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Conserved domains on  [gi|41386751|ref|NP_958822|]
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calcium-activated chloride channel regulator 4 precursor [Rattus norvegicus]

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 ...
2-863 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: 1327.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751     2 MGFSRGIVFLLLLYLLQGSDTSLVKLNENGYEDIIIAIDPAVSEDVTIIDQIKDMVTKASAYLFEATEKRFFFKNVSILI 81
Cdd:TIGR00868   1 MGPFRSVLFFLVLHLLEGAQSSMIQLNNNGYEGIVIAIDPSVPEDERLIQNIKDMVTKASTYLFEATEKRFYFKNVSILI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751    82 PENWTNSDQYRRPKQESYKHADIKVAPPALQGRDEPYTRQFTKCGKKAEYIHFTPDFVLGRKQKEYGDSGRLLVHEWAHL 161
Cdd:TIGR00868  81 PMTWKSKPEYLMPKLESYKNADVIVAEPNLPHGDDPYTLQYGNCGEKGEYIHFTPDFLLGKKLLIYGPRGRVFVHEWAHL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   162 RWGVFDEYNEDQPFYSASSKKIEATRCSTGIKGMNKAQVCQGGSCITRNCRRNSTTQLYEKDCQFFPDKVQTEKSSIMFM 241
Cdd:TIGR00868 161 RWGVFDEYNNDQPFYLSRNKKIEATRCSAAITGTNVVPKCQGGSCVTRPCRRDSVTGLYEKKCTFIPDKQQTEKASIMFM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   242 QSIDSVTEFCKKENHNREAPTLHNQKCDYRSTWEVISNSEDFKNSTPMEMPPSPPFFSLLRISERIVCLVLDVSGSMGSY 321
Cdd:TIGR00868 241 QSIDSVVEFCTEKNHNKEAPNLQNKKCNLRSTWEVIQNSEDFKNTTPMTTQPPPPTFSLLKIRQRIVCLVLDKSGSMTVE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   322 DRLNRMNQAAKFFLQQILESRSWAGMVHFHSSATVKSELIQINSDVERNQLLETLPTSASGGTSICSGIRTAFQVFKNKG 401
Cdd:TIGR00868 321 DRLKRMNQAAKLFLLQTVEKGSWVGMVTFDSAAYIKNELIQITSSAERDALTANLPTAASGGTSICSGLKAAFQVIKKSY 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   402 YQTGGNDILLLSDGEDSTAKDCLDEVKDSGAVVHFIALGKAFDQSISNMANVTGGKQLFATDEAQNNGLIDAFGALASEN 481
Cdd:TIGR00868 401 QSTDGSEIVLLTDGEDNTISSCFEEVKQSGAIIHTIALGPSAAKELEELSDMTGGLRFYASDQADNNGLIDAFGALSSGN 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   482 ADVTEKSLQLESKGAVLTNSRWLNDTVVIDSTVGKDTYFLVTWSQQAPAIHLRDPKGTQITNFTIDTASKMAYLTIPGIA 561
Cdd:TIGR00868 481 GSASQQSIQLESKGLTLQNNAWMNGTVPVDSTVGKDTFFLITWEFLKPEIFLQDPSGKSTSDFLVDKLNKMAYLQIPGTA 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   562 EVGVWTYNLEAKVDSEILTITVTSRASRPSVPPIIVNAKVNTDTNSFPSPMIVYAEVLQGYTPIIGARVTATIESNSGKT 641
Cdd:TIGR00868 561 KVGTWTYSLQASANPQTLTLTVTSRARSPTLPPVTVTAKMNKDTAKFPSPMIVYAKISQGFLPVLGANVTALIESENGHT 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   642 EELVLLDNGAGADAFKDDGVYSRYFTAYSDNGRYSVKVRADGGTNSARRSSRHPSSRAAYIPGWVVDGEIQGNPPRPET- 720
Cdd:TIGR00868 641 VTLELLDNGAGADTVKNDGIYSRYFTAYDGNGRYSLKVRALGGVNTARLSLRPPWNKALYIPGWIENGEIKLNPPRPDIn 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   721 TEDTQPVLENFSRTASGGAFVMSKVPALPLPDQYPPNQITDLQATLDGEKISLTWTAPGDDFDVGRVQQYIIRTSENIID 800
Cdd:TIGR00868 721 KDDLQATQEDFSRTASGGSFVVSGVPPGPHPDVFPPSKITDLEAGFQGDNIILTWTAPGDVLDHGRADRYIIRISTSILD 800
                         810       820       830       840       850       860
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41386751   801 LRDNFNKSLQVNTTHLIPKEANSKETFAFKPETISGENATYIFIAIESVDKSNLHSGLSNIAQ 863
Cdd:TIGR00868 801 LRDDFNDATQVNTTDLIPKEANSKEVFVFKPEGIPIENGTDLFIAVQAIDKANLTSEVSNIAQ 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 ...
2-863 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: 1327.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751     2 MGFSRGIVFLLLLYLLQGSDTSLVKLNENGYEDIIIAIDPAVSEDVTIIDQIKDMVTKASAYLFEATEKRFFFKNVSILI 81
Cdd:TIGR00868   1 MGPFRSVLFFLVLHLLEGAQSSMIQLNNNGYEGIVIAIDPSVPEDERLIQNIKDMVTKASTYLFEATEKRFYFKNVSILI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751    82 PENWTNSDQYRRPKQESYKHADIKVAPPALQGRDEPYTRQFTKCGKKAEYIHFTPDFVLGRKQKEYGDSGRLLVHEWAHL 161
Cdd:TIGR00868  81 PMTWKSKPEYLMPKLESYKNADVIVAEPNLPHGDDPYTLQYGNCGEKGEYIHFTPDFLLGKKLLIYGPRGRVFVHEWAHL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   162 RWGVFDEYNEDQPFYSASSKKIEATRCSTGIKGMNKAQVCQGGSCITRNCRRNSTTQLYEKDCQFFPDKVQTEKSSIMFM 241
Cdd:TIGR00868 161 RWGVFDEYNNDQPFYLSRNKKIEATRCSAAITGTNVVPKCQGGSCVTRPCRRDSVTGLYEKKCTFIPDKQQTEKASIMFM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   242 QSIDSVTEFCKKENHNREAPTLHNQKCDYRSTWEVISNSEDFKNSTPMEMPPSPPFFSLLRISERIVCLVLDVSGSMGSY 321
Cdd:TIGR00868 241 QSIDSVVEFCTEKNHNKEAPNLQNKKCNLRSTWEVIQNSEDFKNTTPMTTQPPPPTFSLLKIRQRIVCLVLDKSGSMTVE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   322 DRLNRMNQAAKFFLQQILESRSWAGMVHFHSSATVKSELIQINSDVERNQLLETLPTSASGGTSICSGIRTAFQVFKNKG 401
Cdd:TIGR00868 321 DRLKRMNQAAKLFLLQTVEKGSWVGMVTFDSAAYIKNELIQITSSAERDALTANLPTAASGGTSICSGLKAAFQVIKKSY 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   402 YQTGGNDILLLSDGEDSTAKDCLDEVKDSGAVVHFIALGKAFDQSISNMANVTGGKQLFATDEAQNNGLIDAFGALASEN 481
Cdd:TIGR00868 401 QSTDGSEIVLLTDGEDNTISSCFEEVKQSGAIIHTIALGPSAAKELEELSDMTGGLRFYASDQADNNGLIDAFGALSSGN 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   482 ADVTEKSLQLESKGAVLTNSRWLNDTVVIDSTVGKDTYFLVTWSQQAPAIHLRDPKGTQITNFTIDTASKMAYLTIPGIA 561
Cdd:TIGR00868 481 GSASQQSIQLESKGLTLQNNAWMNGTVPVDSTVGKDTFFLITWEFLKPEIFLQDPSGKSTSDFLVDKLNKMAYLQIPGTA 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   562 EVGVWTYNLEAKVDSEILTITVTSRASRPSVPPIIVNAKVNTDTNSFPSPMIVYAEVLQGYTPIIGARVTATIESNSGKT 641
Cdd:TIGR00868 561 KVGTWTYSLQASANPQTLTLTVTSRARSPTLPPVTVTAKMNKDTAKFPSPMIVYAKISQGFLPVLGANVTALIESENGHT 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   642 EELVLLDNGAGADAFKDDGVYSRYFTAYSDNGRYSVKVRADGGTNSARRSSRHPSSRAAYIPGWVVDGEIQGNPPRPET- 720
Cdd:TIGR00868 641 VTLELLDNGAGADTVKNDGIYSRYFTAYDGNGRYSLKVRALGGVNTARLSLRPPWNKALYIPGWIENGEIKLNPPRPDIn 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   721 TEDTQPVLENFSRTASGGAFVMSKVPALPLPDQYPPNQITDLQATLDGEKISLTWTAPGDDFDVGRVQQYIIRTSENIID 800
Cdd:TIGR00868 721 KDDLQATQEDFSRTASGGSFVVSGVPPGPHPDVFPPSKITDLEAGFQGDNIILTWTAPGDVLDHGRADRYIIRISTSILD 800
                         810       820       830       840       850       860
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41386751   801 LRDNFNKSLQVNTTHLIPKEANSKETFAFKPETISGENATYIFIAIESVDKSNLHSGLSNIAQ 863
Cdd:TIGR00868 801 LRDDFNDATQVNTTDLIPKEANSKEVFVFKPEGIPIENGTDLFIAVQAIDKANLTSEVSNIAQ 863
CLCA pfam08434
Calcium-activated chloride channel N terminal; The CLCA family of calcium-activated chloride ...
25-289 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: 580.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751    25 VKLNENGYEDIIIAIDPAVSEDVTIIDQIKDMVTKASAYLFEATEKRFFFKNVSILIPENWTNSDQYRRPKQESYKHADI 104
Cdd:pfam08434   1 IKLNNNGYEGIVIAIDPGVPEDEKLIQQIKDMVTEASTYLFEATEKRFYFKNVSILIPETWKSKPEYKRPKHESYKNADV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   105 KVAPPALQGRDEPYTRQFTKCGKKAEYIHFTPDFVLGRKQKEYGDSGRLLVHEWAHLRWGVFDEYNEDQPFYSASSKKIE 184
Cdd:pfam08434  81 IVAPPTLPGGDDPYTLQYGGCGEKGEYIHFTPDFLLGKKLNEYGPRGRVFVHEWAHLRWGVFDEYNEDQPFYSSKSKKIE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   185 ATRCSTGIKGMNKAQVCQGGSCITRNCRRNSTTQLYEKDCQFFPDKVQTEKSSIMFMQSIDSVTEFCKKENHNREAPTLH 264
Cdd:pfam08434 161 ATRCSAGITGKNRVYKCQGGSCITRKCRIDSQTGLYEKGCQFIPDKVQTEKASIMFMQSIDSVVEFCNKKNHNQEAPNLQ 240
                         250       260
                  ....*....|....*....|....*
gi 41386751   265 NQKCDYRSTWEVISNSEDFKNSTPM 289
Cdd:pfam08434 241 NKMCNYRSTWEVISNSEDFKNTTPM 265
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
306-460 2.07e-23

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: 97.64  E-value: 2.07e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 306 RIVCLVLDVSGSMGSyDRLNRMNQAAKFFLQQILES--RSWAGMVHFHSSATVKSELIQINSDVERNQLLETLPTSASGG 383
Cdd:cd00198   1 ADIVFLLDVSGSMGG-EKLDKAKEALKALVSSLSASppGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 384 TSICSGIRTAFQVFKNKGYQTGGNDILLLSDGEDSTAKDCL----DEVKDSGAVVHFIALGKAFDQS-ISNMANVTGGKQ 458
Cdd:cd00198  80 TNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLaeaaRELRKLGITVYTIGIGDDANEDeLKEIADKTTGGA 159

                ..
gi 41386751 459 LF 460
Cdd:cd00198 160 VF 161
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
306-478 2.54e-21

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: 94.62  E-value: 2.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 306 RIVCLVLDVSGSMGSYDRLNRMNQAAKFFLQQiLESRSWAGMVHFHSSATVkseLIQINSDVER-NQLLETLPTsaSGGT 384
Cdd:COG1240  93 RDVVLVVDASGSMAAENRLEAAKGALLDFLDD-YRPRDRVGLVAFGGEAEV---LLPLTRDREAlKRALDELPP--GGGT 166
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 385 SICSGIRTAFQVFKNKGyQTGGNDILLLSDGEDS----TAKDCLDEVKDSGAVVHFIALG-KAFDQSI-SNMANVTGGKQ 458
Cdd:COG1240 167 PLGDALALALELLKRAD-PARRKVIVLLTDGRDNagriDPLEAAELAAAAGIRIYTIGVGtEAVDEGLlREIAEATGGRY 245
                       170       180
                ....*....|....*....|
gi 41386751 459 LFATDeaqNNGLIDAFGALA 478
Cdd:COG1240 246 FRADD---LSELAAIYREID 262
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
308-466 1.50e-16

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: 78.27  E-value: 1.50e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751    308 VCLVLDVSGSMGSyDRLNRMNQAAKFFLQQ--ILESRSWAGMVHFHSSATVKSELIQINSDVERNQLLETLPTSASGGTS 385
Cdd:smart00327   2 VVFLLDGSGSMGG-NRFELAKEFVLKLVEQldIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751    386 ICSGIRTAFQVF--KNKGYQTGG-NDILLLSDGEDST----AKDCLDEVKDSGAVVHFIALGKAFDQS-ISNMANVTGGK 457
Cdd:smart00327  81 LGAALQYALENLfsKSAGSRRGApKVVILITDGESNDgpkdLLKAAKELKRSGVKVFVVGVGNDVDEEeLKKLASAPGGV 160

                   ....*....
gi 41386751    458 QLFATDEAQ 466
Cdd:smart00327 161 YVFLPELLD 169
PRK13685 PRK13685
hypothetical protein; Provisional
307-466 3.38e-03

hypothetical protein; Provisional


Pssm-ID: 184242 [Multi-domain]  Cd Length: 326  Bit Score: 40.84  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751  307 IVCLVLDVSGSMGSYD----RLNRMNQAAKFFLQQILESRSwAGMVHFHSSATVkseLIQINSDVER-NQLLETLPTSAS 381
Cdd:PRK13685  90 VVMLVIDVSQSMRATDvepnRLAAAQEAAKQFADELTPGIN-LGLIAFAGTATV---LVSPTTNREAtKNAIDKLQLADR 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751  382 GGTSicSGIRTAFQVFKNKGYQTGGND------ILLLSDGEDSTAKDCLD---------EVKDSGAVVHFIALGKAF--- 443
Cdd:PRK13685 166 TATG--EAIFTALQAIATVGAVIGGGDtppparIVLMSDGKETVPTNPDNprgaytaarTAKDQGVPISTISFGTPYgsv 243
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 41386751  444 ------------DQSISNMANVTGGKQLFATDEAQ 466
Cdd:PRK13685 244 eingqrqpvpvdDESLKKIAQLSGGEFYTAASLEE 278
 
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 ...
2-863 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: 1327.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751     2 MGFSRGIVFLLLLYLLQGSDTSLVKLNENGYEDIIIAIDPAVSEDVTIIDQIKDMVTKASAYLFEATEKRFFFKNVSILI 81
Cdd:TIGR00868   1 MGPFRSVLFFLVLHLLEGAQSSMIQLNNNGYEGIVIAIDPSVPEDERLIQNIKDMVTKASTYLFEATEKRFYFKNVSILI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751    82 PENWTNSDQYRRPKQESYKHADIKVAPPALQGRDEPYTRQFTKCGKKAEYIHFTPDFVLGRKQKEYGDSGRLLVHEWAHL 161
Cdd:TIGR00868  81 PMTWKSKPEYLMPKLESYKNADVIVAEPNLPHGDDPYTLQYGNCGEKGEYIHFTPDFLLGKKLLIYGPRGRVFVHEWAHL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   162 RWGVFDEYNEDQPFYSASSKKIEATRCSTGIKGMNKAQVCQGGSCITRNCRRNSTTQLYEKDCQFFPDKVQTEKSSIMFM 241
Cdd:TIGR00868 161 RWGVFDEYNNDQPFYLSRNKKIEATRCSAAITGTNVVPKCQGGSCVTRPCRRDSVTGLYEKKCTFIPDKQQTEKASIMFM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   242 QSIDSVTEFCKKENHNREAPTLHNQKCDYRSTWEVISNSEDFKNSTPMEMPPSPPFFSLLRISERIVCLVLDVSGSMGSY 321
Cdd:TIGR00868 241 QSIDSVVEFCTEKNHNKEAPNLQNKKCNLRSTWEVIQNSEDFKNTTPMTTQPPPPTFSLLKIRQRIVCLVLDKSGSMTVE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   322 DRLNRMNQAAKFFLQQILESRSWAGMVHFHSSATVKSELIQINSDVERNQLLETLPTSASGGTSICSGIRTAFQVFKNKG 401
Cdd:TIGR00868 321 DRLKRMNQAAKLFLLQTVEKGSWVGMVTFDSAAYIKNELIQITSSAERDALTANLPTAASGGTSICSGLKAAFQVIKKSY 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   402 YQTGGNDILLLSDGEDSTAKDCLDEVKDSGAVVHFIALGKAFDQSISNMANVTGGKQLFATDEAQNNGLIDAFGALASEN 481
Cdd:TIGR00868 401 QSTDGSEIVLLTDGEDNTISSCFEEVKQSGAIIHTIALGPSAAKELEELSDMTGGLRFYASDQADNNGLIDAFGALSSGN 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   482 ADVTEKSLQLESKGAVLTNSRWLNDTVVIDSTVGKDTYFLVTWSQQAPAIHLRDPKGTQITNFTIDTASKMAYLTIPGIA 561
Cdd:TIGR00868 481 GSASQQSIQLESKGLTLQNNAWMNGTVPVDSTVGKDTFFLITWEFLKPEIFLQDPSGKSTSDFLVDKLNKMAYLQIPGTA 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   562 EVGVWTYNLEAKVDSEILTITVTSRASRPSVPPIIVNAKVNTDTNSFPSPMIVYAEVLQGYTPIIGARVTATIESNSGKT 641
Cdd:TIGR00868 561 KVGTWTYSLQASANPQTLTLTVTSRARSPTLPPVTVTAKMNKDTAKFPSPMIVYAKISQGFLPVLGANVTALIESENGHT 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   642 EELVLLDNGAGADAFKDDGVYSRYFTAYSDNGRYSVKVRADGGTNSARRSSRHPSSRAAYIPGWVVDGEIQGNPPRPET- 720
Cdd:TIGR00868 641 VTLELLDNGAGADTVKNDGIYSRYFTAYDGNGRYSLKVRALGGVNTARLSLRPPWNKALYIPGWIENGEIKLNPPRPDIn 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   721 TEDTQPVLENFSRTASGGAFVMSKVPALPLPDQYPPNQITDLQATLDGEKISLTWTAPGDDFDVGRVQQYIIRTSENIID 800
Cdd:TIGR00868 721 KDDLQATQEDFSRTASGGSFVVSGVPPGPHPDVFPPSKITDLEAGFQGDNIILTWTAPGDVLDHGRADRYIIRISTSILD 800
                         810       820       830       840       850       860
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41386751   801 LRDNFNKSLQVNTTHLIPKEANSKETFAFKPETISGENATYIFIAIESVDKSNLHSGLSNIAQ 863
Cdd:TIGR00868 801 LRDDFNDATQVNTTDLIPKEANSKEVFVFKPEGIPIENGTDLFIAVQAIDKANLTSEVSNIAQ 863
CLCA pfam08434
Calcium-activated chloride channel N terminal; The CLCA family of calcium-activated chloride ...
25-289 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: 580.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751    25 VKLNENGYEDIIIAIDPAVSEDVTIIDQIKDMVTKASAYLFEATEKRFFFKNVSILIPENWTNSDQYRRPKQESYKHADI 104
Cdd:pfam08434   1 IKLNNNGYEGIVIAIDPGVPEDEKLIQQIKDMVTEASTYLFEATEKRFYFKNVSILIPETWKSKPEYKRPKHESYKNADV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   105 KVAPPALQGRDEPYTRQFTKCGKKAEYIHFTPDFVLGRKQKEYGDSGRLLVHEWAHLRWGVFDEYNEDQPFYSASSKKIE 184
Cdd:pfam08434  81 IVAPPTLPGGDDPYTLQYGGCGEKGEYIHFTPDFLLGKKLNEYGPRGRVFVHEWAHLRWGVFDEYNEDQPFYSSKSKKIE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   185 ATRCSTGIKGMNKAQVCQGGSCITRNCRRNSTTQLYEKDCQFFPDKVQTEKSSIMFMQSIDSVTEFCKKENHNREAPTLH 264
Cdd:pfam08434 161 ATRCSAGITGKNRVYKCQGGSCITRKCRIDSQTGLYEKGCQFIPDKVQTEKASIMFMQSIDSVVEFCNKKNHNQEAPNLQ 240
                         250       260
                  ....*....|....*....|....*
gi 41386751   265 NQKCDYRSTWEVISNSEDFKNSTPM 289
Cdd:pfam08434 241 NKMCNYRSTWEVISNSEDFKNTTPM 265
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
306-460 2.07e-23

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: 97.64  E-value: 2.07e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 306 RIVCLVLDVSGSMGSyDRLNRMNQAAKFFLQQILES--RSWAGMVHFHSSATVKSELIQINSDVERNQLLETLPTSASGG 383
Cdd:cd00198   1 ADIVFLLDVSGSMGG-EKLDKAKEALKALVSSLSASppGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 384 TSICSGIRTAFQVFKNKGYQTGGNDILLLSDGEDSTAKDCL----DEVKDSGAVVHFIALGKAFDQS-ISNMANVTGGKQ 458
Cdd:cd00198  80 TNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLaeaaRELRKLGITVYTIGIGDDANEDeLKEIADKTTGGA 159

                ..
gi 41386751 459 LF 460
Cdd:cd00198 160 VF 161
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
306-478 2.54e-21

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: 94.62  E-value: 2.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 306 RIVCLVLDVSGSMGSYDRLNRMNQAAKFFLQQiLESRSWAGMVHFHSSATVkseLIQINSDVER-NQLLETLPTsaSGGT 384
Cdd:COG1240  93 RDVVLVVDASGSMAAENRLEAAKGALLDFLDD-YRPRDRVGLVAFGGEAEV---LLPLTRDREAlKRALDELPP--GGGT 166
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 385 SICSGIRTAFQVFKNKGyQTGGNDILLLSDGEDS----TAKDCLDEVKDSGAVVHFIALG-KAFDQSI-SNMANVTGGKQ 458
Cdd:COG1240 167 PLGDALALALELLKRAD-PARRKVIVLLTDGRDNagriDPLEAAELAAAAGIRIYTIGVGtEAVDEGLlREIAEATGGRY 245
                       170       180
                ....*....|....*....|
gi 41386751 459 LFATDeaqNNGLIDAFGALA 478
Cdd:COG1240 246 FRADD---LSELAAIYREID 262
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
308-466 1.50e-16

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: 78.27  E-value: 1.50e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751    308 VCLVLDVSGSMGSyDRLNRMNQAAKFFLQQ--ILESRSWAGMVHFHSSATVKSELIQINSDVERNQLLETLPTSASGGTS 385
Cdd:smart00327   2 VVFLLDGSGSMGG-NRFELAKEFVLKLVEQldIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751    386 ICSGIRTAFQVF--KNKGYQTGG-NDILLLSDGEDST----AKDCLDEVKDSGAVVHFIALGKAFDQS-ISNMANVTGGK 457
Cdd:smart00327  81 LGAALQYALENLfsKSAGSRRGApKVVILITDGESNDgpkdLLKAAKELKRSGVKVFVVGVGNDVDEEeLKKLASAPGGV 160

                   ....*....
gi 41386751    458 QLFATDEAQ 466
Cdd:smart00327 161 YVFLPELLD 169
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
308-466 2.82e-15

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 77.45  E-value: 2.82e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 308 VCLVLDVSGSMgSYDRLNRMNQAAKFFLQQiLESRSWAGMVHFHSSATVKSELIQINsdvERNQLLETLPT-SASGGTSI 386
Cdd:COG2304  94 LVFVIDVSGSM-SGDKLELAKEAAKLLVDQ-LRPGDRVSIVTFAGDARVLLPPTPAT---DRAKILAAIDRlQAGGGTAL 168
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 387 CSGIRTAFQVFKnKGYQTGG-NDILLLSDGED----STAKDCLDEVK---DSGAVVHFIALGKAFDQSI-SNMANVTGGK 457
Cdd:COG2304 169 GAGLELAYELAR-KHFIPGRvNRVILLTDGDAnvgiTDPEELLKLAEearEEGITLTTLGVGSDYNEDLlERLADAGGGN 247

                ....*....
gi 41386751 458 QLFATDEAQ 466
Cdd:COG2304 248 YYYIDDPEE 256
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
288-447 2.86e-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: 73.95  E-value: 2.86e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 288 PMEMPPSPPFFSLLRISERIVCLVLDVSGSMGSydrlNRMNQA---AKFFLQQILESRSwAGMVHFHSSATVKSELiqiN 364
Cdd:COG2425 101 AALLLLAAPASAAVPLLEGPVVLCVDTSGSMAG----SKEAAAkaaALALLRALRPNRR-FGVILFDTEVVEDLPL---T 172
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 365 SDVERNQLLETLPTS-ASGGTSICSGIRTAFQVFKNKGYQTGgnDILLLSDGED-STAKDCLDEV--KDSGAVVHFIALG 440
Cdd:COG2425 173 ADDGLEDAIEFLSGLfAGGGTDIAPALRAALELLEEPDYRNA--DIVLITDGEAgVSPEELLREVraKESGVRLFTVAIG 250

                ....*..
gi 41386751 441 KAFDQSI 447
Cdd:COG2425 251 DAGNPGL 257
VWA pfam00092
von Willebrand factor type A domain;
308-473 4.84e-09

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 56.51  E-value: 4.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   308 VCLVLDVSGSMGsYDRLNRMNQAAKFFLQQILES-RSW-AGMVHFHSSATVKSELIQINSDVERNQLLETLPTSASGGTS 385
Cdd:pfam00092   2 IVFLLDGSGSIG-GDNFEKVKEFLKKLVESLDIGpDGTrVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   386 ICSGIRTAFQVF--KNKGYQTGGNDIL-LLSDGE--DSTAKDCLDEVKDSGAVVHFIALGKAFDQSISNMANVTGGKQLF 460
Cdd:pfam00092  81 TGKALKYALENLfsSAAGARPGAPKVVvLLTDGRsqDGDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPGEGHVF 160
                         170
                  ....*....|....
gi 41386751   461 -ATDEAQNNGLIDA 473
Cdd:pfam00092 161 tVSDFEALEDLQDQ 174
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
307-454 6.65e-09

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: 55.86  E-value: 6.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 307 IVClVLDVSGSMgSYDRLNRMNQAAKFFLQQiLESRSWAGMVHFHSSATVKSELIQINSDVERnQLLETLP-TSASGGTS 385
Cdd:cd01466   3 LVA-VLDVSGSM-AGDKLQLVKHALRFVISS-LGDADRLSIVTFSTSAKRLSPLRRMTAKGKR-SAKRVVDgLQAGGGTN 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41386751 386 ICSGIRTAFQVFKNKGYQTGGNDILLLSDGEDSTAKDCLdEVKDSGAVVHFIALGK----AFDQSISNMANVT 454
Cdd:cd01466  79 VVGGLKKALKVLGDRRQKNPVASIMLLSDGQDNHGAVVL-RADNAPIPIHTFGLGAshdpALLAFIAEITGGT 150
VWA_2 pfam13519
von Willebrand factor type A domain;
310-399 7.62e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 53.84  E-value: 7.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751   310 LVLDVSGSMGSYDRLNRMNQAAKFFLQQILESR--SWAGMVHFHSSATVkseLIQINSDveRNQLLETLP--TSASGGTS 385
Cdd:pfam13519   3 FVLDTSGSMRNGDYGPTRLEAAKDAVLALLKSLpgDRVGLVTFGDGPEV---LIPLTKD--RAKILRALRrlEPKGGGTN 77
                          90
                  ....*....|....
gi 41386751   386 ICSGIRTAFQVFKN 399
Cdd:pfam13519  78 LAAALQLARAALKH 91
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
308-465 1.31e-07

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: 52.33  E-value: 1.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 308 VCLVLDVSGSMGSYD--RLNRMnQAAKFFLQQILESRS--WAGMVHFHSSATVKSELIQiNSDVERNQLLETLPTSASGG 383
Cdd:cd01467   5 IMIALDVSGSMLAQDfvKPSRL-EAAKEVLSDFIDRREndRIGLVVFAGAAFTQAPLTL-DRESLKELLEDIKIGLAGQG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 384 TSICSGIRTAFQVFKNKgyQTGGNDILLLSDGEDSTAK----DCLDEVKDSGAVVHFIALGK---------AFDQ---SI 447
Cdd:cd01467  83 TAIGDAIGLAIKRLKNS--EAKERVIVLLTDGENNAGEidpaTAAELAKNKGVRIYTIGVGKsgsgpkpdgSTILdedSL 160
                       170
                ....*....|....*...
gi 41386751 448 SNMANVTGGKQLFATDEA 465
Cdd:cd01467 161 VEIADKTGGRIFRALDGF 178
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
308-467 2.80e-07

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 51.85  E-value: 2.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 308 VCLVLDVSGSMGSyDRLNRMNQAAKFFLQQILESRSWAGMVH-----FHSSATVKSELIQInSDVERNQLletlptSASG 382
Cdd:COG4245   8 VYLLLDTSGSMSG-EPIEALNEGLQALIDELRQDPYALETVEvsvitFDGEAKVLLPLTDL-EDFQPPDL------SASG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 383 GTSICSGIRTA---FQVFKNKGYQTGGND----ILLLSDGE--DSTAKDCLDEVKD----SGAVVHFIALGKAFDQSIsn 449
Cdd:COG4245  80 GTPLGAALELLldlIERRVQKYTAEGKGDwrpvVFLITDGEptDSDWEAALQRLKDgeaaKKANIFAIGVGPDADTEV-- 157
                       170
                ....*....|....*...
gi 41386751 450 MANVTGGKQLFATDEAQN 467
Cdd:COG4245 158 LKQLTDPVRALDALDGLD 175
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
309-445 1.23e-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: 49.58  E-value: 1.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 309 CLVLDVSGSMGSyDRLNRMNQAAKFFLQQILESRSWAGMVHFHSSATV-----KSELIQINSDVERnqlletlpTSASGG 383
Cdd:cd01465   4 VFVIDRSGSMDG-PKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAETVlpatpVRDKAAILAAIDR--------LTAGGS 74
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 384 TSICSGIRTAFQVFKnKGYQTGG-NDILLLSDGEDSTAKDCLDEVK-------DSGAVVHFIALGKAFDQ 445
Cdd:cd01465  75 TAGGAGIQLGYQEAQ-KHFVPGGvNRILLATDGDFNVGETDPDELArlvaqkrESGITLSTLGFGDNYNE 143
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
307-441 2.18e-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: 48.50  E-value: 2.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 307 IVCLvlDVSGSMGSYdrlnRMNQAAKFFL----QQILESRSWAGMVhFhSSATVKSELIQInsdVERNQLLETL-PTSAS 381
Cdd:cd01462   4 ILLV--DQSGSMYGA----PEEVAKAVALallrIALAENRDTYLIL-F-DSEFQTKIVDKT---DDLEEPVEFLsGVQLG 72
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41386751 382 GGTSICSGIRTAFQVFKNKGYQTGgnDILLLSDGEDSTAKDCL---DEVKDSG-AVVHFIALGK 441
Cdd:cd01462  73 GGTDINKALRYALELIERRDPRKA--DIVLITDGYEGGVSDELlreVELKRSRvARFVALALGD 134
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
308-450 2.31e-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: 48.88  E-value: 2.31e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 308 VCLVLDVSGSMgSYDRLNRMNQAAKFFLQQILES-----RSWAGMVHFHSSATVKSELIQINsdverNQLLETLPtsASG 382
Cdd:cd01464   6 IYLLLDTSGSM-AGEPIEALNQGLQMLQSELRQDpyaleSVEISVITFDSAARVIVPLTPLE-----SFQPPRLT--ASG 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41386751 383 GTSICSGI-RTAFQVFKNKG-YQTGGND-----ILLLSDGEDS----TAKDCLDEVKDSGAVVHFIALGKAFDQSISNM 450
Cdd:cd01464  78 GTSMGAALeLALDCIDRRVQrYRADQKGdwrpwVFLLTDGEPTddltAAIERIKEARDSKGRIVACAVGPKADLDTLKQ 156
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
306-428 2.64e-06

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: 48.81  E-value: 2.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 306 RIVCLVLDVSGSMGSYDRLNRMNQAAKFFLQQILESRSWAGMVHFH-SSATVkseLIQINSDVERNQ-LLETLPTsaSGG 383
Cdd:cd01451   1 NLVIFVVDASGSMAARHRMAAAKGAVLSLLRDAYQRRDKVALIAFRgTEAEV---LLPPTRSVELAKrRLARLPT--GGG 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 41386751 384 TSICSGIRTAFQVFKNKGYQTGGNDIL-LLSDGEDSTAKDCLDEVK 428
Cdd:cd01451  76 TPLAAGLLAAYELAAEQARDPGQRPLIvVITDGRANVGPDPTADRA 121
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
310-460 7.07e-05

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: 44.20  E-value: 7.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 310 LVLDVSGSMGSYDRlnrmnQAAKFFLQQILES-----RSW-AGMVHFHSSATVKSELIQINSDVERNQLLETLPTSASGG 383
Cdd:cd01450   5 FLLDGSESVGPENF-----EKVKDFIEKLVEKldigpDKTrVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 384 TSICSGIRTAFQVFKNKGyQTGGND---ILLLSDGE---DSTAKDCLDEVKDSGAVVHFIALGKAFDQSISNMANVTGGK 457
Cdd:cd01450  80 TNTGKALQYALEQLFSES-NARENVpkvIIVLTDGRsddGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSER 158

                ...
gi 41386751 458 QLF 460
Cdd:cd01450 159 HVF 161
vWA_ywmD_type cd01456
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ...
308-467 7.91e-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: 41.65  E-value: 7.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 308 VCLVLDVSGSM-----GSYDRLNRMNQAAKFFLQqILESRSWAGMVHFHSSA------TVKSELIQINSDV------ERN 370
Cdd:cd01456  23 VAIVLDNSGSMrevdgGGETRLDNAKAALDETAN-ALPDGTRLGLWTFSGDGdnpldvRVLVPKGCLTAPVngfpsaQRS 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751 371 QLLETL--PTSASGGTSICSGIRTAFQVFKNKGYqtggNDILLLSDGEDSTAKDCLD---EVKDSGAVVHFIAL------ 439
Cdd:cd01456 102 ALDAALnsLQTPTGWTPLAAALAEAAAYVDPGRV----NVVVLITDGEDTCGPDPCEvarELAKRRTPAPPIKVnvidfg 177
                       170       180
                ....*....|....*....|....*...
gi 41386751 440 GKAFDQSISNMANVTGGKQLFATDEAQN 467
Cdd:cd01456 178 GDADRAELEAIAEATGGTYAYNQSDLAS 205
PRK13685 PRK13685
hypothetical protein; Provisional
307-466 3.38e-03

hypothetical protein; Provisional


Pssm-ID: 184242 [Multi-domain]  Cd Length: 326  Bit Score: 40.84  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751  307 IVCLVLDVSGSMGSYD----RLNRMNQAAKFFLQQILESRSwAGMVHFHSSATVkseLIQINSDVER-NQLLETLPTSAS 381
Cdd:PRK13685  90 VVMLVIDVSQSMRATDvepnRLAAAQEAAKQFADELTPGIN-LGLIAFAGTATV---LVSPTTNREAtKNAIDKLQLADR 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386751  382 GGTSicSGIRTAFQVFKNKGYQTGGND------ILLLSDGEDSTAKDCLD---------EVKDSGAVVHFIALGKAF--- 443
Cdd:PRK13685 166 TATG--EAIFTALQAIATVGAVIGGGDtppparIVLMSDGKETVPTNPDNprgaytaarTAKDQGVPISTISFGTPYgsv 243
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 41386751  444 ------------DQSISNMANVTGGKQLFATDEAQ 466
Cdd:PRK13685 244 eingqrqpvpvdDESLKKIAQLSGGEFYTAASLEE 278
 
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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