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Conserved domains on  [gi|1631970699|ref|NP_001028554|]
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voltage-dependent calcium channel subunit alpha-2/delta-4 isoform 1 precursor [Mus musculus]

Protein Classification

VWA_N and vWA_VGCC_like domain-containing protein( domain architecture ID 13750233)

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
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 256-439 8.65e-83

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: 267.34  E-value: 8.65e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  256 RNRGWYIQAATSPKDIVILVDISGSMKGLRMAIAKHTITTILDTLGENDFVNIIAYNDYVHYIEPCFKGILVQADRDNRE 335
Cdd:cd01463      1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFNDTLVQATTSNKK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  336 HFKQLVDELMVKGVGVVSQALIEAFEIL---KQFQESKQGSLCNQAIMLITDGAVEDYEPVFETYNWPDR---KVRVFTY 409
Cdd:cd01463     81 VLKEALDMLEAKGIANYTKALEFAFSLLlknLQSNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNseiPVRVFTY 160

                          170       180       190
                   ....*....|....*....|....*....|
gi 1631970699  410 LIGREVTFADRMKWIACNNKGYYTQISTLA 439
Cdd:cd01463    161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 127-243 3.26e-53

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: 181.73  E-value: 3.26e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  127 AEEADLNHEFNASLVFN--YYNSVLINEKDD---KGNYVELGAEFLLESDAHFSNLRVNVSMSSVQLPTNVYNKDPDILN 201
Cdd:pfam08399    1 AEKAAEDHEWNDNVPNDfqYYNAKYSNDVGEdyeKGNNVPLSKEFVLTPNPHFYNIPVNTNYSAVHVPTNVYDRAPDVLN 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1631970699  202 GVYMSEALNPVFVENFQRDPTLTWQYFGSSTGFFRIYPGIKW 243
Cdd:pfam08399   81 GINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VGCC_alpha2 super family cl07190
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 640-1089 2.90e-22

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: 100.92  E-value: 2.90e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  640 LLGNTSVEEGLHDLLHPDltlasdwiYCITDIDPDHRKLSQLEAVVRFLTGVDPD-LECDEELVREVLFDAVVTAPMEAY 718
Cdd:pfam08473    4 LLLPKFFEEGGYTFIAPR--------YYCKDLKPSNNNTEFLEFFNYIIDKTTPNpPCCNNLLNNLLLLDGGITQLLVKW 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  719 WtalalniSEESEPGVDVAFLGTRAGLLRRslfVGSEKVSDRKFLTPEDEASIFtmdhfplwYRQASEQ-----PPGSFV 793
Cdd:pfam08473   76 W-------KKQLLNGGLLAVFAATDGGITR---VPPKSAGDWWEEAEETYESSF--------YRRSLDNdyyffTPPYFN 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  794 FNLRWAEGPDSPgkpVAVRASTAVTVTVDGKTAIAAAVGIQmqadyLQRQFWAA-------MQQCNAVEGPCLKSceDTD 866
Cdd:pfam08473  138 SSYRPNEEEDDT---SGILVSAAVELIIDGTLLKPAVVGVK-----LDDSWWMEffsnttrKDQCDEECCGCKGN--DDL 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  867 LDCFVIDNNGFVLISERP---QEMGRLLGEADGALMKQLLSMGVFSRVTMYDYQAMCKPPDHHHSAA--ESLFSPLSAFL 941
Cdd:pfam08473  208 LCCVLDDDGGFLMMSNQDdyiEQIGFFFGEDDPLLMSLLNNSSFYTKKTSYDYQSCCPPKESSKAAAgrRSVVVPTIADL 287

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  942 MVARWllhecllflleWS--AWGSWQDK--GSEAKSVFHHSHKHKKQDLLHP----CDTEYPVFVHQTAIQEANGIIECG 1013
Cdd:pfam08473  288 LNLWW-----------WTsaAAWSIQQQllVSLTFPSFLAAEDVADEIMDAMkeesCITEQTQYFFNNSNSSFSGVIDCG 356

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1631970699 1014 GCQKTFVMQQIPRSNLLLLVTD-RTCDCSAHSPILQEATEVKyNASVKCDrmRSQKPRRRPGS--CHAFHPEENAQDCG 1089
Cdd:pfam08473  357 NCSRYFAAEKLNTTNLLFVVADaKGTCSSCDSMLLQQAEQSS-DGPPCCE--LVQNPRYRKGPdcCFDNNAEEDTDDCG 432
HK_sensor super family cl38916
Sensor domains of Histidine Kinase receptors; Histidine kinase (HK) receptors are part of ...
 518-631 3.10e-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: 49.30  E-value: 3.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  518 ELMKLAPRYKLGVHGYAFLNTNNGYILSHPDlrplyregKKLRPKPNYNSvdlsevewEDQAEILRTAMINGETGSHSMD 597
Cdd:cd12912      1 ELSEIISSIKIGETGYAFLVDKDGTIIAHPD--------KELVGKKISDD--------EAAEEELAKKMLAGKSGSVEYT 64

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1631970699  598 vkvplDKGKRVLfltndYFFTDISDTPFSLGVVL 631
Cdd:cd12912     65 -----FNGEKKY-----VAYAPIPGTGWSLVVVV 88
HK_sensor super family cl38916
Sensor domains of Histidine Kinase receptors; Histidine kinase (HK) receptors are part of ...
 463-516 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 1631970699  463 DIIWTEAYMDSrlftSEAQSLMllTTVAMPVFSKknetrshGILLGVVGSDVTL 516
Cdd:cd12913     99 KPVWTEPYIDE----VGTGVLM--ITISVPIYDN-------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 ...
 256-439 8.65e-83

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: 267.34  E-value: 8.65e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  256 RNRGWYIQAATSPKDIVILVDISGSMKGLRMAIAKHTITTILDTLGENDFVNIIAYNDYVHYIEPCFKGILVQADRDNRE 335
Cdd:cd01463      1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFNDTLVQATTSNKK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  336 HFKQLVDELMVKGVGVVSQALIEAFEIL---KQFQESKQGSLCNQAIMLITDGAVEDYEPVFETYNWPDR---KVRVFTY 409
Cdd:cd01463     81 VLKEALDMLEAKGIANYTKALEFAFSLLlknLQSNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNseiPVRVFTY 160

                          170       180       190
                   ....*....|....*....|....*....|
gi 1631970699  410 LIGREVTFADRMKWIACNNKGYYTQISTLA 439
Cdd:cd01463    161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 127-243 3.26e-53

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: 181.73  E-value: 3.26e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  127 AEEADLNHEFNASLVFN--YYNSVLINEKDD---KGNYVELGAEFLLESDAHFSNLRVNVSMSSVQLPTNVYNKDPDILN 201
Cdd:pfam08399    1 AEKAAEDHEWNDNVPNDfqYYNAKYSNDVGEdyeKGNNVPLSKEFVLTPNPHFYNIPVNTNYSAVHVPTNVYDRAPDVLN 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1631970699  202 GVYMSEALNPVFVENFQRDPTLTWQYFGSSTGFFRIYPGIKW 243
Cdd:pfam08399   81 GINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VGCC_alpha2 pfam08473
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 640-1089 2.90e-22

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: 100.92  E-value: 2.90e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  640 LLGNTSVEEGLHDLLHPDltlasdwiYCITDIDPDHRKLSQLEAVVRFLTGVDPD-LECDEELVREVLFDAVVTAPMEAY 718
Cdd:pfam08473    4 LLLPKFFEEGGYTFIAPR--------YYCKDLKPSNNNTEFLEFFNYIIDKTTPNpPCCNNLLNNLLLLDGGITQLLVKW 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  719 WtalalniSEESEPGVDVAFLGTRAGLLRRslfVGSEKVSDRKFLTPEDEASIFtmdhfplwYRQASEQ-----PPGSFV 793
Cdd:pfam08473   76 W-------KKQLLNGGLLAVFAATDGGITR---VPPKSAGDWWEEAEETYESSF--------YRRSLDNdyyffTPPYFN 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  794 FNLRWAEGPDSPgkpVAVRASTAVTVTVDGKTAIAAAVGIQmqadyLQRQFWAA-------MQQCNAVEGPCLKSceDTD 866
Cdd:pfam08473  138 SSYRPNEEEDDT---SGILVSAAVELIIDGTLLKPAVVGVK-----LDDSWWMEffsnttrKDQCDEECCGCKGN--DDL 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  867 LDCFVIDNNGFVLISERP---QEMGRLLGEADGALMKQLLSMGVFSRVTMYDYQAMCKPPDHHHSAA--ESLFSPLSAFL 941
Cdd:pfam08473  208 LCCVLDDDGGFLMMSNQDdyiEQIGFFFGEDDPLLMSLLNNSSFYTKKTSYDYQSCCPPKESSKAAAgrRSVVVPTIADL 287

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  942 MVARWllhecllflleWS--AWGSWQDK--GSEAKSVFHHSHKHKKQDLLHP----CDTEYPVFVHQTAIQEANGIIECG 1013
Cdd:pfam08473  288 LNLWW-----------WTsaAAWSIQQQllVSLTFPSFLAAEDVADEIMDAMkeesCITEQTQYFFNNSNSSFSGVIDCG 356

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1631970699 1014 GCQKTFVMQQIPRSNLLLLVTD-RTCDCSAHSPILQEATEVKyNASVKCDrmRSQKPRRRPGS--CHAFHPEENAQDCG 1089
Cdd:pfam08473  357 NCSRYFAAEKLNTTNLLFVVADaKGTCSSCDSMLLQQAEQSS-DGPPCCE--LVQNPRYRKGPdcCFDNNAEEDTDDCG 432
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 270-446 8.57e-18

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 82.12  E-value: 8.57e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699   270 DIVILVDISGSMKGLRMAIAKHTITTILDTL---GENDFVNIIAYNDYVHYIEPCfkgilvqADRDNREHFKQLVDELMV 346
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPL-------NDSRSKDALLEALASLSY 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699   347 KGVGVVS--QALIEAFEILKQFQESKQGSLcNQAIMLITDGAVEDYEPVFETYNWPDRKVRVFTYLIG-REVTFADRMKW 423
Cdd:smart00327   74 KLGGGTNlgAALQYALENLFSKSAGSRRGA-PKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGvGNDVDEEELKK 152

                           170       180
                    ....*....|....*....|...
gi 1631970699   424 IACNNKGYYTQISTLADAQESVM 446
Cdd:smart00327  153 LASAPGGVYVFLPELLDLLIDLL 175
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 263-443 1.81e-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: 84.38  E-value: 1.81e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  263 QAATSPKDIVILVDISGSMKGLRMAIAKHTITTILDTLGENDFVNIIAYNDYVHYIEPcfkgiLVQAdrDNREHFKQLVD 342
Cdd:COG2304     86 AEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLP-----PTPA--TDRAKILAAID 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  343 ELMVKGVGVVSQALIEAFEILKQFQESKQgslcNQAIMLITDGAV-------EDYEPVFETYNwpDRKVRVFTYLIGREV 415
Cdd:COG2304    159 RLQAGGGTALGAGLELAYELARKHFIPGR----VNRVILLTDGDAnvgitdpEELLKLAEEAR--EEGITLTTLGVGSDY 232

                          170       180
                   ....*....|....*....|....*...
gi 1631970699  416 TfADRMKWIACNNKGYYTQISTLADAQE 443
Cdd:COG2304    233 N-EDLLERLADAGGGNYYYIDDPEEAEK 259
VWA_3 pfam13768
von Willebrand factor type A domain;
269-432 2.20e-12

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 65.88  E-value: 2.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  269 KDIVILVDISGSMKGLRMAIaKHTITTILDTLGENDFVNIIAYNDYVhyiEPCFKGILVQADRDNREHFkQLVDELMVK- 347
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLP---RPLFPGWRVVSPRSLQEAF-QFIKTLQPPl 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  348 GVGVVSQALIEAFEilkqfQESKQGslCNQAIMLITDGAVEDYEPVFETY-NWPDRKVRVFTYLIGREVTfADRMKWIAC 426
Cdd:pfam13768   76 GGSDLLGALKEAVR-----APASPG--YIRHVLLLTDGSPMQGETRVSDLiSRAPGKIRFFAYGLGASIS-APMLQLLAE 147


                   ....*.
gi 1631970699  427 NNKGYY 432
Cdd:pfam13768  148 ASNGTY 153
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 518-631 3.10e-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: 49.30  E-value: 3.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  518 ELMKLAPRYKLGVHGYAFLNTNNGYILSHPDlrplyregKKLRPKPNYNSvdlsevewEDQAEILRTAMINGETGSHSMD 597
Cdd:cd12912      1 ELSEIISSIKIGETGYAFLVDKDGTIIAHPD--------KELVGKKISDD--------EAAEEELAKKMLAGKSGSVEYT 64

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1631970699  598 vkvplDKGKRVLfltndYFFTDISDTPFSLGVVL 631
Cdd:cd12912     65 -----FNGEKKY-----VAYAPIPGTGWSLVVVV 88
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 488-589 3.32e-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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 46.56  E-value: 3.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  488 TVAMPVFSKKNEtrshgiLLGVVGSDVTLRELMKLAPRYKLGVHGYAFLNTNNGYILSHPDLRPLYRE-----GKKLRPK 562
Cdd:pfam02743  129 TIARPIYDDDGE------VIGVLVADLDLDTLQELLSQIKLGEGGYVFIVDSDGRILAHPLGKNLRSLlapflGKSLADA 202

                           90       100
                   ....*....|....*....|....*..
gi 1631970699  563 PNYNSVDLSEVEWEDQAEILRTAMING 589
Cdd:pfam02743  203 LPGSGITEIAVDLDGEDYLVAYAPIPG 229
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 463-516 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 1631970699  463 DIIWTEAYMDSrlftSEAQSLMllTTVAMPVFSKknetrshGILLGVVGSDVTL 516
Cdd:cd12913     99 KPVWTEPYIDE----VGTGVLM--ITISVPIYDN-------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 ...
 256-439 8.65e-83

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: 267.34  E-value: 8.65e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  256 RNRGWYIQAATSPKDIVILVDISGSMKGLRMAIAKHTITTILDTLGENDFVNIIAYNDYVHYIEPCFKGILVQADRDNRE 335
Cdd:cd01463      1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFNDTLVQATTSNKK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  336 HFKQLVDELMVKGVGVVSQALIEAFEIL---KQFQESKQGSLCNQAIMLITDGAVEDYEPVFETYNWPDR---KVRVFTY 409
Cdd:cd01463     81 VLKEALDMLEAKGIANYTKALEFAFSLLlknLQSNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNseiPVRVFTY 160

                          170       180       190
                   ....*....|....*....|....*....|
gi 1631970699  410 LIGREVTFADRMKWIACNNKGYYTQISTLA 439
Cdd:cd01463    161 LIGREVTDRREIQWMACENKGYYSHIQSLD 190
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 127-243 3.26e-53

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: 181.73  E-value: 3.26e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  127 AEEADLNHEFNASLVFN--YYNSVLINEKDD---KGNYVELGAEFLLESDAHFSNLRVNVSMSSVQLPTNVYNKDPDILN 201
Cdd:pfam08399    1 AEKAAEDHEWNDNVPNDfqYYNAKYSNDVGEdyeKGNNVPLSKEFVLTPNPHFYNIPVNTNYSAVHVPTNVYDRAPDVLN 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1631970699  202 GVYMSEALNPVFVENFQRDPTLTWQYFGSSTGFFRIYPGIKW 243
Cdd:pfam08399   81 GINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VGCC_alpha2 pfam08473
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 640-1089 2.90e-22

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: 100.92  E-value: 2.90e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  640 LLGNTSVEEGLHDLLHPDltlasdwiYCITDIDPDHRKLSQLEAVVRFLTGVDPD-LECDEELVREVLFDAVVTAPMEAY 718
Cdd:pfam08473    4 LLLPKFFEEGGYTFIAPR--------YYCKDLKPSNNNTEFLEFFNYIIDKTTPNpPCCNNLLNNLLLLDGGITQLLVKW 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  719 WtalalniSEESEPGVDVAFLGTRAGLLRRslfVGSEKVSDRKFLTPEDEASIFtmdhfplwYRQASEQ-----PPGSFV 793
Cdd:pfam08473   76 W-------KKQLLNGGLLAVFAATDGGITR---VPPKSAGDWWEEAEETYESSF--------YRRSLDNdyyffTPPYFN 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  794 FNLRWAEGPDSPgkpVAVRASTAVTVTVDGKTAIAAAVGIQmqadyLQRQFWAA-------MQQCNAVEGPCLKSceDTD 866
Cdd:pfam08473  138 SSYRPNEEEDDT---SGILVSAAVELIIDGTLLKPAVVGVK-----LDDSWWMEffsnttrKDQCDEECCGCKGN--DDL 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  867 LDCFVIDNNGFVLISERP---QEMGRLLGEADGALMKQLLSMGVFSRVTMYDYQAMCKPPDHHHSAA--ESLFSPLSAFL 941
Cdd:pfam08473  208 LCCVLDDDGGFLMMSNQDdyiEQIGFFFGEDDPLLMSLLNNSSFYTKKTSYDYQSCCPPKESSKAAAgrRSVVVPTIADL 287

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  942 MVARWllhecllflleWS--AWGSWQDK--GSEAKSVFHHSHKHKKQDLLHP----CDTEYPVFVHQTAIQEANGIIECG 1013
Cdd:pfam08473  288 LNLWW-----------WTsaAAWSIQQQllVSLTFPSFLAAEDVADEIMDAMkeesCITEQTQYFFNNSNSSFSGVIDCG 356

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1631970699 1014 GCQKTFVMQQIPRSNLLLLVTD-RTCDCSAHSPILQEATEVKyNASVKCDrmRSQKPRRRPGS--CHAFHPEENAQDCG 1089
Cdd:pfam08473  357 NCSRYFAAEKLNTTNLLFVVADaKGTCSSCDSMLLQQAEQSS-DGPPCCE--LVQNPRYRKGPdcCFDNNAEEDTDDCG 432
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 268-446 1.78e-19

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: 86.89  E-value: 1.78e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  268 PKDIVILVDISGSMKGLRMAIAKHTITTILDTLGENDFVNIIAYNDYVHYIEPCfkgiLVQADRDNREHFKQLVDELMVK 347
Cdd:cd01461      2 PKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPS----SVSATAENVAAAIEYVNRLQAL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  348 GVGVVSQALIEAFEILkqfqESKQGSLcnQAIMLITDGAVEDYEPVFETY-NWPDRKVRVFTYLIGREVTFAdRMKWIAC 426
Cdd:cd01461     78 GGTNMNDALEAALELL----NSSPGSV--PQIILLTDGEVTNESQILKNVrEALSGRIRLFTFGIGSDVNTY-LLERLAR 150

                          170       180
                   ....*....|....*....|
gi 1631970699  427 NNKGYYTQISTLADAQESVM 446
Cdd:cd01461    151 EGRGIARRIYETDDIESQLL 170
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 270-446 8.57e-18

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


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 82.12  E-value: 8.57e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699   270 DIVILVDISGSMKGLRMAIAKHTITTILDTL---GENDFVNIIAYNDYVHYIEPCfkgilvqADRDNREHFKQLVDELMV 346
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPL-------NDSRSKDALLEALASLSY 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699   347 KGVGVVS--QALIEAFEILKQFQESKQGSLcNQAIMLITDGAVEDYEPVFETYNWPDRKVRVFTYLIG-REVTFADRMKW 423
Cdd:smart00327   74 KLGGGTNlgAALQYALENLFSKSAGSRRGA-PKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGvGNDVDEEELKK 152

                           170       180
                    ....*....|....*....|...
gi 1631970699   424 IACNNKGYYTQISTLADAQESVM 446
Cdd:smart00327  153 LASAPGGVYVFLPELLDLLIDLL 175
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 263-443 1.81e-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: 84.38  E-value: 1.81e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  263 QAATSPKDIVILVDISGSMKGLRMAIAKHTITTILDTLGENDFVNIIAYNDYVHYIEPcfkgiLVQAdrDNREHFKQLVD 342
Cdd:COG2304     86 AEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLP-----PTPA--TDRAKILAAID 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  343 ELMVKGVGVVSQALIEAFEILKQFQESKQgslcNQAIMLITDGAV-------EDYEPVFETYNwpDRKVRVFTYLIGREV 415
Cdd:COG2304    159 RLQAGGGTALGAGLELAYELARKHFIPGR----VNRVILLTDGDAnvgitdpEELLKLAEEAR--EEGITLTTLGVGSDY 232

                          170       180
                   ....*....|....*....|....*...
gi 1631970699  416 TfADRMKWIACNNKGYYTQISTLADAQE 443
Cdd:COG2304    233 N-EDLLERLADAGGGNYYYIDDPEEAEK 259
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 267-447 2.61e-15

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: 77.29  E-value: 2.61e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  267 SPKDIVILVDISGSMKGL-RMAIAKHTITTILDTLGENDFVNIIAYNDYVHyiepcfkgiLVQADRDNREHFKQLVDELM 345
Cdd:COG1240     91 RGRDVVLVVDASGSMAAEnRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAE---------VLLPLTRDREALKRALDELP 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  346 VKGVGVVSQALIEAFEILKQFQESKQgslcnQAIMLITDGA--VEDYEPVFETYNWPDRKVRVFTYLIGREVTFADRMKW 423
Cdd:COG1240    162 PGGGTPLGDALALALELLKRADPARR-----KVIVLLTDGRdnAGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEGLLRE 236

                          170       180
                   ....*....|....*....|....
gi 1631970699  424 IACNNKGYYTQISTLADAQESVME 447
Cdd:COG1240    237 IAEATGGRYFRADDLSELAAIYRE 260
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 270-432 3.55e-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: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 71.44  E-value: 3.55e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  270 DIVILVDISGSMKGLRMAIAKHTITTILDTL---GENDFVNIIAYNDYVHYIEPcfkgilvQADRDNREHFKQLVDELMV 346
Cdd:cd00198      2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLsasPPGDRVGLVTFGSNARVVLP-------LTTDTDKADLLEAIDALKK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  347 KGVGV--VSQALIEAFEILKQFQESKQGslcnQAIMLITDGAVEDYEPVFETY--NWPDRKVRVFTYLIGREVTFADrMK 422
Cdd:cd00198     75 GLGGGtnIGAALRLALELLKSAKRPNAR----RVIILLTDGEPNDGPELLAEAarELRKLGITVYTIGIGDDANEDE-LK 149

                          170
                   ....*....|
gi 1631970699  423 WIACNNKGYY 432
Cdd:cd00198    150 EIADKTTGGA 159
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 268-425 5.80e-14

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 73.18  E-value: 5.80e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  268 PKDIVILVDISGSMKGLRMAIAKHTITTILDTLGENDFVNIIAYNDYVHyiepcfkgilVQADRDNREHFKQLVDEL-MV 346
Cdd:COG2425    118 EGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVV----------EDLPLTADDGLEDAIEFLsGL 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  347 KGVG--VVSQALIEAFEILKQFQESkqgslcNQAIMLITDGAV-EDYEPVFETYNWPDRKVRVFTYLIGREVTFAdRMKW 423
Cdd:COG2425    188 FAGGgtDIAPALRAALELLEEPDYR------NADIVLITDGEAgVSPEELLREVRAKESGVRLFTVAIGDAGNPG-LLEA 260


                   ..
gi 1631970699  424 IA 425
Cdd:COG2425    261 LA 262
VWA_3 pfam13768
von Willebrand factor type A domain;
269-432 2.20e-12

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 65.88  E-value: 2.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  269 KDIVILVDISGSMKGLRMAIaKHTITTILDTLGENDFVNIIAYNDYVhyiEPCFKGILVQADRDNREHFkQLVDELMVK- 347
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLP---RPLFPGWRVVSPRSLQEAF-QFIKTLQPPl 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  348 GVGVVSQALIEAFEilkqfQESKQGslCNQAIMLITDGAVEDYEPVFETY-NWPDRKVRVFTYLIGREVTfADRMKWIAC 426
Cdd:pfam13768   76 GGSDLLGALKEAVR-----APASPG--YIRHVLLLTDGSPMQGETRVSDLiSRAPGKIRFFAYGLGASIS-APMLQLLAE 147


                   ....*.
gi 1631970699  427 NNKGYY 432
Cdd:pfam13768  148 ASNGTY 153
VWA pfam00092
von Willebrand factor type A domain;
270-443 8.47e-10

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 59.21  E-value: 8.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  270 DIVILVDISGSMKGLRMAIAKHTITTILDTLG---ENDFVNIIAYNDYVHyiepcfkgILVQADRD-NREHFKQLVDELM 345
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVR--------TEFPLNDYsSKEELLSAVDNLR 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  346 VKGVG--VVSQALIEAfeiLKQFQESKQGSLCN--QAIMLITDGAVEDYEPVFETYNWPDRKVRVFTylIGreVTFADR- 420
Cdd:pfam00092   73 YLGGGttNTGKALKYA---LENLFSSAAGARPGapKVVVLLTDGRSQDGDPEEVARELKSAGVTVFA--VG--VGNADDe 145

                          170       180
                   ....*....|....*....|....*
gi 1631970699  421 -MKWIAC-NNKGYYTQISTLADAQE 443
Cdd:pfam00092  146 eLRKIASePGEGHVFTVSDFEALED 170
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 270-433 2.20e-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: 2.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  270 DIVILVDISGSMKGLRMAIAKHTITTILDTLGENDFVNIIAYNDYVHYIEPcfkgiLVQADRDNREHFKQLVDELmVKGV 349
Cdd:cd01466      2 DLVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSP-----LRRMTAKGKRSAKRVVDGL-QAGG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  350 GV-VSQALIEAFEILKQFQESKQGSlcnqAIMLITDGAVEDYEPVFETYNWPdrkVRVFTYLIGREVTfADRMKWIACNN 428
Cdd:cd01466     76 GTnVVGGLKKALKVLGDRRQKNPVA----SIMLLSDGQDNHGAVVLRADNAP---IPIHTFGLGASHD-PALLAFIAEIT 147


                   ....*
gi 1631970699  429 KGYYT 433
Cdd:cd01466    148 GGTFS 152
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 518-631 3.10e-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: 49.30  E-value: 3.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  518 ELMKLAPRYKLGVHGYAFLNTNNGYILSHPDlrplyregKKLRPKPNYNSvdlsevewEDQAEILRTAMINGETGSHSMD 597
Cdd:cd12912      1 ELSEIISSIKIGETGYAFLVDKDGTIIAHPD--------KELVGKKISDD--------EAAEEELAKKMLAGKSGSVEYT 64

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1631970699  598 vkvplDKGKRVLfltndYFFTDISDTPFSLGVVL 631
Cdd:cd12912     65 -----FNGEKKY-----VAYAPIPGTGWSLVVVV 88
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 272-443 7.32e-07

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: 50.35  E-value: 7.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  272 VILVDISGSMKGLRMAIAKHTITTILDTLGENDFVNIIAYNDYVHYIEPcfkgilVQADRDnREHFKQLVDELMVKGVGV 351
Cdd:cd01465      4 VFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAETVLP------ATPVRD-KAAILAAIDRLTAGGSTA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  352 VSQALIEAFEILKQFQESKQgslcNQAIMLITDGAVEDYEPVFETY-----NWPDRKVRVFTYLIGREVTfADRMKWIAC 426
Cdd:cd01465     77 GGAGIQLGYQEAQKHFVPGG----VNRILLATDGDFNVGETDPDELarlvaQKRESGITLSTLGFGDNYN-EDLMEAIAD 151

                          170
                   ....*....|....*..
gi 1631970699  427 NNKGYYTQISTLADAQE 443
Cdd:cd01465    152 AGNGNTAYIDNLAEARK 168
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 270-395 1.70e-06

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: 49.21  E-value: 1.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  270 DIVILVDISGSMKGLRMAIAKHTITTILDTL---GENDFVNIIAYNDYVHyIEPCFKgilvqaDRDNREHFKQLVDELMV 346
Cdd:cd01450      2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLdigPDKTRVGLVQYSDDVR-VEFSLN------DYKSKDDLLKAVKNLKY 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1631970699  347 KGVGV--VSQALIEAFEILkqFQESKQGSLCNQAIMLITDGAVEDYEPVFE 395
Cdd:cd01450     75 LGGGGtnTGKALQYALEQL--FSESNARENVPKVIIVLTDGRSDDGGDPKE 123
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
270-415 4.69e-06

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 48.38  E-value: 4.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  270 DIVILVDISGSMKGLRMAIAKHTITTILDTL------GENDFVNIIAYNDYVHYIEPcfkgiLVQADRdnrehFKqlVDE 343
Cdd:COG4245      7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELrqdpyaLETVEVSVITFDGEAKVLLP-----LTDLED-----FQ--PPD 74

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1631970699  344 LMVKGV---GVVSQALIEAFEILKQFQESKQGSLCNQAIMLITDGAV--EDYEPVFETY--NWPDRKVRVFTYLIGREV 415
Cdd:COG4245     75 LSASGGtplGAALELLLDLIERRVQKYTAEGKGDWRPVVFLITDGEPtdSDWEAALQRLkdGEAAKKANIFAIGVGPDA 153
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 488-589 3.32e-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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 46.56  E-value: 3.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  488 TVAMPVFSKKNEtrshgiLLGVVGSDVTLRELMKLAPRYKLGVHGYAFLNTNNGYILSHPDLRPLYRE-----GKKLRPK 562
Cdd:pfam02743  129 TIARPIYDDDGE------VIGVLVADLDLDTLQELLSQIKLGEGGYVFIVDSDGRILAHPLGKNLRSLlapflGKSLADA 202

                           90       100
                   ....*....|....*....|....*..
gi 1631970699  563 PNYNSVDLSEVEWEDQAEILRTAMING 589
Cdd:pfam02743  203 LPGSGITEIAVDLDGEDYLVAYAPIPG 229
PDC2_HK_sensor cd18774
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, ...
 518-631 8.92e-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: 42.43  E-value: 8.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  518 ELMKLAPRYKLGVHGYAFLNTNNGYILSHPDlrplyregkklrpkPNYNSVDLSEVEWEDQAEilrtAMINGETGShsmd 597
Cdd:cd18774      1 YLSDLLSSIKLGETGYAFLVDSDGTILAHPP--------------KELVGKGKSLDDLALLAA----LLLAGESGT---- 58

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1631970699  598 VKVPLDKGKRVLfltndYFFTDISDTPFSLGVVL 631
Cdd:cd18774     59 FEYTSDDGVERL-----VAYRPVPGTPWVVVVGV 87
VWA_2 pfam13519
von Willebrand factor type A domain;
271-365 1.16e-04

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 42.28  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  271 IVILVDISGSM-----KGLRMAIAKHTITTILDTLGeNDFVNIIAYNDYVH-YIEPCfkgilvqadrDNREHFKQLVDEL 344
Cdd:pfam13519    1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSLP-GDRVGLVTFGDGPEvLIPLT----------KDRAKILRALRRL 69

                           90       100
                   ....*....|....*....|..
gi 1631970699  345 MVKGVGV-VSQALIEAFEILKQ 365
Cdd:pfam13519   70 EPKGGGTnLAAALQLARAALKH 91
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 269-412 1.62e-04

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


Pssm-ID: 238739 [Multi-domain]  Cd Length: 152  Bit Score: 43.10  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  269 KDIVILVDISGSMKGLRMAIAKHTITTILDTlgendfvnIIAYNDYVHYIepCFKGILVQADRDNREHFKQLVDELM--V 346
Cdd:cd01462      1 GPVILLVDQSGSMYGAPEEVAKAVALALLRI--------ALAENRDTYLI--LFDSEFQTKIVDKTDDLEEPVEFLSgvQ 70

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631970699  347 KGVGV-VSQALIEAFEILKQ--FQESKqgslcnqaIMLITDGavEDYEPVFETYNWPD----RKVRVFTYLIG 412
Cdd:cd01462     71 LGGGTdINKALRYALELIERrdPRKAD--------IVLITDG--YEGGVSDELLREVElkrsRVARFVALALG 133
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 270-385 9.49e-04

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 41.55  E-value: 9.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631970699  270 DIVILVDISGSMKGL------RMAIAKHTITTILDTLgENDFVNIIAYNDYVHYIEPcfkgilVQADrdnREHFKQLVDE 343
Cdd:cd01467      4 DIMIALDVSGSMLAQdfvkpsRLEAAKEVLSDFIDRR-ENDRIGLVVFAGAAFTQAP------LTLD---RESLKELLED 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1631970699  344 LMVKGVGvVSQALIEAFEI-LKQFQESKQGSlcnQAIMLITDG 385
Cdd:cd01467     74 IKIGLAG-QGTAIGDAIGLaIKRLKNSEAKE---RVIVLLTDG 112
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 463-516 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 1631970699  463 DIIWTEAYMDSrlftSEAQSLMllTTVAMPVFSKknetrshGILLGVVGSDVTL 516
Cdd:cd12913     99 KPVWTEPYIDE----VGTGVLM--ITISVPIYDN-------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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