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Conserved domains on  [gi|132566536|ref|NP_758952|]
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voltage-dependent calcium channel subunit alpha-2/delta-4 [Homo sapiens]

Protein Classification

calcium channel subunit alpha-2/delta family protein( domain architecture ID 13750233)

calcium channel subunit alpha-2/delta family protein similar to Homo sapiens voltage-dependent calcium channel subunit alpha-2/delta-4 that regulates calcium current density and activation/inactivation kinetics of the calcium channel

CATH:  3.40.50.410
Gene Ontology:  GO:0005245|GO:0046872|GO:0005891|GO:0070588
PubMed:  12579041|10830113|12388743
SCOP:  3000832
TCDB:  8.A.18

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 ...
 277-460 1.79e-82

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: 266.57  E-value: 1.79e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  277 RNRGWYIQAATSPKDIVILVDVSGSMKGLRMTIAKHTITTILDTLGENDFINIIAYNDYVHYIEPCFKGILVQADRDNRE 356
Cdd:cd01463     1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFNDTLVQATTSNKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  357 HFKLLVEELMVKGVGVVDQALREAFQIL---KQFQEAKQGSLCNQAIMLISDGAVEDYEPVFEKYNWPD---CKVRVFTY 430
Cdd:cd01463    81 VLKEALDMLEAKGIANYTKALEFAFSLLlknLQSNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKnseIPVRVFTY 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 132566536  431 LIGREVSFADRMKWIACNNKGYYTQISTLA 460
Cdd:cd01463   161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 148-264 1.92e-56

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: 190.97  E-value: 1.92e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   148 AEEADLNHEFNES--LVFDYYNSVLINERDE---KGNFVELGAEFLLESNAHFSNLPVNTSISSVQLPTNVYNKDPDILN 222
Cdd:pfam08399    1 AEKAAEDHEWNDNvpNDFQYYNAKYSNDVGEdyeKGNNVPLSKEFVLTPNPHFYNIPVNTNYSAVHVPTNVYDRAPDVLN 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 132566536   223 GVYMSEALNAVFVENFQRDPTLTWQYFGSATGFFRIYPGIKW 264
Cdd:pfam08399   81 GINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VGCC_alpha2 super family cl07190
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 661-1110 7.94e-26

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).


The actual alignment was detected with superfamily member pfam08473:

Pssm-ID: 462488  Cd Length: 432  Bit Score: 112.09  E-value: 7.94e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   661 LLGNTSVEEGLHDLLHPDlalagdwiYCITDIDPDHRKLSQLEAMIRFLTRKDPD-LECDEELVREVLFDAVVTAPMEAY 739
Cdd:pfam08473    4 LLLPKFFEEGGYTFIAPR--------YYCKDLKPSNNNTEFLEFFNYIIDKTTPNpPCCNNLLNNLLLLDGGITQLLVKW 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   740 WtalalnmSEESEHVVDMAFLGTRAGLLRSslfVGSEKVSDRKFLTPEDEASVFtldrfplwYRQASEH-----PAGSFV 814
Cdd:pfam08473   76 W-------KKQLLNGGLLAVFAATDGGITR---VPPKSAGDWWEEAEETYESSF--------YRRSLDNdyyffTPPYFN 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   815 FNLRWAEGPESAGepmVVTASTAVAVTVDKRTAIAAAAGVQMKLEFLQRKFWAATR--QCSTVDGPCTQSceDSDLDCFV 892
Cdd:pfam08473  138 SSYRPNEEEDDTS---GILVSAAVELIIDGTLLKPAVVGVKLDDSWWMEFFSNTTRkdQCDEECCGCKGN--DDLLCCVL 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   893 IDNNGFILISKR---SRETGRFLGEVDGAVLTQLLSMGVFSQVTMYDYQAMCKPSSHHHSAAQP--LVSPISAFLTATRW 967
Cdd:pfam08473  213 DDDGGFLMMSNQddyIEQIGFFFGEDDPLLMSLLNNSSFYTKKTSYDYQSCCPPKESSKAAAGRrsVVVPTIADLLNLWW 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   968 LLQELVLFLLEWSVWGSWYDRGAEAKSVFHHSHKHKKQdplQPCDTEYPVFVYQPAIREANGIVECGPCQKVFVVQQIPN 1047
Cdd:pfam08473  293 WTSAAAWSIQQQLLVSLTFPSFLAAEDVADEIMDAMKE---ESCITEQTQYFFNNSNSSFSGVIDCGNCSRYFAAEKLNT 369

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 132566536  1048 SNLLLLVTD--PTCDCSIFPPVLQEATEVKYNasvKCDRMRSQKLRRR-PDSCHAFHPEENAQDCG 1110
Cdd:pfam08473  370 TNLLFVVADakGTCSSCDSMLLQQAEQSSDGP---PCCELVQNPRYRKgPDCCFDNNAEEDTDDCG 432
HK_sensor super family cl38916
Sensor domains of Histidine Kinase receptors; Histidine kinase (HK) receptors are part of ...
 539-654 5.35e-07

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: 48.53  E-value: 5.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  539 ELMKLAPRYKLGVHGYAFLNTNNGYILSHPDlrplyregKKLKPKPNYNSvdlsevewEDQAESLRTAMINRETGTLSMD 618
Cdd:cd12912     1 ELSEIISSIKIGETGYAFLVDKDGTIIAHPD--------KELVGKKISDD--------EAAEEELAKKMLAGKSGSVEYT 64

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 132566536  619 vkvpmDKGKRVLfltndYFFTDISDTPFSLGVVLSR 654
Cdd:cd12912    65 -----FNGEKKY-----VAYAPIPGTGWSLVVVVPE 90
HK_sensor super family cl38916
Sensor domains of Histidine Kinase receptors; Histidine kinase (HK) receptors are part of ...
 484-537 7.60e-03

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 cd12913:

Pssm-ID: 365792  Cd Length: 139  Bit Score: 37.89  E-value: 7.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 132566536  484 DIIWTEAYMDSKLLSsqaqslTLLTTVAMPVFSKknetrshGILLGVVGSDVAL 537
Cdd:cd12913    99 KPVWTEPYIDEVGTG------VLMITISVPIYDN-------GKFIGVVGVDISL 139
 
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 ...
 277-460 1.79e-82

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: 266.57  E-value: 1.79e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  277 RNRGWYIQAATSPKDIVILVDVSGSMKGLRMTIAKHTITTILDTLGENDFINIIAYNDYVHYIEPCFKGILVQADRDNRE 356
Cdd:cd01463     1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFNDTLVQATTSNKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  357 HFKLLVEELMVKGVGVVDQALREAFQIL---KQFQEAKQGSLCNQAIMLISDGAVEDYEPVFEKYNWPD---CKVRVFTY 430
Cdd:cd01463    81 VLKEALDMLEAKGIANYTKALEFAFSLLlknLQSNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKnseIPVRVFTY 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 132566536  431 LIGREVSFADRMKWIACNNKGYYTQISTLA 460
Cdd:cd01463   161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 148-264 1.92e-56

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: 190.97  E-value: 1.92e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   148 AEEADLNHEFNES--LVFDYYNSVLINERDE---KGNFVELGAEFLLESNAHFSNLPVNTSISSVQLPTNVYNKDPDILN 222
Cdd:pfam08399    1 AEKAAEDHEWNDNvpNDFQYYNAKYSNDVGEdyeKGNNVPLSKEFVLTPNPHFYNIPVNTNYSAVHVPTNVYDRAPDVLN 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 132566536   223 GVYMSEALNAVFVENFQRDPTLTWQYFGSATGFFRIYPGIKW 264
Cdd:pfam08399   81 GINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VGCC_alpha2 pfam08473
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 661-1110 7.94e-26

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: 112.09  E-value: 7.94e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   661 LLGNTSVEEGLHDLLHPDlalagdwiYCITDIDPDHRKLSQLEAMIRFLTRKDPD-LECDEELVREVLFDAVVTAPMEAY 739
Cdd:pfam08473    4 LLLPKFFEEGGYTFIAPR--------YYCKDLKPSNNNTEFLEFFNYIIDKTTPNpPCCNNLLNNLLLLDGGITQLLVKW 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   740 WtalalnmSEESEHVVDMAFLGTRAGLLRSslfVGSEKVSDRKFLTPEDEASVFtldrfplwYRQASEH-----PAGSFV 814
Cdd:pfam08473   76 W-------KKQLLNGGLLAVFAATDGGITR---VPPKSAGDWWEEAEETYESSF--------YRRSLDNdyyffTPPYFN 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   815 FNLRWAEGPESAGepmVVTASTAVAVTVDKRTAIAAAAGVQMKLEFLQRKFWAATR--QCSTVDGPCTQSceDSDLDCFV 892
Cdd:pfam08473  138 SSYRPNEEEDDTS---GILVSAAVELIIDGTLLKPAVVGVKLDDSWWMEFFSNTTRkdQCDEECCGCKGN--DDLLCCVL 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   893 IDNNGFILISKR---SRETGRFLGEVDGAVLTQLLSMGVFSQVTMYDYQAMCKPSSHHHSAAQP--LVSPISAFLTATRW 967
Cdd:pfam08473  213 DDDGGFLMMSNQddyIEQIGFFFGEDDPLLMSLLNNSSFYTKKTSYDYQSCCPPKESSKAAAGRrsVVVPTIADLLNLWW 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   968 LLQELVLFLLEWSVWGSWYDRGAEAKSVFHHSHKHKKQdplQPCDTEYPVFVYQPAIREANGIVECGPCQKVFVVQQIPN 1047
Cdd:pfam08473  293 WTSAAAWSIQQQLLVSLTFPSFLAAEDVADEIMDAMKE---ESCITEQTQYFFNNSNSSFSGVIDCGNCSRYFAAEKLNT 369

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 132566536  1048 SNLLLLVTD--PTCDCSIFPPVLQEATEVKYNasvKCDRMRSQKLRRR-PDSCHAFHPEENAQDCG 1110
Cdd:pfam08473  370 TNLLFVVADakGTCSSCDSMLLQQAEQSSDGP---PCCELVQNPRYRKgPDCCFDNNAEEDTDDCG 432
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 291-467 2.93e-16

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 77.88  E-value: 2.93e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536    291 DIVILVDVSGSMKGLRMTIAKHTITTILDTL---GENDFINIIAYNDYVHYIEPCfkgilvqADRDNREHFKLLVEELMV 367
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPL-------NDSRSKDALLEALASLSY 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536    368 KGVGVVD--QALREAFQILKQFQEAKQGSLcNQAIMLISDGAVEDYEPVFEKYNWPDCK--VRVFTYLIGREVSFaDRMK 443
Cdd:smart00327   74 KLGGGTNlgAALQYALENLFSKSAGSRRGA-PKVVILITDGESNDGPKDLLKAAKELKRsgVKVFVVGVGNDVDE-EELK 151

                           170       180
                    ....*....|....*....|....
gi 132566536    444 WIACNNKGYYTQISTLADTQENVM 467
Cdd:smart00327  152 KLASAPGGVYVFLPELLDLLIDLL 175
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 284-464 3.86e-15

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 77.45  E-value: 3.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  284 QAATSPKDIVILVDVSGSMKGLRMTIAKHTITTILDTLGENDFINIIAYNDYVHYIEPcfkgiLVQAdrDNREHFKLLVE 363
Cdd:COG2304    86 AEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLP-----PTPA--TDRAKILAAID 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  364 ELMVKGVGVVDQALREAFQILKQFQEAKQgslcNQAIMLISDGAV-------EDYEPVFEKYNwpDCKVRVFTYLIGREV 436
Cdd:COG2304   159 RLQAGGGTALGAGLELAYELARKHFIPGR----VNRVILLTDGDAnvgitdpEELLKLAEEAR--EEGITLTTLGVGSDY 232

                         170       180
                  ....*....|....*....|....*...
gi 132566536  437 SfADRMKWIACNNKGYYTQISTLADTQE 464
Cdd:COG2304   233 N-EDLLERLADAGGGNYYYIDDPEEAEK 259
VWA_3 pfam13768
von Willebrand factor type A domain;
290-453 5.88e-14

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 70.50  E-value: 5.88e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   290 KDIVILVDVSGSMKGLRMTIaKHTITTILDTLGENDFINIIAYNDYVhyiEPCFKGILVQADRDNREHFKLLVEELMVKG 369
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLP---RPLFPGWRVVSPRSLQEAFQFIKTLQPPLG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   370 VGVVDQALREAFqilkqfqEAKQGSLCNQAIMLISDGAVEDYEPVFEKY-NWPDCKVRVFTYLIGREVSfADRMKWIACN 448
Cdd:pfam13768   77 GSDLLGALKEAV-------RAPASPGYIRHVLLLTDGSPMQGETRVSDLiSRAPGKIRFFAYGLGASIS-APMLQLLAEA 148


                   ....*
gi 132566536   449 NKGYY 453
Cdd:pfam13768  149 SNGTY 153
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 539-654 5.35e-07

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: 48.53  E-value: 5.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  539 ELMKLAPRYKLGVHGYAFLNTNNGYILSHPDlrplyregKKLKPKPNYNSvdlsevewEDQAESLRTAMINRETGTLSMD 618
Cdd:cd12912     1 ELSEIISSIKIGETGYAFLVDKDGTIIAHPD--------KELVGKKISDD--------EAAEEELAKKMLAGKSGSVEYT 64

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 132566536  619 vkvpmDKGKRVLfltndYFFTDISDTPFSLGVVLSR 654
Cdd:cd12912    65 -----FNGEKKY-----VAYAPIPGTGWSLVVVVPE 90
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 509-584 7.75e-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: 45.41  E-value: 7.75e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 132566536   509 TVAMPVFSKKNEtrshgiLLGVVGSDVALRELMKLAPRYKLGVHGYAFLNTNNGYILSHPDLRPLYREGKKLKPKP 584
Cdd:pfam02743  129 TIARPIYDDDGE------VIGVLVADLDLDTLQELLSQIKLGEGGYVFIVDSDGRILAHPLGKNLRSLLAPFLGKS 198
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 484-537 7.60e-03

first 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 first 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: 350338  Cd Length: 139  Bit Score: 37.89  E-value: 7.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 132566536  484 DIIWTEAYMDSKLLSsqaqslTLLTTVAMPVFSKknetrshGILLGVVGSDVAL 537
Cdd:cd12913    99 KPVWTEPYIDEVGTG------VLMITISVPIYDN-------GKFIGVVGVDISL 139
 
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 ...
 277-460 1.79e-82

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: 266.57  E-value: 1.79e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  277 RNRGWYIQAATSPKDIVILVDVSGSMKGLRMTIAKHTITTILDTLGENDFINIIAYNDYVHYIEPCFKGILVQADRDNRE 356
Cdd:cd01463     1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFNDTLVQATTSNKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  357 HFKLLVEELMVKGVGVVDQALREAFQIL---KQFQEAKQGSLCNQAIMLISDGAVEDYEPVFEKYNWPD---CKVRVFTY 430
Cdd:cd01463    81 VLKEALDMLEAKGIANYTKALEFAFSLLlknLQSNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKnseIPVRVFTY 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 132566536  431 LIGREVSFADRMKWIACNNKGYYTQISTLA 460
Cdd:cd01463   161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 148-264 1.92e-56

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: 190.97  E-value: 1.92e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   148 AEEADLNHEFNES--LVFDYYNSVLINERDE---KGNFVELGAEFLLESNAHFSNLPVNTSISSVQLPTNVYNKDPDILN 222
Cdd:pfam08399    1 AEKAAEDHEWNDNvpNDFQYYNAKYSNDVGEdyeKGNNVPLSKEFVLTPNPHFYNIPVNTNYSAVHVPTNVYDRAPDVLN 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 132566536   223 GVYMSEALNAVFVENFQRDPTLTWQYFGSATGFFRIYPGIKW 264
Cdd:pfam08399   81 GINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VGCC_alpha2 pfam08473
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 661-1110 7.94e-26

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: 112.09  E-value: 7.94e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   661 LLGNTSVEEGLHDLLHPDlalagdwiYCITDIDPDHRKLSQLEAMIRFLTRKDPD-LECDEELVREVLFDAVVTAPMEAY 739
Cdd:pfam08473    4 LLLPKFFEEGGYTFIAPR--------YYCKDLKPSNNNTEFLEFFNYIIDKTTPNpPCCNNLLNNLLLLDGGITQLLVKW 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   740 WtalalnmSEESEHVVDMAFLGTRAGLLRSslfVGSEKVSDRKFLTPEDEASVFtldrfplwYRQASEH-----PAGSFV 814
Cdd:pfam08473   76 W-------KKQLLNGGLLAVFAATDGGITR---VPPKSAGDWWEEAEETYESSF--------YRRSLDNdyyffTPPYFN 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   815 FNLRWAEGPESAGepmVVTASTAVAVTVDKRTAIAAAAGVQMKLEFLQRKFWAATR--QCSTVDGPCTQSceDSDLDCFV 892
Cdd:pfam08473  138 SSYRPNEEEDDTS---GILVSAAVELIIDGTLLKPAVVGVKLDDSWWMEFFSNTTRkdQCDEECCGCKGN--DDLLCCVL 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   893 IDNNGFILISKR---SRETGRFLGEVDGAVLTQLLSMGVFSQVTMYDYQAMCKPSSHHHSAAQP--LVSPISAFLTATRW 967
Cdd:pfam08473  213 DDDGGFLMMSNQddyIEQIGFFFGEDDPLLMSLLNNSSFYTKKTSYDYQSCCPPKESSKAAAGRrsVVVPTIADLLNLWW 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   968 LLQELVLFLLEWSVWGSWYDRGAEAKSVFHHSHKHKKQdplQPCDTEYPVFVYQPAIREANGIVECGPCQKVFVVQQIPN 1047
Cdd:pfam08473  293 WTSAAAWSIQQQLLVSLTFPSFLAAEDVADEIMDAMKE---ESCITEQTQYFFNNSNSSFSGVIDCGNCSRYFAAEKLNT 369

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 132566536  1048 SNLLLLVTD--PTCDCSIFPPVLQEATEVKYNasvKCDRMRSQKLRRR-PDSCHAFHPEENAQDCG 1110
Cdd:pfam08473  370 TNLLFVVADakGTCSSCDSMLLQQAEQSSDGP---PCCELVQNPRYRKgPDCCFDNNAEEDTDDCG 432
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 289-467 1.37e-16

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: 78.41  E-value: 1.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  289 PKDIVILVDVSGSMKGLRMTIAKHTITTILDTLGENDFINIIAYNDYVHYIEPCfkgiLVQADRDNREHFKLLVEELMVK 368
Cdd:cd01461     2 PKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPS----SVSATAENVAAAIEYVNRLQAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  369 GVGVVDQALREAFQILkqfqEAKQGSLcnQAIMLISDGAVEDYEPVFEKY-NWPDCKVRVFTYLIGREVSFAdRMKWIAC 447
Cdd:cd01461    78 GGTNMNDALEAALELL----NSSPGSV--PQIILLTDGEVTNESQILKNVrEALSGRIRLFTFGIGSDVNTY-LLERLAR 150

                         170       180
                  ....*....|....*....|
gi 132566536  448 NNKGYYTQISTLADTQENVM 467
Cdd:cd01461   151 EGRGIARRIYETDDIESQLL 170
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 291-467 2.93e-16

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 77.88  E-value: 2.93e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536    291 DIVILVDVSGSMKGLRMTIAKHTITTILDTL---GENDFINIIAYNDYVHYIEPCfkgilvqADRDNREHFKLLVEELMV 367
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPL-------NDSRSKDALLEALASLSY 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536    368 KGVGVVD--QALREAFQILKQFQEAKQGSLcNQAIMLISDGAVEDYEPVFEKYNWPDCK--VRVFTYLIGREVSFaDRMK 443
Cdd:smart00327   74 KLGGGTNlgAALQYALENLFSKSAGSRRGA-PKVVILITDGESNDGPKDLLKAAKELKRsgVKVFVVGVGNDVDE-EELK 151

                           170       180
                    ....*....|....*....|....
gi 132566536    444 WIACNNKGYYTQISTLADTQENVM 467
Cdd:smart00327  152 KLASAPGGVYVFLPELLDLLIDLL 175
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 284-464 3.86e-15

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 77.45  E-value: 3.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  284 QAATSPKDIVILVDVSGSMKGLRMTIAKHTITTILDTLGENDFINIIAYNDYVHYIEPcfkgiLVQAdrDNREHFKLLVE 363
Cdd:COG2304    86 AEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLP-----PTPA--TDRAKILAAID 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  364 ELMVKGVGVVDQALREAFQILKQFQEAKQgslcNQAIMLISDGAV-------EDYEPVFEKYNwpDCKVRVFTYLIGREV 436
Cdd:COG2304   159 RLQAGGGTALGAGLELAYELARKHFIPGR----VNRVILLTDGDAnvgitdpEELLKLAEEAR--EEGITLTTLGVGSDY 232

                         170       180
                  ....*....|....*....|....*...
gi 132566536  437 SfADRMKWIACNNKGYYTQISTLADTQE 464
Cdd:COG2304   233 N-EDLLERLADAGGGNYYYIDDPEEAEK 259
VWA_3 pfam13768
von Willebrand factor type A domain;
290-453 5.88e-14

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 70.50  E-value: 5.88e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   290 KDIVILVDVSGSMKGLRMTIaKHTITTILDTLGENDFINIIAYNDYVhyiEPCFKGILVQADRDNREHFKLLVEELMVKG 369
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLP---RPLFPGWRVVSPRSLQEAFQFIKTLQPPLG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   370 VGVVDQALREAFqilkqfqEAKQGSLCNQAIMLISDGAVEDYEPVFEKY-NWPDCKVRVFTYLIGREVSfADRMKWIACN 448
Cdd:pfam13768   77 GSDLLGALKEAV-------RAPASPGYIRHVLLLTDGSPMQGETRVSDLiSRAPGKIRFFAYGLGASIS-APMLQLLAEA 148


                   ....*
gi 132566536   449 NKGYY 453
Cdd:pfam13768  149 SNGTY 153
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 291-453 3.01e-13

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: 68.75  E-value: 3.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  291 DIVILVDVSGSMKGLRMTIAKHTITTILDTL---GENDFINIIAYNDYVHYIEPcfkgilvQADRDNREHFKLLVEELMV 367
Cdd:cd00198     2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLsasPPGDRVGLVTFGSNARVVLP-------LTTDTDKADLLEAIDALKK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  368 KGVGV--VDQALREAFQILKQFQEAKQGslcnQAIMLISDGAVEDYEPVFEKY--NWPDCKVRVFTYLIGREVSFADrMK 443
Cdd:cd00198    75 GLGGGtnIGAALRLALELLKSAKRPNAR----RVIILLTDGEPNDGPELLAEAarELRKLGITVYTIGIGDDANEDE-LK 149

                         170
                  ....*....|
gi 132566536  444 WIACNNKGYY 453
Cdd:cd00198   150 EIADKTTGGA 159
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 288-464 5.66e-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: 70.35  E-value: 5.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  288 SPKDIVILVDVSGSMKGL-RMTIAKHTITTILDTLGENDFINIIAYNDYVHyiepcfkgiLVQADRDNREHFKLLVEELM 366
Cdd:COG1240    91 RGRDVVLVVDASGSMAAEnRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAE---------VLLPLTRDREALKRALDELP 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  367 VKGVGVVDQALREAFQILKQFQEAKQgslcnQAIMLISDGA----VEDYEPVFEKYNwpDCKVRVFTYLIGREVSFADRM 442
Cdd:COG1240   162 PGGGTPLGDALALALELLKRADPARR-----KVIVLLTDGRdnagRIDPLEAAELAA--AAGIRIYTIGVGTEAVDEGLL 234

                         170       180
                  ....*....|....*....|..
gi 132566536  443 KWIACNNKGYYTQISTLADTQE 464
Cdd:COG1240   235 REIAEATGGRYFRADDLSELAA 256
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 289-446 1.27e-12

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 69.32  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  289 PKDIVILVDVSGSMKGLRMTIAKHTITTILDTLGENDFINIIAYNDYVHYiepcfkGILVQADRDNREHFKLLveeLMVK 368
Cdd:COG2425   118 EGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVE------DLPLTADDGLEDAIEFL---SGLF 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  369 GVG--VVDQALREAFQILKQFQEAkqgslcNQAIMLISDGAV-EDYEPVFEKYNWPDCKVRVFTYLIGREvSFADRMKWI 445
Cdd:COG2425   189 AGGgtDIAPALRAALELLEEPDYR------NADIVLITDGEAgVSPEELLREVRAKESGVRLFTVAIGDA-GNPGLLEAL 261


                  .
gi 132566536  446 A 446
Cdd:COG2425   262 A 262
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 291-454 2.42e-09

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


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 57.40  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  291 DIVILVDVSGSMKGLRMTIAKHTITTILDTLGENDFINIIAYNDYVHYIEPcfkgiLVQADRDNREHFKLLVEELmVKGV 370
Cdd:cd01466     2 DLVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSP-----LRRMTAKGKRSAKRVVDGL-QAGG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  371 GV-VDQALREAFQILKQFQEAKQGSlcnqAIMLISDGAVEDYEPVFEKYNWPdckVRVFTYLIGREVSfADRMKWIACNN 449
Cdd:cd01466    76 GTnVVGGLKKALKVLGDRRQKNPVA----SIMLLSDGQDNHGAVVLRADNAP---IPIHTFGLGASHD-PALLAFIAEIT 147


                  ....*
gi 132566536  450 KGYYT 454
Cdd:cd01466   148 GGTFS 152
VWA pfam00092
von Willebrand factor type A domain;
291-413 1.87e-07

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 52.28  E-value: 1.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   291 DIVILVDVSGSMKGLRMTIAKHTITTILDTLG---ENDFINIIAYNDYVHyiepcfkgILVQADRD-NREHFKLLVEELM 366
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVR--------TEFPLNDYsSKEELLSAVDNLR 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 132566536   367 VKGVG--VVDQALREAfqiLKQFQEAKQGSLCN--QAIMLISDGAVEDYEP 413
Cdd:pfam00092   73 YLGGGttNTGKALKYA---LENLFSSAAGARPGapKVVVLLTDGRSQDGDP 120
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 539-654 5.35e-07

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: 48.53  E-value: 5.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  539 ELMKLAPRYKLGVHGYAFLNTNNGYILSHPDlrplyregKKLKPKPNYNSvdlsevewEDQAESLRTAMINRETGTLSMD 618
Cdd:cd12912     1 ELSEIISSIKIGETGYAFLVDKDGTIIAHPD--------KELVGKKISDD--------EAAEEELAKKMLAGKSGSVEYT 64

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 132566536  619 vkvpmDKGKRVLfltndYFFTDISDTPFSLGVVLSR 654
Cdd:cd12912    65 -----FNGEKKY-----VAYAPIPGTGWSLVVVVPE 90
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
291-417 2.20e-06

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 49.54  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  291 DIVILVDVSGSMKGLRMTIAKHTITTILDTL------GENDFINIIAYNDYVHYIEPcfkgiLVQADrdnrehfKLLVEE 364
Cdd:COG4245     7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELrqdpyaLETVEVSVITFDGEAKVLLP-----LTDLE-------DFQPPD 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 132566536  365 LMVKGVGVVDQALREA---FQILKQFQEAKQGSLCNQAIMLISDGAV--EDYEPVFEK 417
Cdd:COG4245    75 LSASGGTPLGAALELLldlIERRVQKYTAEGKGDWRPVVFLITDGEPtdSDWEAALQR 132
VWA_2 pfam13519
von Willebrand factor type A domain;
292-386 1.45e-05

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 44.98  E-value: 1.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536   292 IVILVDVSGSM-----KGLRMTIAKHTITTILDTLGeNDFINIIAYNDYVHyiepcfkgILVQADRDNREHFKLLVEELM 366
Cdd:pfam13519    1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSLP-GDRVGLVTFGDGPE--------VLIPLTKDRAKILRALRRLEP 71

                           90       100
                   ....*....|....*....|
gi 132566536   367 VKGVGVVDQALREAFQILKQ 386
Cdd:pfam13519   72 KGGGTNLAAALQLARAALKH 91
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 291-416 1.56e-05

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 46.52  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  291 DIVILVDVSGSMKGLRMTIAKHTITTILDTL---GENDFINIIAYNDYVHyIEPCFKgilvqaDRDNREHFKLLVEELMV 367
Cdd:cd01450     2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLdigPDKTRVGLVQYSDDVR-VEFSLN------DYKSKDDLLKAVKNLKY 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 132566536  368 KGVGV--VDQALREAFQILkqFQEAKQGSLCNQAIMLISDGAVEDYEPVFE 416
Cdd:cd01450    75 LGGGGtnTGKALQYALEQL--FSESNARENVPKVIIVLTDGRSDDGGDPKE 123
PDC2_HK_sensor cd18774
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, ...
 539-654 3.17e-05

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: 43.59  E-value: 3.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  539 ELMKLAPRYKLGVHGYAFLNTNNGYILSHPDlrplyrEGKKLKPKPNYNSVDLSEvewedqaeslrtAMINRETGTLSMd 618
Cdd:cd18774     1 YLSDLLSSIKLGETGYAFLVDSDGTILAHPP------KELVGKGKSLDDLALLAA------------LLLAGESGTFEY- 61

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 132566536  619 vkvPMDKGKRVLfltndYFFTDISDTPFSLGVVLSR 654
Cdd:cd18774    62 ---TSDDGVERL-----VAYRPVPGTPWVVVVGVPE 89
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 293-406 7.16e-05

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: 44.57  E-value: 7.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  293 VILVDVSGSMKGLRMTIAKHTITTILDTLGENDFINIIAYNDYVHYIEPcfkgilVQADRDnREHFKLLVEELMVKGVGV 372
Cdd:cd01465     4 VFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAETVLP------ATPVRD-KAAILAAIDRLTAGGSTA 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 132566536  373 VDQALREAFQILKQFQEAKQgslcNQAIMLISDG 406
Cdd:cd01465    77 GGAGIQLGYQEAQKHFVPGG----VNRILLATDG 106
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 509-584 7.75e-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: 45.41  E-value: 7.75e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 132566536   509 TVAMPVFSKKNEtrshgiLLGVVGSDVALRELMKLAPRYKLGVHGYAFLNTNNGYILSHPDLRPLYREGKKLKPKP 584
Cdd:pfam02743  129 TIARPIYDDDGE------VIGVLVADLDLDTLQELLSQIKLGEGGYVFIVDSDGRILAHPLGKNLRSLLAPFLGKS 198
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 290-406 1.01e-03

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


Pssm-ID: 238739 [Multi-domain]  Cd Length: 152  Bit Score: 40.79  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132566536  290 KDIVILVDVSGSMKGLRMTIAKHTITTILDTlgendfinIIAYNDYVHYIepCFKGILVQADRDNREHFKLLVEELM-VK 368
Cdd:cd01462     1 GPVILLVDQSGSMYGAPEEVAKAVALALLRI--------ALAENRDTYLI--LFDSEFQTKIVDKTDDLEEPVEFLSgVQ 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 132566536  369 GVGVVD--QALREAFQILKqfQEAKQGSlcnqAIMLISDG 406
Cdd:cd01462    71 LGGGTDinKALRYALELIE--RRDPRKA----DIVLITDG 104
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 484-537 7.60e-03

first 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 first 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: 350338  Cd Length: 139  Bit Score: 37.89  E-value: 7.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 132566536  484 DIIWTEAYMDSKLLSsqaqslTLLTTVAMPVFSKknetrshGILLGVVGSDVAL 537
Cdd:cd12913    99 KPVWTEPYIDEVGTG------VLMITISVPIYDN-------GKFIGVVGVDISL 139
 
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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