIDAS motif.


Pssm-ID: 238733 [Multi-domain]  Cd Length: 206  Bit Score: 44.34  E-value: 1.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 291 ETPPAPPFFSLLRISE--RIVCLVLDVSGSMSSSD-----RLNRMNQAAKYFLSqIIENRSWVGMVHFSSQA------TI 357
Cdd:cd01456   3 LGSPAFALEPVETEPQlpPNVAIVLDNSGSMREVDgggetRLDNAKAALDETAN-ALPDGTRLGLWTFSGDGdnpldvRV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 358 VHELIQMNSDI------ERNKLLQTL--PTSAIGGTSICSGIKTAFQVFKNGEYQTdgteILLLSDGEDSTAKDCIDEVK 429
Cdd:cd01456  82 LVPKGCLTAPVngfpsaQRSALDAALnsLQTPTGWTPLAAALAEAAAYVDPGRVNV----VVLITDGEDTCGPDPCEVAR 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 85701714 430 DS--------GSIVHFIALGPSADLAVTN-MSILTGGNHKLATDEAQN 468
Cdd:cd01456 158 ELakrrtpapPIKVNVIDFGGDADRAELEaIAEATGGTYAYNQSDLAS 205
vWA_transcription_factor_IIH_type cd01453
Transcription factors IIH type: TFIIH is a multiprotein complex that is one of the five ...
 307-466 5.06e-04

Transcription factors IIH type: TFIIH is a multiprotein complex that is one of the five general transcription factors that binds RNA polymerase II holoenzyme. Orthologues of these genes are found in all completed eukaryotic genomes and all these proteins contain a VWA domain. The p44 subunit of TFIIH functions as a DNA helicase in RNA polymerase II transcription initiation and DNA repair, and its transcriptional activity is dependent on its C-terminal Zn-binding domains. The function of the vWA domain is unclear, but may be involved in complex assembly. The MIDAS motif is not conserved in this sub-group.


Pssm-ID: 238730  Cd Length: 183  Bit Score: 41.93  E-value: 5.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 307 RIVCLVLDVSGSMSSSD----RLNRMNQAAKYFLSQIIENR--SWVGMVhfSSQATIVHELIQMNSDIERN-KLLQTLPT 379
Cdd:cd01453   4 RHLIIVIDCSRSMEEQDlkpsRLAVVLKLLELFIEEFFDQNpiSQLGII--SIKNGRAEKLTDLTGNPRKHiQALKTARE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85701714 380 sAIGGTSICSGIKTAFQVFKngEYQTDGT-EILL----LSDGEDSTAKDCIDEVKDSGSIVHFIALgpSADLAV-TNMSI 453
Cdd:cd01453  82 -CSGEPSLQNGLEMALESLK--HMPSHGSrEVLIifssLSTCDPGNIYETIDKLKKENIRVSVIGL--SAEMHIcKEICK 156

                       170
                ....*....|...
gi 85701714 454 LTGGNHKLATDEA 466
Cdd:cd01453 157 ATNGTYKVILDET 169
 
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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