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Conserved domains on  [gi|530386383|ref|XP_005250630|]
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voltage-dependent calcium channel subunit alpha-2/delta-1 isoform X8 [Homo sapiens]

Protein Classification

vWA_VGCC_like and VGCC_alpha2 domain-containing protein( domain architecture ID 13750239)

protein containing domains VWA_N, vWA_VGCC_like, HK_sensor, and VGCC_alpha2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VGCC_alpha2 pfam08473
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 625-1053 0e+00

Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found in the neuronal voltage-dependent calcium channel (VGCC) alpha 2a, 2c, and 2d subunits. It is also found in other calcium channel alpha-2 delta subunits to the C-terminus of a Cache domain (pfam02743).


:

Pssm-ID: 462488  Cd Length: 432  Bit Score: 672.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   625 YSETLKPDNFEESGYTFIAPRDYCNDLKISDNNTEFLLNFNEFIDRKTPNNPSCNADLINRVLLDAGFTNELVQnYWSKQ 704
Cdd:pfam08473    1 FEELLLPKFFEEGGYTFIAPRYYCKDLKPSNNNTEFLEFFNYIIDKTTPNPPCCNNLLNNLLLLDGGITQLLVK-WWKKQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   705 KNIKGVKARFVVTDGGITRVYPKEAGENWQENPETYEDSFYKRSLDNDNYVFTAPYFNKSGPGAYE----SGIMVSKAVE 780
Cdd:pfam08473   80 LLNGGLLAVFAATDGGITRVPPKSAGDWWEEAEETYESSFYRRSLDNDYYFFTPPYFNSSYRPNEEeddtSGILVSAAVE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   781 IYIQGKLLKPAVVGIKIDVNSWIENFTKTSIRDPCAGPVCDCKRNSDVMDCVILDDGGFLLMANHDDYTNQIGRFFGEID 860
Cdd:pfam08473  160 LIIDGTLLKPAVVGVKLDDSWWMEFFSNTTRKDQCDEECCGCKGNDDLLCCVLDDDGGFLMMSNQDDYIEQIGFFFGEDD 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   861 PSLMRHLVNISVYAFNKSYDYQSVCEPGAAPKQGAGHRSAYVPSVADILQIGWWATAAAWSILQQFLLSLTFPRLLEAVE 940
Cdd:pfam08473  240 PLLMSLLNNSSFYTKKTSYDYQSCCPPKESSKAAAGRRSVVVPTIADLLNLWWWTSAAAWSIQQQLLVSLTFPSFLAAED 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   941 MEDDDFTASlSKQSCITEQTQYFFDNDSKSFSGVLDCGNCSRIFHGEKLMNTNLIFIMVESKGTCP-CDTRLLIQAEQTS 1019
Cdd:pfam08473  320 VADEIMDAM-KEESCITEQTQYFFNNSNSSFSGVIDCGNCSRYFAAEKLNTTNLLFVVADAKGTCSsCDSMLLQQAEQSS 398

                          410       420       430
                   ....*....|....*....|....*....|....
gi 530386383  1020 DGPNPCDMVKQPRYRKGPDVCFDNNVLEDYTDCG 1053
Cdd:pfam08473  399 DGPPCCELVQNPRYRKGPDCCFDNNAEEDTDDCG 432
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 239-417 4.24e-85

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: 273.12  E-value: 4.24e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  239 RRRPWYIQGAASPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQD-VSCFQH-LVQANVRNKK 316
Cdd:cd01463     1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPvVPCFNDtLVQATTSNKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  317 VLKDAVNNITAKGITDYKKGFSFAFEQLL-----NYNVSRANCNKIIMLFTDGGEERAQEIFNKYNKDKK----VRVFTF 387
Cdd:cd01463    81 VLKEALDMLEAKGIANYTKALEFAFSLLLknlqsNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNseipVRVFTY 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 530386383  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 8.50e-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: 177.49  E-value: 8.50e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   104 AEKVQAAHQWREDFAsNEVVYYNAKDDLDPEKNDSEPGSQRIKPVF--IEDANFGRQ-ISYQHAAVHIPTDIYEGSTIVL 180
Cdd:pfam08399    1 AEKAAEDHEWNDNVP-NDFQYYNAKYSNDVGEDYEKGNNVPLSKEFvlTPNPHFYNIpVNTNYSAVHVPTNVYDRAPDVL 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 530386383   181 NELNWTSALDEVFKKNREEDPSLLWQVFGSATGLARYYPASPW 223
Cdd:pfam08399   80 NGINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
HK_sensor super family cl38916
Sensor domains of Histidine Kinase receptors; Histidine kinase (HK) receptors are part of ...
 509-606 1.08e-06

Sensor domains of Histidine Kinase receptors; Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution.


The actual alignment was detected with superfamily member cd12912:

Pssm-ID: 365792 [Multi-domain]  Cd Length: 92  Bit Score: 47.76  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  509 NGYYFAIDPNGYVLLHPNlqpknpksQEPVTLDFLDaelENDIKVEIRNKMIDGESGEKTFRtlvksqderyIDKGNRTY 588
Cdd:cd12912    14 TGYAFLVDKDGTIIAHPD--------KELVGKKISD---DEAAEEELAKKMLAGKSGSVEYT----------FNGEKKYV 72

                          90
                  ....*....|....*...
gi 530386383  589 TWTPVNGTDYSLALVLPT 606
Cdd:cd12912    73 AYAPIPGTGWSLVVVVPE 90
 
Name Accession Description Interval E-value
VGCC_alpha2 pfam08473
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 625-1053 0e+00

Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found in the neuronal voltage-dependent calcium channel (VGCC) alpha 2a, 2c, and 2d subunits. It is also found in other calcium channel alpha-2 delta subunits to the C-terminus of a Cache domain (pfam02743).


Pssm-ID: 462488  Cd Length: 432  Bit Score: 672.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   625 YSETLKPDNFEESGYTFIAPRDYCNDLKISDNNTEFLLNFNEFIDRKTPNNPSCNADLINRVLLDAGFTNELVQnYWSKQ 704
Cdd:pfam08473    1 FEELLLPKFFEEGGYTFIAPRYYCKDLKPSNNNTEFLEFFNYIIDKTTPNPPCCNNLLNNLLLLDGGITQLLVK-WWKKQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   705 KNIKGVKARFVVTDGGITRVYPKEAGENWQENPETYEDSFYKRSLDNDNYVFTAPYFNKSGPGAYE----SGIMVSKAVE 780
Cdd:pfam08473   80 LLNGGLLAVFAATDGGITRVPPKSAGDWWEEAEETYESSFYRRSLDNDYYFFTPPYFNSSYRPNEEeddtSGILVSAAVE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   781 IYIQGKLLKPAVVGIKIDVNSWIENFTKTSIRDPCAGPVCDCKRNSDVMDCVILDDGGFLLMANHDDYTNQIGRFFGEID 860
Cdd:pfam08473  160 LIIDGTLLKPAVVGVKLDDSWWMEFFSNTTRKDQCDEECCGCKGNDDLLCCVLDDDGGFLMMSNQDDYIEQIGFFFGEDD 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   861 PSLMRHLVNISVYAFNKSYDYQSVCEPGAAPKQGAGHRSAYVPSVADILQIGWWATAAAWSILQQFLLSLTFPRLLEAVE 940
Cdd:pfam08473  240 PLLMSLLNNSSFYTKKTSYDYQSCCPPKESSKAAAGRRSVVVPTIADLLNLWWWTSAAAWSIQQQLLVSLTFPSFLAAED 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   941 MEDDDFTASlSKQSCITEQTQYFFDNDSKSFSGVLDCGNCSRIFHGEKLMNTNLIFIMVESKGTCP-CDTRLLIQAEQTS 1019
Cdd:pfam08473  320 VADEIMDAM-KEESCITEQTQYFFNNSNSSFSGVIDCGNCSRYFAAEKLNTTNLLFVVADAKGTCSsCDSMLLQQAEQSS 398

                          410       420       430
                   ....*....|....*....|....*....|....
gi 530386383  1020 DGPNPCDMVKQPRYRKGPDVCFDNNVLEDYTDCG 1053
Cdd:pfam08473  399 DGPPCCELVQNPRYRKGPDCCFDNNAEEDTDDCG 432
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 239-417 4.24e-85

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: 273.12  E-value: 4.24e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  239 RRRPWYIQGAASPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQD-VSCFQH-LVQANVRNKK 316
Cdd:cd01463     1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPvVPCFNDtLVQATTSNKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  317 VLKDAVNNITAKGITDYKKGFSFAFEQLL-----NYNVSRANCNKIIMLFTDGGEERAQEIFNKYNKDKK----VRVFTF 387
Cdd:cd01463    81 VLKEALDMLEAKGIANYTKALEFAFSLLLknlqsNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNseipVRVFTY 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 530386383  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 8.50e-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: 177.49  E-value: 8.50e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   104 AEKVQAAHQWREDFAsNEVVYYNAKDDLDPEKNDSEPGSQRIKPVF--IEDANFGRQ-ISYQHAAVHIPTDIYEGSTIVL 180
Cdd:pfam08399    1 AEKAAEDHEWNDNVP-NDFQYYNAKYSNDVGEDYEKGNNVPLSKEFvlTPNPHFYNIpVNTNYSAVHVPTNVYDRAPDVL 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 530386383   181 NELNWTSALDEVFKKNREEDPSLLWQVFGSATGLARYYPASPW 223
Cdd:pfam08399   80 NGINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 253-416 2.62e-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: 92.13  E-value: 2.62e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383    253 DMLILVDVSGSVSGLTLKLIRTSVSEMLETLS---DDDFVNVASFNSNAQDVSCFQhlvqaNVRNKKVLKDAVNNI--TA 327
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLN-----DSRSKDALLEALASLsyKL 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383    328 KGITDYKKGFSFAFEQLLNYNV-SRANCNKIIMLFTDG----GEERAQEIFNKYnKDKKVRVFTFSVGQHnYDRGPIQWM 402
Cdd:smart00327   76 GGGTNLGAALQYALENLFSKSAgSRRGAPKVVILITDGesndGPKDLLKAAKEL-KRSGVKVFVVGVGND-VDEEELKKL 153

                           170
                    ....*....|....
gi 530386383    403 ACENKGYYYEIPSI 416
Cdd:smart00327  154 ASAPGGVYVFLPEL 167
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 246-420 3.75e-17

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 83.23  E-value: 3.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  246 QGAASPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQDVSCFQHlvqanVRNKKVLKDAVNNI 325
Cdd:COG2304    86 AEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPPTP-----ATDRAKILAAIDRL 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  326 TAKGITDYKKGFSFAFEQLLNYNVSRANcNKIIMLfTDG----GEERAQEIFN--KYNKDKKVRVFTFSVGQhNYDRGPI 399
Cdd:COG2304   161 QAGGGTALGAGLELAYELARKHFIPGRV-NRVILL-TDGdanvGITDPEELLKlaEEAREEGITLTTLGVGS-DYNEDLL 237

                         170       180
                  ....*....|....*....|.
gi 530386383  400 QWMACENKGYYYEIPSIGAIR 420
Cdd:COG2304   238 ERLADAGGGNYYYIDDPEEAE 258
VWA pfam00092
von Willebrand factor type A domain;
253-419 8.06e-13

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 67.69  E-value: 8.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   253 DMLILVDVSGSVSGLTLKLIRTSVSEMLETLS-DDDFVNVA--SFNSNAQDVSCFQhlvqaNVRNKKVLKDAVNNITAKG 329
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDiGPDGTRVGlvQYSSDVRTEFPLN-----DYSSKEELLSAVDNLRYLG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   330 ITDYK--KGFSFAFEQLLN-YNVSRANCNKIIMLFTDGG------EERAQEIfnkynKDKKVRVFTFSVGQHnyDRGPIQ 400
Cdd:pfam00092   76 GGTTNtgKALKYALENLFSsAAGARPGAPKVVVLLTDGRsqdgdpEEVAREL-----KSAGVTVFAVGVGNA--DDEELR 148

                          170       180
                   ....*....|....*....|
gi 530386383   401 WMACE-NKGYYYEIPSIGAI 419
Cdd:pfam00092  149 KIASEpGEGHVFTVSDFEAL 168
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 509-606 1.08e-06

second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the second PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350337 [Multi-domain]  Cd Length: 92  Bit Score: 47.76  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  509 NGYYFAIDPNGYVLLHPNlqpknpksQEPVTLDFLDaelENDIKVEIRNKMIDGESGEKTFRtlvksqderyIDKGNRTY 588
Cdd:cd12912    14 TGYAFLVDKDGTIIAHPD--------KELVGKKISD---DEAAEEELAKKMLAGKSGSVEYT----------FNGEKKYV 72

                          90
                  ....*....|....*...
gi 530386383  589 TWTPVNGTDYSLALVLPT 606
Cdd:cd12912    73 AYAPIPGTGWSLVVVVPE 90
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 435-603 4.29e-05

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://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 46.18  E-value: 4.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   435 VLAGDKAKQVQWTNVYLDALELGLVITGTLPVFNITGQFenktnlknqliLGVMGVDVSLEDIKRLTPRFTLCPNGYYFA 514
Cdd:pfam02743  103 ALKGGGGIIWVFSSPYPSSESGEPVLTIARPIYDDDGEV-----------IGVLVADLDLDTLQELLSQIKLGEGGYVFI 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   515 IDPNGYVLLHPNLQPKNpksqepVTLDFLDAELENDIKveirnkmidgeSGEKTFRTLVKSQDERYIDkgnrtyTWTPVN 594
Cdd:pfam02743  172 VDSDGRILAHPLGKNLR------SLLAPFLGKSLADAL-----------PGSGITEIAVDLDGEDYLV------AYAPIP 228


                   ....*....
gi 530386383   595 GTDYSLALV 603
Cdd:pfam02743  229 GTGWTLVVV 237
 
Name Accession Description Interval E-value
VGCC_alpha2 pfam08473
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 625-1053 0e+00

Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found in the neuronal voltage-dependent calcium channel (VGCC) alpha 2a, 2c, and 2d subunits. It is also found in other calcium channel alpha-2 delta subunits to the C-terminus of a Cache domain (pfam02743).


Pssm-ID: 462488  Cd Length: 432  Bit Score: 672.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   625 YSETLKPDNFEESGYTFIAPRDYCNDLKISDNNTEFLLNFNEFIDRKTPNNPSCNADLINRVLLDAGFTNELVQnYWSKQ 704
Cdd:pfam08473    1 FEELLLPKFFEEGGYTFIAPRYYCKDLKPSNNNTEFLEFFNYIIDKTTPNPPCCNNLLNNLLLLDGGITQLLVK-WWKKQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   705 KNIKGVKARFVVTDGGITRVYPKEAGENWQENPETYEDSFYKRSLDNDNYVFTAPYFNKSGPGAYE----SGIMVSKAVE 780
Cdd:pfam08473   80 LLNGGLLAVFAATDGGITRVPPKSAGDWWEEAEETYESSFYRRSLDNDYYFFTPPYFNSSYRPNEEeddtSGILVSAAVE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   781 IYIQGKLLKPAVVGIKIDVNSWIENFTKTSIRDPCAGPVCDCKRNSDVMDCVILDDGGFLLMANHDDYTNQIGRFFGEID 860
Cdd:pfam08473  160 LIIDGTLLKPAVVGVKLDDSWWMEFFSNTTRKDQCDEECCGCKGNDDLLCCVLDDDGGFLMMSNQDDYIEQIGFFFGEDD 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   861 PSLMRHLVNISVYAFNKSYDYQSVCEPGAAPKQGAGHRSAYVPSVADILQIGWWATAAAWSILQQFLLSLTFPRLLEAVE 940
Cdd:pfam08473  240 PLLMSLLNNSSFYTKKTSYDYQSCCPPKESSKAAAGRRSVVVPTIADLLNLWWWTSAAAWSIQQQLLVSLTFPSFLAAED 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   941 MEDDDFTASlSKQSCITEQTQYFFDNDSKSFSGVLDCGNCSRIFHGEKLMNTNLIFIMVESKGTCP-CDTRLLIQAEQTS 1019
Cdd:pfam08473  320 VADEIMDAM-KEESCITEQTQYFFNNSNSSFSGVIDCGNCSRYFAAEKLNTTNLLFVVADAKGTCSsCDSMLLQQAEQSS 398

                          410       420       430
                   ....*....|....*....|....*....|....
gi 530386383  1020 DGPNPCDMVKQPRYRKGPDVCFDNNVLEDYTDCG 1053
Cdd:pfam08473  399 DGPPCCELVQNPRYRKGPDCCFDNNAEEDTDDCG 432
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 239-417 4.24e-85

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: 273.12  E-value: 4.24e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  239 RRRPWYIQGAASPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQD-VSCFQH-LVQANVRNKK 316
Cdd:cd01463     1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPvVPCFNDtLVQATTSNKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  317 VLKDAVNNITAKGITDYKKGFSFAFEQLL-----NYNVSRANCNKIIMLFTDGGEERAQEIFNKYNKDKK----VRVFTF 387
Cdd:cd01463    81 VLKEALDMLEAKGIANYTKALEFAFSLLLknlqsNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNseipVRVFTY 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 530386383  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 8.50e-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: 177.49  E-value: 8.50e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   104 AEKVQAAHQWREDFAsNEVVYYNAKDDLDPEKNDSEPGSQRIKPVF--IEDANFGRQ-ISYQHAAVHIPTDIYEGSTIVL 180
Cdd:pfam08399    1 AEKAAEDHEWNDNVP-NDFQYYNAKYSNDVGEDYEKGNNVPLSKEFvlTPNPHFYNIpVNTNYSAVHVPTNVYDRAPDVL 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 530386383   181 NELNWTSALDEVFKKNREEDPSLLWQVFGSATGLARYYPASPW 223
Cdd:pfam08399   80 NGINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 253-416 2.62e-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: 92.13  E-value: 2.62e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383    253 DMLILVDVSGSVSGLTLKLIRTSVSEMLETLS---DDDFVNVASFNSNAQDVSCFQhlvqaNVRNKKVLKDAVNNI--TA 327
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDigpDGDRVGLVTFSDDARVLFPLN-----DSRSKDALLEALASLsyKL 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383    328 KGITDYKKGFSFAFEQLLNYNV-SRANCNKIIMLFTDG----GEERAQEIFNKYnKDKKVRVFTFSVGQHnYDRGPIQWM 402
Cdd:smart00327   76 GGGTNLGAALQYALENLFSKSAgSRRGAPKVVILITDGesndGPKDLLKAAKEL-KRSGVKVFVVGVGND-VDEEELKKL 153

                           170
                    ....*....|....
gi 530386383    403 ACENKGYYYEIPSI 416
Cdd:smart00327  154 ASAPGGVYVFLPEL 167
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 246-420 3.75e-17

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 83.23  E-value: 3.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  246 QGAASPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQDVSCFQHlvqanVRNKKVLKDAVNNI 325
Cdd:COG2304    86 AEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLPPTP-----ATDRAKILAAIDRL 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  326 TAKGITDYKKGFSFAFEQLLNYNVSRANcNKIIMLfTDG----GEERAQEIFN--KYNKDKKVRVFTFSVGQhNYDRGPI 399
Cdd:COG2304   161 QAGGGTALGAGLELAYELARKHFIPGRV-NRVILL-TDGdanvGITDPEELLKlaEEAREEGITLTTLGVGS-DYNEDLL 237

                         170       180
                  ....*....|....*....|.
gi 530386383  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 1.08e-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: 75.68  E-value: 1.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  253 DMLILVDVSGSVSGLTLKLIRTSVSEMLETLS---DDDFVNVASFNSNAQDVSCFQhlvqaNVRNKKVLKDAVNNI--TA 327
Cdd:cd00198     2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSaspPGDRVGLVTFGSNARVVLPLT-----TDTDKADLLEAIDALkkGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  328 KGITDYKKGFSFAFEQLLNYNvsRANCNKIIMLFTDG----GEERAQEIFNKYnKDKKVRVFTFSVGQhNYDRGPIQWMA 403
Cdd:cd00198    77 GGGTNIGAALRLALELLKSAK--RPNARRVIILLTDGepndGPELLAEAAREL-RKLGITVYTIGIGD-DANEDELKEIA 152


                  ....*....
gi 530386383  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 1.26e-14

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 72.71  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  253 DMLILVDVSGSVSGLTLKLIRTSVSEMLETLS---DDDFVNVASFNSNAQDVSCFqhlvqANVRNKKVLKDAVNNITAKG 329
Cdd:cd01450     2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDigpDKTRVGLVQYSDDVRVEFSL-----NDYKSKDDLLKAVKNLKYLG 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530386383  330 --ITDYKKGFSFAFEQLLNYNVSRANCNKIIMLFTDG-------GEERAQEIfnkynKDKKVRVFTFSVGQHNYDR 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 1.61e-13

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: 71.89  E-value: 1.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  241 RPWYIQGAASPKDMLILVDVSGSVSGLT-LKLIRTSVSEMLETLSDDDFVNVASFNSNAQdvscfqhLVQANVRNKKVLK 319
Cdd:COG1240    82 APLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRDRVGLVAFGGEAE-------VLLPLTRDREALK 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  320 DAVNNITAKGITDYKKGFSFAFEQLLNYNVSRancNKIIMLFTDG----GEERAQEIFNKYnKDKKVRVFTFSVGQHNYD 395
Cdd:COG1240   155 RALDELPPGGGTPLGDALALALELLKRADPAR---RKVIVLLTDGrdnaGRIDPLEAAELA-AAAGIRIYTIGVGTEAVD 230

                         170       180
                  ....*....|....*....|....*
gi 530386383  396 RGPIQWMACENKGYYYEIPSIGAIR 420
Cdd:COG1240   231 EGLLREIAEATGGRYFRADDLSELA 255
VWA pfam00092
von Willebrand factor type A domain;
253-419 8.06e-13

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 67.69  E-value: 8.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   253 DMLILVDVSGSVSGLTLKLIRTSVSEMLETLS-DDDFVNVA--SFNSNAQDVSCFQhlvqaNVRNKKVLKDAVNNITAKG 329
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDiGPDGTRVGlvQYSSDVRTEFPLN-----DYSSKEELLSAVDNLRYLG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   330 ITDYK--KGFSFAFEQLLN-YNVSRANCNKIIMLFTDGG------EERAQEIfnkynKDKKVRVFTFSVGQHnyDRGPIQ 400
Cdd:pfam00092   76 GGTTNtgKALKYALENLFSsAAGARPGAPKVVVLLTDGRsqdgdpEEVAREL-----KSAGVTVFAVGVGNA--DDEELR 148

                          170       180
                   ....*....|....*....|
gi 530386383   401 WMACE-NKGYYYEIPSIGAI 419
Cdd:pfam00092  149 KIASEpGEGHVFTVSDFEAL 168
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 257-420 3.11e-12

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: 65.76  E-value: 3.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  257 LVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQDVscfqhLVQANVRNKKVLKDAVNNITAKGITDYKKG 336
Cdd:cd01465     6 VIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAETV-----LPATPVRDKAAILAAIDRLTAGGSTAGGAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  337 FSFAFEQLLNYNVSRANcNKIImLFTDG----GEERAQEI--FNKYNKDKKVRVFTFSVGQhNYDRGPIQWMACENKGYY 410
Cdd:cd01465    81 IQLGYQEAQKHFVPGGV-NRIL-LATDGdfnvGETDPDELarLVAQKRESGITLSTLGFGD-NYNEDLMEAIADAGNGNT 157

                         170
                  ....*....|
gi 530386383  411 YEIPSIGAIR 420
Cdd:cd01465   158 AYIDNLAEAR 167
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 251-410 4.90e-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: 65.31  E-value: 4.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  251 PKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQDVscFQHLVQANVRNKKVLKDAVNNITAKGI 330
Cdd:cd01461     2 PKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEF--SPSSVSATAENVAAAIEYVNRLQALGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  331 TDYKKGFSFAFEQLLNYNVSrancNKIIMLFTDGGEERAQEIFN--KYNKDKKVRVFTFSVGqHNYDRGPIQWMACENKG 408
Cdd:cd01461    80 TNMNDALEAALELLNSSPGS----VPQIILLTDGEVTNESQILKnvREALSGRIRLFTFGIG-SDVNTYLLERLAREGRG 154


                  ..
gi 530386383  409 YY 410
Cdd:cd01461   155 IA 156
VWA_3 pfam13768
von Willebrand factor type A domain;
252-411 6.76e-12

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 64.72  E-value: 6.76e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   252 KDMLILVDVSGSVSGLTlKLIRTSVSEMLETLSDDDFVNVASFNSNAqdVSCFQHLVQANVRNKKVLKDAVNNITAK-GI 330
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEP-KLQKDALSVALRQLPTGDKFAVLGFGTLP--RPLFPGWRVVSPRSLQEAFQFIKTLQPPlGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   331 TDYKKGFSFAFEQLlnynvSRANCNKIIMLFTDGGEERAQEIFNKYNKD--KKVRVFTFSVG-QHNYDrgPIQWMACENK 407
Cdd:pfam13768   78 SDLLGALKEAVRAP-----ASPGYIRHVLLLTDGSPMQGETRVSDLISRapGKIRFFAYGLGaSISAP--MLQLLAEASN 150


                   ....
gi 530386383   408 GYYY 411
Cdd:pfam13768  151 GTYE 154
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 251-393 1.97e-09

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 59.69  E-value: 1.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  251 PKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQdvscFQHLVQANVRNKKVLkDAVNNITAKGI 330
Cdd:COG2425   118 EGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVV----EDLPLTADDGLEDAI-EFLSGLFAGGG 192

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530386383  331 TDYKKGFSFAFEQLLNYNVSRAncnkIIMLFTDGGEER-AQEIFNKYN-KDKKVRVFTFSVGQHN 393
Cdd:COG2425   193 TDIAPALRAALELLEEPDYRNA----DIVLITDGEAGVsPEELLREVRaKESGVRLFTVAIGDAG 253
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
256-391 1.02e-07

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 53.39  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  256 ILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDF----VNVA--SFNSNAQDVSCFQHLVQAnvrnkkvlkdAVNNITAKG 329
Cdd:COG4245    10 LLLDTSGSMSGEPIEALNEGLQALIDELRQDPYaletVEVSviTFDGEAKVLLPLTDLEDF----------QPPDLSASG 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530386383  330 ITDYKKGFSFAFEQLLNYNVSRANCNK-----IIMLFTDGGE-----ERAQEIFNKYNKDKKVRVFTFSVGQ 391
Cdd:COG4245    80 GTPLGAALELLLDLIERRVQKYTAEGKgdwrpVVFLITDGEPtdsdwEAALQRLKDGEAAKKANIFAIGVGP 151
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 250-396 4.06e-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: 51.62  E-value: 4.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  250 SPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNA------QDVScFQHLVQANVRNKKVLKDAVN 323
Cdd:cd01480     1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRKDPAGSWRVgvvqysDQQE-VEAGFLRDIRNYTSLKEAVD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530386383  324 NI--TAKGiTDYKKGFSFAFEQLLNYnvSRANCNKIIMLFTDGGE--ERAQEIFNKYNKDKK--VRVFTFSVGQHNYDR 396
Cdd:cd01480    80 NLeyIGGG-TFTDCALKYATEQLLEG--SHQKENKFLLVITDGHSdgSPDGGIEKAVNEADHlgIKIFFVAVGSQNEEP 155
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 252-405 5.92e-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: 5.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  252 KDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSD-DDFVNVAsfnsnaqdvscfqhLVQ-----------ANVRNKKVLK 319
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIgPDGVRVG--------------VVQysddprtefylNTYRSKDDVL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  320 DAVNNITAKG-ITDYKKGFSFAFEQLLNYNV-SRANCNKIIMLFTDG-----GEERAQEIfnkynkdKKVRVFTFSVGQH 392
Cdd:cd01472    67 EAVKNLRYIGgGTNTGKALKYVRENLFTEASgSREGVPKVLVVITDGksqddVEEPAVEL-------KQAGIEVFAVGVK 139

                         170
                  ....*....|...
gi 530386383  393 NYDRGPIQWMACE 405
Cdd:cd01472   140 NADEEELKQIASD 152
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 509-606 1.08e-06

second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the second PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350337 [Multi-domain]  Cd Length: 92  Bit Score: 47.76  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  509 NGYYFAIDPNGYVLLHPNlqpknpksQEPVTLDFLDaelENDIKVEIRNKMIDGESGEKTFRtlvksqderyIDKGNRTY 588
Cdd:cd12912    14 TGYAFLVDKDGTIIAHPD--------KELVGKKISD---DEAAEEELAKKMLAGKSGSVEYT----------FNGEKKYV 72

                          90
                  ....*....|....*...
gi 530386383  589 TWTPVNGTDYSLALVLPT 606
Cdd:cd12912    73 AYAPIPGTGWSLVVVVPE 90
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 253-414 2.91e-06

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: 48.15  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  253 DMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQDVScfqHLVQANVRNKKVLKDAVNNITAKGITD 332
Cdd:cd01466     2 DLVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLS---PLRRMTAKGKRSAKRVVDGLQAGGGTN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  333 YKKGFSFAFEQLLNynvsRANCNKI--IMLFTDGGEERAQEIFNKynKDKKVRVFTFSVGqHNYDRGPIQWMACENKGYY 410
Cdd:cd01466    79 VVGGLKKALKVLGD----RRQKNPVasIMLLSDGQDNHGAVVLRA--DNAPIPIHTFGLG-ASHDPALLAFIAEITGGTF 151


                  ....
gi 530386383  411 YEIP 414
Cdd:cd01466   152 SYVK 155
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 252-364 6.80e-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: 6.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  252 KDMLILVDVSGSVSGL---TLKLIRtSVSEMLETLSDDDFVNVASFNSNAQDVSCFQhLVQANVRNKkvLKDAVNNITA- 327
Cdd:cd01476     1 LDLLFVLDSSGSVRGKfekYKKYIE-RIVEGLEIGPTATRVALITYSGRGRQRVRFN-LPKHNDGEE--LLEKVDNLRFi 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 530386383  328 KGITDYKKGFSFAFEQLLNYNVSRANCNKIIMLFTDG 364
Cdd:cd01476    77 GGTTATGAAIEVALQQLDPSEGRREGIPKVVVVLTDG 113
PDC2_HK_sensor cd18774
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, ...
 496-606 9.79e-06

second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase and similar domains; Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution.


Pssm-ID: 350342 [Multi-domain]  Cd Length: 89  Bit Score: 45.13  E-value: 9.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  496 DIKRLTPRFTLCPNGYYFAIDPNGYVLLHPNLQPKNPKSQEPVTLDFldaelendikveiRNKMIDGESGEKTFrtlvks 575
Cdd:cd18774     1 YLSDLLSSIKLGETGYAFLVDSDGTILAHPPKELVGKGKSLDDLALL-------------AALLLAGESGTFEY------ 61

                          90       100       110
                  ....*....|....*....|....*....|.
gi 530386383  576 qdeRYIDKGNRTYTWTPVNGTDYSLALVLPT 606
Cdd:cd18774    62 ---TSDDGVERLVAYRPVPGTPWVVVVGVPE 89
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 253-396 3.63e-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: 45.84  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  253 DMLILVDVSGSvsgltlklIRTS-----VSEMLET------LSDDDfVNVA--SFNSNAQDvscFQHLVQANVRNKK--- 316
Cdd:cd01471     2 DLYLLVDGSGS--------IGYSnwvthVVPFLHTfvqnlnISPDE-INLYlvTFSTNAKE---LIRLSSPNSTNKDlal 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383  317 -VLKDAVNNITAKGITDYKKGFSFAFEQLLNYNVSRANCNKIIMLFTDGGEERAQEIFNKYN--KDKKVRVFTFSVGQ-- 391
Cdd:cd01471    70 nAIRALLSLYYPNGSTNTTSALLVVEKHLFDTRGNRENAPQLVIIMTDGIPDSKFRTLKEARklRERGVIIAVLGVGQgv 149


                  ....*.
gi 530386383  392 -HNYDR 396
Cdd:cd01471   150 nHEENR 155
VWA_2 pfam13519
von Willebrand factor type A domain;
254-361 3.90e-05

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 43.82  E-value: 3.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   254 MLILVDVSGSVSG-----LTLKLIRTSVSEMLETLsDDDFVNVASFNSNAqdvscfqHLVQANVRNKKVLKDAVNNITAK 328
Cdd:pfam13519    1 LVFVLDTSGSMRNgdygpTRLEAAKDAVLALLKSL-PGDRVGLVTFGDGP-------EVLIPLTKDRAKILRALRRLEPK 72

                           90       100       110
                   ....*....|....*....|....*....|....
gi 530386383   329 -GITDYKKGFSFAFEQLLNYnvsRANCNKIIMLF 361
Cdd:pfam13519   73 gGGTNLAAALQLARAALKHR---RKNQPRRIVLI 103
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 435-603 4.29e-05

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://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 46.18  E-value: 4.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   435 VLAGDKAKQVQWTNVYLDALELGLVITGTLPVFNITGQFenktnlknqliLGVMGVDVSLEDIKRLTPRFTLCPNGYYFA 514
Cdd:pfam02743  103 ALKGGGGIIWVFSSPYPSSESGEPVLTIARPIYDDDGEV-----------IGVLVADLDLDTLQELLSQIKLGEGGYVFI 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530386383   515 IDPNGYVLLHPNLQPKNpksqepVTLDFLDAELENDIKveirnkmidgeSGEKTFRTLVKSQDERYIDkgnrtyTWTPVN 594
Cdd:pfam02743  172 VDSDGRILAHPLGKNLR------SLLAPFLGKSLADAL-----------PGSGITEIAVDLDGEDYLV------AYAPIP 228


                   ....*....
gi 530386383   595 GTDYSLALV 603
Cdd:pfam02743  229 GTGWTLVVV 237
 
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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