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Conserved domains on  [gi|568932996|ref|XP_006535682|]
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voltage-dependent calcium channel subunit alpha-2/delta-1 isoform X4 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 239-417 7.95e-91

VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The alpha 2 and delta subunits result from proteolytic processing of a single gene product and carries at its N-terminus the VWA and cache domains, The alpha 2 delta gene family has orthologues in D. melanogaster and C. elegans but none have been detected in aither A. thaliana or yeast. The exact biochemical function of the VWA domain is not known but the alpha 2 delta complex has been shown to regulate various functional properties of the channel complex.


:

Pssm-ID: 238740 [Multi-domain]  Cd Length: 190  Bit Score: 276.97  E-value: 7.95e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 239 RRRPWYIQGAASPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQD-VSCFQH-LVQANVRNKK 316
Cdd:cd01463    1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPvVPCFNDtLVQATTSNKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 317 VLKDAVNNITAKGITDYKKGFSFAFEQLL-----NYNVSRANCNKIIMLFTDGGEERAQEIFAKYNKDKK----VRVFTF 387
Cdd:cd01463   81 VLKEALDMLEAKGIANYTKALEFAFSLLLknlqsNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNseipVRVFTY 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 568932996 388 SVGQHNYDRGPIQWMACENKGYYYEIPSIG 417
Cdd:cd01463  161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 104-223 1.18e-52

VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand factor type A (VWA, pfam00092) and Cache (pfam02743) domains. It has been found in vertebrates, Drosophila and C. elegans but has not yet been identified in other eukaryotes. It is probably involved in the function of some voltage-dependent calcium channel subunits.


:

Pssm-ID: 462464  Cd Length: 122  Bit Score: 175.18  E-value: 1.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996  104 AEKVQAAHQWREDFAsNEVVYYNAKDDLDPERNESEPGSQRIKPVF--IEDANFGRQ-ISYQHAAVHIPTDIYEGSTIVL 180
Cdd:pfam08399   1 AEKAAEDHEWNDNVP-NDFQYYNAKYSNDVGEDYEKGNNVPLSKEFvlTPNPHFYNIpVNTNYSAVHVPTNVYDRAPDVL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568932996  181 NELNWTSALDEVFKRNRDEDPTLLWQVFGSATGLARYYPASPW 223
Cdd:pfam08399  80 NGINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
dCache_1 super family cl24147
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 435-529 8.24e-04

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


The actual alignment was detected with superfamily member pfam02743:

Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 41.17  E-value: 8.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996  435 VLAGDKAKQVQWTNVYLDALELGLVITGTLPVFNVTGQsenktnlknqlILGVMGVDVSLEDIKRLTPRFTLCPNGYYFA 514
Cdd:pfam02743 103 ALKGGGGIIWVFSSPYPSSESGEPVLTIARPIYDDDGE-----------VIGVLVADLDLDTLQELLSQIKLGEGGYVFI 171

                          90
                  ....*....|....*
gi 568932996  515 IDPNGYVLLHPNLQP 529
Cdd:pfam02743 172 VDSDGRILAHPLGKN 186
 
Name Accession Description Interval E-value
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 239-417 7.95e-91

VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The alpha 2 and delta subunits result from proteolytic processing of a single gene product and carries at its N-terminus the VWA and cache domains, The alpha 2 delta gene family has orthologues in D. melanogaster and C. elegans but none have been detected in aither A. thaliana or yeast. The exact biochemical function of the VWA domain is not known but the alpha 2 delta complex has been shown to regulate various functional properties of the channel complex.


Pssm-ID: 238740 [Multi-domain]  Cd Length: 190  Bit Score: 276.97  E-value: 7.95e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 239 RRRPWYIQGAASPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQD-VSCFQH-LVQANVRNKK 316
Cdd:cd01463    1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPvVPCFNDtLVQATTSNKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 317 VLKDAVNNITAKGITDYKKGFSFAFEQLL-----NYNVSRANCNKIIMLFTDGGEERAQEIFAKYNKDKK----VRVFTF 387
Cdd:cd01463   81 VLKEALDMLEAKGIANYTKALEFAFSLLLknlqsNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNseipVRVFTY 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 568932996 388 SVGQHNYDRGPIQWMACENKGYYYEIPSIG 417
Cdd:cd01463  161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 104-223 1.18e-52

VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand factor type A (VWA, pfam00092) and Cache (pfam02743) domains. It has been found in vertebrates, Drosophila and C. elegans but has not yet been identified in other eukaryotes. It is probably involved in the function of some voltage-dependent calcium channel subunits.


Pssm-ID: 462464  Cd Length: 122  Bit Score: 175.18  E-value: 1.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996  104 AEKVQAAHQWREDFAsNEVVYYNAKDDLDPERNESEPGSQRIKPVF--IEDANFGRQ-ISYQHAAVHIPTDIYEGSTIVL 180
Cdd:pfam08399   1 AEKAAEDHEWNDNVP-NDFQYYNAKYSNDVGEDYEKGNNVPLSKEFvlTPNPHFYNIpVNTNYSAVHVPTNVYDRAPDVL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568932996  181 NELNWTSALDEVFKRNRDEDPTLLWQVFGSATGLARYYPASPW 223
Cdd:pfam08399  80 NGINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 253-416 2.98e-21

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: 90.98  E-value: 2.98e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996   253 DMLILVDVSGSVSGLTLKLIRTSVSEMLETLS---DDDFVNVASFNSNAQDVSCFQhlvqaNVRNKKVLKDAVNNI--TA 327
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLN-----DSRSKDALLEALASLsyKL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996   328 KGITDYKKGFSFAFEQLLNYNV-SRANCNKIIMLFTDG----GEERAQEIFAKYnKDKKVRVFTFSVGQHnYDRGPIQWM 402
Cdd:smart00327  76 GGGTNLGAALQYALENLFSKSAgSRRGAPKVVILITDGesndGPKDLLKAAKEL-KRSGVKVFVVGVGND-VDEEELKKL 153

                          170
                   ....*....|....
gi 568932996   403 ACENKGYYYEIPSI 416
Cdd:smart00327 154 ASAPGGVYVFLPEL 167
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 246-420 2.28e-18

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 85.54  E-value: 2.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 246 QGAASPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQDVSCFQHlvqanVRNKKVLKDAVNNI 325
Cdd:COG2304   86 AEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPPTP-----ATDRAKILAAIDRL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 326 TAKGITDYKKGFSFAFEQLLNYNVSRANcNKIIMLfTDG----GEERAQEI--FAKYNKDKKVRVFTFSVGQhNYDRGPI 399
Cdd:COG2304  161 QAGGGTALGAGLELAYELARKHFIPGRV-NRVILL-TDGdanvGITDPEELlkLAEEAREEGITLTTLGVGS-DYNEDLL 237

                        170       180
                 ....*....|....*....|.
gi 568932996 400 QWMACENKGYYYEIPSIGAIR 420
Cdd:COG2304  238 ERLADAGGGNYYYIDDPEEAE 258
VWA pfam00092
von Willebrand factor type A domain;
253-419 5.94e-13

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 67.30  E-value: 5.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996  253 DMLILVDVSGSVSGLTLKLIRTSVSEMLETLS-DDDFVNVA--SFNSNAQDVSCFQhlvqaNVRNKKVLKDAVNNITAKG 329
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDiGPDGTRVGlvQYSSDVRTEFPLN-----DYSSKEELLSAVDNLRYLG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996  330 ITDYK--KGFSFAFEQLLN-YNVSRANCNKIIMLFTDGG------EERAQEIfakynKDKKVRVFTFSVGQHnyDRGPIQ 400
Cdd:pfam00092  76 GGTTNtgKALKYALENLFSsAAGARPGAPKVVVLLTDGRsqdgdpEEVAREL-----KSAGVTVFAVGVGNA--DDEELR 148

                         170       180
                  ....*....|....*....|
gi 568932996  401 WMACE-NKGYYYEIPSIGAI 419
Cdd:pfam00092 149 KIASEpGEGHVFTVSDFEAL 168
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 435-529 8.24e-04

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 41.17  E-value: 8.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996  435 VLAGDKAKQVQWTNVYLDALELGLVITGTLPVFNVTGQsenktnlknqlILGVMGVDVSLEDIKRLTPRFTLCPNGYYFA 514
Cdd:pfam02743 103 ALKGGGGIIWVFSSPYPSSESGEPVLTIARPIYDDDGE-----------VIGVLVADLDLDTLQELLSQIKLGEGGYVFI 171

                          90
                  ....*....|....*
gi 568932996  515 IDPNGYVLLHPNLQP 529
Cdd:pfam02743 172 VDSDGRILAHPLGKN 186
 
Name Accession Description Interval E-value
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 239-417 7.95e-91

VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The alpha 2 and delta subunits result from proteolytic processing of a single gene product and carries at its N-terminus the VWA and cache domains, The alpha 2 delta gene family has orthologues in D. melanogaster and C. elegans but none have been detected in aither A. thaliana or yeast. The exact biochemical function of the VWA domain is not known but the alpha 2 delta complex has been shown to regulate various functional properties of the channel complex.


Pssm-ID: 238740 [Multi-domain]  Cd Length: 190  Bit Score: 276.97  E-value: 7.95e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 239 RRRPWYIQGAASPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQD-VSCFQH-LVQANVRNKK 316
Cdd:cd01463    1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPvVPCFNDtLVQATTSNKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 317 VLKDAVNNITAKGITDYKKGFSFAFEQLL-----NYNVSRANCNKIIMLFTDGGEERAQEIFAKYNKDKK----VRVFTF 387
Cdd:cd01463   81 VLKEALDMLEAKGIANYTKALEFAFSLLLknlqsNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNseipVRVFTY 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 568932996 388 SVGQHNYDRGPIQWMACENKGYYYEIPSIG 417
Cdd:cd01463  161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 104-223 1.18e-52

VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand factor type A (VWA, pfam00092) and Cache (pfam02743) domains. It has been found in vertebrates, Drosophila and C. elegans but has not yet been identified in other eukaryotes. It is probably involved in the function of some voltage-dependent calcium channel subunits.


Pssm-ID: 462464  Cd Length: 122  Bit Score: 175.18  E-value: 1.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996  104 AEKVQAAHQWREDFAsNEVVYYNAKDDLDPERNESEPGSQRIKPVF--IEDANFGRQ-ISYQHAAVHIPTDIYEGSTIVL 180
Cdd:pfam08399   1 AEKAAEDHEWNDNVP-NDFQYYNAKYSNDVGEDYEKGNNVPLSKEFvlTPNPHFYNIpVNTNYSAVHVPTNVYDRAPDVL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568932996  181 NELNWTSALDEVFKRNRDEDPTLLWQVFGSATGLARYYPASPW 223
Cdd:pfam08399  80 NGINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 253-416 2.98e-21

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: 90.98  E-value: 2.98e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996   253 DMLILVDVSGSVSGLTLKLIRTSVSEMLETLS---DDDFVNVASFNSNAQDVSCFQhlvqaNVRNKKVLKDAVNNI--TA 327
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLN-----DSRSKDALLEALASLsyKL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996   328 KGITDYKKGFSFAFEQLLNYNV-SRANCNKIIMLFTDG----GEERAQEIFAKYnKDKKVRVFTFSVGQHnYDRGPIQWM 402
Cdd:smart00327  76 GGGTNLGAALQYALENLFSKSAgSRRGAPKVVILITDGesndGPKDLLKAAKEL-KRSGVKVFVVGVGND-VDEEELKKL 153

                          170
                   ....*....|....
gi 568932996   403 ACENKGYYYEIPSI 416
Cdd:smart00327 154 ASAPGGVYVFLPEL 167
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 246-420 2.28e-18

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 85.54  E-value: 2.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 246 QGAASPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQDVSCFQHlvqanVRNKKVLKDAVNNI 325
Cdd:COG2304   86 AEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPPTP-----ATDRAKILAAIDRL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 326 TAKGITDYKKGFSFAFEQLLNYNVSRANcNKIIMLfTDG----GEERAQEI--FAKYNKDKKVRVFTFSVGQhNYDRGPI 399
Cdd:COG2304  161 QAGGGTALGAGLELAYELARKHFIPGRV-NRVILL-TDGdanvGITDPEELlkLAEEAREEGITLTTLGVGS-DYNEDLL 237

                        170       180
                 ....*....|....*....|.
gi 568932996 400 QWMACENKGYYYEIPSIGAIR 420
Cdd:COG2304  238 ERLADAGGGNYYYIDDPEEAE 258
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 253-411 1.09e-15

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: 74.91  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 253 DMLILVDVSGSVSGLTLKLIRTSVSEMLETLS---DDDFVNVASFNSNAQDVSCFQhlvqaNVRNKKVLKDAVNNI--TA 327
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSaspPGDRVGLVTFGSNARVVLPLT-----TDTDKADLLEAIDALkkGL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 328 KGITDYKKGFSFAFEQLLNYNvsRANCNKIIMLFTDG----GEERAQEIFAKYnKDKKVRVFTFSVGQhNYDRGPIQWMA 403
Cdd:cd00198   77 GGGTNIGAALRLALELLKSAK--RPNARRVIILLTDGepndGPELLAEAAREL-RKLGITVYTIGIGD-DANEDELKEIA 152


                 ....*....
gi 568932996 404 -CENKGYYY 411
Cdd:cd00198  153 dKTTGGAVF 161
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 253-396 9.15e-15

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: 71.94  E-value: 9.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 253 DMLILVDVSGSVSGLTLKLIRTSVSEMLETLS---DDDFVNVASFNSNAQDVSCFqhlvqANVRNKKVLKDAVNNITAKG 329
Cdd:cd01450    2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDigpDKTRVGLVQYSDDVRVEFSL-----NDYKSKDDLLKAVKNLKYLG 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568932996 330 --ITDYKKGFSFAFEQLLNYNVSRANCNKIIMLFTDG-------GEERAQEIfakynKDKKVRVFTFSVGQHNYDR 396
Cdd:cd01450   77 ggGTNTGKALQYALEQLFSESNARENVPKVIIVLTDGrsddggdPKEAAAKL-----KDEGIKVFVVGVGPADEEE 147
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 241-420 1.54e-14

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: 73.82  E-value: 1.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 241 RPWYIQGAASPKDMLILVDVSGSVSGLT-LKLIRTSVSEMLETLSDDDFVNVASFNSNAQdvscfqhLVQANVRNKKVLK 319
Cdd:COG1240   82 APLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRDRVGLVAFGGEAE-------VLLPLTRDREALK 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 320 DAVNNITAKGITDYKKGFSFAFEQLLNYNVSRancNKIIMLFTDG----GEERAQEIfAKYNKDKKVRVFTFSVGQHNYD 395
Cdd:COG1240  155 RALDELPPGGGTPLGDALALALELLKRADPAR---RKVIVLLTDGrdnaGRIDPLEA-AELAAAAGIRIYTIGVGTEAVD 230

                        170       180
                 ....*....|....*....|....*
gi 568932996 396 RGPIQWMACENKGYYYEIPSIGAIR 420
Cdd:COG1240  231 EGLLREIAEATGGRYFRADDLSELA 255
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 257-420 2.17e-13

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: 68.45  E-value: 2.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 257 LVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQDVscfqhLVQANVRNKKVLKDAVNNITAKGITDYKKG 336
Cdd:cd01465    6 VIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAETV-----LPATPVRDKAAILAAIDRLTAGGSTAGGAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 337 FSFAFEQLLNYNVSRANcNKIImLFTDG----GEERAQEI--FAKYNKDKKVRVFTFSVGQhNYDRGPIQWMACENKGYY 410
Cdd:cd01465   81 IQLGYQEAQKHFVPGGV-NRIL-LATDGdfnvGETDPDELarLVAQKRESGITLSTLGFGD-NYNEDLMEAIADAGNGNT 157

                        170
                 ....*....|
gi 568932996 411 YEIPSIGAIR 420
Cdd:cd01465  158 AYIDNLAEAR 167
VWA pfam00092
von Willebrand factor type A domain;
253-419 5.94e-13

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 67.30  E-value: 5.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996  253 DMLILVDVSGSVSGLTLKLIRTSVSEMLETLS-DDDFVNVA--SFNSNAQDVSCFQhlvqaNVRNKKVLKDAVNNITAKG 329
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDiGPDGTRVGlvQYSSDVRTEFPLN-----DYSSKEELLSAVDNLRYLG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996  330 ITDYK--KGFSFAFEQLLN-YNVSRANCNKIIMLFTDGG------EERAQEIfakynKDKKVRVFTFSVGQHnyDRGPIQ 400
Cdd:pfam00092  76 GGTTNtgKALKYALENLFSsAAGARPGAPKVVVLLTDGRsqdgdpEEVAREL-----KSAGVTVFAVGVGNA--DDEELR 148

                         170       180
                  ....*....|....*....|
gi 568932996  401 WMACE-NKGYYYEIPSIGAI 419
Cdd:pfam00092 149 KIASEpGEGHVFTVSDFEAL 168
VWA_3 pfam13768
von Willebrand factor type A domain;
252-411 2.59e-12

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 64.72  E-value: 2.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996  252 KDMLILVDVSGSVSGLTlKLIRTSVSEMLETLSDDDFVNVASFNSNAqdVSCFQHLVQANVRNKKVLKDAVNNITAK-GI 330
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEP-KLQKDALSVALRQLPTGDKFAVLGFGTLP--RPLFPGWRVVSPRSLQEAFQFIKTLQPPlGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996  331 TDYKKGFSFAFEQLlnynvSRANCNKIIMLFTDGGEERAQEIFAKYNKD--KKVRVFTFSVG-QHNYDrgPIQWMACENK 407
Cdd:pfam13768  78 SDLLGALKEAVRAP-----ASPGYIRHVLLLTDGSPMQGETRVSDLISRapGKIRFFAYGLGaSISAP--MLQLLAEASN 150


                  ....
gi 568932996  408 GYYY 411
Cdd:pfam13768 151 GTYE 154
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 251-410 4.39e-12

vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix.


Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 64.54  E-value: 4.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 251 PKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQDVscFQHLVQANVRNKKVLKDAVNNITAKGI 330
Cdd:cd01461    2 PKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEF--SPSSVSATAENVAAAIEYVNRLQALGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 331 TDYKKGFSFAFEQLLNYNVSrancNKIIMLFTDGGEERAQEIFA--KYNKDKKVRVFTFSVGqHNYDRGPIQWMACENKG 408
Cdd:cd01461   80 TNMNDALEAALELLNSSPGS----VPQIILLTDGEVTNESQILKnvREALSGRIRLFTFGIG-SDVNTYLLERLAREGRG 154


                 ..
gi 568932996 409 YY 410
Cdd:cd01461  155 IA 156
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 179-393 2.28e-10

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 61.62  E-value: 2.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 179 VLNELNWTSALDEVFKRNRDEDPTLLWQVFGSATGLARYYPASPWVDNSRTPNKIDLYDVRRRPWYIQGAAS-----PKD 253
Cdd:COG2425   41 ALRAALLALLLLLLRAALALLTLLAGLVLLALDALLLAALLAALLDALLLAVLLLALLLLAALLLLAAPASAavpllEGP 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 254 MLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQdvscFQHLVQANVRNKKVLkDAVNNITAKGITDY 333
Cdd:COG2425  121 VVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVV----EDLPLTADDGLEDAI-EFLSGLFAGGGTDI 195

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932996 334 KKGFSFAFEQLLNYNVSRAncnkIIMLFTDGGEER-AQEIFAKYN-KDKKVRVFTFSVGQHN 393
Cdd:COG2425  196 APALRAALELLEEPDYRNA----DIVLITDGEAGVsPEELLREVRaKESGVRLFTVAIGDAG 253
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
256-391 8.70e-08

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 52.62  E-value: 8.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 256 ILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDF----VNVA--SFNSNAQDVSCFQHLVQAnvrnkkvlkdAVNNITAKG 329
Cdd:COG4245   10 LLLDTSGSMSGEPIEALNEGLQALIDELRQDPYaletVEVSviTFDGEAKVLLPLTDLEDF----------QPPDLSASG 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568932996 330 ITDYKKGFSFAFEQLLNYNVSRANCNK-----IIMLFTDGGE-----ERAQEIFAKYNKDKKVRVFTFSVGQ 391
Cdd:COG4245   80 GTPLGAALELLLDLIERRVQKYTAEGKgdwrpVVFLITDGEPtdsdwEAALQRLKDGEAAKKANIFAIGVGP 151
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 252-405 3.62e-07

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 50.30  E-value: 3.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 252 KDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSD-DDFVNVAsfnsnaqdvscfqhLVQ-----------ANVRNKKVLK 319
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIgPDGVRVG--------------VVQysddprtefylNTYRSKDDVL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 320 DAVNNITAKG-ITDYKKGFSFAFEQLLNYNV-SRANCNKIIMLFTDG-----GEERAQEIfakynkdKKVRVFTFSVGQH 392
Cdd:cd01472   67 EAVKNLRYIGgGTNTGKALKYVRENLFTEASgSREGVPKVLVVITDGksqddVEEPAVEL-------KQAGIEVFAVGVK 139

                        170
                 ....*....|...
gi 568932996 393 NYDRGPIQWMACE 405
Cdd:cd01472  140 NADEEELKQIASD 152
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 250-396 3.75e-07

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 50.46  E-value: 3.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 250 SPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNA------QDVScFQHLVQANVRNKKVLKDAVN 323
Cdd:cd01480    1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRKDPAGSWRVgvvqysDQQE-VEAGFLRDIRNYTSLKEAVD 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932996 324 NI--TAKGiTDYKKGFSFAFEQLLNYnvSRANCNKIIMLFTDGG----EERAQEIFAKYNKDKKVRVFTFSVGQHNYDR 396
Cdd:cd01480   80 NLeyIGGG-TFTDCALKYATEQLLEG--SHQKENKFLLVITDGHsdgsPDGGIEKAVNEADHLGIKIFFVAVGSQNEEP 155
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 253-414 4.31e-07

VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known.


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 49.70  E-value: 4.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 253 DMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQDVScfqHLVQANVRNKKVLKDAVNNITAKGITD 332
Cdd:cd01466    2 DLVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLS---PLRRMTAKGKRSAKRVVDGLQAGGGTN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 333 YKKGFSFAFEQLLNynvsRANCNKI--IMLFTDGgeeRAQEIFAK-YNKDKKVRVFTFSVGqHNYDRGPIQWMACENKGY 409
Cdd:cd01466   79 VVGGLKKALKVLGD----RRQKNPVasIMLLSDG---QDNHGAVVlRADNAPIPIHTFGLG-ASHDPALLAFIAEITGGT 150


                 ....*
gi 568932996 410 YYEIP 414
Cdd:cd01466  151 FSYVK 155
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 252-364 3.22e-06

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 47.39  E-value: 3.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 252 KDMLILVDVSGSVSGL---TLKLIRtSVSEMLETLSDDDFVNVASFNSNAQDVSCFQhLVQANVRNKkvLKDAVNNITA- 327
Cdd:cd01476    1 LDLLFVLDSSGSVRGKfekYKKYIE-RIVEGLEIGPTATRVALITYSGRGRQRVRFN-LPKHNDGEE--LLEKVDNLRFi 76

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568932996 328 KGITDYKKGFSFAFEQLLNYNVSRANCNKIIMLFTDG 364
Cdd:cd01476   77 GGTTATGAAIEVALQQLDPSEGRREGIPKVVVVLTDG 113
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 253-396 2.08e-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: 45.45  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 253 DMLILVDVSGSvsgltlklIRTS-----VSEMLET------LSDDDfVNVA--SFNSNAQDvscFQHLVQANVRNKK--- 316
Cdd:cd01471    2 DLYLLVDGSGS--------IGYSnwvthVVPFLHTfvqnlnISPDE-INLYlvTFSTNAKE---LIRLSSPNSTNKDlal 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996 317 -VLKDAVNNITAKGITDYKKGFSFAFEQLLNYNVSRANCNKIIMLFTDGGEERAQEIF--AKYNKDKKVRVFTFSVGQ-- 391
Cdd:cd01471   70 nAIRALLSLYYPNGSTNTTSALLVVEKHLFDTRGNRENAPQLVIIMTDGIPDSKFRTLkeARKLRERGVIIAVLGVGQgv 149


                 ....*.
gi 568932996 392 -HNYDR 396
Cdd:cd01471  150 nHEENR 155
VWA_2 pfam13519
von Willebrand factor type A domain;
254-361 3.08e-05

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 43.05  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996  254 MLILVDVSGSVSG-----LTLKLIRTSVSEMLETLsDDDFVNVASFNSNAqdvscfqHLVQANVRNKKVLKDAVNNITAK 328
Cdd:pfam13519   1 LVFVLDTSGSMRNgdygpTRLEAAKDAVLALLKSL-PGDRVGLVTFGDGP-------EVLIPLTKDRAKILRALRRLEPK 72

                          90       100       110
                  ....*....|....*....|....*....|....
gi 568932996  329 -GITDYKKGFSFAFEQLLNynvSRANCNKIIMLF 361
Cdd:pfam13519  73 gGGTNLAAALQLARAALKH---RRKNQPRRIVLI 103
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 435-529 8.24e-04

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 41.17  E-value: 8.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932996  435 VLAGDKAKQVQWTNVYLDALELGLVITGTLPVFNVTGQsenktnlknqlILGVMGVDVSLEDIKRLTPRFTLCPNGYYFA 514
Cdd:pfam02743 103 ALKGGGGIIWVFSSPYPSSESGEPVLTIARPIYDDDGE-----------VIGVLVADLDLDTLQELLSQIKLGEGGYVFI 171

                          90
                  ....*....|....*
gi 568932996  515 IDPNGYVLLHPNLQP 529
Cdd:pfam02743 172 VDSDGRILAHPLGKN 186
 
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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